- INFO: Beginning work on ACVR2A... {November 17, 2007 10:37:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:37:57 PM PST}
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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_ACVR2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bte.
| PDB = {{PDB2|1bte}}, {{PDB2|1lx5}}, {{PDB2|2goo}}
| Name = Activin A receptor, type IIA
| HGNCid = 173
| Symbol = ACVR2A
| AltSymbols =; ACTRII; ACVR2
| OMIM = 102581
| ECnumber =
| Homologene = 20391
| MGIid = 102806
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0017002 |text = activin receptor activity}} {{GNF_GO|id=GO:0019838 |text = growth factor binding}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0048186 |text = inhibin beta-A binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007178 |text = transmembrane receptor protein serine/threonine kinase signaling pathway}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}} {{GNF_GO|id=GO:0009952 |text = anterior/posterior pattern formation}} {{GNF_GO|id=GO:0045648 |text = positive regulation of erythrocyte differentiation}} {{GNF_GO|id=GO:0048276 |text = gastrulation (sensu Vertebrata)}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 92
| Hs_Ensembl = ENSG00000121989
| Hs_RefseqProtein = NP_001607
| Hs_RefseqmRNA = NM_001616
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 148319067
| Hs_GenLoc_end = 148404863
| Hs_Uniprot = P27037
| Mm_EntrezGene = 11480
| Mm_Ensembl = ENSMUSG00000052155
| Mm_RefseqmRNA = NM_007396
| Mm_RefseqProtein = NP_031422
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 48636166
| Mm_GenLoc_end = 48724172
| Mm_Uniprot = Q8BRV4
}}
}}
'''Activin A receptor, type IIA''', also known as '''ACVR2A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACVR2A activin A receptor, type IIA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=92| 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 activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.<ref name="entrez">{{cite web | title = Entrez Gene: ACVR2A activin A receptor, type IIA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=92| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Welt CK |title=The physiology and pathophysiology of inhibin, activin and follistatin in female reproduction. |journal=Curr. Opin. Obstet. Gynecol. |volume=14 |issue= 3 |pages= 317-23 |year= 2002 |pmid= 12032389 |doi= }}
*{{cite journal | author=Matzuk MM, Bradley A |title=Cloning of the human activin receptor cDNA reveals high evolutionary conservation. |journal=Biochim. Biophys. Acta |volume=1130 |issue= 1 |pages= 105-8 |year= 1992 |pmid= 1311955 |doi= }}
*{{cite journal | author=Donaldson CJ, Mathews LS, Vale WW |title=Molecular cloning and binding properties of the human type II activin receptor. |journal=Biochem. Biophys. Res. Commun. |volume=184 |issue= 1 |pages= 310-6 |year= 1992 |pmid= 1314589 |doi= }}
*{{cite journal | author=Mathews LS, Vale WW |title=Expression cloning of an activin receptor, a predicted transmembrane serine kinase. |journal=Cell |volume=65 |issue= 6 |pages= 973-82 |year= 1991 |pmid= 1646080 |doi= }}
*{{cite journal | author=Xu J, McKeehan K, Matsuzaki K, McKeehan WL |title=Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism. |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6308-13 |year= 1995 |pmid= 7890768 |doi= }}
*{{cite journal | author=Attisano L, Cárcamo J, Ventura F, ''et al.'' |title=Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors. |journal=Cell |volume=75 |issue= 4 |pages= 671-80 |year= 1993 |pmid= 8242742 |doi= }}
*{{cite journal | author=Peng C, Huang TH, Jeung EB, ''et al.'' |title=Expression of the type II activin receptor gene in the human placenta. |journal=Endocrinology |volume=133 |issue= 6 |pages= 3046-9 |year= 1994 |pmid= 8243335 |doi= }}
*{{cite journal | author=De Winter JP, De Vries CJ, Van Achterberg TA, ''et al.'' |title=Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors. |journal=Exp. Cell Res. |volume=224 |issue= 2 |pages= 323-34 |year= 1996 |pmid= 8612709 |doi= }}
*{{cite journal | author=Attisano L, Wrana JL, Montalvo E, Massagué J |title=Activation of signalling by the activin receptor complex. |journal=Mol. Cell. Biol. |volume=16 |issue= 3 |pages= 1066-73 |year= 1996 |pmid= 8622651 |doi= }}
*{{cite journal | author=Liu QY, Niranjan B, Gomes P, ''et al.'' |title=Inhibitory effects of activin on the growth and morpholgenesis of primary and transformed mammary epithelial cells. |journal=Cancer Res. |volume=56 |issue= 5 |pages= 1155-63 |year= 1996 |pmid= 8640777 |doi= }}
*{{cite journal | author=Nishitoh H, Ichijo H, Kimura M, ''et al.'' |title=Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21345-52 |year= 1996 |pmid= 8702914 |doi= }}
*{{cite journal | author=Lebrun JJ, Vale WW |title=Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation. |journal=Mol. Cell. Biol. |volume=17 |issue= 3 |pages= 1682-91 |year= 1997 |pmid= 9032295 |doi= }}
*{{cite journal | author=Macías-Silva M, Hoodless PA, Tang SJ, ''et al.'' |title=Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2. |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 25628-36 |year= 1998 |pmid= 9748228 |doi= }}
*{{cite journal | author=Barbara NP, Wrana JL, Letarte M |title=Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 584-94 |year= 1999 |pmid= 9872992 |doi= }}
*{{cite journal | author=Lux A, Attisano L, Marchuk DA |title=Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 9984-92 |year= 1999 |pmid= 10187774 |doi= }}
*{{cite journal | author=D'Abronzo FH, Swearingen B, Klibanski A, Alexander JM |title=Mutational analysis of activin/transforming growth factor-beta type I and type II receptor kinases in human pituitary tumors. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 5 |pages= 1716-21 |year= 1999 |pmid= 10323406 |doi= }}
*{{cite journal | author=Ebisawa T, Tada K, Kitajima I, ''et al.'' |title=Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation. |journal=J. Cell. Sci. |volume=112 ( Pt 20) |issue= |pages= 3519-27 |year= 2000 |pmid= 10504300 |doi= }}
*{{cite journal | author=van Schaik RH, Wierikx CD, Timmerman MA, ''et al.'' |title=Variations in activin receptor, inhibin/activin subunit and follistatin mRNAs in human prostate tumour tissues. |journal=Br. J. Cancer |volume=82 |issue= 1 |pages= 112-7 |year= 2000 |pmid= 10638976 |doi= 10.1054/bjoc.1999.0886 }}
*{{cite journal | author=Shoji H, Tsuchida K, Kishi H, ''et al.'' |title=Identification and characterization of a PDZ protein that interacts with activin type II receptors. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5485-92 |year= 2000 |pmid= 10681527 |doi= }}
*{{cite journal | author=Bondestam J, Horelli-Kuitunen N, Hildén K, ''et al.'' |title=Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH. |journal=Cytogenet. Cell Genet. |volume=87 |issue= 3-4 |pages= 219-20 |year= 2000 |pmid= 10702675 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BEST1... {November 17, 2007 10:47:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:48:24 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 =
| image_source =
| PDB =
| Name = Bestrophin 1
| HGNCid = 12703
| Symbol = BEST1
| AltSymbols =; BMD; BEST; TU15B; VMD2
| OMIM = 607854
| ECnumber =
| Homologene = 37895
| MGIid = 1346332
| GeneAtlas_image1 = PBB_GE_BEST1_207671_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005254 |text = chloride channel activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0031404 |text = chloride ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7439
| Hs_Ensembl = ENSG00000167995
| Hs_RefseqProtein = NP_004174
| Hs_RefseqmRNA = NM_004183
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 61474408
| Hs_GenLoc_end = 61488509
| Hs_Uniprot = O76090
| Mm_EntrezGene = 24115
| Mm_Ensembl = ENSMUSG00000037418
| Mm_RefseqmRNA = XM_980943
| Mm_RefseqProtein = XP_986037
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 10052219
| Mm_GenLoc_end = 10064259
| Mm_Uniprot = O88870
}}
}}
'''Bestrophin 1''', also known as '''BEST1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BEST1 bestrophin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7439| 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=White K, Marquardt A, Weber BH |title=VMD2 mutations in vitelliform macular dystrophy (Best disease) and other maculopathies. |journal=Hum. Mutat. |volume=15 |issue= 4 |pages= 301-8 |year= 2000 |pmid= 10737974 |doi= 10.1002/(SICI)1098-1004(200004)15:4<301::AID-HUMU1>3.0.CO;2-N }}
*{{cite journal | author=Nordström S, Barkman Y |title=Hereditary maculardegeneration (HMD) in 246 cases traced to one gene-source in central Sweden. |journal=Hereditas |volume=84 |issue= 2 |pages= 163-76 |year= 1977 |pmid= 838599 |doi= }}
*{{cite journal | author=Stone EM, Nichols BE, Streb LM, ''et al.'' |title=Genetic linkage of vitelliform macular degeneration (Best's disease) to chromosome 11q13. |journal=Nat. Genet. |volume=1 |issue= 4 |pages= 246-50 |year= 1993 |pmid= 1302019 |doi= 10.1038/ng0792-246 }}
*{{cite journal | author=Forsman K, Graff C, Nordström S, ''et al.'' |title=The gene for Best's macular dystrophy is located at 11q13 in a Swedish family. |journal=Clin. Genet. |volume=42 |issue= 3 |pages= 156-9 |year= 1992 |pmid= 1395087 |doi= }}
*{{cite journal | author=Stöhr H, Marquardt A, Rivera A, ''et al.'' |title=A gene map of the Best's vitelliform macular dystrophy region in chromosome 11q12-q13.1. |journal=Genome Res. |volume=8 |issue= 1 |pages= 48-56 |year= 1998 |pmid= 9445487 |doi= }}
*{{cite journal | author=Petrukhin K, Koisti MJ, Bakall B, ''et al.'' |title=Identification of the gene responsible for Best macular dystrophy. |journal=Nat. Genet. |volume=19 |issue= 3 |pages= 241-7 |year= 1998 |pmid= 9662395 |doi= 10.1038/915 }}
*{{cite journal | author=Pennisi E |title=New gene found for inherited macular degeneration. |journal=Science |volume=281 |issue= 5373 |pages= 31 |year= 1998 |pmid= 9679014 |doi= }}
*{{cite journal | author=Marquardt A, Stöhr H, Passmore LA, ''et al.'' |title=Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best's disease). |journal=Hum. Mol. Genet. |volume=7 |issue= 9 |pages= 1517-25 |year= 1998 |pmid= 9700209 |doi= }}
