- INFO: Beginning work on ACE2... {November 16, 2007 4:39:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:40:08 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACE2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1r42.
| PDB = {{PDB2|1r42}}, {{PDB2|1r4l}}, {{PDB2|2ajf}}
| Name = Angiotensin I converting enzyme (peptidyl-dipeptidase A) 2
| HGNCid = 13557
| Symbol = ACE2
| AltSymbols =; ACEH; DKFZP434A014
| OMIM = 300335
| ECnumber =
| Homologene = 41448
| MGIid = 1917258
| GeneAtlas_image1 = PBB_GE_ACE2_219962_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACE2_222257_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001618 |text = viral receptor activity}} {{GNF_GO|id=GO:0004180 |text = carboxypeptidase activity}} {{GNF_GO|id=GO:0004246 |text = peptidyl-dipeptidase A activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0031404 |text = chloride ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0046718 |text = entry of virus into host cell}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 59272
| Hs_Ensembl = ENSG00000130234
| Hs_RefseqProtein = NP_068576
| Hs_RefseqmRNA = NM_021804
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 15489077
| Hs_GenLoc_end = 15530199
| Hs_Uniprot = Q9BYF1
| Mm_EntrezGene = 70008
| Mm_Ensembl = ENSMUSG00000015405
| Mm_RefseqmRNA = NM_027286
| Mm_RefseqProtein = NP_081562
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 159484737
| Mm_GenLoc_end = 159532523
| Mm_Uniprot = Q3URC9
}}
}}
'''Angiotensin I converting enzyme (peptidyl-dipeptidase A) 2''', also known as '''ACE2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACE2 angiotensin I converting enzyme (peptidyl-dipeptidase A) 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=59272| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the angiotensin-converting enzyme family of dipeptidyl carboxydipeptidases and has considerable homology to human angiotensin 1 converting enzyme. This protein catalyzes the cleavage of angiotensin I into angiotensin 1-9. The organ- and cell-specific expression of this gene suggests that it may play a role in the regulation of cardiovascular and renal function, as well as fertility.<ref name="entrez">{{cite web | title = Entrez Gene: ACE2 angiotensin I converting enzyme (peptidyl-dipeptidase A) 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=59272| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Turner AJ, Tipnis SR, Guy JL, ''et al.'' |title=ACEH/ACE2 is a novel mammalian metallocarboxypeptidase and a homologue of angiotensin-converting enzyme insensitive to ACE inhibitors. |journal=Can. J. Physiol. Pharmacol. |volume=80 |issue= 4 |pages= 346-53 |year= 2002 |pmid= 12025971 |doi= }}
*{{cite journal | author=Turner AJ, Hiscox JA, Hooper NM |title=ACE2: from vasopeptidase to SARS virus receptor. |journal=Trends Pharmacol. Sci. |volume=25 |issue= 6 |pages= 291-4 |year= 2004 |pmid= 15165741 |doi= 10.1016/j.tips.2004.04.001 }}
*{{cite journal | author=Katovich MJ, Grobe JL, Huentelman M, Raizada MK |title=Angiotensin-converting enzyme 2 as a novel target for gene therapy for hypertension. |journal=Exp. Physiol. |volume=90 |issue= 3 |pages= 299-305 |year= 2005 |pmid= 15640278 |doi= 10.1113/expphysiol.2004.028522 }}
*{{cite journal | author=Ferrario CM, Trask AJ, Jessup JA |title=Advances in biochemical and functional roles of angiotensin-converting enzyme 2 and angiotensin-(1-7) in regulation of cardiovascular function. |journal=Am. J. Physiol. Heart Circ. Physiol. |volume=289 |issue= 6 |pages= H2281-90 |year= 2006 |pmid= 16055515 |doi= 10.1152/ajpheart.00618.2005 }}
*{{cite journal | author=Jia HP, Look DC, Hickey M, ''et al.'' |title=Infection of human airway epithelia by SARS coronavirus is associated with ACE2 expression and localization. |journal=Adv. Exp. Med. Biol. |volume=581 |issue= |pages= 479-84 |year= 2006 |pmid= 17037581 |doi= }}
*{{cite journal | author=Lazartigues E, Feng Y, Lavoie JL |title=The two fACEs of the tissue renin-angiotensin systems: implication in cardiovascular diseases. |journal=Curr. Pharm. Des. |volume=13 |issue= 12 |pages= 1231-45 |year= 2007 |pmid= 17504232 |doi= }}
*{{cite journal | author=Raizada MK, Ferreira AJ |title=ACE2: a new target for cardiovascular disease therapeutics. |journal=J. Cardiovasc. Pharmacol. |volume=50 |issue= 2 |pages= 112-9 |year= 2007 |pmid= 17703127 |doi= 10.1097/FJC.0b013e3180986219 }}
*{{cite journal | author=Dean RG, Burrell LM |title=ACE2 and diabetic complications. |journal=Curr. Pharm. Des. |volume=13 |issue= 26 |pages= 2730-5 |year= 2007 |pmid= 17897017 |doi= }}
*{{cite journal | author=Tipnis SR, Hooper NM, Hyde R, ''et al.'' |title=A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33238-43 |year= 2000 |pmid= 10924499 |doi= 10.1074/jbc.M002615200 }}
*{{cite journal | author=Donoghue M, Hsieh F, Baronas E, ''et al.'' |title=A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. |journal=Circ. Res. |volume=87 |issue= 5 |pages= E1-9 |year= 2000 |pmid= 10969042 |doi= }}
*{{cite journal | author=Vickers C, Hales P, Kaushik V, ''et al.'' |title=Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase. |journal=J. Biol. Chem. |volume=277 |issue= 17 |pages= 14838-43 |year= 2002 |pmid= 11815627 |doi= 10.1074/jbc.M200581200 }}
*{{cite journal | author=Crackower MA, Sarao R, Oudit GY, ''et al.'' |title=Angiotensin-converting enzyme 2 is an essential regulator of heart function. |journal=Nature |volume=417 |issue= 6891 |pages= 822-8 |year= 2002 |pmid= 12075344 |doi= 10.1038/nature00786 }}
*{{cite journal | author=Harmer D, Gilbert M, Borman R, Clark KL |title=Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme. |journal=FEBS Lett. |volume=532 |issue= 1-2 |pages= 107-10 |year= 2003 |pmid= 12459472 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Donoghue M, Wakimoto H, Maguire CT, ''et al.'' |title=Heart block, ventricular tachycardia, and sudden death in ACE2 transgenic mice with downregulated connexins. |journal=J. Mol. Cell. Cardiol. |volume=35 |issue= 9 |pages= 1043-53 |year= 2004 |pmid= 12967627 |doi= }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal | author=Li W, Moore MJ, Vasilieva N, ''et al.'' |title=Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. |journal=Nature |volume=426 |issue= 6965 |pages= 450-4 |year= 2003 |pmid= 14647384 |doi= 10.1038/nature02145 }}
*{{cite journal | author=Wong SK, Li W, Moore MJ, ''et al.'' |title=A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2. |journal=J. Biol. Chem. |volume=279 |issue= 5 |pages= 3197-201 |year= 2004 |pmid= 14670965 |doi= 10.1074/jbc.C300520200 }}
*{{cite journal | author=Towler P, Staker B, Prasad SG, ''et al.'' |title=ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. |journal=J. Biol. Chem. |volume=279 |issue= 17 |pages= 17996-8007 |year= 2004 |pmid= 14754895 |doi= 10.1074/jbc.M311191200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ACPP... {November 16, 2007 4:26:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:26:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACPP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cvi.
| PDB = {{PDB2|1cvi}}, {{PDB2|1nd5}}, {{PDB2|1nd6}}, {{PDB2|2hpa}}
| Name = Acid phosphatase, prostate
| HGNCid = 125
| Symbol = ACPP
| AltSymbols =; ACP-3; ACP3; PAP
| OMIM = 171790
| ECnumber =
| Homologene = 55552
| MGIid = 1928480
| GeneAtlas_image1 = PBB_GE_ACPP_204393_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003993 |text = acid phosphatase activity}} {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 55
| Hs_Ensembl = ENSG00000014257
| Hs_RefseqProtein = NP_001090
| Hs_RefseqmRNA = NM_001099
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 133518941
| Hs_GenLoc_end = 133569831
| Hs_Uniprot = P15309
| Mm_EntrezGene = 56318
| Mm_Ensembl = ENSMUSG00000032561
| Mm_RefseqmRNA = NM_019807
| Mm_RefseqProtein = NP_062781
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 104146585
| Mm_GenLoc_end = 104196067
| Mm_Uniprot =
}}
}}
'''Acid phosphatase, prostate''', also known as '''ACPP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACPP acid phosphatase, prostate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Prostatic acid phosphatase precursor catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. ACPP is synthesized under androgen regulation and secreted by the epithelial cells of the prostrate gland. Sequence comparison has indicated the presence of several polymorphisms. ACPP undergoes alternative splicing in the 3' UTR.<ref name="entrez">{{cite web | title = Entrez Gene: ACPP acid phosphatase, prostate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ostrowski WS, Kuciel R |title=Human prostatic acid phosphatase: selected properties and practical applications. |journal=Clin. Chim. Acta |volume=226 |issue= 2 |pages= 121-9 |year= 1994 |pmid= 7923807 |doi= }}
*{{cite journal | author=Cooper JF, Foti AG, Shank PW |title=Radioimmunochemical measurement of bone marrow prostatic acid phosphatase. |journal=J. Urol. |volume=119 |issue= 3 |pages= 392-5 |year= 1978 |pmid= 76687 |doi= }}
*{{cite journal | author=Cooper JF, Foti A, Herschman H |title=Combined serum and bone marrow radioimmunoassays for prostatic acid phosphatase. |journal=J. Urol. |volume=122 |issue= 4 |pages= 498-502 |year= 1979 |pmid= 480493 |doi= }}
*{{cite journal | author=Sharief FS, Li SS |title=Structure of human prostatic acid phosphatase gene. |journal=Biochem. Biophys. Res. Commun. |volume=184 |issue= 3 |pages= 1468-76 |year= 1992 |pmid= 1375464 |doi= }}
*{{cite journal | author=Nguyen L, Chapdelaine A, Chevalier S |title=Prostatic acid phosphatase in serum of patients with prostatic cancer is a specific phosphotyrosine acid phosphatase. |journal=Clin. Chem. |volume=36 |issue= 8 Pt 1 |pages= 1450-5 |year= 1990 |pmid= 1696855 |doi= }}
*{{cite journal | author=Kamoshida S, Tsutsumi Y |title=Extraprostatic localization of prostatic acid phosphatase and prostate-specific antigen: distribution in cloacogenic glandular epithelium and sex-dependent expression in human anal gland. |journal=Hum. Pathol. |volume=21 |issue= 11 |pages= 1108-11 |year= 1990 |pmid= 1699876 |doi= }}
*{{cite journal | author=Van Etten RL, Davidson R, Stevis PE, ''et al.'' |title=Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. |journal=J. Biol. Chem. |volume=266 |issue= 4 |pages= 2313-9 |year= 1991 |pmid= 1989985 |doi= }}
*{{cite journal | author=Tailor PG, Govindan MV, Patel PC |title=Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone. |journal=Nucleic Acids Res. |volume=18 |issue= 16 |pages= 4928 |year= 1990 |pmid= 2395659 |doi= }}
*{{cite journal | author=Warhol MJ, Longtine JA |title=The ultrastructural localization of prostatic specific antigen and prostatic acid phosphatase in hyperplastic and neoplastic human prostates. |journal=J. Urol. |volume=134 |issue= 3 |pages= 607-13 |year= 1985 |pmid= 2411954 |doi= }}
*{{cite journal | author=Sharief FS, Lee H, Leuderman MM, ''et al.'' |title=Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. |journal=Biochem. Biophys. Res. Commun. |volume=160 |issue= 1 |pages= 79-86 |year= 1989 |pmid= 2712834 |doi= }}
*{{cite journal | author=Vihko P, Virkkunen P, Henttu P, ''et al.'' |title=Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. |journal=FEBS Lett. |volume=236 |issue= 2 |pages= 275-81 |year= 1988 |pmid= 2842184 |doi= }}
*{{cite journal | author=Yeh LC, Lee AJ, Lee NE, ''et al.'' |title=Molecular cloning of cDNA for human prostatic acid phosphatase. |journal=Gene |volume=60 |issue= 2-3 |pages= 191-6 |year= 1988 |pmid= 2965059 |doi= }}
*{{cite journal | author=Sharief FS, Li SS |title=Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats. |journal=Biochem. Mol. Biol. Int. |volume=33 |issue= 3 |pages= 561-5 |year= 1994 |pmid= 7951074 |doi= }}
*{{cite journal | author=Virkkunen P, Hedberg P, Palvimo JJ, ''et al.'' |title=Structural comparison of human and rat prostate-specific acid phosphatase genes and their promoters: identification of putative androgen response elements. |journal=Biochem. Biophys. Res. Commun. |volume=202 |issue= 1 |pages= 49-57 |year= 1994 |pmid= 8037752 |doi= 10.1006/bbrc.1994.1892 }}
*{{cite journal | author=Banas B, Blaschke D, Fittler F, Hörz W |title=Analysis of the promoter of the human prostatic acid phosphatase gene. |journal=Biochim. Biophys. Acta |volume=1217 |issue= 2 |pages= 188-94 |year= 1994 |pmid= 8110833 |doi= }}
*{{cite journal | author=Ostanin K, Saeed A, Van Etten RL |title=Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site. |journal=J. Biol. Chem. |volume=269 |issue= 12 |pages= 8971-8 |year= 1994 |pmid= 8132635 |doi= }}
*{{cite journal | author=Li SS, Sharief FS |title=The prostatic acid phosphatase (ACPP) gene is localized to human chromosome 3q21-q23. |journal=Genomics |volume=17 |issue= 3 |pages= 765-6 |year= 1993 |pmid= 8244395 |doi= 10.1006/geno.1993.1403 }}
*{{cite journal | author=Lindqvist Y, Schneider G, Vihko P |title=Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate. |journal=J. Biol. Chem. |volume=268 |issue= 28 |pages= 20744-6 |year= 1993 |pmid= 8407898 |doi= }}
*{{cite journal | author=Darson MF, Pacelli A, Roche P, ''et al.'' |title=Human glandular kallikrein 2 (hK2) expression in prostatic intraepithelial neoplasia and adenocarcinoma: a novel prostate cancer marker. |journal=Urology |volume=49 |issue= 6 |pages= 857-62 |year= 1997 |pmid= 9187691 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADH1B... {November 16, 2007 4:26:45 PM PST}
- SEARCH REDIRECT: Control Box Found: ADH1B {November 16, 2007 4:27:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:27:08 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:27:08 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:27:08 PM PST}
- UPDATED: Updated protein page: ADH1B {November 16, 2007 4:27:13 PM PST}
- INFO: Beginning work on CCL20... {November 16, 2007 4:38:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:38:49 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CCL20_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1m8a.