*{{cite journal | author=Caldwell GM, Kakuk LE, Griesinger IB, ''et al.'' |title=Bestrophin gene mutations in patients with Best vitelliform macular dystrophy. |journal=Genomics |volume=58 |issue= 1 |pages= 98-101 |year= 1999 |pmid= 10331951 |doi= 10.1006/geno.1999.5808 }}
*{{cite journal | author=Bakall B, Marknell T, Ingvast S, ''et al.'' |title=The mutation spectrum of the bestrophin protein--functional implications. |journal=Hum. Genet. |volume=104 |issue= 5 |pages= 383-9 |year= 1999 |pmid= 10394929 |doi= }}
*{{cite journal | author=Allikmets R, Seddon JM, Bernstein PS, ''et al.'' |title=Evaluation of the Best disease gene in patients with age-related macular degeneration and other maculopathies. |journal=Hum. Genet. |volume=104 |issue= 6 |pages= 449-53 |year= 1999 |pmid= 10453731 |doi= }}
*{{cite journal | author=Palomba G, Rozzo C, Angius A, ''et al.'' |title=A novel spontaneous missense mutation in VMD2 gene is a cause of a best macular dystrophy sporadic case. |journal=Am. J. Ophthalmol. |volume=129 |issue= 2 |pages= 260-2 |year= 2000 |pmid= 10682987 |doi= }}
*{{cite journal | author=Lotery AJ, Namperumalsamy P, Jacobson SG, ''et al.'' |title=Mutation analysis of 3 genes in patients with Leber congenital amaurosis. |journal=Arch. Ophthalmol. |volume=118 |issue= 4 |pages= 538-43 |year= 2000 |pmid= 10766140 |doi= }}
*{{cite journal | author=Lotery AJ, Munier FL, Fishman GA, ''et al.'' |title=Allelic variation in the VMD2 gene in best disease and age-related macular degeneration. |journal=Invest. Ophthalmol. Vis. Sci. |volume=41 |issue= 6 |pages= 1291-6 |year= 2000 |pmid= 10798642 |doi= }}
*{{cite journal | author=Krämer F, White K, Pauleikhoff D, ''et al.'' |title=Mutations in the VMD2 gene are associated with juvenile-onset vitelliform macular dystrophy (Best disease) and adult vitelliform macular dystrophy but not age-related macular degeneration. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 4 |pages= 286-92 |year= 2000 |pmid= 10854112 |doi= 10.1038/sj.ejhg.5200447 }}
*{{cite journal | author=Marmorstein AD, Marmorstein LY, Rayborn M, ''et al.'' |title=Bestrophin, the product of the Best vitelliform macular dystrophy gene (VMD2), localizes to the basolateral plasma membrane of the retinal pigment epithelium. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 23 |pages= 12758-63 |year= 2001 |pmid= 11050159 |doi= 10.1073/pnas.220402097 }}
*{{cite journal | author=Marchant D, Gogat K, Boutboul S, ''et al.'' |title=Identification of novel VMD2 gene mutations in patients with best vitelliform macular dystrophy. |journal=Hum. Mutat. |volume=17 |issue= 3 |pages= 235 |year= 2001 |pmid= 11241846 |doi= 10.1002/humu.9 }}
*{{cite journal | author=Eksandh L, Bakall B, Bauer B, ''et al.'' |title=Best's vitelliform macular dystrophy caused by a new mutation (Val89Ala) in the VMD2 gene. |journal=Ophthalmic Genet. |volume=22 |issue= 2 |pages= 107-15 |year= 2001 |pmid= 11449320 |doi= }}
*{{cite journal | author=Sun H, Tsunenari T, Yau KW, Nathans J |title=The vitelliform macular dystrophy protein defines a new family of chloride channels. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 6 |pages= 4008-13 |year= 2002 |pmid= 11904445 |doi= 10.1073/pnas.052692999 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD3D... {November 17, 2007 10:37:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:38:27 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_CD3D_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xiw.
| PDB = {{PDB2|1xiw}}
| Name = CD3d molecule, delta (CD3-TCR complex)
| HGNCid = 1673
| Symbol = CD3D
| AltSymbols =; CD3-DELTA; T3D
| OMIM = 186790
| ECnumber =
| Homologene = 585
| MGIid = 88331
| GeneAtlas_image1 = PBB_GE_CD3D_213539_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042105 |text = alpha-beta T cell receptor complex}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0042110 |text = T cell activation}} {{GNF_GO|id=GO:0045059 |text = positive thymic T cell selection}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 915
| Hs_Ensembl = ENSG00000167286
| Hs_RefseqProtein = NP_000723
| Hs_RefseqmRNA = NM_000732
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 117715001
| Hs_GenLoc_end = 117718669
| Hs_Uniprot = P04234
| Mm_EntrezGene = 12500
| Mm_Ensembl = ENSMUSG00000032094
| Mm_RefseqmRNA = NM_013487
| Mm_RefseqProtein = NP_038515
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 44732876
| Mm_GenLoc_end = 44737418
| Mm_Uniprot = A0N8K9
}}
}}
'''CD3d molecule, delta (CD3-TCR complex)''', also known as '''CD3D''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD3D CD3d molecule, delta (CD3-TCR complex)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=915| 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=Balk SP, Polischuk JE, Probert C, ''et al.'' |title=Composition of TCR-CD3 complex in human intestinal intraepithelial lymphocytes: lack of Fc epsilon RI gamma chain. |journal=Int. Immunol. |volume=7 |issue= 8 |pages= 1237-41 |year= 1996 |pmid= 7495730 |doi= }}
*{{cite journal | author=Li CJ |title=Therapeutic biology: checkpoint pathway activation therapy, HIV Tat, and transkingdom RNA interference. |journal=J. Cell. Physiol. |volume=209 |issue= 3 |pages= 695-700 |year= 2007 |pmid= 17001685 |doi= 10.1002/jcp.20817 }}
*{{cite journal | author=Phillips JH, Hori T, Nagler A, ''et al.'' |title=Ontogeny of human natural killer (NK) cells: fetal NK cells mediate cytolytic function and express cytoplasmic CD3 epsilon,delta proteins. |journal=J. Exp. Med. |volume=175 |issue= 4 |pages= 1055-66 |year= 1992 |pmid= 1372642 |doi= }}
*{{cite journal | author=Luzzati AL, Giacomini E, Giordani L, ''et al.'' |title=The antigen-specific induction of normal human lymphocytes in vitro is down-regulated by a conserved HIV p24 epitope. |journal=Immunol. Lett. |volume=33 |issue= 3 |pages= 307-14 |year= 1992 |pmid= 1385321 |doi= }}
*{{cite journal | author=Alarcón B, Ley SC, Sánchez-Madrid F, ''et al.'' |title=The CD3-gamma and CD3-delta subunits of the T cell antigen receptor can be expressed within distinct functional TCR/CD3 complexes. |journal=EMBO J. |volume=10 |issue= 4 |pages= 903-12 |year= 1991 |pmid= 1826255 |doi= }}
*{{cite journal | author=Hori T, de Waal Malefyt R, Duncan BW, ''et al.'' |title=Cloning of a novel cell type from human fetal liver expressing cytoplasmic CD3 delta and epsilon but not membrane CD3. |journal=Int. Immunol. |volume=3 |issue= 4 |pages= 353-7 |year= 1991 |pmid= 1831653 |doi= }}
*{{cite journal | author=Ruegg CL, Strand M |title=A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1-13 |year= 1991 |pmid= 1832084 |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=Luzzati AL, Pugliese O, Giacomini E, ''et al.'' |title=Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV. |journal=Folia Biol. (Praha) |volume=36 |issue= 1 |pages= 71-7 |year= 1990 |pmid= 2111780 |doi= }}
*{{cite journal | author=Koning F, Maloy WL, Coligan JE |title=The implications of subunit interactions for the structure of the T cell receptor-CD3 complex. |journal=Eur. J. Immunol. |volume=20 |issue= 2 |pages= 299-305 |year= 1990 |pmid= 2138083 |doi= }}
*{{cite journal | author=Alexander D, Goris J, Marais R, ''et al.'' |title=Dephosphorylation of the human T lymphocyte CD3 antigen. |journal=Eur. J. Biochem. |volume=181 |issue= 1 |pages= 55-65 |year= 1989 |pmid= 2540970 |doi= }}
*{{cite journal | author=Tunnacliffe A, Buluwela L, Rabbitts TH |title=Physical linkage of three CD3 genes on human chromosome 11. |journal=EMBO J. |volume=6 |issue= 10 |pages= 2953-7 |year= 1988 |pmid= 2826124 |doi= }}
*{{cite journal | author=van den Elsen P, Shepley BA, Cho M, Terhorst C |title=Isolation and characterization of a cDNA clone encoding the murine homologue of the human 20K T3/T-cell receptor glycoprotein. |journal=Nature |volume=314 |issue= 6011 |pages= 542-4 |year= 1985 |pmid= 2859526 |doi= }}
*{{cite journal | author=van den Elsen P, Georgopoulos K, Shepley BA, ''et al.'' |title=Exon/intron organization of the genes coding for the delta chains of the human and murine T-cell receptor/T3 complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 9 |pages= 2944-8 |year= 1986 |pmid= 2939461 |doi= }}
*{{cite journal | author=Gold DP, Clevers H, Alarcon B, ''et al.'' |title=Evolutionary relationship between the T3 chains of the T-cell receptor complex and the immunoglobulin supergene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 21 |pages= 7649-53 |year= 1987 |pmid= 3478717 |doi= }}
*{{cite journal | author=Tunnacliffe A, Sims JE, Rabbitts TH |title=T3 delta pre-mRNA is transcribed from a non-TATA promoter and is alternatively spliced in human T cells. |journal=EMBO J. |volume=5 |issue= 6 |pages= 1245-52 |year= 1986 |pmid= 3488209 |doi= }}
*{{cite journal | author=van den Elsen P, Shepley BA, Borst J, ''et al.'' |title=Isolation of cDNA clones encoding the 20K T3 glycoprotein of human T-cell receptor complex. |journal=Nature |volume=312 |issue= 5993 |pages= 413-8 |year= 1985 |pmid= 6095101 |doi= }}
*{{cite journal | author=Oravecz T, Norcross MA |title=Costimulatory properties of the human CD4 molecule: enhancement of CD3-induced T cell activation by human immunodeficiency virus type 1 through viral envelope glycoprotein gp120. |journal=AIDS Res. Hum. Retroviruses |volume=9 |issue= 10 |pages= 945-55 |year= 1994 |pmid= 7506554 |doi= }}
*{{cite journal | author=Luzzati AL, Giacomini E, Giordani L, ''et al.'' |title=An HIV p24 heptapeptide down-regulates antigen-specific responses in vitro interfering at the level of the T3-Ti complex. |journal=Cell. Immunol. |volume=156 |issue= 2 |pages= 286-95 |year= 1994 |pmid= 7517794 |doi= 10.1006/cimm.1994.1175 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COMP... {November 17, 2007 10:39:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:40:00 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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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_COMP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fbm.