| PDB = {{PDB2|1m8a}}, {{PDB2|2hci}}
| Name = Chemokine (C-C motif) ligand 20
| HGNCid = 10619
| Symbol = CCL20
| AltSymbols =; CKb4; LARC; MIP-3a; MIP3A; SCYA20; ST38
| OMIM = 601960
| ECnumber =
| Homologene = 3375
| MGIid = 1329031
| GeneAtlas_image1 = PBB_GE_CCL20_205476_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008009 |text = chemokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6364
| Hs_Ensembl = ENSG00000115009
| Hs_RefseqProtein = NP_004582
| Hs_RefseqmRNA = NM_004591
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 228386814
| Hs_GenLoc_end = 228390494
| Hs_Uniprot = P78556
| Mm_EntrezGene = 20297
| Mm_Ensembl = ENSMUSG00000026166
| Mm_RefseqmRNA = NM_016960
| Mm_RefseqProtein = NP_058656
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 82995806
| Mm_GenLoc_end = 83005701
| Mm_Uniprot = Q54AI7
}}
}}
'''Chemokine (C-C motif) ligand 20''', also known as '''CCL20''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCL20 chemokine (C-C motif) ligand 20| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6364| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Matoba R, Okubo K, Hori N, ''et al.'' |title=The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression. |journal=Gene |volume=146 |issue= 2 |pages= 199-207 |year= 1994 |pmid= 8076819 |doi= }}
*{{cite journal | author=Rossi DL, Vicari AP, Franz-Bacon K, ''et al.'' |title=Identification through bioinformatics of two new macrophage proinflammatory human chemokines: MIP-3alpha and MIP-3beta. |journal=J. Immunol. |volume=158 |issue= 3 |pages= 1033-6 |year= 1997 |pmid= 9013939 |doi= }}
*{{cite journal | author=Hieshima K, Imai T, Opdenakker G, ''et al.'' |title=Molecular cloning of a novel human CC chemokine liver and activation-regulated chemokine (LARC) expressed in liver. Chemotactic activity for lymphocytes and gene localization on chromosome 2. |journal=J. Biol. Chem. |volume=272 |issue= 9 |pages= 5846-53 |year= 1997 |pmid= 9038201 |doi= }}
*{{cite journal | author=Hromas R, Gray PW, Chantry D, ''et al.'' |title=Cloning and characterization of exodus, a novel beta-chemokine. |journal=Blood |volume=89 |issue= 9 |pages= 3315-22 |year= 1997 |pmid= 9129037 |doi= }}
*{{cite journal | author=Baba M, Imai T, Nishimura M, ''et al.'' |title=Identification of CCR6, the specific receptor for a novel lymphocyte-directed CC chemokine LARC. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14893-8 |year= 1997 |pmid= 9169459 |doi= }}
*{{cite journal | author=Liao F, Alderson R, Su J, ''et al.'' |title=STRL22 is a receptor for the CC chemokine MIP-3alpha. |journal=Biochem. Biophys. Res. Commun. |volume=236 |issue= 1 |pages= 212-7 |year= 1997 |pmid= 9223454 |doi= 10.1006/bbrc.1997.6936 }}
*{{cite journal | author=Power CA, Church DJ, Meyer A, ''et al.'' |title=Cloning and characterization of a specific receptor for the novel CC chemokine MIP-3alpha from lung dendritic cells. |journal=J. Exp. Med. |volume=186 |issue= 6 |pages= 825-35 |year= 1997 |pmid= 9294137 |doi= }}
*{{cite journal | author=Tanaka Y, Imai T, Baba M, ''et al.'' |title=Selective expression of liver and activation-regulated chemokine (LARC) in intestinal epithelium in mice and humans. |journal=Eur. J. Immunol. |volume=29 |issue= 2 |pages= 633-42 |year= 1999 |pmid= 10064080 |doi= }}
*{{cite journal | author=Yang D, Howard OM, Chen Q, Oppenheim JJ |title=Cutting edge: immature dendritic cells generated from monocytes in the presence of TGF-beta 1 express functional C-C chemokine receptor 6. |journal=J. Immunol. |volume=163 |issue= 4 |pages= 1737-41 |year= 1999 |pmid= 10438902 |doi= }}
*{{cite journal | author=Yang D, Chertov O, Bykovskaia SN, ''et al.'' |title=Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6. |journal=Science |volume=286 |issue= 5439 |pages= 525-8 |year= 1999 |pmid= 10521347 |doi= }}
*{{cite journal | author=Charbonnier AS, Kohrgruber N, Kriehuber E, ''et al.'' |title=Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells. |journal=J. Exp. Med. |volume=190 |issue= 12 |pages= 1755-68 |year= 2000 |pmid= 10601351 |doi= }}
*{{cite journal | author=Schutyser E, Struyf S, Menten P, ''et al.'' |title=Regulated production and molecular diversity of human liver and activation-regulated chemokine/macrophage inflammatory protein-3 alpha from normal and transformed cells. |journal=J. Immunol. |volume=165 |issue= 8 |pages= 4470-7 |year= 2000 |pmid= 11035086 |doi= }}
*{{cite journal | author=Hirose J, Kawashima H, Yoshie O, ''et al.'' |title=Versican interacts with chemokines and modulates cellular responses. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 5228-34 |year= 2001 |pmid= 11083865 |doi= 10.1074/jbc.M007542200 }}
*{{cite journal | author=Nakayama T, Fujisawa R, Yamada H, ''et al.'' |title=Inducible expression of a CC chemokine liver- and activation-regulated chemokine (LARC)/macrophage inflammatory protein (MIP)-3 alpha/CCL20 by epidermal keratinocytes and its role in atopic dermatitis. |journal=Int. Immunol. |volume=13 |issue= 1 |pages= 95-103 |year= 2001 |pmid= 11133838 |doi= }}
*{{cite journal | author=Nelson RT, Boyd J, Gladue RP, ''et al.'' |title=Genomic organization of the CC chemokine mip-3alpha/CCL20/larc/exodus/SCYA20, showing gene structure, splice variants, and chromosome localization. |journal=Genomics |volume=73 |issue= 1 |pages= 28-37 |year= 2001 |pmid= 11352563 |doi= 10.1006/geno.2001.6482 }}
*{{cite journal | author=Tohyama M, Shirakara Y, Yamasaki K, ''et al.'' |title=Differentiated keratinocytes are responsible for TNF-alpha regulated production of macrophage inflammatory protein 3alpha/CCL20, a potent chemokine for Langerhans cells. |journal=J. Dermatol. Sci. |volume=27 |issue= 2 |pages= 130-9 |year= 2001 |pmid= 11532377 |doi= }}
*{{cite journal | author=Giannini SL, Hubert P, Doyen J, ''et al.'' |title=Influence of the mucosal epithelium microenvironment on Langerhans cells: implications for the development of squamous intraepithelial lesions of the cervix. |journal=Int. J. Cancer |volume=97 |issue= 5 |pages= 654-9 |year= 2002 |pmid= 11807793 |doi= }}
*{{cite journal | author=Casamayor-Pallejà M, Mondière P, Verschelde C, ''et al.'' |title=BCR ligation reprograms B cells for migration to the T zone and B-cell follicle sequentially. |journal=Blood |volume=99 |issue= 6 |pages= 1913-21 |year= 2002 |pmid= 11877260 |doi= }}
*{{cite journal | author=Schmuth M, Neyer S, Rainer C, ''et al.'' |title=Expression of the C-C chemokine MIP-3 alpha/CCL20 in human epidermis with impaired permeability barrier function. |journal=Exp. Dermatol. |volume=11 |issue= 2 |pages= 135-42 |year= 2002 |pmid= 11994140 |doi= }}
*{{cite journal | author=Liao F, Shirakawa AK, Foley JF, ''et al.'' |title=Human B cells become highly responsive to macrophage-inflammatory protein-3 alpha/CC chemokine ligand-20 after cellular activation without changes in CCR6 expression or ligand binding. |journal=J. Immunol. |volume=168 |issue= 10 |pages= 4871-80 |year= 2002 |pmid= 11994436 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COL17A1... {November 16, 2007 4:27:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:27:47 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Collagen, type XVII, alpha 1
| HGNCid = 2194
| Symbol = COL17A1
| AltSymbols =; BA16H23.2; BP180; BPAG2; KIAA0204; LAD-1
| OMIM = 113811
| ECnumber =
| Homologene = 7276
| MGIid = 88450
| GeneAtlas_image1 = PBB_GE_COL17A1_204636_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0005911 |text = intercellular junction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030056 |text = hemidesmosome}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0008544 |text = epidermis development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1308
| Hs_Ensembl = ENSG00000065618
| Hs_RefseqProtein = NP_570134
| Hs_RefseqmRNA = NM_130778
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 105781034
| Hs_GenLoc_end = 105835750
| Hs_Uniprot = Q9UMD9
| Mm_EntrezGene = 12821
| Mm_Ensembl = ENSMUSG00000025064
| Mm_RefseqmRNA = NM_007732
| Mm_RefseqProtein = NP_031758
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 47699673
| Mm_GenLoc_end = 47745405
| Mm_Uniprot = Q08AT3
}}
}}
'''Collagen, type XVII, alpha 1''', also known as '''COL17A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COL17A1 collagen, type XVII, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1308| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the alpha chain of type XVII collagen. Unlike most collagens, collagen XVII is a transmembrane protein. Collagen XVII is a structural component of hemidesmosomes, multiprotein complexes at the dermal-epidermal basement membrane zone that mediate adhesion of keratinocytes to the underlying membrane. Mutations in this gene are associated with both generalized atrophic benign and junctional epidermolysis bullosa. Two homotrimeric forms of type XVII collagen exist. The full length form is the transmembrane protein. A soluble form, referred to as either ectodomain or LAD-1, is generated by proteolytic processing of the full length form.<ref name="entrez">{{cite web | title = Entrez Gene: COL17A1 collagen, type XVII, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1308| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Giudice GJ, Emery DJ, Diaz LA |title=Cloning and primary structural analysis of the bullous pemphigoid autoantigen BP180. |journal=J. Invest. Dermatol. |volume=99 |issue= 3 |pages= 243-50 |year= 1992 |pmid= 1324962 |doi= }}
*{{cite journal | author=Li KH, Sawamura D, Giudice GJ, ''et al.'' |title=Genomic organization of collagenous domains and chromosomal assignment of human 180-kDa bullous pemphigoid antigen-2, a novel collagen of stratified squamous epithelium. |journal=J. Biol. Chem. |volume=266 |issue= 35 |pages= 24064-9 |year= 1992 |pmid= 1748679 |doi= }}
*{{cite journal | author=Sawamura D, Li KH, Nomura K, ''et al.'' |title=Bullous pemphigoid antigen: cDNA cloning, cellular expression, and evidence for polymorphism of the human gene. |journal=J. Invest. Dermatol. |volume=96 |issue= 6 |pages= 908-15 |year= 1991 |pmid= 2045679 |doi= }}
*{{cite journal | author=McGrath JA, Gatalica B, Christiano AM, ''et al.'' |title=Mutations in the 180-kD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa. |journal=Nat. Genet. |volume=11 |issue= 1 |pages= 83-6 |year= 1995 |pmid= 7550320 |doi= 10.1038/ng0995-83 }}
*{{cite journal | author=Myers JC, Sun MJ, D'Ippolito JA, ''et al.'' |title=Human cDNA clones transcribed from an unusually high-molecular-weight RNA encode a new collagen chain. |journal=Gene |volume=123 |issue= 2 |pages= 211-7 |year= 1993 |pmid= 7916703 |doi= }}
*{{cite journal | author=Hirako Y, Usukura J, Nishizawa Y, Owaribe K |title=Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation. |journal=J. Biol. Chem. |volume=271 |issue= 23 |pages= 13739-45 |year= 1996 |pmid= 8662839 |doi= }}
*{{cite journal | author=McGrath JA, Gatalica B, Li K, ''et al.'' |title=Compound heterozygosity for a dominant glycine substitution and a recessive internal duplication mutation in the type XVII collagen gene results in junctional epidermolysis bullosa and abnormal dentition. |journal=Am. J. Pathol. |volume=148 |issue= 6 |pages= 1787-96 |year= 1996 |pmid= 8669466 |doi= }}
*{{cite journal | author=Gatalica B, Pulkkinen L, Li K, ''et al.'' |title=Cloning of the human type XVII collagen gene (COL17A1), and detection of novel mutations in generalized atrophic benign epidermolysis bullosa. |journal=Am. J. Hum. Genet. |volume=60 |issue= 2 |pages= 352-65 |year= 1997 |pmid= 9012408 |doi= }}
*{{cite journal | author=Jonkman MF, Scheffer H, Stulp R, ''et al.'' |title=Revertant mosaicism in epidermolysis bullosa caused by mitotic gene conversion. |journal=Cell |volume=88 |issue= 4 |pages= 543-51 |year= 1997 |pmid= 9038345 |doi= }}
*{{cite journal | author=Borradori L, Koch PJ, Niessen CM, ''et al.'' |title=The localization of bullous pemphigoid antigen 180 (BP180) in hemidesmosomes is mediated by its cytoplasmic domain and seems to be regulated by the beta4 integrin subunit. |journal=J. Cell Biol. |volume=136 |issue= 6 |pages= 1333-47 |year= 1997 |pmid= 9087447 |doi= }}
*{{cite journal | author=Schumann H, Hammami-Hauasli N, Pulkkinen L, ''et al.'' |title=Three novel homozygous point mutations and a new polymorphism in the COL17A1 gene: relation to biological and clinical phenotypes of junctional epidermolysis bullosa. |journal=Am. J. Hum. Genet. |volume=60 |issue= 6 |pages= 1344-53 |year= 1997 |pmid= 9199555 |doi= }}
*{{cite journal | author=Chavanas S, Gache Y, Tadini G, ''et al.'' |title=A homozygous in-frame deletion in the collagenous domain of bullous pemphigoid antigen BP180 (type XVII collagen) causes generalized atrophic benign epidermolysis bullosa. |journal=J. Invest. Dermatol. |volume=109 |issue= 1 |pages= 74-8 |year= 1997 |pmid= 9204958 |doi= }}
*{{cite journal | author=Darling TN, Yee C, Koh B, ''et al.'' |title=Cycloheximide facilitates the identification of aberrant transcripts resulting from a novel splice-site mutation in COL17A1 in a patient with generalized atrophic benign epidermolysis bullosa. |journal=J. Invest. Dermatol. |volume=110 |issue= 2 |pages= 165-9 |year= 1998 |pmid= 9457913 |doi= 10.1046/j.1523-1747.1998.00103.x }}
*{{cite journal | author=Aho S, Uitto J |title=Direct interaction between the intracellular domains of bullous pemphigoid antigen 2 (BP180) and beta 4 integrin, hemidesmosomal components of basal keratinocytes. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 3 |pages= 694-9 |year= 1998 |pmid= 9500991 |doi= 10.1006/bbrc.1998.8162 }}
*{{cite journal | author=Aho S, McLean WH, Li K, Uitto J |title=cDNA cloning, mRNA expression, and chromosomal mapping of human and mouse periplakin genes. |journal=Genomics |volume=48 |issue= 2 |pages= 242-7 |year= 1998 |pmid= 9521878 |doi= 10.1006/geno.1997.5188 }}
*{{cite journal | author=Schaapveld RQ, Borradori L, Geerts D, ''et al.'' |title=Hemidesmosome formation is initiated by the beta4 integrin subunit, requires complex formation of beta4 and HD1/plectin, and involves a direct interaction between beta4 and the bullous pemphigoid antigen 180. |journal=J. Cell Biol. |volume=142 |issue= 1 |pages= 271-84 |year= 1998 |pmid= 9660880 |doi= }}
*{{cite journal | author=Ishiko A, Shimizu H, Masunaga T, ''et al.'' |title=97 kDa linear IgA bullous dermatosis antigen localizes in the lamina lucida between the NC16A and carboxyl terminal domains of the 180 kDa bullous pemphigoid antigen. |journal=J. Invest. Dermatol. |volume=111 |issue= 1 |pages= 93-6 |year= 1998 |pmid= 9665393 |doi= 10.1046/j.1523-1747.1998.00231.x }}
*{{cite journal | author=Floeth M, Fiedorowicz J, Schäcke H, ''et al.'' |title=Novel homozygous and compound heterozygous COL17A1 mutations associated with junctional epidermolysis bullosa. |journal=J. Invest. Dermatol. |volume=111 |issue= 3 |pages= 528-33 |year= 1998 |pmid= 9740252 |doi= 10.1046/j.1523-1747.1998.00325.x }}
*{{cite journal | author=Schäcke H, Schumann H, Hammami-Hauasli N, ''et al.'' |title=Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain. |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 25937-43 |year= 1998 |pmid= 9748270 |doi= }}
*{{cite journal | author=Aho S, Uitto J |title=180-kD bullous pemphigoid antigen/type XVII collagen: tissue-specific expression and molecular interactions with keratin 18. |journal=J. Cell. Biochem. |volume=72 |issue= 3 |pages= 356-67 |year= 1999 |pmid= 10022517 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CRYAA... {November 16, 2007 4:27:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:28:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Crystallin, alpha A
| HGNCid = 2388
| Symbol = CRYAA
| AltSymbols =; CRYA1; HSPB4
| OMIM = 123580
| ECnumber =
| Homologene = 48053
| MGIid = 88515
| GeneAtlas_image1 = PBB_GE_CRYAA_210199_at_tn.png
| Function = {{GNF_GO|id=GO:0005212 |text = structural constituent of eye lens}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000072 |text = M phase specific microtubule process}} {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1409
| Hs_Ensembl = ENSG00000160202
| Hs_RefseqProtein = NP_000385
| Hs_RefseqmRNA = NM_000394
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 43462210
| Hs_GenLoc_end = 43465982
| Hs_Uniprot = P02489
| Mm_EntrezGene = 12954
| Mm_Ensembl = ENSMUSG00000024041
| Mm_RefseqmRNA = NM_013501
| Mm_RefseqProtein = NP_038529
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 31406661
| Mm_GenLoc_end = 31410057
| Mm_Uniprot = Q546L9
}}
}}
'''Crystallin, alpha A''', also known as '''CRYAA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRYAA crystallin, alpha A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1409| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC).<ref name="entrez">{{cite web | title = Entrez Gene: CRYAA crystallin, alpha A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1409| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Derham BK, Harding JJ |title=Alpha-crystallin as a molecular chaperone. |journal=Progress in retinal and eye research |volume=18 |issue= 4 |pages= 463-509 |year= 1999 |pmid= 10217480 |doi= }}
*{{cite journal | author=de Jong WW, Terwindt EC, Bloemendal H |title=The amino acid sequence of the A chain of human alpha-crystallin. |journal=FEBS Lett. |volume=58 |issue= 1 |pages= 310-3 |year= 1976 |pmid= 817940 |doi= }}
*{{cite journal | author=Ortwerth BJ, Slight SH, Prabhakaram M, ''et al.'' |title=Site-specific glycation of lens crystallins by ascorbic acid. |journal=Biochim. Biophys. Acta |volume=1117 |issue= 2 |pages= 207-15 |year= 1992 |pmid= 1525182 |doi= }}
*{{cite journal | author=Roquemore EP, Dell A, Morris HR, ''et al.'' |title=Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 555-63 |year= 1992 |pmid= 1730617 |doi= }}
*{{cite journal | author=Jaworski CJ, Piatigorsky J |title=A pseudo-exon in the functional human alpha A-crystallin gene. |journal=Nature |volume=337 |issue= 6209 |pages= 752-4 |year= 1989 |pmid= 2918909 |doi= 10.1038/337752a0 }}
*{{cite journal | author=Hawkins JW, Van Keuren ML, Piatigorsky J, ''et al.'' |title=Confirmation of assignment of the human alpha 1-crystallin gene (CRYA1) to chromosome 21 with regional localization to q22.3. |journal=Hum. Genet. |volume=76 |issue= 4 |pages= 375-80 |year= 1987 |pmid= 3610158 |doi= }}
*{{cite journal | author=McDevitt DS, Hawkins JW, Jaworski CJ, Piatigorsky J |title=Isolation and partial characterization of the human alpha A-crystallin gene. |journal=Exp. Eye Res. |volume=43 |issue= 2 |pages= 285-91 |year= 1986 |pmid= 3758227 |doi= }}
*{{cite journal | author=Caspers GJ, Pennings J, De Jong WW |title=A partial cDNA sequence corrects the human alpha A-crystallin primary structure. |journal=Exp. Eye Res. |volume=59 |issue= 1 |pages= 125-6 |year= 1995 |pmid= 7835394 |doi= 10.1006/exer.1994.1089 }}
*{{cite journal | author=Miesbauer LR, Zhou X, Yang Z, ''et al.'' |title=Post-translational modifications of water-soluble human lens crystallins from young adults. |journal=J. Biol. Chem. |volume=269 |issue= 17 |pages= 12494-502 |year= 1994 |pmid= 8175657 |doi= }}
*{{cite journal | author=Jaworski CJ |title=A reassessment of mammalian alpha A-crystallin sequences using DNA sequencing: implications for anthropoid affinities of tarsier. |journal=J. Mol. Evol. |volume=41 |issue= 6 |pages= 901-8 |year= 1996 |pmid= 8587135 |doi= }}
*{{cite journal | author=Takemoto LJ |title=Differential phosphorylation of alpha-A crystallin in human lens of different age. |journal=Exp. Eye Res. |volume=62 |issue= 5 |pages= 499-504 |year= 1996 |pmid= 8759518 |doi= 10.1006/exer.1996.0060 }}
*{{cite journal | author=Prabhakaram M, Katz ML, Ortwerth BJ |title=Glycation mediated crosslinking between alpha-crystallin and MP26 in intact lens membranes. |journal=Mech. Ageing Dev. |volume=91 |issue= 1 |pages= 65-78 |year= 1997 |pmid= 8910261 |doi= }}
*{{cite journal | author=Andley UP, Mathur S, Griest TA, Petrash JM |title=Cloning, expression, and chaperone-like activity of human alphaA-crystallin. |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 31973-80 |year= 1997 |pmid= 8943244 |doi= }}
*{{cite journal | author=Lampi KJ, Ma Z, Shih M, ''et al.'' |title=Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2268-75 |year= 1997 |pmid= 8999933 |doi= }}
*{{cite journal | author=Lindner RA, Kapur A, Carver JA |title=The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27722-9 |year= 1997 |pmid= 9346914 |doi= }}
*{{cite journal | author=Litt M, Kramer P, LaMorticella DM, ''et al.'' |title=Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. |journal=Hum. Mol. Genet. |volume=7 |issue= 3 |pages= 471-4 |year= 1998 |pmid= 9467006 |doi= }}
*{{cite journal | author=Takemoto LJ |title=Quantitation of asparagine-101 deamidation from alpha-A crystallin during aging of the human lens. |journal=Curr. Eye Res. |volume=17 |issue= 3 |pages= 247-50 |year= 1998 |pmid= 9543632 |doi= }}
*{{cite journal | author=Doss EW, Ward KA, Koretz JF |title=Investigation of the 'fines' hypothesis of primary open-angle glaucoma: the possible role of alpha-crystallin. |journal=Ophthalmic Res. |volume=30 |issue= 3 |pages= 142-56 |year= 1998 |pmid= 9618718 |doi= }}
*{{cite journal | author=Lin PP, Barry RC, Smith DL, Smith JB |title=In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin. |journal=Protein Sci. |volume=7 |issue= 6 |pages= 1451-7 |year= 1998 |pmid= 9655350 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSF3R... {November 16, 2007 4:28:11 PM PST}
- SEARCH REDIRECT: Control Box Found: CSF3R {November 16, 2007 4:28:41 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:28:42 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:28:42 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:28:42 PM PST}
- UPDATED: Updated protein page: CSF3R {November 16, 2007 4:28:48 PM PST}
- INFO: Beginning work on GADD45A... {November 16, 2007 4:28:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:29:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Growth arrest and DNA-damage-inducible, alpha
| HGNCid = 4095
| Symbol = GADD45A
| AltSymbols =; DDIT1; GADD45
| OMIM = 126335
| ECnumber =
| Homologene = 1449
| MGIid = 107799
| GeneAtlas_image1 = PBB_GE_GADD45A_203725_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006469 |text = negative regulation of protein kinase activity}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007098 |text = centrosome cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1647
| Hs_Ensembl = ENSG00000116717
| Hs_RefseqProtein = NP_001915
| Hs_RefseqmRNA = NM_001924
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 67923332
| Hs_GenLoc_end = 67926609
| Hs_Uniprot = P24522
| Mm_EntrezGene = 13197
| Mm_Ensembl = ENSMUSG00000036390
| Mm_RefseqmRNA = NM_007836
| Mm_RefseqProtein = NP_031862
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 66964674
| Mm_GenLoc_end = 66966985
| Mm_Uniprot = Q3UMH6
}}
}}
'''Growth arrest and DNA-damage-inducible, alpha''', also known as '''GADD45A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GADD45A growth arrest and DNA-damage-inducible, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1647| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of a group of genes whose transcript levels are increased following stressful growth arrest conditions and treatment with DNA-damaging agents. The protein encoded by this gene responds to environmental stresses by mediating activation of the p38/JNK pathway via MTK1/MEKK4 kinase. The DNA damage-induced transcription of this gene is mediated by both p53-dependent and -independent mechanisms.<ref name="entrez">{{cite web | title = Entrez Gene: GADD45A growth arrest and DNA-damage-inducible, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1647| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hildesheim J, Fornace AJ |title=Gadd45a: an elusive yet attractive candidate gene in pancreatic cancer. |journal=Clin. Cancer Res. |volume=8 |issue= 8 |pages= 2475-9 |year= 2003 |pmid= 12171872 |doi= }}
*{{cite journal | author=Papathanasiou MA, Kerr NC, Robbins JH, ''et al.'' |title=Induction by ionizing radiation of the gadd45 gene in cultured human cells: lack of mediation by protein kinase C. |journal=Mol. Cell. Biol. |volume=11 |issue= 2 |pages= 1009-16 |year= 1991 |pmid= 1990262 |doi= }}
*{{cite journal | author=Chen IT, Smith ML, O'Connor PM, Fornace AJ |title=Direct interaction of Gadd45 with PCNA and evidence for competitive interaction of Gadd45 and p21Waf1/Cip1 with PCNA. |journal=Oncogene |volume=11 |issue= 10 |pages= 1931-7 |year= 1995 |pmid= 7478510 |doi= }}
*{{cite journal | author=Kearsey JM, Coates PJ, Prescott AR, ''et al.'' |title=Gadd45 is a nuclear cell cycle regulated protein which interacts with p21Cip1. |journal=Oncogene |volume=11 |issue= 9 |pages= 1675-83 |year= 1995 |pmid= 7478594 |doi= }}
*{{cite journal | author=Hall PA, Kearsey JM, Coates PJ, ''et al.'' |title=Characterisation of the interaction between PCNA and Gadd45. |journal=Oncogene |volume=10 |issue= 12 |pages= 2427-33 |year= 1995 |pmid= 7784094 |doi= }}
*{{cite journal | author=Carrier F, Smith ML, Bae I, ''et al.'' |title=Characterization of human Gadd45, a p53-regulated protein. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32672-7 |year= 1995 |pmid= 7798274 |doi= }}
*{{cite journal | author=Smith ML, Chen IT, Zhan Q, ''et al.'' |title=Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen. |journal=Science |volume=266 |issue= 5189 |pages= 1376-80 |year= 1994 |pmid= 7973727 |doi= }}
*{{cite journal | author=Hollander MC, Alamo I, Jackman J, ''et al.'' |title=Analysis of the mammalian gadd45 gene and its response to DNA damage. |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 24385-93 |year= 1993 |pmid= 8226988 |doi= }}
*{{cite journal | author=Warbrick E, Lane DP, Glover DM, Cox LS |title=Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: a potential mechanism to co-ordinate DNA replication and repair. |journal=Oncogene |volume=14 |issue= 19 |pages= 2313-21 |year= 1997 |pmid= 9178907 |doi= 10.1038/sj.onc.1201072 }}
*{{cite journal | author=Warbrick E, Heatherington W, Lane DP, Glover DM |title=PCNA binding proteins in Drosophila melanogaster : the analysis of a conserved PCNA binding domain. |journal=Nucleic Acids Res. |volume=26 |issue= 17 |pages= 3925-32 |year= 1998 |pmid= 9705499 |doi= }}
*{{cite journal | author=Takekawa M, Saito H |title=A family of stress-inducible GADD45-like proteins mediate activation of the stress-responsive MTK1/MEKK4 MAPKKK. |journal=Cell |volume=95 |issue= 4 |pages= 521-30 |year= 1998 |pmid= 9827804 |doi= }}
*{{cite journal | author=Carrier F, Georgel PT, Pourquier P, ''et al.'' |title=Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 1673-85 |year= 1999 |pmid= 10022855 |doi= }}
*{{cite journal | author=Zhan Q, Antinore MJ, Wang XW, ''et al.'' |title=Association with Cdc2 and inhibition of Cdc2/Cyclin B1 kinase activity by the p53-regulated protein Gadd45. |journal=Oncogene |volume=18 |issue= 18 |pages= 2892-900 |year= 1999 |pmid= 10362260 |doi= 10.1038/sj.onc.1202667 }}
*{{cite journal | author=Jin S, Antinore MJ, Lung FD, ''et al.'' |title=The GADD45 inhibition of Cdc2 kinase correlates with GADD45-mediated growth suppression. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16602-8 |year= 2000 |pmid= 10747892 |doi= 10.1074/jbc.M000284200 }}
*{{cite journal | author=Vairapandi M, Azam N, Balliet AG, ''et al.'' |title=Characterization of MyD118, Gadd45, and proliferating cell nuclear antigen (PCNA) interacting domains. PCNA impedes MyD118 AND Gadd45-mediated negative growth control. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16810-9 |year= 2000 |pmid= 10828065 |doi= }}
*{{cite journal | author=Yi YW, Kim D, Jung N, ''et al.'' |title=Gadd45 family proteins are coactivators of nuclear hormone receptors. |journal=Biochem. Biophys. Res. Commun. |volume=272 |issue= 1 |pages= 193-8 |year= 2000 |pmid= 10872826 |doi= }}
*{{cite journal | author=Zhao H, Jin S, Antinore MJ, ''et al.'' |title=The central region of Gadd45 is required for its interaction with p21/WAF1. |journal=Exp. Cell Res. |volume=258 |issue= 1 |pages= 92-100 |year= 2000 |pmid= 10912791 |doi= 10.1006/excr.2000.4906 }}
*{{cite journal | author=Yang Q, Manicone A, Coursen JD, ''et al.'' |title=Identification of a functional domain in a GADD45-mediated G2/M checkpoint. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36892-8 |year= 2001 |pmid= 10973963 |doi= 10.1074/jbc.M005319200 }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Kovalsky O, Lung FD, Roller PP, Fornace AJ |title=Oligomerization of human Gadd45a protein. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39330-9 |year= 2001 |pmid= 11498536 |doi= 10.1074/jbc.M105115200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GGT1... {November 16, 2007 4:29:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:30:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Gamma-glutamyltransferase 1
| HGNCid = 4250
| Symbol = GGT1
| AltSymbols =; CD224; D22S672; D22S732; GGT; GTG; MGC96892; MGC96904; MGC96963
| OMIM = 231950
| ECnumber =
| Homologene = 68450
| MGIid = 95706
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003840 |text = gamma-glutamyltransferase activity}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006520 |text = amino acid metabolic process}} {{GNF_GO|id=GO:0006750 |text = glutathione biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2678
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001027536
| Hs_RefseqmRNA = NM_001032364
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 14598
| Mm_Ensembl = ENSMUSG00000006345
| Mm_RefseqmRNA = NM_008116
| Mm_RefseqProtein = NP_032142
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 75012380
| Mm_GenLoc_end = 75029906
| Mm_Uniprot = Q4FK56
}}
}}
'''Gamma-glutamyltransferase 1''', also known as '''GGT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GGT1 gamma-glutamyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2678| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Human gamma-glutamyltransferase catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. This heteroduplex enzyme is composed of a heavy chain and a light chain, which are derived from a single precursor protein, and is present in tissues involved in absorption and secretion. This enzyme is a member of the gamma-glutamyltransferase protein family, of which many members have not yet been fully characterized. This gene encodes several transcript variants; studies suggest that many transcripts of this gene family may be non-functional or represent pseudogenes. The functional transcripts which have been fully characterized have been grouped and classified as type I gamma-glutamyltransferase. Complex splicing events may take place in a tissue-specific manner, resulting in marked dissimilarity in the 5' UTRs. Several 5' UTR transcript variants of the type I gene have been identified in different tissues and cancer cells.<ref name="entrez">{{cite web | title = Entrez Gene: GGT1 gamma-glutamyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2678| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chikhi N, Holic N, Guellaen G, Laperche Y |title=Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. |journal=Comp. Biochem. Physiol. B, Biochem. Mol. Biol. |volume=122 |issue= 4 |pages= 367-80 |year= 1999 |pmid= 10392451 |doi= }}
*{{cite journal | author=Indirani N, Hill PG |title=Partial purification and some properties of gamma-glutamyl transpeptidase from human bile. |journal=Biochim. Biophys. Acta |volume=483 |issue= 1 |pages= 57-62 |year= 1977 |pmid= 18198 |doi= }}
*{{cite journal | author=Tate SS, Ross ME |title=Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. |journal=J. Biol. Chem. |volume=252 |issue= 17 |pages= 6042-5 |year= 1977 |pmid= 19463 |doi= }}
*{{cite journal | author=Welbourne TC |title=Cytoplasmic gamma-glutamyltransferase: isolation, product formation and physiological role. |journal=Current problems in clinical biochemistry |volume=8 |issue= |pages= 201-15 |year= 1978 |pmid= 28899 |doi= }}
*{{cite journal | author=Courtay C, Oster T, Michelet F, ''et al.'' |title=Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues. |journal=Biochem. Pharmacol. |volume=43 |issue= 12 |pages= 2527-33 |year= 1992 |pmid= 1378736 |doi= }}
*{{cite journal | author=Pawlak A, Cohen EH, Octave JN, ''et al.'' |title=An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues. |journal=J. Biol. Chem. |volume=265 |issue= 6 |pages= 3256-62 |year= 1990 |pmid= 1968061 |doi= }}
*{{cite journal | author=Pitot HC, Goodspeed D, Dunn T, ''et al.'' |title=Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis. |journal=Toxicol. Appl. Pharmacol. |volume=97 |issue= 1 |pages= 23-34 |year= 1989 |pmid= 2563599 |doi= }}
*{{cite journal | author=Goodspeed DC, Dunn TJ, Miller CD, Pitot HC |title=Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat. |journal=Gene |volume=76 |issue= 1 |pages= 1-9 |year= 1989 |pmid= 2568315 |doi= }}
*{{cite journal | author=Pawlak A, Wu SJ, Bulle F, ''et al.'' |title=Different gamma-glutamyl transpeptidase mRNAs are expressed in human liver and kidney. |journal=Biochem. Biophys. Res. Commun. |volume=164 |issue= 2 |pages= 912-8 |year= 1989 |pmid= 2573352 |doi= }}
*{{cite journal | author=Laperche Y, Bulle F, Aissani T, ''et al.'' |title=Molecular cloning and nucleotide sequence of rat kidney gamma-glutamyl transpeptidase cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 4 |pages= 937-41 |year= 1986 |pmid= 2869484 |doi= }}
*{{cite journal | author=Bulle F, Mattei MG, Siegrist S, ''et al.'' |title=Assignment of the human gamma-glutamyl transferase gene to the long arm of chromosome 22. |journal=Hum. Genet. |volume=76 |issue= 3 |pages= 283-6 |year= 1987 |pmid= 2885259 |doi= }}
*{{cite journal | author=Tate SS, Khadse V, Wellner D |title=Renal gamma-glutamyl transpeptidases: structural and immunological studies. |journal=Arch. Biochem. Biophys. |volume=262 |issue= 2 |pages= 397-408 |year= 1988 |pmid= 2896486 |doi= }}
*{{cite journal | author=Tate SS, Galbraith RA |title=In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase. |journal=Biochem. Biophys. Res. Commun. |volume=154 |issue= 3 |pages= 1167-73 |year= 1988 |pmid= 2900635 |doi= }}
*{{cite journal | author=Rajpert-De Meyts E, Heisterkamp N, Groffen J |title=Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 8840-4 |year= 1988 |pmid= 2904146 |doi= }}
*{{cite journal | author=Sakamuro D, Yamazoe M, Matsuda Y, ''et al.'' |title=The primary structure of human gamma-glutamyl transpeptidase. |journal=Gene |volume=73 |issue= 1 |pages= 1-9 |year= 1989 |pmid= 2907498 |doi= }}
*{{cite journal | author=Ikeda Y, Fujii J, Anderson ME, ''et al.'' |title=Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22223-8 |year= 1995 |pmid= 7673200 |doi= }}