| PDB = {{PDB2|1fbm}}, {{PDB2|1mz9}}, {{PDB2|1vdf}}
| Name = Cartilage oligomeric matrix protein
| HGNCid = 2227
| Symbol = COMP
| AltSymbols =; MED; EDM1; EPD1; MGC131819; MGC149768; PSACH; THBS5
| OMIM = 600310
| ECnumber =
| Homologene = 74
| MGIid = 88469
| GeneAtlas_image1 = PBB_GE_COMP_205713_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1311
| Hs_Ensembl = ENSG00000105664
| Hs_RefseqProtein = NP_000086
| Hs_RefseqmRNA = NM_000095
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 18754584
| Hs_GenLoc_end = 18763114
| Hs_Uniprot = P49747
| Mm_EntrezGene = 12845
| Mm_Ensembl = ENSMUSG00000031849
| Mm_RefseqmRNA = NM_016685
| Mm_RefseqProtein = NP_057894
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 73302547
| Mm_GenLoc_end = 73311055
| Mm_Uniprot = A1A557
}}
}}
'''Cartilage oligomeric matrix protein''', also known as '''COMP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COMP cartilage oligomeric matrix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1311| 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 is a noncollagenous extracellular matrix (ECM) protein. It consists of five identical glycoprotein subunits, each with EGF-like and calcium-binding (thrombospondin-like) domains. Oligomerization results from formation of a five-stranded coiled coil and disulfides. Binding to other ECM proteins such as collagen appears to depend on divalent cations. Mutations can cause the osteochondrodysplasias pseudochondroplasia (PSACH) and multiple epiphyseal dysplasia (MED).<ref name="entrez">{{cite web | title = Entrez Gene: COMP cartilage oligomeric matrix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1311| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Unger S, Hecht JT |title=Pseudoachondroplasia and multiple epiphyseal dysplasia: New etiologic developments. |journal=Am. J. Med. Genet. |volume=106 |issue= 4 |pages= 244-50 |year= 2002 |pmid= 11891674 |doi= }}
*{{cite journal | author=Liu C |title=Transcriptional mechanism of COMP gene expression and chondrogenesis. |journal=Journal of musculoskeletal & neuronal interactions |volume=5 |issue= 4 |pages= 340-1 |year= 2006 |pmid= 16340129 |doi= }}
*{{cite journal | author=Morozzi G, Fabbroni M, Bellisai F, ''et al.'' |title=Cartilage oligomeric matrix protein level in rheumatic diseases: potential use as a marker for measuring articular cartilage damage and/or the therapeutic efficacy of treatments. |journal=Ann. N. Y. Acad. Sci. |volume=1108 |issue= |pages= 398-407 |year= 2007 |pmid= 17894003 |doi= }}
*{{cite journal | author=Månsson B, Carey D, Alini M, ''et al.'' |title=Cartilage and bone metabolism in rheumatoid arthritis. Differences between rapid and slow progression of disease identified by serum markers of cartilage metabolism. |journal=J. Clin. Invest. |volume=95 |issue= 3 |pages= 1071-7 |year= 1995 |pmid= 7533784 |doi= }}
*{{cite journal | author=Hecht JT, Nelson LD, Crowder E, ''et al.'' |title=Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia. |journal=Nat. Genet. |volume=10 |issue= 3 |pages= 325-9 |year= 1995 |pmid= 7670471 |doi= 10.1038/ng0795-325 }}
*{{cite journal | author=Briggs MD, Hoffman SM, King LM, ''et al.'' |title=Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene. |journal=Nat. Genet. |volume=10 |issue= 3 |pages= 330-6 |year= 1995 |pmid= 7670472 |doi= 10.1038/ng0795-330 }}
*{{cite journal | author=Newton G, Weremowicz S, Morton CC, ''et al.'' |title=Characterization of human and mouse cartilage oligomeric matrix protein. |journal=Genomics |volume=24 |issue= 3 |pages= 435-9 |year= 1995 |pmid= 7713493 |doi= 10.1006/geno.1994.1649 }}
*{{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=Oehlmann R, Summerville GP, Yeh G, ''et al.'' |title=Genetic linkage mapping of multiple epiphyseal dysplasia to the pericentromeric region of chromosome 19. |journal=Am. J. Hum. Genet. |volume=54 |issue= 1 |pages= 3-10 |year= 1994 |pmid= 8279467 |doi= }}
*{{cite journal | author=Briggs MD, Rasmussen IM, Weber JL, ''et al.'' |title=Genetic linkage of mild pseudoachondroplasia (PSACH) to markers in the pericentromeric region of chromosome 19. |journal=Genomics |volume=18 |issue= 3 |pages= 656-60 |year= 1994 |pmid= 8307576 |doi= }}
*{{cite journal | author=Ballo R, Briggs MD, Cohn DH, ''et al.'' |title=Multiple epiphyseal dysplasia, ribbing type: a novel point mutation in the COMP gene in a South African family. |journal=Am. J. Med. Genet. |volume=68 |issue= 4 |pages= 396-400 |year= 1997 |pmid= 9021009 |doi= }}
*{{cite journal | author=Susic S, McGrory J, Ahier J, Cole WG |title=Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein. |journal=Clin. Genet. |volume=51 |issue= 4 |pages= 219-24 |year= 1997 |pmid= 9184241 |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=Briggs MD, Mortier GR, Cole WG, ''et al.'' |title=Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum. |journal=Am. J. Hum. Genet. |volume=62 |issue= 2 |pages= 311-9 |year= 1998 |pmid= 9463320 |doi= }}
*{{cite journal | author=Rosenberg K, Olsson H, Mörgelin M, Heinegård D |title=Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen. |journal=J. Biol. Chem. |volume=273 |issue= 32 |pages= 20397-403 |year= 1998 |pmid= 9685393 |doi= }}
*{{cite journal | author=Hecht JT, Deere M, Putnam E, ''et al.'' |title=Characterization of cartilage oligomeric matrix protein (COMP) in human normal and pseudoachondroplasia musculoskeletal tissues. |journal=Matrix Biol. |volume=17 |issue= 4 |pages= 269-78 |year= 1998 |pmid= 9749943 |doi= }}
*{{cite journal | author=Délot E, King LM, Briggs MD, ''et al.'' |title=Trinucleotide expansion mutations in the cartilage oligomeric matrix protein (COMP) gene. |journal=Hum. Mol. Genet. |volume=8 |issue= 1 |pages= 123-8 |year= 1999 |pmid= 9887340 |doi= }}
*{{cite journal | author=Ikegawa S, Ohashi H, Nishimura G, ''et al.'' |title=Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia. |journal=Hum. Genet. |volume=103 |issue= 6 |pages= 633-8 |year= 1999 |pmid= 9921895 |doi= }}
*{{cite journal | author=Deere M, Sanford T, Francomano CA, ''et al.'' |title=Identification of nine novel mutations in cartilage oligomeric matrix protein in patients with pseudoachondroplasia and multiple epiphyseal dysplasia. |journal=Am. J. Med. Genet. |volume=85 |issue= 5 |pages= 486-90 |year= 1999 |pmid= 10405447 |doi= }}
*{{cite journal | author=Thur J, Rosenberg K, Nitsche DP, ''et al.'' |title=Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX. |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6083-92 |year= 2001 |pmid= 11084047 |doi= 10.1074/jbc.M009512200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSTA... {November 17, 2007 10:40:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:40:38 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 = PBB_Protein_CSTA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cyu.