*{{cite journal | author=Wetmore LA, Gerard C, Drazen JM |title=Human lung expresses unique gamma-glutamyl transpeptidase transcripts. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 16 |pages= 7461-5 |year= 1993 |pmid= 7689219 |doi= }}
*{{cite journal | author=Ikeda Y, Fujii J, Taniguchi N, Meister A |title=Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. |journal=J. Biol. Chem. |volume=270 |issue= 21 |pages= 12471-5 |year= 1995 |pmid= 7759490 |doi= }}
*{{cite journal | author=Courtay C, Heisterkamp N, Siest G, Groffen J |title=Expression of multiple gamma-glutamyltransferase genes in man. |journal=Biochem. J. |volume=297 ( Pt 3) |issue= |pages= 503-8 |year= 1994 |pmid= 7906515 |doi= }}
*{{cite journal | author=Ikeda Y, Fujii J, Taniguchi N |title=Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. |journal=J. Biol. Chem. |volume=268 |issue= 6 |pages= 3980-5 |year= 1993 |pmid= 8095045 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on H3F3A... {November 16, 2007 4:30:03 PM PST}
- SEARCH REDIRECT: Control Box Found: H3F3A {November 16, 2007 4:30:41 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:30:42 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:30:42 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:30:42 PM PST}
- UPDATED: Updated protein page: H3F3A {November 16, 2007 4:30:49 PM PST}
- INFO: Beginning work on KCNMA1... {November 16, 2007 4:30:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:31:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Potassium large conductance calcium-activated channel, subfamily M, alpha member 1
| HGNCid = 6284
| Symbol = KCNMA1
| AltSymbols =; BKTM; DKFZp686K1437; KCa1.1; MGC71881; MaxiK; SAKCA; SLO; SLO-ALPHA
| OMIM = 600150
| ECnumber =
| Homologene = 1693
| MGIid = 99923
| GeneAtlas_image1 = PBB_GE_KCNMA1_221583_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_KCNMA1_221584_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_KCNMA1_214921_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005249 |text = voltage-gated potassium channel activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015269 |text = calcium-activated potassium channel activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0008076 |text = voltage-gated potassium channel complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007269 |text = neurotransmitter secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3778
| Hs_Ensembl = ENSG00000156113
| Hs_RefseqProtein = NP_001014797
| Hs_RefseqmRNA = NM_001014797
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 78307361
| Hs_GenLoc_end = 79068359
| Hs_Uniprot = Q12791
| Mm_EntrezGene = 16531
| Mm_Ensembl = ENSMUSG00000063142
| Mm_RefseqmRNA = NM_010610
| Mm_RefseqProtein = NP_034740
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 22077983
| Mm_GenLoc_end = 22792677
| Mm_Uniprot = Q3TSL8
}}
}}
'''Potassium large conductance calcium-activated channel, subfamily M, alpha member 1''', also known as '''KCNMA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNMA1 potassium large conductance calcium-activated channel, subfamily M, alpha member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3778| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = MaxiK channels are large conductance, voltage and calcium-sensitive potassium channels which are fundamental to the control of smooth muscle tone and neuronal excitability. MaxiK channels can be formed by 2 subunits: the pore-forming alpha subunit, which is the product of this gene, and the modulatory beta subunit. Intracellular calcium regulates the physical association between the alpha and beta subunits. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: KCNMA1 potassium large conductance calcium-activated channel, subfamily M, alpha member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3778| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Magleby KL |title=Gating mechanism of BK (Slo1) channels: so near, yet so far. |journal=J. Gen. Physiol. |volume=121 |issue= 2 |pages= 81-96 |year= 2003 |pmid= 12566537 |doi= }}
*{{cite journal | author=Wei AD, Gutman GA, Aldrich R, ''et al.'' |title=International Union of Pharmacology. LII. Nomenclature and molecular relationships of calcium-activated potassium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 463-72 |year= 2006 |pmid= 16382103 |doi= 10.1124/pr.57.4.9 }}
*{{cite journal | author=McCobb DP, Fowler NL, Featherstone T, ''et al.'' |title=A human calcium-activated potassium channel gene expressed in vascular smooth muscle. |journal=Am. J. Physiol. |volume=269 |issue= 3 Pt 2 |pages= H767-77 |year= 1995 |pmid= 7573516 |doi= }}
*{{cite journal | author=Butler A, Tsunoda S, McCobb DP, ''et al.'' |title=mSlo, a complex mouse gene encoding "maxi" calcium-activated potassium channels. |journal=Science |volume=261 |issue= 5118 |pages= 221-4 |year= 1993 |pmid= 7687074 |doi= }}
*{{cite journal | author=Dworetzky SI, Trojnacki JT, Gribkoff VK |title=Cloning and expression of a human large-conductance calcium-activated potassium channel. |journal=Brain Res. Mol. Brain Res. |volume=27 |issue= 1 |pages= 189-93 |year= 1995 |pmid= 7877450 |doi= }}
*{{cite journal | author=Pallanck L, Ganetzky B |title=Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke. |journal=Hum. Mol. Genet. |volume=3 |issue= 8 |pages= 1239-43 |year= 1995 |pmid= 7987297 |doi= }}
*{{cite journal | author=Tseng-Crank J, Foster CD, Krause JD, ''et al.'' |title=Cloning, expression, and distribution of functionally distinct Ca(2+)-activated K+ channel isoforms from human brain. |journal=Neuron |volume=13 |issue= 6 |pages= 1315-30 |year= 1995 |pmid= 7993625 |doi= }}
*{{cite journal | author=Knaus HG, Folander K, Garcia-Calvo M, ''et al.'' |title=Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle. |journal=J. Biol. Chem. |volume=269 |issue= 25 |pages= 17274-8 |year= 1994 |pmid= 8006036 |doi= }}
*{{cite journal | author=Meera P, Wallner M, Jiang Z, Toro L |title=A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels. |journal=FEBS Lett. |volume=382 |issue= 1-2 |pages= 84-8 |year= 1996 |pmid= 8612769 |doi= }}
*{{cite journal | author=Wallner M, Meera P, Ottolia M, ''et al.'' |title=Characterization of and modulation by a beta-subunit of a human maxi KCa channel cloned from myometrium. |journal=Recept. Channels |volume=3 |issue= 3 |pages= 185-99 |year= 1996 |pmid= 8821792 |doi= }}
*{{cite journal | author=Wallner M, Meera P, Toro L |title=Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N terminus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 25 |pages= 14922-7 |year= 1997 |pmid= 8962157 |doi= }}
*{{cite journal | author=Meera P, Wallner M, Song M, Toro L |title=Large conductance voltage- and calcium-dependent K+ channel, a distinct member of voltage-dependent ion channels with seven N-terminal transmembrane segments (S0-S6), an extracellular N terminus, and an intracellular (S9-S10) C terminus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 25 |pages= 14066-71 |year= 1998 |pmid= 9391153 |doi= }}
*{{cite journal | author=Díaz L, Meera P, Amigo J, ''et al.'' |title=Role of the S4 segment in a voltage-dependent calcium-sensitive potassium (hSlo) channel. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32430-6 |year= 1999 |pmid= 9829973 |doi= }}
*{{cite journal | author=Wallner M, Meera P, Toro L |title=Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 7 |pages= 4137-42 |year= 1999 |pmid= 10097176 |doi= }}
*{{cite journal | author=Valverde MA, Rojas P, Amigo J, ''et al.'' |title=Acute activation of Maxi-K channels (hSlo) by estradiol binding to the beta subunit. |journal=Science |volume=285 |issue= 5435 |pages= 1929-31 |year= 1999 |pmid= 10489376 |doi= }}
*{{cite journal | author=Brenner R, Jegla TJ, Wickenden A, ''et al.'' |title=Cloning and functional characterization of novel large conductance calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4. |journal=J. Biol. Chem. |volume=275 |issue= 9 |pages= 6453-61 |year= 2000 |pmid= 10692449 |doi= }}
*{{cite journal | author=Liu QH, Williams DA, McManus C, ''et al.'' |title=HIV-1 gp120 and chemokines activate ion channels in primary macrophages through CCR5 and CXCR4 stimulation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 9 |pages= 4832-7 |year= 2000 |pmid= 10758170 |doi= 10.1073/pnas.090521697 }}
*{{cite journal | author=Quirk JC, Reinhart PH |title=Identification of a novel tetramerization domain in large conductance K(ca) channels. |journal=Neuron |volume=32 |issue= 1 |pages= 13-23 |year= 2001 |pmid= 11604135 |doi= }}
*{{cite journal | author=Soto MA, González C, Lissi E, ''et al.'' |title=Ca(2+)-activated K+ channel inhibition by reactive oxygen species. |journal=Am. J. Physiol., Cell Physiol. |volume=282 |issue= 3 |pages= C461-71 |year= 2002 |pmid= 11832330 |doi= 10.1152/ajpcell.00167.2001 }}
*{{cite journal | author=Wang YW, Ding JP, Xia XM, Lingle CJ |title=Consequences of the stoichiometry of Slo1 alpha and auxiliary beta subunits on functional properties of large-conductance Ca2+-activated K+ channels. |journal=J. Neurosci. |volume=22 |issue= 5 |pages= 1550-61 |year= 2002 |pmid= 11880485 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KCNQ2... {November 16, 2007 4:31:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:32:40 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Potassium voltage-gated channel, KQT-like subfamily, member 2
| HGNCid = 6296
| Symbol = KCNQ2
| AltSymbols =; BFNC; EBN; EBN1; ENB1; HNSPC; KCNA11; KV7.2; KVEBN1
| OMIM = 602235
| ECnumber =
| Homologene = 26174
| MGIid = 1309503
| GeneAtlas_image1 = PBB_GE_KCNQ2_210508_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_KCNQ2_211486_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_KCNQ2_205737_at_tn.png
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005249 |text = voltage-gated potassium channel activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0008076 |text = voltage-gated potassium channel complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007399 |text = nervous system development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3785
| Hs_Ensembl = ENSG00000075043
| Hs_RefseqProtein = NP_004509
| Hs_RefseqmRNA = NM_004518
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 61502007
| Hs_GenLoc_end = 61574437
| Hs_Uniprot = O43526
| Mm_EntrezGene = 16536
| Mm_Ensembl = ENSMUSG00000016346
| Mm_RefseqmRNA = NM_001003824
| Mm_RefseqProtein = NP_001003824
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 181004987
| Mm_GenLoc_end = 181064662
| Mm_Uniprot = Q9Z351
}}
}}
'''Potassium voltage-gated channel, KQT-like subfamily, member 2''', also known as '''KCNQ2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNQ2 potassium voltage-gated channel, KQT-like subfamily, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3785| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The M channel is a slowly activating and deactivating potassium channel that plays a critical role in the regulation of neuronal excitability. The M channel is formed by the association of the protein encoded by this gene and a related protein encoded by the KCNQ3 gene, both integral membrane proteins. M channel currents are inhibited by M1 muscarinic acetylcholine receptors and activated by retigabine, a novel anti-convulsant drug. Defects in this gene are a cause of benign familial neonatal convulsions type 1 (BFNC), also known as epilepsy, benign neonatal type 1 (EBN1). At least five transcript variants encoding five different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: KCNQ2 potassium voltage-gated channel, KQT-like subfamily, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3785| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gutman GA, Chandy KG, Grissmer S, ''et al.'' |title=International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 473-508 |year= 2006 |pmid= 16382104 |doi= 10.1124/pr.57.4.10 }}
*{{cite journal | author=Yokoyama M, Nishi Y, Yoshii J, ''et al.'' |title=Identification and cloning of neuroblastoma-specific and nerve tissue-specific genes through compiled expression profiles. |journal=DNA Res. |volume=3 |issue= 5 |pages= 311-20 |year= 1997 |pmid= 9039501 |doi= }}
*{{cite journal | author=Singh NA, Charlier C, Stauffer D, ''et al.'' |title=A novel potassium channel gene, KCNQ2, is mutated in an inherited epilepsy of newborns. |journal=Nat. Genet. |volume=18 |issue= 1 |pages= 25-9 |year= 1998 |pmid= 9425895 |doi= 10.1038/ng0198-25 }}
*{{cite journal | author=Biervert C, Schroeder BC, Kubisch C, ''et al.'' |title=A potassium channel mutation in neonatal human epilepsy. |journal=Science |volume=279 |issue= 5349 |pages= 403-6 |year= 1998 |pmid= 9430594 |doi= }}
*{{cite journal | author=Yang WP, Levesque PC, Little WA, ''et al.'' |title=Functional expression of two KvLQT1-related potassium channels responsible for an inherited idiopathic epilepsy. |journal=J. Biol. Chem. |volume=273 |issue= 31 |pages= 19419-23 |year= 1998 |pmid= 9677360 |doi= }}
*{{cite journal | author=Tinel N, Lauritzen I, Chouabe C, ''et al.'' |title=The KCNQ2 potassium channel: splice variants, functional and developmental expression. Brain localization and comparison with KCNQ3. |journal=FEBS Lett. |volume=438 |issue= 3 |pages= 171-6 |year= 1998 |pmid= 9827540 |doi= }}
*{{cite journal | author=Wang HS, Pan Z, Shi W, ''et al.'' |title=KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel. |journal=Science |volume=282 |issue= 5395 |pages= 1890-3 |year= 1998 |pmid= 9836639 |doi= }}
*{{cite journal | author=Schroeder BC, Kubisch C, Stein V, Jentsch TJ |title=Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy. |journal=Nature |volume=396 |issue= 6712 |pages= 687-90 |year= 1999 |pmid= 9872318 |doi= 10.1038/25367 }}
*{{cite journal | author=Biervert C, Steinlein OK |title=Structural and mutational analysis of KCNQ2, the major gene locus for benign familial neonatal convulsions. |journal=Hum. Genet. |volume=104 |issue= 3 |pages= 234-40 |year= 1999 |pmid= 10323247 |doi= }}
*{{cite journal | author=Selyanko AA, Hadley JK, Wood IC, ''et al.'' |title=Two types of K(+) channel subunit, Erg1 and KCNQ2/3, contribute to the M-like current in a mammalian neuronal cell. |journal=J. Neurosci. |volume=19 |issue= 18 |pages= 7742-56 |year= 1999 |pmid= 10479678 |doi= }}
*{{cite journal | author=Shapiro MS, Roche JP, Kaftan EJ, ''et al.'' |title=Reconstitution of muscarinic modulation of the KCNQ2/KCNQ3 K(+) channels that underlie the neuronal M current. |journal=J. Neurosci. |volume=20 |issue= 5 |pages= 1710-21 |year= 2000 |pmid= 10684873 |doi= }}
*{{cite journal | author=Rundfeldt C, Netzer R |title=The novel anticonvulsant retigabine activates M-currents in Chinese hamster ovary-cells tranfected with human KCNQ2/3 subunits. |journal=Neurosci. Lett. |volume=282 |issue= 1-2 |pages= 73-6 |year= 2000 |pmid= 10713399 |doi= }}
*{{cite journal | author=Selyanko AA, Hadley JK, Wood IC, ''et al.'' |title=Inhibition of KCNQ1-4 potassium channels expressed in mammalian cells via M1 muscarinic acetylcholine receptors. |journal=J. Physiol. (Lond.) |volume=522 Pt 3 |issue= |pages= 349-55 |year= 2000 |pmid= 10713961 |doi= }}
*{{cite journal | author=Cooper EC, Aldape KD, Abosch A, ''et al.'' |title=Colocalization and coassembly of two human brain M-type potassium channel subunits that are mutated in epilepsy. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 9 |pages= 4914-9 |year= 2000 |pmid= 10781098 |doi= 10.1073/pnas.090092797 }}
*{{cite journal | author=Schwake M, Pusch M, Kharkovets T, Jentsch TJ |title=Surface expression and single channel properties of KCNQ2/KCNQ3, M-type K+ channels involved in epilepsy. |journal=J. Biol. Chem. |volume=275 |issue= 18 |pages= 13343-8 |year= 2000 |pmid= 10788442 |doi= }}
*{{cite journal | author=Main MJ, Cryan JE, Dupere JR, ''et al.'' |title=Modulation of KCNQ2/3 potassium channels by the novel anticonvulsant retigabine. |journal=Mol. Pharmacol. |volume=58 |issue= 2 |pages= 253-62 |year= 2000 |pmid= 10908292 |doi= }}
*{{cite journal | author=Wickenden AD, Yu W, Zou A, ''et al.'' |title=Retigabine, a novel anti-convulsant, enhances activation of KCNQ2/Q3 potassium channels. |journal=Mol. Pharmacol. |volume=58 |issue= 3 |pages= 591-600 |year= 2000 |pmid= 10953053 |doi= }}
*{{cite journal | author=Tinel N, Diochot S, Lauritzen I, ''et al.'' |title=M-type KCNQ2-KCNQ3 potassium channels are modulated by the KCNE2 subunit. |journal=FEBS Lett. |volume=480 |issue= 2-3 |pages= 137-41 |year= 2000 |pmid= 11034315 |doi= }}
*{{cite journal | author=Smith JS, Iannotti CA, Dargis P, ''et al.'' |title=Differential expression of kcnq2 splice variants: implications to m current function during neuronal development. |journal=J. Neurosci. |volume=21 |issue= 4 |pages= 1096-103 |year= 2001 |pmid= 11160379 |doi= }}
*{{cite journal | author=Miraglia del Giudice E, Coppola G, Scuccimarra G, ''et al.'' |title=Benign familial neonatal convulsions (BFNC) resulting from mutation of the KCNQ2 voltage sensor. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 12 |pages= 994-7 |year= 2001 |pmid= 11175290 |doi= 10.1038/sj.ejhg.5200570 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAD2L1... {November 16, 2007 4:32:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:33:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MAD2L1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1duj.
| PDB = {{PDB2|1duj}}, {{PDB2|1go4}}, {{PDB2|1klq}}, {{PDB2|1s2h}}
| Name = MAD2 mitotic arrest deficient-like 1 (yeast)
| HGNCid = 6763
| Symbol = MAD2L1
| AltSymbols =; HSMAD2; MAD2
| OMIM = 601467
| ECnumber =
| Homologene = 1768
| MGIid = 1860374
| GeneAtlas_image1 = PBB_GE_MAD2L1_203362_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000776 |text = kinetochore}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005816 |text = spindle pole body}}
| Process = {{GNF_GO|id=GO:0000070 |text = mitotic sister chromatid segregation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007094 |text = mitotic cell cycle spindle assembly checkpoint}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4085
| Hs_Ensembl = ENSG00000164109
| Hs_RefseqProtein = NP_002349
| Hs_RefseqmRNA = NM_002358
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 121200029
| Hs_GenLoc_end = 121207411
| Hs_Uniprot = Q13257
| Mm_EntrezGene = 56150
| Mm_Ensembl = ENSMUSG00000029910
| Mm_RefseqmRNA = NM_019499
| Mm_RefseqProtein = NP_062372
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 66465046
| Mm_GenLoc_end = 66470571
| Mm_Uniprot = Q3TV93
}}
}}
'''MAD2 mitotic arrest deficient-like 1 (yeast)''', also known as '''MAD2L1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAD2L1 MAD2 mitotic arrest deficient-like 1 (yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4085| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = MAD2L1 is a component of the mitotic spindle assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. MAD2L1 is related to the MAD2L2 gene located on chromosome 1. A MAD2 pseudogene has been mapped to chromosome 14.<ref name="entrez">{{cite web | title = Entrez Gene: MAD2L1 MAD2 mitotic arrest deficient-like 1 (yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4085| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Li Y, Benezra R |title=Identification of a human mitotic checkpoint gene: hsMAD2. |journal=Science |volume=274 |issue= 5285 |pages= 246-8 |year= 1996 |pmid= 8824189 |doi= }}
*{{cite journal | author=O'Neill TJ, Zhu Y, Gustafson TA |title=Interaction of MAD2 with the carboxyl terminus of the insulin receptor but not with the IGFIR. Evidence for release from the insulin receptor after activation. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 10035-40 |year= 1997 |pmid= 9092546 |doi= }}
*{{cite journal | author=Xu L, Deng HX, Yang Y, ''et al.'' |title=Assignment of mitotic arrest deficient protein 2 (MAD2L1) to human chromosome band 5q23.3 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=78 |issue= 1 |pages= 63-4 |year= 1997 |pmid= 9345911 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Jin DY, Spencer F, Jeang KT |title=Human T cell leukemia virus type 1 oncoprotein Tax targets the human mitotic checkpoint protein MAD1. |journal=Cell |volume=93 |issue= 1 |pages= 81-91 |year= 1998 |pmid= 9546394 |doi= }}
*{{cite journal | author=Krishnan R, Goodman B, Jin DY, ''et al.'' |title=Map location and gene structure of the Homo sapiens mitotic arrest deficient 2 (MAD2L1) gene at 4q27. |journal=Genomics |volume=49 |issue= 3 |pages= 475-8 |year= 1998 |pmid= 9615237 |doi= 10.1006/geno.1998.5233 }}
*{{cite journal | author=Kallio M, Weinstein J, Daum JR, ''et al.'' |title=Mammalian p55CDC mediates association of the spindle checkpoint protein Mad2 with the cyclosome/anaphase-promoting complex, and is involved in regulating anaphase onset and late mitotic events. |journal=J. Cell Biol. |volume=141 |issue= 6 |pages= 1393-406 |year= 1998 |pmid= 9628895 |doi= }}
*{{cite journal | author=Fang G, Yu H, Kirschner MW |title=The checkpoint protein MAD2 and the mitotic regulator CDC20 form a ternary complex with the anaphase-promoting complex to control anaphase initiation. |journal=Genes Dev. |volume=12 |issue= 12 |pages= 1871-83 |year= 1998 |pmid= 9637688 |doi= }}
*{{cite journal | author=Wassmann K, Benezra R |title=Mad2 transiently associates with an APC/p55Cdc complex during mitosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 19 |pages= 11193-8 |year= 1998 |pmid= 9736712 |doi= }}
*{{cite journal | author=Liu YC, Pan J, Zhang C, ''et al.'' |title=A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 8 |pages= 4313-8 |year= 1999 |pmid= 10200259 |doi= }}
*{{cite journal | author=Cahill DP, da Costa LT, Carson-Walter EB, ''et al.'' |title=Characterization of MAD2B and other mitotic spindle checkpoint genes. |journal=Genomics |volume=58 |issue= 2 |pages= 181-7 |year= 1999 |pmid= 10366450 |doi= 10.1006/geno.1999.5831 }}
*{{cite journal | author=Nelson KK, Schlöndorff J, Blobel CP |title=Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta. |journal=Biochem. J. |volume=343 Pt 3 |issue= |pages= 673-80 |year= 2000 |pmid= 10527948 |doi= }}
*{{cite journal | author=Murakumo Y, Roth T, Ishii H, ''et al.'' |title=A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4391-7 |year= 2000 |pmid= 10660610 |doi= }}
*{{cite journal | author=Luo X, Fang G, Coldiron M, ''et al.'' |title=Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20. |journal=Nat. Struct. Biol. |volume=7 |issue= 3 |pages= 224-9 |year= 2000 |pmid= 10700282 |doi= 10.1038/73338 }}
*{{cite journal | author=Poelzl G, Kasai Y, Mochizuki N, ''et al.'' |title=Specific association of estrogen receptor beta with the cell cycle spindle assembly checkpoint protein, MAD2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 6 |pages= 2836-9 |year= 2000 |pmid= 10706629 |doi= 10.1073/pnas.050580997 }}
*{{cite journal | author=Steuerwald N, Cohen J, Herrera RJ, ''et al.'' |title=Association between spindle assembly checkpoint expression and maternal age in human oocytes. |journal=Mol. Hum. Reprod. |volume=7 |issue= 1 |pages= 49-55 |year= 2001 |pmid= 11134360 |doi= }}
*{{cite journal | author=Campbell MS, Chan GK, Yen TJ |title=Mitotic checkpoint proteins HsMAD1 and HsMAD2 are associated with nuclear pore complexes in interphase. |journal=J. Cell. Sci. |volume=114 |issue= Pt 5 |pages= 953-63 |year= 2001 |pmid= 11181178 |doi= }}
*{{cite journal | author=Zhang Y, Lees E |title=Identification of an overlapping binding domain on Cdc20 for Mad2 and anaphase-promoting complex: model for spindle checkpoint regulation. |journal=Mol. Cell. Biol. |volume=21 |issue= 15 |pages= 5190-9 |year= 2001 |pmid= 11438673 |doi= 10.1128/MCB.21.15.5190-5199.2001 }}
*{{cite journal | author=Sudakin V, Chan GK, Yen TJ |title=Checkpoint inhibition of the APC/C in HeLa cells is mediated by a complex of BUBR1, BUB3, CDC20, and MAD2. |journal=J. Cell Biol. |volume=154 |issue= 5 |pages= 925-36 |year= 2001 |pmid= 11535616 |doi= 10.1083/jcb.200102093 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MCM7... {November 16, 2007 4:33:07 PM PST}
- SEARCH REDIRECT: Control Box Found: MCM7 {November 16, 2007 4:33:43 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:33:45 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:33:45 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:33:45 PM PST}
- UPDATED: Updated protein page: MCM7 {November 16, 2007 4:33:51 PM PST}
- INFO: Beginning work on NEDD4... {November 16, 2007 4:33:51 PM PST}
- SEARCH REDIRECT: Control Box Found: NEDD4 {November 16, 2007 4:34:12 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:34:15 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:34:15 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:34:15 PM PST}
- UPDATED: Updated protein page: NEDD4 {November 16, 2007 4:34:21 PM PST}
- INFO: Beginning work on OPA1... {November 16, 2007 4:34:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:34:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Optic atrophy 1 (autosomal dominant)
| HGNCid = 8140
| Symbol = OPA1
| AltSymbols =; FLJ12460; KIAA0567; NPG; NTG; largeG
| OMIM = 605290
| ECnumber =
| Homologene = 14618
| MGIid = 1921393
| GeneAtlas_image1 = PBB_GE_OPA1_212213_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_OPA1_212214_at_tn.png
| GeneAtlas_image3 = PBB_GE_OPA1_214306_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005741 |text = mitochondrial outer membrane}} {{GNF_GO|id=GO:0005758 |text = mitochondrial intermembrane space}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030061 |text = mitochondrial crista}} {{GNF_GO|id=GO:0030425 |text = dendrite}}
| Process = {{GNF_GO|id=GO:0000266 |text = mitochondrial fission}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007007 |text = inner mitochondrial membrane organization and biogenesis}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008053 |text = mitochondrial fusion}} {{GNF_GO|id=GO:0019896 |text = axon transport of mitochondrion}} {{GNF_GO|id=GO:0045768 |text = positive regulation of anti-apoptosis}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4976
| Hs_Ensembl = ENSG00000198836
| Hs_RefseqProtein = NP_056375
| Hs_RefseqmRNA = NM_015560
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 194793806
| Hs_GenLoc_end = 194898009
| Hs_Uniprot = O60313
| Mm_EntrezGene = 74143
| Mm_Ensembl = ENSMUSG00000038084
| Mm_RefseqmRNA = XM_001000561
| Mm_RefseqProtein = XP_001000561
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 29499089
| Mm_GenLoc_end = 29572237
| Mm_Uniprot = P58281
}}
}}
'''Optic atrophy 1 (autosomal dominant)''', also known as '''OPA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OPA1 optic atrophy 1 (autosomal dominant)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4976| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene product is a nuclear-encoded mitochondrial protein with similarity to dynamin-related GTPases. It is a component of the mitochondrial network. Mutations in this gene have been associated with optic atrophy type 1, which is a dominantly inherited optic neuropathy resulting in progressive loss of visual acuity, leading in many cases to legal blindness. Eight transcript variants encoding different isoforms, resulting from alternative splicing of exon 4 and two novel exons named 4b and 5b, have been reported for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: OPA1 optic atrophy 1 (autosomal dominant)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4976| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Olichon A, Guillou E, Delettre C, ''et al.'' |title=Mitochondrial dynamics and disease, OPA1. |journal=Biochim. Biophys. Acta |volume=1763 |issue= 5-6 |pages= 500-9 |year= 2006 |pmid= 16737747 |doi= 10.1016/j.bbamcr.2006.04.003 }}
*{{cite journal | author=Pawlikowska P, Orzechowski A |title=[Role of transmembrane GTPases in mitochondrial morphology and activity] |journal=Postepy Biochem. |volume=53 |issue= 1 |pages= 53-9 |year= 2007 |pmid= 17718388 |doi= }}
*{{cite journal | author=Votruba M, Moore AT, Bhattacharya SS |title=Demonstration of a founder effect and fine mapping of dominant optic atrophy locus on 3q28-qter by linkage disequilibrium method: a study of 38 British Isles pedigrees. |journal=Hum. Genet. |volume=102 |issue= 1 |pages= 79-86 |year= 1998 |pmid= 9490303 |doi= }}
*{{cite journal | author=Nagase T, Ishikawa K, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 1 |pages= 31-9 |year= 1998 |pmid= 9628581 |doi= }}
*{{cite journal | author=Johnston RL, Seller MJ, Behnam JT, ''et al.'' |title=Dominant optic atrophy. Refining the clinical diagnostic criteria in light of genetic linkage studies. |journal=Ophthalmology |volume=106 |issue= 1 |pages= 123-8 |year= 1999 |pmid= 9917792 |doi= 10.1016/S0161-6420(99)90013-1 }}
*{{cite journal | author=Delettre C, Lenaers G, Griffoin JM, ''et al.'' |title=Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy. |journal=Nat. Genet. |volume=26 |issue= 2 |pages= 207-10 |year= 2000 |pmid= 11017079 |doi= 10.1038/79936 }}
*{{cite journal | author=Alexander C, Votruba M, Pesch UE, ''et al.'' |title=OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. |journal=Nat. Genet. |volume=26 |issue= 2 |pages= 211-5 |year= 2000 |pmid= 11017080 |doi= 10.1038/79944 }}
*{{cite journal | author=Toomes C, Marchbank NJ, Mackey DA, ''et al.'' |title=Spectrum, frequency and penetrance of OPA1 mutations in dominant optic atrophy. |journal=Hum. Mol. Genet. |volume=10 |issue= 13 |pages= 1369-78 |year= 2001 |pmid= 11440989 |doi= }}
*{{cite journal | author=Thiselton DL, Alexander C, Morris A, ''et al.'' |title=A frameshift mutation in exon 28 of the OPA1 gene explains the high prevalence of dominant optic atrophy in the Danish population: evidence for a founder effect. |journal=Hum. Genet. |volume=109 |issue= 5 |pages= 498-502 |year= 2001 |pmid= 11735024 |doi= 10.1007/s004390100600 }}
*{{cite journal | author=Delettre C, Griffoin JM, Kaplan J, ''et al.'' |title=Mutation spectrum and splicing variants in the OPA1 gene. |journal=Hum. Genet. |volume=109 |issue= 6 |pages= 584-91 |year= 2002 |pmid= 11810270 |doi= 10.1007/s00439-001-0633-y }}
*{{cite journal | author=Aung T, Ocaka L, Ebenezer ND, ''et al.'' |title=A major marker for normal tension glaucoma: association with polymorphisms in the OPA1 gene. |journal=Hum. Genet. |volume=110 |issue= 1 |pages= 52-6 |year= 2002 |pmid= 11810296 |doi= 10.1007/s00439-001-0645-7 }}
*{{cite journal | author=Misaka T, Miyashita T, Kubo Y |title=Primary structure of a dynamin-related mouse mitochondrial GTPase and its distribution in brain, subcellular localization, and effect on mitochondrial morphology. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15834-42 |year= 2002 |pmid= 11847212 |doi= 10.1074/jbc.M109260200 }}
*{{cite journal | author=Thiselton DL, Alexander C, Taanman JW, ''et al.'' |title=A comprehensive survey of mutations in the OPA1 gene in patients with autosomal dominant optic atrophy. |journal=Invest. Ophthalmol. Vis. Sci. |volume=43 |issue= 6 |pages= 1715-24 |year= 2002 |pmid= 12036970 |doi= }}
*{{cite journal | author=Aung T, Ocaka L, Ebenezer ND, ''et al.'' |title=Investigating the association between OPA1 polymorphisms and glaucoma: comparison between normal tension and high tension primary open angle glaucoma. |journal=Hum. Genet. |volume=110 |issue= 5 |pages= 513-4 |year= 2002 |pmid= 12073024 |doi= 10.1007/s00439-002-0711-9 }}
*{{cite journal | author=Olichon A, Emorine LJ, Descoins E, ''et al.'' |title=The human dynamin-related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter-membrane space. |journal=FEBS Lett. |volume=523 |issue= 1-3 |pages= 171-6 |year= 2002 |pmid= 12123827 |doi= }}
*{{cite journal | author=Marchbank NJ, Craig JE, Leek JP, ''et al.'' |title=Deletion of the OPA1 gene in a dominant optic atrophy family: evidence that haploinsufficiency is the cause of disease. |journal=J. Med. Genet. |volume=39 |issue= 8 |pages= e47 |year= 2002 |pmid= 12161614 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Satoh M, Hamamoto T, Seo N, ''et al.'' |title=Differential sublocalization of the dynamin-related protein OPA1 isoforms in mitochondria. |journal=Biochem. Biophys. Res. Commun. |volume=300 |issue= 2 |pages= 482-93 |year= 2003 |pmid= 12504110 |doi= }}
*{{cite journal | author=Olichon A, Baricault L, Gas N, ''et al.'' |title=Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. |journal=J. Biol. Chem. |volume=278 |issue= 10 |pages= 7743-6 |year= 2003 |pmid= 12509422 |doi= 10.1074/jbc.C200677200 }}
*{{cite journal | author=Shimizu S, Mori N, Kishi M, ''et al.'' |title=A novel mutation in the OPA1 gene in a Japanese patient with optic atrophy. |journal=Am. J. Ophthalmol. |volume=135 |issue= 2 |pages= 256-7 |year= 2003 |pmid= 12566046 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PGF... {November 16, 2007 4:35:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:35:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PGF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rv6.