| PDB = {{PDB2|1cyu}}, {{PDB2|1cyv}}, {{PDB2|1dvc}}, {{PDB2|1dvd}}, {{PDB2|1gd3}}, {{PDB2|1gd4}}, {{PDB2|1n9j}}, {{PDB2|1nb3}}, {{PDB2|1nb5}}
| Name = Cystatin A (stefin A)
| HGNCid = 2481
| Symbol = CSTA
| AltSymbols =; STF1; STFA
| OMIM = 184600
| ECnumber =
| Homologene = 3819
| MGIid = 3524930
| GeneAtlas_image1 = PBB_GE_CSTA_204971_at_tn.png
| Function = {{GNF_GO|id=GO:0004869 |text = cysteine protease inhibitor activity}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}}
| Component = {{GNF_GO|id=GO:0001533 |text = cornified envelope}} {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0018149 |text = peptide cross-linking}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1475
| Hs_Ensembl = ENSG00000121552
| Hs_RefseqProtein = NP_005204
| Hs_RefseqmRNA = NM_005213
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 123526701
| Hs_GenLoc_end = 123543501
| Hs_Uniprot = P01040
| Mm_EntrezGene = 209294
| Mm_Ensembl = ENSMUSG00000034362
| Mm_RefseqmRNA = NM_001033239
| Mm_RefseqProtein = NP_001028411
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 36039245
| Mm_GenLoc_end = 36050490
| Mm_Uniprot = P56567
}}
}}
'''Cystatin A (stefin A)''', also known as '''CSTA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CSTA cystatin A (stefin A)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1475| 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 cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins, and kininogens. This gene encodes a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. The protein is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Stefins have been proposed as prognostic and diagnostic tools for cancer.<ref name="entrez">{{cite web | title = Entrez Gene: CSTA cystatin A (stefin A)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1475| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Järvinen M, Rinne A, Hopsu-Havu VK |title=Human cystatins in normal and diseased tissues--a review. |journal=Acta Histochem. |volume=82 |issue= 1 |pages= 5-18 |year= 1988 |pmid= 3122506 |doi= }}
*{{cite journal | author=Brown WM, Dziegielewska KM |title=Friends and relations of the cystatin superfamily--new members and their evolution. |journal=Protein Sci. |volume=6 |issue= 1 |pages= 5-12 |year= 1997 |pmid= 9007972 |doi= }}
*{{cite journal | author=Kos J, Lah TT |title=Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and therapy in cancer (review). |journal=Oncol. Rep. |volume=5 |issue= 6 |pages= 1349-61 |year= 1998 |pmid= 9769367 |doi= }}
*{{cite journal | author=Rinne A, Järvinen M, Räsänen O |title=A protein reminiscent of the epidermal SH-protease inhibitor occurs in squamous epithelia of man and rat. |journal=Acta Histochem. |volume=63 |issue= 2 |pages= 183-92 |year= 1979 |pmid= 107702 |doi= }}
*{{cite journal | author=Räsänen O, Järvinen M, Rinne A |title=Localization of the human SH-protease inhibitor in the epidermis. Immunofluorescent studies. |journal=Acta Histochem. |volume=63 |issue= 2 |pages= 193-6 |year= 1979 |pmid= 107703 |doi= }}
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Hsieh WT, Barrick JL, Berrettini WH, ''et al.'' |title=A PstI DNA polymorphism in the human stefin A gene (STF 1). |journal=Nucleic Acids Res. |volume=19 |issue= 7 |pages= 1722 |year= 1991 |pmid= 1674139 |doi= }}
*{{cite journal | author=Madsen P, Rasmussen HH, Leffers H, ''et al.'' |title=Molecular cloning, occurrence, and expression of a novel partially secreted protein "psoriasin" that is highly up-regulated in psoriatic skin. |journal=J. Invest. Dermatol. |volume=97 |issue= 4 |pages= 701-12 |year= 1991 |pmid= 1940442 |doi= }}
*{{cite journal | author=Hsieh WT, Fong D, Sloane BF, ''et al.'' |title=Mapping of the gene for human cysteine proteinase inhibitor stefin A, STF1, to chromosome 3cen-q21. |journal=Genomics |volume=9 |issue= 1 |pages= 207-9 |year= 1991 |pmid= 2004763 |doi= }}
*{{cite journal | author=Rinne A, Järvinen M, Dorn A, ''et al.'' |title=[Low-molecular cysteine protease inhibitors in the human palatal tonsil] |journal=Anatomischer Anzeiger |volume=161 |issue= 3 |pages= 215-30 |year= 1986 |pmid= 2424340 |doi= }}
*{{cite journal | author=Kartasova T, Cornelissen BJ, Belt P, van de Putte P |title=Effects of UV, 4-NQO and TPA on gene expression in cultured human epidermal keratinocytes. |journal=Nucleic Acids Res. |volume=15 |issue= 15 |pages= 5945-62 |year= 1987 |pmid= 2442723 |doi= }}
*{{cite journal | author=Takeda A, Kaji H, Nakaya K, ''et al.'' |title=Comparative studies on the primary structure of human cystatin as from epidermis, liver, spleen, and leukocytes. |journal=J. Biochem. |volume=105 |issue= 6 |pages= 986-91 |year= 1989 |pmid= 2768224 |doi= }}
*{{cite journal | author=Strauss M, Stollwerk J, Lenarcic B, ''et al.'' |title=Chemical synthesis of a gene for human stefin A and its expression in E. coli. |journal=Biol. Chem. Hoppe-Seyler |volume=369 |issue= 9 |pages= 1019-30 |year= 1989 |pmid= 3067731 |doi= }}
*{{cite journal | author=Davies ME, Barrett AJ |title=Immunolocalization of human cystatins in neutrophils and lymphocytes. |journal=Histochemistry |volume=80 |issue= 4 |pages= 373-7 |year= 1984 |pmid= 6429090 |doi= }}
*{{cite journal | author=Machleidt W, Borchart U, Fritz H, ''et al.'' |title=Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. |journal=Hoppe-Seyler's Z. Physiol. Chem. |volume=364 |issue= 11 |pages= 1481-6 |year= 1984 |pmid= 6689312 |doi= }}
*{{cite journal | author=Söderström KO, Laato M, Wu P, ''et al.'' |title=Expression of acid cysteine proteinase inhibitor (ACPI) in the normal human prostate, benign prostatic hyperplasia and adenocarcinoma. |journal=Int. J. Cancer |volume=62 |issue= 1 |pages= 1-4 |year= 1995 |pmid= 7541394 |doi= }}
*{{cite journal | author=Tate S, Ushioda T, Utsunomiya-Tate N, ''et al.'' |title=Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the interactions between the N- and C-termini to maintain the inhibitory active form of cystatin A. |journal=Biochemistry |volume=34 |issue= 45 |pages= 14637-48 |year= 1995 |pmid= 7578072 |doi= }}
*{{cite journal | author=Martin JR, Craven CJ, Jerala R, ''et al.'' |title=The three-dimensional solution structure of human stefin A. |journal=J. Mol. Biol. |volume=246 |issue= 2 |pages= 331-43 |year= 1995 |pmid= 7869384 |doi= }}
*{{cite journal | author=Steinert PM, Marekov LN |title=Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 2021-30 |year= 1997 |pmid= 8999895 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTSC... {November 17, 2007 10:38:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:39:22 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_CTSC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k3b.
| PDB = {{PDB2|1k3b}}, {{PDB2|2djf}}, {{PDB2|2djg}}
| Name = Cathepsin C
| HGNCid = 2528
| Symbol = CTSC
| AltSymbols =; CPPI; DPP1; DPPI; HMS; JP; JPD; PALS; PLS
| OMIM = 602365
| ECnumber =
| Homologene = 1373
| MGIid = 109553
| GeneAtlas_image1 = PBB_GE_CTSC_201487_at_tn.png
| Function = {{GNF_GO|id=GO:0004197 |text = cysteine-type endopeptidase activity}} {{GNF_GO|id=GO:0004214 |text = dipeptidyl-peptidase I activity}} {{GNF_GO|id=GO:0031404 |text = chloride ion binding}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1075
| Hs_Ensembl = ENSG00000109861
| Hs_RefseqProtein = NP_001805
| Hs_RefseqmRNA = NM_001814
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 87666421
| Hs_GenLoc_end = 87710586
| Hs_Uniprot = P53634
| Mm_EntrezGene = 13032
| Mm_Ensembl = ENSMUSG00000030560
| Mm_RefseqmRNA = NM_009982
| Mm_RefseqProtein = NP_034112
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 88153327
| Mm_GenLoc_end = 88186080
| Mm_Uniprot = Q3TIF1
}}
}}
'''Cathepsin C''', also known as '''CTSC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTSC cathepsin C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1075| 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, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in immune/inflammatory cells. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It requires chloride ions for activity and can degrade glucagon. Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CTSC cathepsin C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1075| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=McGuire MJ, Lipsky PE, Thiele DL |title=Purification and characterization of dipeptidyl peptidase I from human spleen. |journal=Arch. Biochem. Biophys. |volume=295 |issue= 2 |pages= 280-8 |year= 1992 |pmid= 1586157 |doi= }}
*{{cite journal | author=Paris A, Strukelj B, Pungercar J, ''et al.'' |title=Molecular cloning and sequence analysis of human preprocathepsin C. |journal=FEBS Lett. |volume=369 |issue= 2-3 |pages= 326-30 |year= 1995 |pmid= 7649281 |doi= }}
*{{cite journal | author=Dolenc I, Turk B, Pungercic G, ''et al.'' |title=Oligomeric structure and substrate induced inhibition of human cathepsin C. |journal=J. Biol. Chem. |volume=270 |issue= 37 |pages= 21626-31 |year= 1995 |pmid= 7665576 |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=Rao NV, Rao GV, Hoidal JR |title=Human dipeptidyl-peptidase I. Gene characterization, localization, and expression. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 10260-5 |year= 1997 |pmid= 9092576 |doi= }}
*{{cite journal | author=Fischer J, Blanchet-Bardon C, Prud'homme JF, ''et al.'' |title=Mapping of Papillon-Lefevre syndrome to the chromosome 11q14 region. |journal=Eur. J. Hum. Genet. |volume=5 |issue= 3 |pages= 156-60 |year= 1997 |pmid= 9272739 |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=Cigić B, Krizaj I, Kralj B, ''et al.'' |title=Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C. |journal=Biochim. Biophys. Acta |volume=1382 |issue= 1 |pages= 143-50 |year= 1998 |pmid= 9507095 |doi= }}