| PDB = {{PDB2|1rv6}}
| Name = Placental growth factor, vascular endothelial growth factor-related protein
| HGNCid = 8893
| Symbol = PGF
| AltSymbols =; PLGF; PlGF-2
| OMIM = 601121
| ECnumber =
| Homologene = 1978
| MGIid = 105095
| GeneAtlas_image1 = PBB_GE_PGF_209652_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PGF_215179_x_at_tn.png
| Function = {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001658 |text = ureteric bud branching}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5228
| Hs_Ensembl = ENSG00000119630
| Hs_RefseqProtein = NP_002623
| Hs_RefseqmRNA = NM_002632
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 74479162
| Hs_GenLoc_end = 74492220
| Hs_Uniprot = P49763
| Mm_EntrezGene = 18654
| Mm_Ensembl = ENSMUSG00000004791
| Mm_RefseqmRNA = NM_008827
| Mm_RefseqProtein = NP_032853
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 86058457
| Mm_GenLoc_end = 86066066
| Mm_Uniprot = Q544A5
}}
}}
'''Placental growth factor, vascular endothelial growth factor-related protein''', also known as '''PGF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PGF placental growth factor, vascular endothelial growth factor-related protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5228| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Luttun A, Tjwa M, Carmeliet P |title=Placental growth factor (PlGF) and its receptor Flt-1 (VEGFR-1): novel therapeutic targets for angiogenic disorders. |journal=Ann. N. Y. Acad. Sci. |volume=979 |issue= |pages= 80-93 |year= 2003 |pmid= 12543719 |doi= }}
*{{cite journal | author=Maglione D, Guerriero V, Viglietto G, ''et al.'' |title=Isolation of a human placenta cDNA coding for a protein related to the vascular permeability factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 20 |pages= 9267-71 |year= 1991 |pmid= 1924389 |doi= }}
*{{cite journal | author=Maglione D, Guerriero V, Viglietto G, ''et al.'' |title=Two alternative mRNAs coding for the angiogenic factor, placenta growth factor (PlGF), are transcribed from a single gene of chromosome 14. |journal=Oncogene |volume=8 |issue= 4 |pages= 925-31 |year= 1993 |pmid= 7681160 |doi= }}
*{{cite journal | author=Park JE, Chen HH, Winer J, ''et al.'' |title=Placenta growth factor. Potentiation of vascular endothelial growth factor bioactivity, in vitro and in vivo, and high affinity binding to Flt-1 but not to Flk-1/KDR. |journal=J. Biol. Chem. |volume=269 |issue= 41 |pages= 25646-54 |year= 1994 |pmid= 7929268 |doi= }}
*{{cite journal | author=Hauser S, Weich HA |title=A heparin-binding form of placenta growth factor (PlGF-2) is expressed in human umbilical vein endothelial cells and in placenta. |journal=Growth Factors |volume=9 |issue= 4 |pages= 259-68 |year= 1994 |pmid= 8148155 |doi= }}
*{{cite journal | author=Mattei MG, Borg JP, Rosnet O, ''et al.'' |title=Assignment of vascular endothelial growth factor (VEGF) and placenta growth factor (PLGF) genes to human chromosome 6p12-p21 and 14q24-q31 regions, respectively. |journal=Genomics |volume=32 |issue= 1 |pages= 168-9 |year= 1996 |pmid= 8786112 |doi= 10.1006/geno.1996.0098 }}
*{{cite journal | author=Ziche M, Maglione D, Ribatti D, ''et al.'' |title=Placenta growth factor-1 is chemotactic, mitogenic, and angiogenic. |journal=Lab. Invest. |volume=76 |issue= 4 |pages= 517-31 |year= 1997 |pmid= 9111514 |doi= }}
*{{cite journal | author=Vuorela P, Hatva E, Lymboussaki A, ''et al.'' |title=Expression of vascular endothelial growth factor and placenta growth factor in human placenta. |journal=Biol. Reprod. |volume=56 |issue= 2 |pages= 489-94 |year= 1997 |pmid= 9116151 |doi= }}
*{{cite journal | author=Cao Y, Ji WR, Qi P, ''et al.'' |title=Placenta growth factor: identification and characterization of a novel isoform generated by RNA alternative splicing. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 493-8 |year= 1997 |pmid= 9207183 |doi= 10.1006/bbrc.1997.6813 }}
*{{cite journal | author=Davis-Smyth T, Presta LG, Ferrara N |title=Mapping the charged residues in the second immunoglobulin-like domain of the vascular endothelial growth factor/placenta growth factor receptor Flt-1 required for binding and structural stability. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3216-22 |year= 1998 |pmid= 9452434 |doi= }}
*{{cite journal | author=Landgren E, Schiller P, Cao Y, Claesson-Welsh L |title=Placenta growth factor stimulates MAP kinase and mitogenicity but not phospholipase C-gamma and migration of endothelial cells expressing Flt 1. |journal=Oncogene |volume=16 |issue= 3 |pages= 359-67 |year= 1998 |pmid= 9467961 |doi= 10.1038/sj.onc.1201545 }}
*{{cite journal | author=Gluzman-Poltorak Z, Cohen T, Herzog Y, Neufeld G |title=Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected]. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18040-5 |year= 2000 |pmid= 10748121 |doi= 10.1074/jbc.M909259199 }}
*{{cite journal | author=Renedo M, Arce I, Montgomery K, ''et al.'' |title=A sequence-ready physical map of the region containing the human natural killer gene complex on chromosome 12p12.3-p13.2. |journal=Genomics |volume=65 |issue= 2 |pages= 129-36 |year= 2000 |pmid= 10783260 |doi= 10.1006/geno.2000.6163 }}
*{{cite journal | author=Maglione D, Battisti M, Tucci M |title=Recombinant production of PIGF-1 and its activity in animal models. |journal=Farmaco |volume=55 |issue= 3 |pages= 165-7 |year= 2000 |pmid= 10919072 |doi= }}
*{{cite journal | author=Roberts-Clark DJ, Smith AJ |title=Angiogenic growth factors in human dentine matrix. |journal=Arch. Oral Biol. |volume=45 |issue= 11 |pages= 1013-6 |year= 2000 |pmid= 11000388 |doi= }}
*{{cite journal | author=Iyer S, Leonidas DD, Swaminathan GJ, ''et al.'' |title=The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 A resolution. |journal=J. Biol. Chem. |volume=276 |issue= 15 |pages= 12153-61 |year= 2001 |pmid= 11069911 |doi= 10.1074/jbc.M008055200 }}
*{{cite journal | author=Li XF, Charnock-Jones DS, Zhang E, ''et al.'' |title=Angiogenic growth factor messenger ribonucleic acids in uterine natural killer cells. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 4 |pages= 1823-34 |year= 2001 |pmid= 11297624 |doi= }}
*{{cite journal | author=Su YN, Hsu JJ, Lee CN, ''et al.'' |title=Raised maternal serum placenta growth factor concentration during the second trimester is associated with Down syndrome. |journal=Prenat. Diagn. |volume=22 |issue= 1 |pages= 8-12 |year= 2002 |pmid= 11810642 |doi= }}
*{{cite journal | author=Angelucci C, Lama G, Iacopino F, ''et al.'' |title=Effect of placenta growth factor-1 on proliferation and release of nitric oxide, cyclic AMP and cyclic GMP in human epithelial cells expressing the FLT-1 receptor. |journal=Growth Factors |volume=19 |issue= 3 |pages= 193-206 |year= 2002 |pmid= 11811792 |doi= }}
*{{cite journal | author=Mamluk R, Gechtman Z, Kutcher ME, ''et al.'' |title=Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain. |journal=J. Biol. Chem. |volume=277 |issue= 27 |pages= 24818-25 |year= 2002 |pmid= 11986311 |doi= 10.1074/jbc.M200730200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PIGR... {November 16, 2007 4:35:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:36:25 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PIGR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xed.
| PDB = {{PDB2|1xed}}, {{PDB2|2ocw}}
| Name = Polymeric immunoglobulin receptor
| HGNCid = 8968
| Symbol = PIGR
| AltSymbols =; MGC125361; MGC125362
| OMIM = 173880
| ECnumber =
| Homologene = 1984
| MGIid = 103080
| GeneAtlas_image1 = PBB_GE_PIGR_204213_at_tn.png
| Function = {{GNF_GO|id=GO:0008565 |text = protein transporter activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0009306 |text = protein secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5284
| Hs_Ensembl = ENSG00000162896
| Hs_RefseqProtein = NP_002635
| Hs_RefseqmRNA = NM_002644
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 205168486
| Hs_GenLoc_end = 205186434
| Hs_Uniprot = P01833
| Mm_EntrezGene = 18703
| Mm_Ensembl = ENSMUSG00000026417
| Mm_RefseqmRNA = NM_011082
| Mm_RefseqProtein = NP_035212
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 132654297
| Mm_GenLoc_end = 132866011
| Mm_Uniprot = Q8R544
}}
}}
'''Polymeric immunoglobulin receptor''', also known as '''PIGR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PIGR polymeric immunoglobulin receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5284| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The poly-Ig receptor is expressed on several glandular epithelia including those of liver and breast. It mediates transcellular transport of polymeric immunoglobulin molecules. It is a member of the immunoglobulin superfamily (Hood et al., 1985). The receptor has 5 units with homology to the variable (V) units of immunoglobulins and a transmembrane region, which also has some homology to certain immunoglobulin variable regions.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PIGR polymeric immunoglobulin receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5284| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kaetzel CS |title=The polymeric immunoglobulin receptor: bridging innate and adaptive immune responses at mucosal surfaces. |journal=Immunol. Rev. |volume=206 |issue= |pages= 83-99 |year= 2005 |pmid= 16048543 |doi= 10.1111/j.0105-2896.2005.00278.x }}
*{{cite journal | author=Krajci P, Kvale D, Taskén K, Brandtzaeg P |title=Molecular cloning and exon-intron mapping of the gene encoding human transmembrane secretory component (the poly-Ig receptor) |journal=Eur. J. Immunol. |volume=22 |issue= 9 |pages= 2309-15 |year= 1992 |pmid= 1355431 |doi= }}
*{{cite journal | author=Krajci P, Grzeschik KH, Geurts van Kessel AH, ''et al.'' |title=The human transmembrane secretory component (poly-Ig receptor): molecular cloning, restriction fragment length polymorphism and chromosomal sublocalization. |journal=Hum. Genet. |volume=87 |issue= 6 |pages= 642-8 |year= 1991 |pmid= 1682231 |doi= }}
*{{cite journal | author=Eiffert H, Quentin E, Wiederhold M, ''et al.'' |title=Determination of the molecular structure of the human free secretory component. |journal=Biol. Chem. Hoppe-Seyler |volume=372 |issue= 2 |pages= 119-28 |year= 1991 |pmid= 1859628 |doi= }}
*{{cite journal | author=Bakos MA, Kurosky A, Goldblum RM |title=Characterization of a critical binding site for human polymeric Ig on secretory component. |journal=J. Immunol. |volume=147 |issue= 10 |pages= 3419-26 |year= 1991 |pmid= 1940346 |doi= }}
*{{cite journal | author=Krajci P, Solberg R, Sandberg M, ''et al.'' |title=Molecular cloning of the human transmembrane secretory component (poly-Ig receptor) and its mRNA expression in human tissues. |journal=Biochem. Biophys. Res. Commun. |volume=158 |issue= 3 |pages= 783-9 |year= 1989 |pmid= 2920039 |doi= }}
*{{cite journal | author=Davidson MK, Le Beau MM, Eddy RL, ''et al.'' |title=Genetic mapping of the human polymeric immunoglobulin receptor gene to chromosome region 1q31----q41. |journal=Cytogenet. Cell Genet. |volume=48 |issue= 2 |pages= 107-11 |year= 1989 |pmid= 3197448 |doi= }}
*{{cite journal | author=Hood L, Kronenberg M, Hunkapiller T |title=T cell antigen receptors and the immunoglobulin supergene family. |journal=Cell |volume=40 |issue= 2 |pages= 225-9 |year= 1985 |pmid= 3917857 |doi= }}
*{{cite journal | author=Eiffert H, Quentin E, Decker J, ''et al.'' |title=[The primary structure of human free secretory component and the arrangement of disulfide bonds] |journal=Hoppe-Seyler's Z. Physiol. Chem. |volume=365 |issue= 12 |pages= 1489-95 |year= 1985 |pmid= 6526384 |doi= }}
*{{cite journal | author=Mizoguchi A, Mizuochi T, Kobata A |title=Structures of the carbohydrate moieties of secretory component purified from human milk. |journal=J. Biol. Chem. |volume=257 |issue= 16 |pages= 9612-21 |year= 1982 |pmid= 7107583 |doi= }}
*{{cite journal | author=Coyne RS, Siebrecht M, Peitsch MC, Casanova JE |title=Mutational analysis of polymeric immunoglobulin receptor/ligand interactions. Evidence for the involvement of multiple complementarity determining region (CDR)-like loops in receptor domain I. |journal=J. Biol. Chem. |volume=269 |issue= 50 |pages= 31620-5 |year= 1995 |pmid= 7989333 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Piskurich JF, France JA, Tamer CM, ''et al.'' |title=Interferon-gamma induces polymeric immunoglobulin receptor mRNA in human intestinal epithelial cells by a protein synthesis dependent mechanism. |journal=Mol. Immunol. |volume=30 |issue= 4 |pages= 413-21 |year= 1993 |pmid= 8455639 |doi= }}
*{{cite journal | author=Piskurich JF, Youngman KR, Phillips KM, ''et al.'' |title=Transcriptional regulation of the human polymeric immunoglobulin receptor gene by interferon-gamma. |journal=Mol. Immunol. |volume=34 |issue= 1 |pages= 75-91 |year= 1997 |pmid= 9182878 |doi= }}
*{{cite journal | author=Hughes GJ, Frutiger S, Savoy LA, ''et al.'' |title=Human free secretory component is composed of the first 585 amino acid residues of the polymeric immunoglobulin receptor. |journal=FEBS Lett. |volume=410 |issue= 2-3 |pages= 443-6 |year= 1997 |pmid= 9237679 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Ackermann LW, Wollenweber LA, Denning GM |title=IL-4 and IFN-gamma increase steady state levels of polymeric Ig receptor mRNA in human airway and intestinal epithelial cells. |journal=J. Immunol. |volume=162 |issue= 9 |pages= 5112-8 |year= 1999 |pmid= 10227981 |doi= }}
*{{cite journal | author=Røe M, Norderhaug IN, Brandtzaeg P, Johansen FE |title=Fine specificity of ligand-binding domain 1 in the polymeric Ig receptor: importance of the CDR2-containing region for IgM interaction. |journal=J. Immunol. |volume=162 |issue= 10 |pages= 6046-52 |year= 1999 |pmid= 10229845 |doi= }}
*{{cite journal | author=Norderhaug IN, Johansen FE, Krajci P, Brandtzaeg P |title=Domain deletions in the human polymeric Ig receptor disclose differences between its dimeric IgA and pentameric IgM interaction. |journal=Eur. J. Immunol. |volume=29 |issue= 10 |pages= 3401-9 |year= 1999 |pmid= 10540352 |doi= }}
*{{cite journal | author=Hughes GJ, Reason AJ, Savoy L, ''et al.'' |title=Carbohydrate moieties in human secretory component. |journal=Biochim. Biophys. Acta |volume=1434 |issue= 1 |pages= 86-93 |year= 1999 |pmid= 10556562 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLCG2... {November 16, 2007 4:36:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:36:47 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Phospholipase C, gamma 2 (phosphatidylinositol-specific)
| HGNCid = 9066
| Symbol = PLCG2
| AltSymbols =;
| OMIM = 600220
| ECnumber =
| Homologene = 55671
| MGIid = 97616
| GeneAtlas_image1 = PBB_GE_PLCG2_204613_at_tn.png
| Function = {{GNF_GO|id=GO:0004435 |text = phosphoinositide phospholipase C activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006644 |text = phospholipid metabolic process}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5336
| Hs_Ensembl = ENSG00000197943
| Hs_RefseqProtein = NP_002652
| Hs_RefseqmRNA = NM_002661
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 80370408
| Hs_GenLoc_end = 80549399
| Hs_Uniprot = P16885
| Mm_EntrezGene = 234779
| Mm_Ensembl = ENSMUSG00000034330
| Mm_RefseqmRNA = NM_172285
| Mm_RefseqProtein = NP_758489
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 120384268
| Mm_GenLoc_end = 120521119
| Mm_Uniprot =
}}
}}
'''Phospholipase C, gamma 2 (phosphatidylinositol-specific)''', also known as '''PLCG2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLCG2 phospholipase C, gamma 2 (phosphatidylinositol-specific)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5336| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Enzymes of the phospholipase C family catalyze the hydrolysis of phospholipids to yield diacylglycerols and water-soluble phosphorylated derivatives of the lipid head groups. A number of these enzymes have specificity for phosphoinositides. Of the phosphoinositide-specific phospholipase C enzymes, C-beta is regulated by heterotrimeric G protein-coupled receptors, while the closely related C-gamma-1 (PLCG1; MIM 172420) and C-gamma-2 enzymes are controlled by receptor tyrosine kinases. The C-gamma-1 and C-gamma-2 enzymes are composed of phospholipase domains that flank regions of homology to noncatalytic domains of the SRC oncogene product, SH2 and SH3.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PLCG2 phospholipase C, gamma 2 (phosphatidylinositol-specific)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5336| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Fruman DA, Satterthwaite AB, Witte ON |title=Xid-like phenotypes: a B cell signalosome takes shape. |journal=Immunity |volume=13 |issue= 1 |pages= 1-3 |year= 2000 |pmid= 10933389 |doi= }}
*{{cite journal | author=Cefai D, Debre P, Kaczorek M, ''et al.'' |title=Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway. |journal=J. Clin. Invest. |volume=86 |issue= 6 |pages= 2117-24 |year= 1991 |pmid= 1979339 |doi= }}
*{{cite journal | author=Ohta S, Matsui A, Nazawa Y, Kagawa Y |title=Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes. |journal=FEBS Lett. |volume=242 |issue= 1 |pages= 31-5 |year= 1989 |pmid= 2849563 |doi= }}
*{{cite journal | author=Yan W, Ratnam M |title=Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal. |journal=Biochemistry |volume=34 |issue= 44 |pages= 14594-600 |year= 1995 |pmid= 7578066 |doi= }}
*{{cite journal | author=Zauli G, Previati M, Caramelli E, ''et al.'' |title=Exogenous human immunodeficiency virus type-1 Tat protein selectively stimulates a phosphatidylinositol-specific phospholipase C nuclear pathway in the Jurkat T cell line. |journal=Eur. J. Immunol. |volume=25 |issue= 9 |pages= 2695-700 |year= 1995 |pmid= 7589147 |doi= }}
*{{cite journal | author=Liao F, Shin HS, Rhee SG |title=In vitro tyrosine phosphorylation of PLC-gamma 1 and PLC-gamma 2 by src-family protein tyrosine kinases. |journal=Biochem. Biophys. Res. Commun. |volume=191 |issue= 3 |pages= 1028-33 |year= 1993 |pmid= 7682059 |doi= 10.1006/bbrc.1993.1320 }}
*{{cite journal | author=Hernandez D, Egan SE, Yulug IG, Fisher EM |title=Mapping the gene that encodes phosphatidylinositol-specific phospholipase C-gamma 2 in the human and the mouse. |journal=Genomics |volume=23 |issue= 2 |pages= 504-7 |year= 1995 |pmid= 7835906 |doi= 10.1006/geno.1994.1533 }}
*{{cite journal | author=Daniel JL, Dangelmaier C, Smith JB |title=Evidence for a role for tyrosine phosphorylation of phospholipase C gamma 2 in collagen-induced platelet cytosolic calcium mobilization. |journal=Biochem. J. |volume=302 ( Pt 2) |issue= |pages= 617-22 |year= 1994 |pmid= 8093016 |doi= }}
*{{cite journal | author=Obermeier A, Lammers R, Wiesmüller KH, ''et al.'' |title=Identification of Trk binding sites for SHC and phosphatidylinositol 3'-kinase and formation of a multimeric signaling complex. |journal=J. Biol. Chem. |volume=268 |issue= 31 |pages= 22963-6 |year= 1993 |pmid= 8226808 |doi= }}
*{{cite journal | author=Pleiman CM, Clark MR, Gauen LK, ''et al.'' |title=Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase. |journal=Mol. Cell. Biol. |volume=13 |issue= 9 |pages= 5877-87 |year= 1993 |pmid= 8395016 |doi= }}
*{{cite journal | author=Sidorenko SP, Law CL, Klaus SJ, ''et al.'' |title=Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling. |journal=Immunity |volume=5 |issue= 4 |pages= 353-63 |year= 1996 |pmid= 8885868 |doi= }}
*{{cite journal | author=Kang JS, Kohlhuber F, Hug H, ''et al.'' |title=Cloning and functional analysis of the hematopoietic cell-specific phospholipase C(gamma)2 promoter. |journal=FEBS Lett. |volume=399 |issue= 1-2 |pages= 14-20 |year= 1997 |pmid= 8980110 |doi= }}
*{{cite journal | author=Chen P, Mayne M, Power C, Nath A |title=The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases. |journal=J. Biol. Chem. |volume=272 |issue= 36 |pages= 22385-8 |year= 1997 |pmid= 9278385 |doi= }}
*{{cite journal | author=Cunningham SA, Arrate MP, Brock TA, Waxham MN |title=Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites. |journal=Biochem. Biophys. Res. Commun. |volume=240 |issue= 3 |pages= 635-9 |year= 1998 |pmid= 9398617 |doi= 10.1006/bbrc.1997.7719 }}
*{{cite journal | author=Mayne M, Bratanich AC, Chen P, ''et al.'' |title=HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease. |journal=Neuroimmunomodulation |volume=5 |issue= 3-4 |pages= 184-92 |year= 1998 |pmid= 9730685 |doi= }}
*{{cite journal | author=Bai RY, Dieter P, Peschel C, ''et al.'' |title=Nucleophosmin-anaplastic lymphoma kinase of large-cell anaplastic lymphoma is a constitutively active tyrosine kinase that utilizes phospholipase C-gamma to mediate its mitogenicity. |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 6951-61 |year= 1998 |pmid= 9819383 |doi= }}
*{{cite journal | author=Tomassetti A, Bottero F, Mazzi M, ''et al.'' |title=Molecular requirements for attachment of the glycosylphosphatidylinositol anchor to the human alpha folate receptor. |journal=J. Cell. Biochem. |volume=72 |issue= 1 |pages= 111-8 |year= 1999 |pmid= 10025672 |doi= }}
*{{cite journal | author=Shen Z, Batzer A, Koehler JA, ''et al.'' |title=Evidence for SH3 domain directed binding and phosphorylation of Sam68 by Src. |journal=Oncogene |volume=18 |issue= 33 |pages= 4647-53 |year= 1999 |pmid= 10467411 |doi= 10.1038/sj.onc.1203079 }}
*{{cite journal | author=Gross BS, Melford SK, Watson SP |title=Evidence that phospholipase C-gamma2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets. |journal=Eur. J. Biochem. |volume=263 |issue= 3 |pages= 612-23 |year= 1999 |pmid= 10469124 |doi= }}
*{{cite journal | author=Haughey NJ, Holden CP, Nath A, Geiger JD |title=Involvement of inositol 1,4,5-trisphosphate-regulated stores of intracellular calcium in calcium dysregulation and neuron cell death caused by HIV-1 protein tat. |journal=J. Neurochem. |volume=73 |issue= 4 |pages= 1363-74 |year= 1999 |pmid= 10501179 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLTP... {November 16, 2007 4:36:47 PM PST}
- SEARCH REDIRECT: Control Box Found: PLTP {November 16, 2007 4:37:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 4:37:09 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 4:37:09 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 4:37:09 PM PST}
- UPDATED: Updated protein page: PLTP {November 16, 2007 4:37:15 PM PST}
- INFO: Beginning work on PSMD4... {November 16, 2007 4:37:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:37:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSMD4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p9c.
| PDB = {{PDB2|1p9c}}, {{PDB2|1p9d}}, {{PDB2|1uel}}, {{PDB2|1yx4}}, {{PDB2|1yx5}}, {{PDB2|1yx6}}
| Name = Proteasome (prosome, macropain) 26S subunit, non-ATPase, 4
| HGNCid = 9561
| Symbol = PSMD4
| AltSymbols =; ASF; AF-1; AF; MCB1; Rpn10; S5A; pUB-R5
| OMIM = 601648
| ECnumber =
| Homologene = 55691
| MGIid = 1201670
| GeneAtlas_image1 = PBB_GE_PSMD4_200882_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMD4_210460_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PSMD4_211609_x_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5710
| Hs_Ensembl = ENSG00000159352
| Hs_RefseqProtein = NP_002801
| Hs_RefseqmRNA = NM_002810
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 149493803
| Hs_GenLoc_end = 149506579
| Hs_Uniprot = P55036
| Mm_EntrezGene = 19185
| Mm_Ensembl = ENSMUSG00000005625
| Mm_RefseqmRNA = NM_008951
| Mm_RefseqProtein = NP_032977
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 95118218
| Mm_GenLoc_end = 95122172
| Mm_Uniprot = Q3ULG4
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, non-ATPase, 4''', also known as '''PSMD4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMD4 proteasome (prosome, macropain) 26S subunit, non-ATPase, 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5710| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the non-ATPase subunits of the 19S regulator lid. Pseudogenes have been identified on chromosomes 10 and 21.<ref name="entrez">{{cite web | title = Entrez Gene: PSMD4 proteasome (prosome, macropain) 26S subunit, non-ATPase, 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5710| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Lönnroth I, Lange S |title=Purification and characterization of the antisecretory factor: a protein in the central nervous system and in the gut which inhibits intestinal hypersecretion induced by cholera toxin. |journal=Biochim. Biophys. Acta |volume=883 |issue= 1 |pages= 138-44 |year= 1986 |pmid= 3524692 |doi= }}
*{{cite journal | author=Johansson E, Lönnroth I, Lange S, ''et al.'' |title=Molecular cloning and expression of a pituitary gland protein modulating intestinal fluid secretion. |journal=J. Biol. Chem. |volume=270 |issue= 35 |pages= 20615-20 |year= 1995 |pmid= 7657640 |doi= }}
*{{cite journal | author=Ferrell K, Deveraux Q, van Nocker S, Rechsteiner M |title=Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease. |journal=FEBS Lett. |volume=381 |issue= 1-2 |pages= 143-8 |year= 1996 |pmid= 8641424 |doi= }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Anand G, Yin X, Shahidi AK, ''et al.'' |title=Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26 S proteasome. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19140-51 |year= 1997 |pmid= 9235903 |doi= }}
*{{cite journal | author=Young P, Deveraux Q, Beal RE, ''et al.'' |title=Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5461-7 |year= 1998 |pmid= 9488668 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Hiyama H, Yokoi M, Masutani C, ''et al.'' |title=Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome. |journal=J. Biol. Chem. |volume=274 |issue= 39 |pages= 28019-25 |year= 1999 |pmid= 10488153 |doi= }}
*{{cite journal | author=Tateishi K, Misumi Y, Ikehara Y, ''et al.'' |title=Molecular cloning and expression of rat antisecretory factor and its intracellular localization. |journal=Biochem. Cell Biol. |volume=77 |issue= 3 |pages= 223-8 |year= 1999 |pmid= 10505793 |doi= }}
*{{cite journal | author=Tanahashi N, Murakami Y, Minami Y, ''et al.'' |title=Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14336-45 |year= 2000 |pmid= 10799514 |doi= }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Kawahara H, Kasahara M, Nishiyama A, ''et al.'' |title=Developmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomes. |journal=EMBO J. |volume=19 |issue= 15 |pages= 4144-53 |year= 2000 |pmid= 10921894 |doi= 10.1093/emboj/19.15.4144 }}
*{{cite journal | author=Connell P, Ballinger CA, Jiang J, ''et al.'' |title=The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. |journal=Nat. Cell Biol. |volume=3 |issue= 1 |pages= 93-6 |year= 2001 |pmid= 11146632 |doi= 10.1038/35050618 }}
*{{cite journal | author=Kamitani T, Kito K, Fukuda-Kamitani T, Yeh ET |title=Targeting of NEDD8 and its conjugates for proteasomal degradation by NUB1. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 46655-60 |year= 2002 |pmid= 11585840 |doi= 10.1074/jbc.M108636200 }}
*{{cite journal | author=Walters KJ, Kleijnen MF, Goh AM, ''et al.'' |title=Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a. |journal=Biochemistry |volume=41 |issue= 6 |pages= 1767-77 |year= 2002 |pmid= 11827521 |doi= }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAB5A... {November 16, 2007 4:37:55 PM PST}
- SEARCH: Multiple Conflicting Pages. Need Resolution. {November 16, 2007 4:38:19 PM PST}
- AMBIGUITY: More than one potential page found for updating, RAB5A RAB5A {November 16, 2007 4:38:19 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RAB5A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1huq.
| PDB = {{PDB2|1huq}}, {{PDB2|1n6h}}, {{PDB2|1n6i}}, {{PDB2|1n6k}}, {{PDB2|1n6l}}, {{PDB2|1n6n}}, {{PDB2|1n6o}}, {{PDB2|1n6p}}, {{PDB2|1n6r}}, {{PDB2|1r2q}}, {{PDB2|1tu3}}, {{PDB2|1tu4}}, {{PDB2|1z07}}, {{PDB2|1z0d}}
| Name = RAB5A, member RAS oncogene family
| HGNCid = 9783
| Symbol = RAB5A
| AltSymbols =; RAB5
| OMIM = 179512
| ECnumber =
| Homologene = 68142
| MGIid = 105926
| GeneAtlas_image1 = PBB_GE_RAB5A_209089_at_tn.png
| GeneAtlas_image2 = PBB_GE_RAB5A_206113_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005769 |text = early endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0030139 |text = endocytic vesicle}} {{GNF_GO|id=GO:0045121 |text = lipid raft}}
| Process = {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5868
| Hs_Ensembl = ENSG00000144566
| Hs_RefseqProtein = NP_004153
| Hs_RefseqmRNA = NM_004162
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 19963749
| Hs_GenLoc_end = 20001647
| Hs_Uniprot = P20339
| Mm_EntrezGene = 271457
| Mm_Ensembl = ENSMUSG00000017831
| Mm_RefseqmRNA = NM_025887
| Mm_RefseqProtein = NP_080163
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 52944163
| Mm_GenLoc_end = 52972607
| Mm_Uniprot = Q3UCX7
}}
}}
'''RAB5A, member RAS oncogene family''', also known as '''RAB5A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAB5A RAB5A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5868| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bucci C, Parton RG, Mather IH, ''et al.'' |title=The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. |journal=Cell |volume=70 |issue= 5 |pages= 715-28 |year= 1992 |pmid= 1516130 |doi= }}
*{{cite journal | author=Rousseau-Merck MF, Zahraoui A, Touchot N, ''et al.'' |title=Chromosome assignment of four RAS-related RAB genes. |journal=Hum. Genet. |volume=86 |issue= 4 |pages= 350-4 |year= 1991 |pmid= 1999336 |doi= }}
*{{cite journal | author=Zahraoui A, Touchot N, Chardin P, Tavitian A |title=The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. |journal=J. Biol. Chem. |volume=264 |issue= 21 |pages= 12394-401 |year= 1989 |pmid= 2501306 |doi= }}
*{{cite journal | author=Farnsworth CC, Seabra MC, Ericsson LH, ''et al.'' |title=Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 11963-7 |year= 1995 |pmid= 7991565 |doi= }}
*{{cite journal | author=Cremers FP, Armstrong SA, Seabra MC, ''et al.'' |title=REP-2, a Rab escort protein encoded by the choroideremia-like gene. |journal=J. Biol. Chem. |volume=269 |issue= 3 |pages= 2111-7 |year= 1994 |pmid= 8294464 |doi= }}
*{{cite journal | author=Stenmark H, Vitale G, Ullrich O, Zerial M |title=Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. |journal=Cell |volume=83 |issue= 3 |pages= 423-32 |year= 1996 |pmid= 8521472 |doi= }}
*{{cite journal | author=Vita F, Soranzo MR, Borelli V, ''et al.'' |title=Subcellular localization of the small GTPase Rab5a in resting and stimulated human neutrophils. |journal=Exp. Cell Res. |volume=227 |issue= 2 |pages= 367-73 |year= 1996 |pmid= 8831575 |doi= 10.1006/excr.1996.0286 }}
*{{cite journal | author=Xiao GH, Shoarinejad F, Jin F, ''et al.'' |title=The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6097-100 |year= 1997 |pmid= 9045618 |doi= }}
*{{cite journal | author=Simonsen A, Lippé R, Christoforidis S, ''et al.'' |title=EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. |journal=Nature |volume=394 |issue= 6692 |pages= 494-8 |year= 1998 |pmid= 9697774 |doi= 10.1038/28879 }}
*{{cite journal | author=Anant JS, Desnoyers L, Machius M, ''et al.'' |title=Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex. |journal=Biochemistry |volume=37 |issue= 36 |pages= 12559-68 |year= 1999 |pmid= 9730828 |doi= 10.1021/bi980881a }}
*{{cite journal | author=Bucci C, Chiariello M, Lattero D, ''et al.'' |title=Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1). |journal=Biochem. Biophys. Res. Commun. |volume=258 |issue= 3 |pages= 657-62 |year= 1999 |pmid= 10329441 |doi= 10.1006/bbrc.1999.0651 }}
*{{cite journal | author=Callaghan J, Nixon S, Bucci C, ''et al.'' |title=Direct interaction of EEA1 with Rab5b. |journal=Eur. J. Biochem. |volume=265 |issue= 1 |pages= 361-6 |year= 1999 |pmid= 10491193 |doi= }}
*{{cite journal | author=Shisheva A, Chinni SR, DeMarco C |title=General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications. |journal=Biochemistry |volume=38 |issue= 36 |pages= 11711-21 |year= 1999 |pmid= 10512627 |doi= }}
*{{cite journal | author=Masuda ES, Luo Y, Young C, ''et al.'' |title=Rab37 is a novel mast cell specific GTPase localized to secretory granules. |journal=FEBS Lett. |volume=470 |issue= 1 |pages= 61-4 |year= 2000 |pmid= 10722846 |doi= }}
*{{cite journal | author=Hoffenberg S, Liu X, Nikolova L, ''et al.'' |title=A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24661-9 |year= 2000 |pmid= 10818110 |doi= 10.1074/jbc.M909600199 }}
*{{cite journal | author=Nielsen E, Christoforidis S, Uttenweiler-Joseph S, ''et al.'' |title=Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain. |journal=J. Cell Biol. |volume=151 |issue= 3 |pages= 601-12 |year= 2000 |pmid= 11062261 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Lanzetti L, Rybin V, Malabarba MG, ''et al.'' |title=The Eps8 protein coordinates EGF receptor signalling through Rac and trafficking through Rab5. |journal=Nature |volume=408 |issue= 6810 |pages= 374-7 |year= 2000 |pmid= 11099046 |doi= 10.1038/35042605 }}
*{{cite journal | author=Wolf RM, Wilkes JJ, Chao MV, Resh MD |title=Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte differentiation. |journal=J. Neurobiol. |volume=49 |issue= 1 |pages= 62-78 |year= 2001 |pmid= 11536198 |doi= }}
*{{cite journal | author=Seachrist JL, Laporte SA, Dale LB, ''et al.'' |title=Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 679-85 |year= 2002 |pmid= 11682489 |doi= 10.1074/jbc.M109022200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINA5... {November 16, 2007 4:34:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:35:29 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SERPINA5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lq8.