*{{cite journal | author=Toomes C, James J, Wood AJ, ''et al.'' |title=Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis. |journal=Nat. Genet. |volume=23 |issue= 4 |pages= 421-4 |year= 1999 |pmid= 10581027 |doi= 10.1038/70525 }}
*{{cite journal | author=Hart TC, Hart PS, Bowden DW, ''et al.'' |title=Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome. |journal=J. Med. Genet. |volume=36 |issue= 12 |pages= 881-7 |year= 2000 |pmid= 10593994 |doi= }}
*{{cite journal | author=Hart TC, Hart PS, Michalec MD, ''et al.'' |title=Haim-Munk syndrome and Papillon-Lefèvre syndrome are allelic mutations in cathepsin C. |journal=J. Med. Genet. |volume=37 |issue= 2 |pages= 88-94 |year= 2000 |pmid= 10662807 |doi= }}
*{{cite journal | author=Hart TC, Hart PS, Michalec MD, ''et al.'' |title=Localisation of a gene for prepubertal periodontitis to chromosome 11q14 and identification of a cathepsin C gene mutation. |journal=J. Med. Genet. |volume=37 |issue= 2 |pages= 95-101 |year= 2000 |pmid= 10662808 |doi= }}
*{{cite journal | author=Suzuki Y, Ishihara D, Sasaki M, ''et al.'' |title=Statistical analysis of the 5' untranslated region of human mRNA using "Oligo-Capped" cDNA libraries. |journal=Genomics |volume=64 |issue= 3 |pages= 286-97 |year= 2000 |pmid= 10756096 |doi= 10.1006/geno.2000.6076 }}
*{{cite journal | author=Cigić B, Dahl SW, Pain RH |title=The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme. |journal=Biochemistry |volume=39 |issue= 40 |pages= 12382-90 |year= 2000 |pmid= 11015218 |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=Hart PS, Zhang Y, Firatli E, ''et al.'' |title=Identification of cathepsin C mutations in ethnically diverse papillon-Lefèvre syndrome patients. |journal=J. Med. Genet. |volume=37 |issue= 12 |pages= 927-32 |year= 2001 |pmid= 11106356 |doi= }}
*{{cite journal | author=Zhang Y, Lundgren T, Renvert S, ''et al.'' |title=Evidence of a founder effect for four cathepsin C gene mutations in Papillon-Lefèvre syndrome patients. |journal=J. Med. Genet. |volume=38 |issue= 2 |pages= 96-101 |year= 2001 |pmid= 11158173 |doi= }}
*{{cite journal | author=Nakano A, Nomura K, Nakano H, ''et al.'' |title=Papillon-Lefèvre syndrome: mutations and polymorphisms in the cathepsin C gene. |journal=J. Invest. Dermatol. |volume=116 |issue= 2 |pages= 339-43 |year= 2001 |pmid= 11180012 |doi= 10.1046/j.1523-1747.2001.01244.x }}
*{{cite journal | author=Allende LM, García-Pérez MA, Moreno A, ''et al.'' |title=Cathepsin C gene: First compound heterozygous patient with Papillon-Lefèvre syndrome and a novel symptomless mutation. |journal=Hum. Mutat. |volume=17 |issue= 2 |pages= 152-3 |year= 2001 |pmid= 11180601 |doi= 10.1002/1098-1004(200102)17:2<152::AID-HUMU10>3.0.CO;2-# }}
*{{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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DAPK1... {November 17, 2007 10:40:38 PM PST}
- SEARCH REDIRECT: Control Box Found: DAPK1 {November 17, 2007 10:41:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:41:08 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:41:08 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:41:08 PM PST}
- UPDATED: Updated protein page: DAPK1 {November 17, 2007 10:41:15 PM PST}
- INFO: Beginning work on EDG1... {November 17, 2007 10:41:15 PM PST}
- SEARCH REDIRECT: Control Box Found: EDG1 {November 17, 2007 10:42:01 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:42:05 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:42:05 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:42:05 PM PST}
- UPDATED: Updated protein page: EDG1 {November 17, 2007 10:42:12 PM PST}
- INFO: Beginning work on ERCC5... {November 17, 2007 10:42:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:42:45 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 = Excision repair cross-complementing rodent repair deficiency, complementation group 5 (xeroderma pigmentosum, complementation group G (Cockayne syndrome))
| HGNCid = 3437
| Symbol = ERCC5
| AltSymbols =; ERCM2; UVDR; XPG; XPGC
| OMIM = 133530
| ECnumber =
| Homologene = 37265
| MGIid = 103582
| GeneAtlas_image1 = PBB_GE_ERCC5_202414_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003697 |text = single-stranded DNA binding}} {{GNF_GO|id=GO:0004518 |text = nuclease activity}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004520 |text = endodeoxyribonuclease activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006283 |text = transcription-coupled nucleotide-excision repair}} {{GNF_GO|id=GO:0006289 |text = nucleotide-excision repair}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2073
| Hs_Ensembl = ENSG00000134899
| Hs_RefseqProtein = NP_000114
| Hs_RefseqmRNA = NM_000123
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 102295195
| Hs_GenLoc_end = 102326346
| Hs_Uniprot = P28715
| Mm_EntrezGene = 22592
| Mm_Ensembl = ENSMUSG00000026048
| Mm_RefseqmRNA = NM_011729
| Mm_RefseqProtein = NP_035859
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 44092393
| Mm_GenLoc_end = 44125806
| Mm_Uniprot = Q3TPQ3
}}
}}
'''Excision repair cross-complementing rodent repair deficiency, complementation group 5 (xeroderma pigmentosum, complementation group G (Cockayne syndrome))''', also known as '''ERCC5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ERCC5 excision repair cross-complementing rodent repair deficiency, complementation group 5 (xeroderma pigmentosum, complementation group G (Cockayne syndrome))| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2073| 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 = Excision repair cross-complementing rodent repair deficiency, complementation group 5 (xeroderma pigmentosum, complementation group G) is involved in excision repair of UV-induced DNA damage. Mutations cause Cockayne syndrome, which is characterized by severe growth defects, mental retardation, and cachexia. Multiple alternatively spliced transcript variants encoding distinct isoforms have been described, but the biological validity of all variants has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: ERCC5 excision repair cross-complementing rodent repair deficiency, complementation group 5 (xeroderma pigmentosum, complementation group G (Cockayne syndrome))| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2073| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Miura M |title=Detection of chromatin-bound PCNA in mammalian cells and its use to study DNA excision repair. |journal=J. Radiat. Res. |volume=40 |issue= 1 |pages= 1-12 |year= 1999 |pmid= 10408173 |doi= }}
*{{cite journal | author=Cleaver JE, Thompson LH, Richardson AS, States JC |title=A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. |journal=Hum. Mutat. |volume=14 |issue= 1 |pages= 9-22 |year= 1999 |pmid= 10447254 |doi= 10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6 }}
*{{cite journal | author=Takahashi E, Shiomi N, Shiomi T |title=Precise localization of the excision repair gene, ERCC5, to human chromosome 13q32.3-q33.1 by direct R-banding fluorescence in situ hybridization. |journal=Jpn. J. Cancer Res. |volume=83 |issue= 11 |pages= 1117-9 |year= 1993 |pmid= 1483924 |doi= }}
*{{cite journal | author=Mudgett JS, MacInnes MA |title=Isolation of the functional human excision repair gene ERCC5 by intercosmid recombination. |journal=Genomics |volume=8 |issue= 4 |pages= 623-33 |year= 1991 |pmid= 2276736 |doi= }}
*{{cite journal | author=Shiomi T, Harada Y, Saito T, ''et al.'' |title=An ERCC5 gene with homology to yeast RAD2 is involved in group G xeroderma pigmentosum. |journal=Mutat. Res. |volume=314 |issue= 2 |pages= 167-75 |year= 1994 |pmid= 7510366 |doi= }}
*{{cite journal | author=Lehmann AR, Bootsma D, Clarkson SG, ''et al.'' |title=Nomenclature of human DNA repair genes. |journal=Mutat. Res. |volume=315 |issue= 1 |pages= 41-2 |year= 1994 |pmid= 7517009 |doi= }}
*{{cite journal | author=Cloud KG, Shen B, Strniste GF, Park MS |title=XPG protein has a structure-specific endonuclease activity. |journal=Mutat. Res. |volume=347 |issue= 2 |pages= 55-60 |year= 1995 |pmid= 7651464 |doi= }}
*{{cite journal | author=Nouspikel T, Clarkson SG |title=Mutations that disable the DNA repair gene XPG in a xeroderma pigmentosum group G patient. |journal=Hum. Mol. Genet. |volume=3 |issue= 6 |pages= 963-7 |year= 1994 |pmid= 7951246 |doi= }}
*{{cite journal | author=Habraken Y, Sung P, Prakash L, Prakash S |title=Human xeroderma pigmentosum group G gene encodes a DNA endonuclease. |journal=Nucleic Acids Res. |volume=22 |issue= 16 |pages= 3312-6 |year= 1994 |pmid= 8078765 |doi= }}
*{{cite journal | author=Samec S, Jones TA, Corlet J, ''et al.'' |title=The human gene for xeroderma pigmentosum complementation group G (XPG) maps to 13q33 by fluorescence in situ hybridization. |journal=Genomics |volume=21 |issue= 1 |pages= 283-5 |year= 1994 |pmid= 8088806 |doi= 10.1006/geno.1994.1261 }}
*{{cite journal | author=O'Donovan A, Davies AA, Moggs JG, ''et al.'' |title=XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair. |journal=Nature |volume=371 |issue= 6496 |pages= 432-5 |year= 1994 |pmid= 8090225 |doi= 10.1038/371432a0 }}
*{{cite journal | author=O'Donovan A, Scherly D, Clarkson SG, Wood RD |title=Isolation of active recombinant XPG protein, a human DNA repair endonuclease. |journal=J. Biol. Chem. |volume=269 |issue= 23 |pages= 15965-8 |year= 1994 |pmid= 8206890 |doi= }}