| PDB = {{PDB2|1lq8}}, {{PDB2|2hi9}}, {{PDB2|2ol2}}
| Name = Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 5
| HGNCid = 8723
| Symbol = SERPINA5
| AltSymbols =; PAI3; PCI; PLANH3; PROCI
| OMIM = 601841
| ECnumber =
| Homologene = 20159
| MGIid = 107817
| GeneAtlas_image1 = PBB_GE_SERPINA5_209443_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0032190 |text = acrosin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0007342 |text = fusion of sperm to egg plasma membrane}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5104
| Hs_Ensembl = ENSG00000188488
| Hs_RefseqProtein = NP_000615
| Hs_RefseqmRNA = NM_000624
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 94123453
| Hs_GenLoc_end = 94129204
| Hs_Uniprot = P05154
| Mm_EntrezGene = 268591
| Mm_Ensembl = ENSMUSG00000041550
| Mm_RefseqmRNA = NM_172953
| Mm_RefseqProtein = NP_766541
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 104502163
| Mm_GenLoc_end = 104507187
| Mm_Uniprot = Q5BKQ8
}}
}}
'''Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 5''', also known as '''SERPINA5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SERPINA5 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5104| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Suzuki K, Hayashi T |title=cis-elements required for expression of human protein C inhibitor gene in HepG2 cells and its androgen-dependent expression in rat reproductive organs. |journal=Semin. Thromb. Hemost. |volume=26 |issue= 1 |pages= 75-83 |year= 2000 |pmid= 10805286 |doi= }}
*{{cite journal | author=Yasuda T, Nadano D, Iida R, ''et al.'' |title=Discovery of a genetic polymorphism of human plasma protein C inhibitor (PCI): genetic survey utilizing isoelectric focusing followed by immunoblotting, immunological and biochemical characterization. |journal=Hum. Genet. |volume=89 |issue= 3 |pages= 265-9 |year= 1992 |pmid= 1318261 |doi= }}
*{{cite journal | author=Laurell M, Christensson A, Abrahamsson PA, ''et al.'' |title=Protein C inhibitor in human body fluids. Seminal plasma is rich in inhibitor antigen deriving from cells throughout the male reproductive system. |journal=J. Clin. Invest. |volume=89 |issue= 4 |pages= 1094-101 |year= 1992 |pmid= 1372913 |doi= }}
*{{cite journal | author=Meijers JC, Chung DW |title=Organization of the gene coding for human protein C inhibitor (plasminogen activator inhibitor-3). Assignment of the gene to chromosome 14. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15028-34 |year= 1991 |pmid= 1714450 |doi= }}
*{{cite journal | author=Kuhn LA, Griffin JH, Fisher CL, ''et al.'' |title=Elucidating the structural chemistry of glycosaminoglycan recognition by protein C inhibitor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 21 |pages= 8506-10 |year= 1990 |pmid= 2172989 |doi= }}
*{{cite journal | author=Meijers JC, Chung DW |title=Evidence for a glycine residue at position 316 in human protein C inhibitor. |journal=Thromb. Res. |volume=59 |issue= 2 |pages= 389-93 |year= 1990 |pmid= 2173165 |doi= }}
*{{cite journal | author=España F, Berrettini M, Griffin JH |title=Purification and characterization of plasma protein C inhibitor. |journal=Thromb. Res. |volume=55 |issue= 3 |pages= 369-84 |year= 1989 |pmid= 2551064 |doi= }}
*{{cite journal | author=Laurell M, Stenflo J |title=Protein C inhibitor from human plasma: characterization of native and cleaved inhibitor and demonstration of inhibitor complexes with plasma kallikrein. |journal=Thromb. Haemost. |volume=62 |issue= 3 |pages= 885-91 |year= 1990 |pmid= 2556811 |doi= }}
*{{cite journal | author=Geiger M, Huber K, Wojta J, ''et al.'' |title=Complex formation between urokinase and plasma protein C inhibitor in vitro and in vivo. |journal=Blood |volume=74 |issue= 2 |pages= 722-8 |year= 1989 |pmid= 2752144 |doi= }}
*{{cite journal | author=Suzuki K, Deyashiki Y, Nishioka J, ''et al.'' |title=Characterization of a cDNA for human protein C inhibitor. A new member of the plasma serine protease inhibitor superfamily. |journal=J. Biol. Chem. |volume=262 |issue= 2 |pages= 611-6 |year= 1987 |pmid= 3027058 |doi= }}
*{{cite journal | author=Suzuki K, Nishioka J, Hashimoto S |title=Protein C inhibitor. Purification from human plasma and characterization. |journal=J. Biol. Chem. |volume=258 |issue= 1 |pages= 163-8 |year= 1983 |pmid= 6294098 |doi= }}
*{{cite journal | author=Christensson A, Lilja H |title=Complex formation between protein C inhibitor and prostate-specific antigen in vitro and in human semen. |journal=Eur. J. Biochem. |volume=220 |issue= 1 |pages= 45-53 |year= 1994 |pmid= 7509746 |doi= }}
*{{cite journal | author=Zheng X, Geiger M, Ecke S, ''et al.'' |title=Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa. |journal=Am. J. Physiol. |volume=267 |issue= 2 Pt 1 |pages= C466-72 |year= 1994 |pmid= 7521127 |doi= }}
*{{cite journal | author=Radtke KP, Fernández JA, Greengard JS, ''et al.'' |title=Protein C inhibitor is expressed in tubular cells of human kidney. |journal=J. Clin. Invest. |volume=94 |issue= 5 |pages= 2117-24 |year= 1994 |pmid= 7525654 |doi= }}
*{{cite journal | author=Hayashi S |title=Urinary protein C inhibitor binding region in the B beta-chain of human fibrinogen. |journal=Blood Coagul. Fibrinolysis |volume=4 |issue= 6 |pages= 921-6 |year= 1994 |pmid= 8148485 |doi= }}
*{{cite journal | author=Hayashi T, Suzuki K |title=Gene organization of human protein C inhibitor, a member of SERPIN family proteins encoded in five exons. |journal=Int. J. Hematol. |volume=58 |issue= 3 |pages= 213-24 |year= 1994 |pmid= 8148499 |doi= }}
*{{cite journal | author=Billingsley GD, Walter MA, Hammond GL, Cox DW |title=Physical mapping of four serpin genes: alpha 1-antitrypsin, alpha 1-antichymotrypsin, corticosteroid-binding globulin, and protein C inhibitor, within a 280-kb region on chromosome I4q32.1. |journal=Am. J. Hum. Genet. |volume=52 |issue= 2 |pages= 343-53 |year= 1993 |pmid= 8381582 |doi= }}
*{{cite journal | author=Hayashi S, Yamada K |title=Binding of urinary protein C inhibitor to fibrin(ogen) and its binding mechanism. |journal=Blood Coagul. Fibrinolysis |volume=4 |issue= 1 |pages= 153-8 |year= 1993 |pmid= 8384496 |doi= }}
*{{cite journal | author=Moore A, Penfold LM, Johnson JL, ''et al.'' |title=Human sperm-egg binding is inhibited by peptides corresponding to core region of an acrosomal serine protease inhibitor. |journal=Mol. Reprod. Dev. |volume=34 |issue= 3 |pages= 280-91 |year= 1993 |pmid= 8471250 |doi= 10.1002/mrd.1080340308 }}
*{{cite journal | author=Hayashi S, Wakizaka A |title=Urinary protein C inhibitor binding region in the A alpha-chain of human fibrinogen. |journal=Blood Coagul. Fibrinolysis |volume=6 |issue= 5 |pages= 382-7 |year= 1996 |pmid= 8589203 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SIRT1... {November 16, 2007 4:39:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:39:42 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae)
| HGNCid = 14929
| Symbol = SIRT1
| AltSymbols =; SIR2L1
| OMIM = 604479
| ECnumber =
| Homologene = 56556
| MGIid = 2135607
| GeneAtlas_image1 = PBB_GE_SIRT1_218878_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003950 |text = NAD+ ADP-ribosyltransferase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0017136 |text = NAD-dependent histone deacetylase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005677 |text = chromatin silencing complex}}
| Process = {{GNF_GO|id=GO:0001542 |text = ovulation (sensu Mammalia)}} {{GNF_GO|id=GO:0006342 |text = chromatin silencing}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006471 |text = protein amino acid ADP-ribosylation}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0007519 |text = striated muscle development}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0016575 |text = histone deacetylation}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 23411
| Hs_Ensembl = ENSG00000096717
| Hs_RefseqProtein = NP_036370
| Hs_RefseqmRNA = NM_012238
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 69314433
| Hs_GenLoc_end = 69348153
| Hs_Uniprot = Q96EB6
| Mm_EntrezGene = 93759
| Mm_Ensembl = ENSMUSG00000020063
| Mm_RefseqmRNA = XM_975350
| Mm_RefseqProtein = XP_980444
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 62714364
| Mm_GenLoc_end = 62734366
| Mm_Uniprot = Q3USJ2
}}
}}
'''Sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae)''', also known as '''SIRT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SIRT1 sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23411| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family.<ref name="entrez">{{cite web | title = Entrez Gene: SIRT1 sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23411| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Frye RA |title=Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. |journal=Biochem. Biophys. Res. Commun. |volume=260 |issue= 1 |pages= 273-9 |year= 1999 |pmid= 10381378 |doi= 10.1006/bbrc.1999.0897 }}
*{{cite journal | author=Frye RA |title=Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. |journal=Biochem. Biophys. Res. Commun. |volume=273 |issue= 2 |pages= 793-8 |year= 2000 |pmid= 10873683 |doi= 10.1006/bbrc.2000.3000 }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal | author=Luo J, Nikolaev AY, Imai S, ''et al.'' |title=Negative control of p53 by Sir2alpha promotes cell survival under stress. |journal=Cell |volume=107 |issue= 2 |pages= 137-48 |year= 2001 |pmid= 11672522 |doi= }}
*{{cite journal | author=Vaziri H, Dessain SK, Ng Eaton E, ''et al.'' |title=hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. |journal=Cell |volume=107 |issue= 2 |pages= 149-59 |year= 2001 |pmid= 11672523 |doi= }}
*{{cite journal | author=Langley E, Pearson M, Faretta M, ''et al.'' |title=Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. |journal=EMBO J. |volume=21 |issue= 10 |pages= 2383-96 |year= 2002 |pmid= 12006491 |doi= 10.1093/emboj/21.10.2383 }}
*{{cite journal | author=Bitterman KJ, Anderson RM, Cohen HY, ''et al.'' |title=Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 45099-107 |year= 2003 |pmid= 12297502 |doi= 10.1074/jbc.M205670200 }}
*{{cite journal | author=Travers H, Spotswood HT, Moss PA, Turner BM |title=Human CD34+ hematopoietic progenitor cells hyperacetylate core histones in response to sodium butyrate, but not trichostatin A. |journal=Exp. Cell Res. |volume=280 |issue= 2 |pages= 149-58 |year= 2002 |pmid= 12413881 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Takata T, Ishikawa F |title=Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression. |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 1 |pages= 250-7 |year= 2003 |pmid= 12535671 |doi= }}
*{{cite journal | author=Senawong T, Peterson VJ, Avram D, ''et al.'' |title=Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression. |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 43041-50 |year= 2003 |pmid= 12930829 |doi= 10.1074/jbc.M307477200 }}
*{{cite journal | author=Howitz KT, Bitterman KJ, Cohen HY, ''et al.'' |title=Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. |journal=Nature |volume=425 |issue= 6954 |pages= 191-6 |year= 2003 |pmid= 12939617 |doi= 10.1038/nature01960 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Brunet A, Sweeney LB, Sturgill JF, ''et al.'' |title=Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. |journal=Science |volume=303 |issue= 5666 |pages= 2011-5 |year= 2004 |pmid= 14976264 |doi= 10.1126/science.1094637 }}
*{{cite journal | author=Motta MC, Divecha N, Lemieux M, ''et al.'' |title=Mammalian SIRT1 represses forkhead transcription factors. |journal=Cell |volume=116 |issue= 4 |pages= 551-63 |year= 2004 |pmid= 14980222 |doi= }}
*{{cite journal | author=van der Horst A, Tertoolen LG, de Vries-Smits LM, ''et al.'' |title=FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). |journal=J. Biol. Chem. |volume=279 |issue= 28 |pages= 28873-9 |year= 2004 |pmid= 15126506 |doi= 10.1074/jbc.M401138200 }}
*{{cite journal | author=Yeung F, Hoberg JE, Ramsey CS, ''et al.'' |title=Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. |journal=EMBO J. |volume=23 |issue= 12 |pages= 2369-80 |year= 2004 |pmid= 15152190 |doi= 10.1038/sj.emboj.7600244 }}
*{{cite journal | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
*{{cite journal | author=Picard F, Kurtev M, Chung N, ''et al.'' |title=Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma. |journal=Nature |volume=429 |issue= 6993 |pages= 771-6 |year= 2004 |pmid= 15175761 |doi= 10.1038/nature02583 }}
*{{cite journal | author=Cohen HY, Miller C, Bitterman KJ, ''et al.'' |title=Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. |journal=Science |volume=305 |issue= 5682 |pages= 390-2 |year= 2004 |pmid= 15205477 |doi= 10.1126/science.1099196 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SPINK1... {November 16, 2007 4:38:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 4:39:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SPINK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cgi.
| PDB = {{PDB2|1cgi}}, {{PDB2|1cgj}}, {{PDB2|1hpt}}
| Name = Serine peptidase inhibitor, Kazal type 1
| HGNCid = 11244
| Symbol = SPINK1
| AltSymbols =; PCTT; PSTI; Spink3; TATI
| OMIM = 167790
| ECnumber =
| Homologene = 68300
| MGIid = 106202
| GeneAtlas_image1 = PBB_GE_SPINK1_206239_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6690
| Hs_Ensembl = ENSG00000164266
| Hs_RefseqProtein = NP_003113
| Hs_RefseqmRNA = NM_003122
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 147184339
| Hs_GenLoc_end = 147191453
| Hs_Uniprot = P00995
| Mm_EntrezGene = 20730
| Mm_Ensembl = ENSMUSG00000024503
| Mm_RefseqmRNA = NM_009258
| Mm_RefseqProtein = NP_033284
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 43853416
| Mm_GenLoc_end = 43862528
| Mm_Uniprot = P09036
}}
}}
'''Serine peptidase inhibitor, Kazal type 1''', also known as '''SPINK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SPINK1 serine peptidase inhibitor, Kazal type 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6690| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Marchbank T, Freeman TC, Playford RJ |title=Human pancreatic secretory trypsin inhibitor. Distribution, actions and possible role in mucosal integrity and repair. |journal=Digestion |volume=59 |issue= 3 |pages= 167-74 |year= 1998 |pmid= 9643675 |doi= }}
*{{cite journal | author=Pfützer RH, Whitcomb DC |title=SPINK1 mutations are associated with multiple phenotypes. |journal=Pancreatology |volume=1 |issue= 5 |pages= 457-60 |year= 2002 |pmid= 12120224 |doi= }}
*{{cite journal | author=Schneider A |title=Serine protease inhibitor kazal type 1 mutations and pancreatitis. |journal=Clin. Lab. Med. |volume=25 |issue= 1 |pages= 61-78 |year= 2005 |pmid= 15749232 |doi= 10.1016/j.cll.2004.12.005 }}
*{{cite journal | author=Cohn JA, Mitchell RM, Jowell PS |title=The impact of cystic fibrosis and PSTI/SPINK1 gene mutations on susceptibility to chronic pancreatitis. |journal=Clin. Lab. Med. |volume=25 |issue= 1 |pages= 79-100 |year= 2005 |pmid= 15749233 |doi= 10.1016/j.cll.2004.12.007 }}
*{{cite journal | author=Kandula L, Whitcomb DC, Lowe ME |title=Genetic issues in pediatric pancreatitis. |journal=Current gastroenterology reports |volume=8 |issue= 3 |pages= 248-53 |year= 2006 |pmid= 16764792 |doi= }}
*{{cite journal | author=Bartelt DC, Shapanka R, Greene LJ |title=The primary structure of the human pancreatic secretory trypsin inhibitor. Amino acid sequence of the reduced S-aminoethylated protein. |journal=Arch. Biochem. Biophys. |volume=179 |issue= 1 |pages= 189-99 |year= 1977 |pmid= 843082 |doi= }}
*{{cite journal | author=Hecht HJ, Szardenings M, Collins J, Schomburg D |title=Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (Kazal type). |journal=J. Mol. Biol. |volume=225 |issue= 4 |pages= 1095-103 |year= 1992 |pmid= 1613792 |doi= }}
*{{cite journal | author=Hecht HJ, Szardenings M, Collins J, Schomburg D |title=Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type). |journal=J. Mol. Biol. |volume=220 |issue= 3 |pages= 711-22 |year= 1991 |pmid= 1870127 |doi= }}
*{{cite journal | author=Freeman TC, Davies R, Calam J |title=Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice: its hydrolysis and protection by intraluminal factors. |journal=Clin. Chim. Acta |volume=195 |issue= 1-2 |pages= 27-39 |year= 1991 |pmid= 2093478 |doi= }}
*{{cite journal | author=Kido H, Yokogoshi Y, Katunuma N |title=A low-molecular-mass Kazal-type protease inhibitor isolated from rat hepatocytes is identical to rat pancreatic secretory trypsin inhibitor II. Purification and amino acid sequence. |journal=Eur. J. Biochem. |volume=188 |issue= 3 |pages= 501-6 |year= 1990 |pmid= 2110056 |doi= }}
*{{cite journal | author=Tomita N, Horii A, Yamamoto T, ''et al.'' |title=Expression of pancreatic secretory trypsin inhibitor gene in neoplastic tissues. |journal=FEBS Lett. |volume=225 |issue= 1-2 |pages= 113-9 |year= 1988 |pmid= 2961612 |doi= }}
*{{cite journal | author=Horii A, Kobayashi T, Tomita N, ''et al.'' |title=Primary structure of human pancreatic secretory trypsin inhibitor (PSTI) gene. |journal=Biochem. Biophys. Res. Commun. |volume=149 |issue= 2 |pages= 635-41 |year= 1988 |pmid= 3501289 |doi= }}
*{{cite journal | author=Yamamoto T, Nakamura Y, Nishide J, ''et al.'' |title=Molecular cloning and nucleotide sequence of human pancreatic secretory trypsin inhibitor (PSTI) cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=132 |issue= 2 |pages= 605-12 |year= 1985 |pmid= 3877508 |doi= }}
*{{cite journal | author=Huhtala ML, Pesonen K, Kalkkinen N, Stenman UH |title=Purification and characterization of a tumor-associated trypsin inhibitor from the urine of a patient with ovarian cancer. |journal=J. Biol. Chem. |volume=257 |issue= 22 |pages= 13713-6 |year= 1983 |pmid= 7142173 |doi= }}
*{{cite journal | author=Klaus W, Schomburg D |title=Solution structure of a variant of human pancreatic secretory trypsin inhibitor determined by nuclear magnetic resonance spectroscopy. |journal=J. Mol. Biol. |volume=229 |issue= 3 |pages= 695-706 |year= 1993 |pmid= 8433367 |doi= 10.1006/jmbi.1993.1073 }}
*{{cite journal | author=Chen JM, Mercier B, Audrezet MP, Ferec C |title=Mutational analysis of the human pancreatic secretory trypsin inhibitor (PSTI) gene in hereditary and sporadic chronic pancreatitis. |journal=J. Med. Genet. |volume=37 |issue= 1 |pages= 67-9 |year= 2000 |pmid= 10691414 |doi= }}
*{{cite journal | author=Witt H, Luck W, Hennies HC, ''et al.'' |title=Mutations in the gene encoding the serine protease inhibitor, Kazal type 1 are associated with chronic pancreatitis. |journal=Nat. Genet. |volume=25 |issue= 2 |pages= 213-6 |year= 2000 |pmid= 10835640 |doi= 10.1038/76088 }}
*{{cite journal | author=Pfützer RH, Barmada MM, Brunskill AP, ''et al.'' |title=SPINK1/PSTI polymorphisms act as disease modifiers in familial and idiopathic chronic pancreatitis. |journal=Gastroenterology |volume=119 |issue= 3 |pages= 615-23 |year= 2000 |pmid= 10982753 |doi= }}
*{{cite journal | author=Kaneko K, Nagasaki Y, Furukawa T, ''et al.'' |title=Analysis of the human pancreatic secretory trypsin inhibitor (PSTI) gene mutations in Japanese patients with chronic pancreatitis. |journal=J. Hum. Genet. |volume=46 |issue= 5 |pages= 293-7 |year= 2001 |pmid= 11355022 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