*{{cite journal | author=MacInnes MA, Dickson JA, Hernandez RR, ''et al.'' |title=Human ERCC5 cDNA-cosmid complementation for excision repair and bipartite amino acid domains conserved with RAD proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe. |journal=Mol. Cell. Biol. |volume=13 |issue= 10 |pages= 6393-402 |year= 1993 |pmid= 8413238 |doi= }}
*{{cite journal | author=Scherly D, Nouspikel T, Corlet J, ''et al.'' |title=Complementation of the DNA repair defect in xeroderma pigmentosum group G cells by a human cDNA related to yeast RAD2. |journal=Nature |volume=363 |issue= 6425 |pages= 182-5 |year= 1993 |pmid= 8483504 |doi= 10.1038/363182a0 }}
*{{cite journal | author=O'Donovan A, Wood RD |title=Identical defects in DNA repair in xeroderma pigmentosum group G and rodent ERCC group 5. |journal=Nature |volume=363 |issue= 6425 |pages= 185-8 |year= 1993 |pmid= 8483505 |doi= 10.1038/363185a0 }}
*{{cite journal | author=Iyer N, Reagan MS, Wu KJ, ''et al.'' |title=Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. |journal=Biochemistry |volume=35 |issue= 7 |pages= 2157-67 |year= 1996 |pmid= 8652557 |doi= 10.1021/bi9524124 }}
*{{cite journal | author=Park MS, Knauf JA, Pendergrass SH, ''et al.'' |title=Ultraviolet-induced movement of the human DNA repair protein, Xeroderma pigmentosum type G, in the nucleus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 16 |pages= 8368-73 |year= 1996 |pmid= 8710877 |doi= }}
*{{cite journal | author=Cooper PK, Nouspikel T, Clarkson SG, Leadon SA |title=Defective transcription-coupled repair of oxidative base damage in Cockayne syndrome patients from XP group G. |journal=Science |volume=275 |issue= 5302 |pages= 990-3 |year= 1997 |pmid= 9020084 |doi= }}
*{{cite journal | author=Nouspikel T, Lalle P, Leadon SA, ''et al.'' |title=A common mutational pattern in Cockayne syndrome patients from xeroderma pigmentosum group G: implications for a second XPG function. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 7 |pages= 3116-21 |year= 1997 |pmid= 9096355 |doi= }}
*{{cite journal | author=Gary R, Ludwig DL, Cornelius HL, ''et al.'' |title=The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24522-9 |year= 1997 |pmid= 9305916 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAP3K14... {November 17, 2007 10:50:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:50:29 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 =
| image_source =
| PDB =
| Name = Mitogen-activated protein kinase kinase kinase 14
| HGNCid = 6853
| Symbol = MAP3K14
| AltSymbols =; FTDCR1B; HS; HSNIK; NIK
| OMIM = 604655
| ECnumber =
| Homologene = 2940
| MGIid = 1858204
| GeneAtlas_image1 = PBB_GE_MAP3K14_205192_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9020
| Hs_Ensembl = ENSG00000006062
| Hs_RefseqProtein = NP_003945
| Hs_RefseqmRNA = NM_003954
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 40696278
| Hs_GenLoc_end = 40750148
| Hs_Uniprot = Q99558
| Mm_EntrezGene = 53859
| Mm_Ensembl = ENSMUSG00000020941
| Mm_RefseqmRNA = NM_016896
| Mm_RefseqProtein = NP_058592
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 103035854
| Mm_GenLoc_end = 103083835
| Mm_Uniprot = Q544K4
}}
}}
'''Mitogen-activated protein kinase kinase kinase 14''', also known as '''MAP3K14''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAP3K14 mitogen-activated protein kinase kinase kinase 14| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9020| 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 mitogen-activated protein kinase kinase kinase 14, which is a serine/threonine protein-kinase. This kinase binds to TRAF2 and stimulates NF-kappaB activity. It shares sequence similarity with several other MAPKK kinases. It participates in an NF-kappaB-inducing signalling cascade common to receptors of the tumour-necrosis/nerve-growth factor (TNF/NGF) family and to the interleukin-1 type-I receptor.<ref name="entrez">{{cite web | title = Entrez Gene: MAP3K14 mitogen-activated protein kinase kinase kinase 14| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9020| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Malinin NL, Boldin MP, Kovalenko AV, Wallach D |title=MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1. |journal=Nature |volume=385 |issue= 6616 |pages= 540-4 |year= 1997 |pmid= 9020361 |doi= 10.1038/385540a0 }}
*{{cite journal | author=Régnier CH, Song HY, Gao X, ''et al.'' |title=Identification and characterization of an IkappaB kinase. |journal=Cell |volume=90 |issue= 2 |pages= 373-83 |year= 1997 |pmid= 9244310 |doi= }}
*{{cite journal | author=Song HY, Régnier CH, Kirschning CJ, ''et al.'' |title=Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 18 |pages= 9792-6 |year= 1997 |pmid= 9275204 |doi= }}
*{{cite journal | author=Woronicz JD, Gao X, Cao Z, ''et al.'' |title=IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK. |journal=Science |volume=278 |issue= 5339 |pages= 866-9 |year= 1997 |pmid= 9346485 |doi= }}
*{{cite journal | author=Ling L, Cao Z, Goeddel DV |title=NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 7 |pages= 3792-7 |year= 1998 |pmid= 9520446 |doi= }}
*{{cite journal | author=Lee FS, Peters RT, Dang LC, Maniatis T |title=MEKK1 activates both IkappaB kinase alpha and IkappaB kinase beta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 16 |pages= 9319-24 |year= 1998 |pmid= 9689078 |doi= }}
*{{cite journal | author=Lin X, Mu Y, Cunningham ET, ''et al.'' |title=Molecular determinants of NF-kappaB-inducing kinase action. |journal=Mol. Cell. Biol. |volume=18 |issue= 10 |pages= 5899-907 |year= 1998 |pmid= 9742107 |doi= }}
*{{cite journal | author=Cohen L, Henzel WJ, Baeuerle PA |title=IKAP is a scaffold protein of the IkappaB kinase complex. |journal=Nature |volume=395 |issue= 6699 |pages= 292-6 |year= 1998 |pmid= 9751059 |doi= 10.1038/26254 }}
*{{cite journal | author=Aronsson FC, Magnusson P, Andersson B, ''et al.'' |title=The NIK protein kinase and C17orf1 genes: chromosomal mapping, gene structures and mutational screening in frontotemporal dementia and parkinsonism linked to chromosome 17. |journal=Hum. Genet. |volume=103 |issue= 3 |pages= 340-5 |year= 1998 |pmid= 9799091 |doi= }}
*{{cite journal | author=Nemoto S, DiDonato JA, Lin A |title=Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase. |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 7336-43 |year= 1998 |pmid= 9819420 |doi= }}
*{{cite journal | author=Li Y, Kang J, Friedman J, ''et al.'' |title=Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 3 |pages= 1042-7 |year= 1999 |pmid= 9927690 |doi= }}
*{{cite journal | author=Lallena MJ, Diaz-Meco MT, Bren G, ''et al.'' |title=Activation of IkappaB kinase beta by protein kinase C isoforms. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 2180-8 |year= 1999 |pmid= 10022904 |doi= }}
*{{cite journal | author=Lin X, Cunningham ET, Mu Y, ''et al.'' |title=The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-kappaB acting through the NF-kappaB-inducing kinase and IkappaB kinases. |journal=Immunity |volume=10 |issue= 2 |pages= 271-80 |year= 1999 |pmid= 10072079 |doi= }}
*{{cite journal | author=Ninomiya-Tsuji J, Kishimoto K, Hiyama A, ''et al.'' |title=The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway. |journal=Nature |volume=398 |issue= 6724 |pages= 252-6 |year= 1999 |pmid= 10094049 |doi= 10.1038/18465 }}
*{{cite journal | author=Delhase M, Hayakawa M, Chen Y, Karin M |title=Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation. |journal=Science |volume=284 |issue= 5412 |pages= 309-13 |year= 1999 |pmid= 10195894 |doi= }}
*{{cite journal | author=Hu WH, Johnson H, Shu HB |title=Tumor necrosis factor-related apoptosis-inducing ligand receptors signal NF-kappaB and JNK activation and apoptosis through distinct pathways. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30603-10 |year= 1999 |pmid= 10521444 |doi= }}
*{{cite journal | author=Yamamoto Y, Yin MJ, Gaynor RB |title=IkappaB kinase alpha (IKKalpha) regulation of IKKbeta kinase activity. |journal=Mol. Cell. Biol. |volume=20 |issue= 10 |pages= 3655-66 |year= 2000 |pmid= 10779355 |doi= }}
*{{cite journal | author=Xiao G, Sun SC |title=Negative regulation of the nuclear factor kappa B-inducing kinase by a cis-acting domain. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21081-5 |year= 2000 |pmid= 10887201 |doi= 10.1074/jbc.M002552200 }}
*{{cite journal | author=Chaudhary PM, Eby MT, Jasmin A, ''et al.'' |title=Activation of the NF-kappaB pathway by caspase 8 and its homologs. |journal=Oncogene |volume=19 |issue= 39 |pages= 4451-60 |year= 2000 |pmid= 11002417 |doi= 10.1038/sj.onc.1203812 }}
*{{cite journal | author=Kumar A, Eby MT, Sinha S, ''et al.'' |title=The ectodermal dysplasia receptor activates the nuclear factor-kappaB, JNK, and cell death pathways and binds to ectodysplasin A. |journal=J. Biol. Chem. |volume=276 |issue= 4 |pages= 2668-77 |year= 2001 |pmid= 11035039 |doi= 10.1074/jbc.M008356200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PINK1... {November 17, 2007 10:53:15 PM PST}
- SEARCH REDIRECT: Control Box Found: PINK1 {November 17, 2007 10:53:52 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:53:55 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:53:55 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:53:55 PM PST}
- UPDATED: Updated protein page: PINK1 {November 17, 2007 10:54:02 PM PST}
- INFO: Beginning work on PSMC4... {November 17, 2007 10:42:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:43:15 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_PSMC4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2dvw.
| PDB = {{PDB2|2dvw}}
| Name = Proteasome (prosome, macropain) 26S subunit, ATPase, 4
| HGNCid = 9551
| Symbol = PSMC4
| AltSymbols =; MGC13687; MGC23214; MGC8570; MIP224; S6; TBP7
| OMIM = 602707
| ECnumber =
| Homologene = 4744
| MGIid = 1346093
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}}
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5704
| Hs_Ensembl =
| Hs_RefseqProtein = NP_006494
| Hs_RefseqmRNA = NM_006503
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 23996
| Mm_Ensembl = ENSMUSG00000030603
| Mm_RefseqmRNA = NM_011874
| Mm_RefseqProtein = NP_036004
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 27750473
| Mm_GenLoc_end = 27758829
| Mm_Uniprot = Q3TFA5
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, ATPase, 4''', also known as '''PSMC4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMC4 proteasome (prosome, macropain) 26S subunit, ATPase, 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5704| 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 ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. This subunit has been shown to interact with an orphan member of the nuclear hormone receptor superfamily highly expressed in liver, and with gankyrin, a liver oncoprotein. Two transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: PSMC4 proteasome (prosome, macropain) 26S subunit, ATPase, 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5704| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{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=Nelbock P, Dillon PJ, Perkins A, Rosen CA |title=A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator. |journal=Science |volume=248 |issue= 4963 |pages= 1650-3 |year= 1990 |pmid= 2194290 |doi= }}
*{{cite journal | author=Dubiel W, Ferrell K, Rechsteiner M |title=Tat-binding protein 7 is a subunit of the 26S protease. |journal=Biol. Chem. Hoppe-Seyler |volume=375 |issue= 4 |pages= 237-40 |year= 1994 |pmid= 8060531 |doi= }}
*{{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=Shaw DR, Ennis HL |title=Molecular cloning and developmental regulation of Dictyostelium discoideum homologues of the human and yeast HIV1 Tat-binding protein. |journal=Biochem. Biophys. Res. Commun. |volume=193 |issue= 3 |pages= 1291-6 |year= 1993 |pmid= 8323548 |doi= 10.1006/bbrc.1993.1765 }}
*{{cite journal | author=Ohana B, Moore PA, Ruben SM, ''et al.'' |title=The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 1 |pages= 138-42 |year= 1993 |pmid= 8419915 |doi= }}
*{{cite journal | author=Dubiel W, Ferrell K, Rechsteiner M |title=Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease. |journal=FEBS Lett. |volume=323 |issue= 3 |pages= 276-8 |year= 1993 |pmid= 8500623 |doi= }}
*{{cite journal | author=Choi HS, Seol W, Moore DD |title=A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily. |journal=J. Steroid Biochem. Mol. Biol. |volume=56 |issue= 1-6 Spec No |pages= 23-30 |year= 1996 |pmid= 8603043 |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=Tanahashi N, Suzuki M, Fujiwara T, ''et al.'' |title=Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 229-32 |year= 1998 |pmid= 9473509 |doi= }}
*{{cite journal | author=Nakamura T, Tanaka T, Takagi H, Sato M |title=Cloning and heterogeneous in vivo expression of Tat binding protein-1 (TBP-1) in the mouse. |journal=Biochim. Biophys. Acta |volume=1399 |issue= 1 |pages= 93-100 |year= 1998 |pmid= 9714759 |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=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=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi= }}
*{{cite journal | author=Hartmann-Petersen R, Tanaka K, Hendil KB |title=Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 89-94 |year= 2001 |pmid= 11361004 |doi= 10.1006/abbi.2000.2178 }}
*{{cite journal | author=Ishizuka T, Satoh T, Monden T, ''et al.'' |title=Human immunodeficiency virus type 1 Tat binding protein-1 is a transcriptional coactivator specific for TR. |journal=Mol. Endocrinol. |volume=15 |issue= 8 |pages= 1329-43 |year= 2001 |pmid= 11463857 |doi= }}
*{{cite journal | author=Dawson S, Apcher S, Mee M, ''et al.'' |title=Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasome. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 10893-902 |year= 2002 |pmid= 11779854 |doi= 10.1074/jbc.M107313200 }}
*{{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 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMD7... {November 17, 2007 10:43:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:43:47 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 = Proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)
| HGNCid = 9565
| Symbol = PSMD7
| AltSymbols =; S12; P40; MOV34
| OMIM = 157970
| ECnumber =
| Homologene = 2104
| MGIid = 1351511
| GeneAtlas_image1 = PBB_GE_PSMD7_201705_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMD7_gnf1h06716_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005838 |text = proteasome regulatory particle (sensu Eukaryota)}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5713
| Hs_Ensembl = ENSG00000103035
| Hs_RefseqProtein = NP_002802
| Hs_RefseqmRNA = NM_002811
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 72888182
| Hs_GenLoc_end = 72897685
| Hs_Uniprot = P51665
| Mm_EntrezGene = 17463
| Mm_Ensembl = ENSMUSG00000039067
| Mm_RefseqmRNA = NM_010817
| Mm_RefseqProtein = NP_034947
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 110469510
| Mm_GenLoc_end = 110477611
| Mm_Uniprot = P26516
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)''', also known as '''PSMD7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMD7 proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5713| 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 a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 17.<ref name="entrez">{{cite web | title = Entrez Gene: PSMD7 proteasome (prosome, macropain) 26S subunit, non-ATPase, 7 (Mov34 homolog)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5713| 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=Gridley T, Gray DA, Orr-Weaver T, ''et al.'' |title=Molecular analysis of the Mov 34 mutation: transcript disrupted by proviral integration in mice is conserved in Drosophila. |journal=Development |volume=109 |issue= 1 |pages= 235-42 |year= 1990 |pmid= 2209467 |doi= }}
*{{cite journal | author=Winkelmann DA, Kahan L |title=Immunochemical accessibility of ribosomal protein S4 in the 30 S ribosome. The interaction of S4 with S5 and S12. |journal=J. Mol. Biol. |volume=165 |issue= 2 |pages= 357-74 |year= 1983 |pmid= 6188845 |doi= }}
*{{cite journal | author=Tsurumi C, DeMartino GN, Slaughter CA, ''et al.'' |title=cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and a homolog of the Mov-34 gene product. |journal=Biochem. Biophys. Res. Commun. |volume=210 |issue= 2 |pages= 600-8 |year= 1995 |pmid= 7755639 |doi= 10.1006/bbrc.1995.1701 }}
*{{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=Mahalingam S, Ayyavoo V, Patel M, ''et al.'' |title=HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor linked to the G2/M phase transition of the mammalian cell cycle. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 7 |pages= 3419-24 |year= 1998 |pmid= 9520381 |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=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=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 }}
*{{cite journal | author=Ramanathan MP, Curley E, Su M, ''et al.'' |title=Carboxyl terminus of hVIP/mov34 is critical for HIV-1-Vpr interaction and glucocorticoid-mediated signaling. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47854-60 |year= 2003 |pmid= 12237292 |doi= 10.1074/jbc.M203905200 }}
*{{cite journal | author=Thompson HG, Harris JW, Wold BJ, ''et al.'' |title=Identification and confirmation of a module of coexpressed genes. |journal=Genome Res. |volume=12 |issue= 10 |pages= 1517-22 |year= 2003 |pmid= 12368243 |doi= 10.1101/gr.418402 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |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=Gaddis NC, Chertova E, Sheehy AM, ''et al.'' |title=Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=77 |issue= 10 |pages= 5810-20 |year= 2003 |pmid= 12719574 |doi= }}
*{{cite journal | author=Lecossier D, Bouchonnet F, Clavel F, Hance AJ |title=Hypermutation of HIV-1 DNA in the absence of the Vif protein. |journal=Science |volume=300 |issue= 5622 |pages= 1112 |year= 2003 |pmid= 12750511 |doi= 10.1126/science.1083338 }}
*{{cite journal | author=Zhang H, Yang B, Pomerantz RJ, ''et al.'' |title=The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. |journal=Nature |volume=424 |issue= 6944 |pages= 94-8 |year= 2003 |pmid= 12808465 |doi= 10.1038/nature01707 }}
*{{cite journal | author=Mangeat B, Turelli P, Caron G, ''et al.'' |title=Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. |journal=Nature |volume=424 |issue= 6944 |pages= 99-103 |year= 2003 |pmid= 12808466 |doi= 10.1038/nature01709 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTGIR... {November 17, 2007 10:43:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:44:17 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 = Prostaglandin I2 (prostacyclin) receptor (IP)
| HGNCid = 9602
| Symbol = PTGIR
| AltSymbols =; IP; MGC102830; PRIPR
| OMIM = 600022
| ECnumber =
| Homologene = 7496
| MGIid = 99535
| GeneAtlas_image1 = PBB_GE_PTGIR_206187_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004960 |text = thromboxane receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5739
| Hs_Ensembl = ENSG00000160013
| Hs_RefseqProtein = NP_000951
| Hs_RefseqmRNA = NM_000960
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 51815566
| Hs_GenLoc_end = 51820194
| Hs_Uniprot = P43119
| Mm_EntrezGene = 19222
| Mm_Ensembl = ENSMUSG00000043017
| Mm_RefseqmRNA = NM_008967
| Mm_RefseqProtein = NP_032993
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 16065012
| Mm_GenLoc_end = 16069427
| Mm_Uniprot = Q3U4F1
}}
}}
'''Prostaglandin I2 (prostacyclin) receptor (IP)''', also known as '''PTGIR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTGIR prostaglandin I2 (prostacyclin) receptor (IP)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5739| 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 is a member of the G-protein coupled receptor family 1 and has been shown to be a receptor for prostacyclin. Prostacyclin, the major product of cyclooxygenase in macrovascular endothelium, elicits a potent vasodilation and inhibition of platelet aggregation through binding to this receptor.<ref name="entrez">{{cite web | title = Entrez Gene: PTGIR prostaglandin I2 (prostacyclin) receptor (IP)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5739| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coleman RA, Smith WL, Narumiya S |title=International Union of Pharmacology classification of prostanoid receptors: properties, distribution, and structure of the receptors and their subtypes. |journal=Pharmacol. Rev. |volume=46 |issue= 2 |pages= 205-29 |year= 1994 |pmid= 7938166 |doi= }}
*{{cite journal | author=Rauvala H, Peng HB |title=HB-GAM (heparin-binding growth-associated molecule) and heparin-type glycans in the development and plasticity of neuron-target contacts. |journal=Prog. Neurobiol. |volume=52 |issue= 2 |pages= 127-44 |year= 1997 |pmid= 9185236 |doi= }}
*{{cite journal | author=Smyth EM, FitzGerald GA |title=Human prostacyclin receptor. |journal=Vitam. Horm. |volume=65 |issue= |pages= 149-65 |year= 2003 |pmid= 12481546 |doi= }}
*{{cite journal | author=Boie Y, Rushmore TH, Darmon-Goodwin A, ''et al.'' |title=Cloning and expression of a cDNA for the human prostanoid IP receptor. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 12173-8 |year= 1994 |pmid= 7512962 |doi= }}
*{{cite journal | author=Katsuyama M, Sugimoto Y, Namba T, ''et al.'' |title=Cloning and expression of a cDNA for the human prostacyclin receptor. |journal=FEBS Lett. |volume=344 |issue= 1 |pages= 74-8 |year= 1994 |pmid= 7514139 |doi= }}
*{{cite journal | author=Ogawa Y, Tanaka I, Inoue M, ''et al.'' |title=Structural organization and chromosomal assignment of the human prostacyclin receptor gene. |journal=Genomics |volume=27 |issue= 1 |pages= 142-8 |year= 1995 |pmid= 7665161 |doi= }}
*{{cite journal | author=Duncan AM, Anderson LL, Funk CD, ''et al.'' |title=Chromosomal localization of the human prostanoid receptor gene family. |journal=Genomics |volume=25 |issue= 3 |pages= 740-2 |year= 1995 |pmid= 7759114 |doi= }}
*{{cite journal | author=Nakagawa O, Tanaka I, Usui T, ''et al.'' |title=Molecular cloning of human prostacyclin receptor cDNA and its gene expression in the cardiovascular system. |journal=Circulation |volume=90 |issue= 4 |pages= 1643-7 |year= 1994 |pmid= 7923647 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Sasaki Y, Takahashi T, Tanaka I, ''et al.'' |title=Expression of prostacyclin receptor in human megakaryocytes. |journal=Blood |volume=90 |issue= 3 |pages= 1039-46 |year= 1997 |pmid= 9242534 |doi= }}
*{{cite journal | author=Fisch A, Tobusch K, Veit K, ''et al.'' |title=Prostacyclin receptor desensitization is a reversible phenomenon in human platelets. |journal=Circulation |volume=96 |issue= 3 |pages= 756-60 |year= 1997 |pmid= 9264479 |doi= }}
*{{cite journal | author=Smyth EM, Li WH, FitzGerald GA |title=Phosphorylation of the prostacyclin receptor during homologous desensitization. A critical role for protein kinase c. |journal=J. Biol. Chem. |volume=273 |issue= 36 |pages= 23258-66 |year= 1998 |pmid= 9722557 |doi= }}
*{{cite journal | author=Kömhoff M, Lesener B, Nakao K, ''et al.'' |title=Localization of the prostacyclin receptor in human kidney. |journal=Kidney Int. |volume=54 |issue= 6 |pages= 1899-908 |year= 1999 |pmid= 9853255 |doi= 10.1046/j.1523-1755.1998.00213.x }}
*{{cite journal | author=Hayes JS, Lawler OA, Walsh MT, Kinsella BT |title=The prostacyclin receptor is isoprenylated. Isoprenylation is required for efficient receptor-effector coupling. |journal=J. Biol. Chem. |volume=274 |issue= 34 |pages= 23707-18 |year= 1999 |pmid= 10446129 |doi= }}
*{{cite journal | author=Smyth EM, Austin SC, Reilly MP, FitzGerald GA |title=Internalization and sequestration of the human prostacyclin receptor. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 32037-45 |year= 2000 |pmid= 10889200 |doi= 10.1074/jbc.M003873200 }}
*{{cite journal | author=Lawler OA, Miggin SM, Kinsella BT |title=Protein kinase A-mediated phosphorylation of serine 357 of the mouse prostacyclin receptor regulates its coupling to G(s)-, to G(i)-, and to G(q)-coupled effector signaling. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 33596-607 |year= 2001 |pmid= 11443126 |doi= 10.1074/jbc.M104434200 }}
*{{cite journal | author=Zhang Z, Austin SC, Smyth EM |title=Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction. |journal=Mol. Pharmacol. |volume=60 |issue= 3 |pages= 480-7 |year= 2001 |pmid= 11502878 |doi= }}
*{{cite journal | author=Fortier I, Patry C, Lora M, ''et al.'' |title=Immunohistochemical localization of the prostacyclin receptor (IP) human bone. |journal=Prostaglandins Leukot. Essent. Fatty Acids |volume=65 |issue= 2 |pages= 79-83 |year= 2001 |pmid= 11545623 |doi= 10.1054/plef.2001.0292 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAB27A... {November 17, 2007 10:44:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:45:14 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 =
| image_source =
| PDB =
| Name = RAB27A, member RAS oncogene family
| HGNCid = 9766
| Symbol = RAB27A
| AltSymbols =; GS2; HsT18676; MGC117246; RAB27; RAM
| OMIM = 603868
| ECnumber =
| Homologene = 3069
| MGIid = 1861441
| GeneAtlas_image1 = PBB_GE_RAB27A_209514_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RAB27A_209515_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_RAB27A_210951_x_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:0030425 |text = dendrite}} {{GNF_GO|id=GO:0042470 |text = melanosome}}
| Process = {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0015031 |text = protein transport}} {{GNF_GO|id=GO:0016192 |text = vesicle-mediated transport}} {{GNF_GO|id=GO:0051875 |text = pigment granule localization}} {{GNF_GO|id=GO:0051904 |text = pigment granule transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5873
| Hs_Ensembl = ENSG00000069974
| Hs_RefseqProtein = NP_004571
| Hs_RefseqmRNA = NM_004580
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 53283094
| Hs_GenLoc_end = 53369293
| Hs_Uniprot = P51159
| Mm_EntrezGene = 11891
| Mm_Ensembl = ENSMUSG00000032202
| Mm_RefseqmRNA = XM_988908
| Mm_RefseqProtein = XP_994002
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 72841997
| Mm_GenLoc_end = 72894724
| Mm_Uniprot = Q544U7
}}
}}
'''RAB27A, member RAS oncogene family''', also known as '''RAB27A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAB27A RAB27A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5873| 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 small GTPase superfamily, Rab family. The protein is membrane-bound and may be involved in protein transport and small GTPase mediated signal transduction. Mutations in this gene are associated with Griscelli syndrome type 2. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: RAB27A RAB27A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5873| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nagata K, Itoh H, Katada T, ''et al.'' |title=Purification, identification, and characterization of two GTP-binding proteins with molecular weights of 25,000 and 21,000 in human platelet cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-binding protein. |journal=J. Biol. Chem. |volume=264 |issue= 29 |pages= 17000-5 |year= 1989 |pmid= 2507536 |doi= }}
*{{cite journal | author=Seabra MC, Ho YK, Anant JS |title=Deficient geranylgeranylation of Ram/Rab27 in choroideremia. |journal=J. Biol. Chem. |volume=270 |issue= 41 |pages= 24420-7 |year= 1995 |pmid= 7592656 |doi= }}
*{{cite journal | author=Chen D, Guo J, Miki T, ''et al.'' |title=Molecular cloning and characterization of rab27a and rab27b, novel human rab proteins shared by melanocytes and platelets. |journal=Biochem. Mol. Med. |volume=60 |issue= 1 |pages= 27-37 |year= 1997 |pmid= 9066979 |doi= }}
*{{cite journal | author=Tolmachova T, Ramalho JS, Anant JS, ''et al.'' |title=Cloning, mapping and characterization of the human RAB27A gene. |journal=Gene |volume=239 |issue= 1 |pages= 109-16 |year= 1999 |pmid= 10571040 |doi= }}
*{{cite journal | author=Ménasché G, Pastural E, Feldmann J, ''et al.'' |title=Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. |journal=Nat. Genet. |volume=25 |issue= 2 |pages= 173-6 |year= 2000 |pmid= 10835631 |doi= 10.1038/76024 }}
*{{cite journal | author=Hu RM, Han ZG, Song HD, ''et al.'' |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543-8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997 }}
*{{cite journal | author=Haddad EK, Wu X, Hammer JA, Henkart PA |title=Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice. |journal=J. Cell Biol. |volume=152 |issue= 4 |pages= 835-42 |year= 2001 |pmid= 11266473 |doi= }}
*{{cite journal | author=Bahadoran P, Aberdam E, Mantoux F, ''et al.'' |title=Rab27a: A key to melanosome transport in human melanocytes. |journal=J. Cell Biol. |volume=152 |issue= 4 |pages= 843-50 |year= 2001 |pmid= 11266474 |doi= }}
*{{cite journal | author=Xu XR, Huang J, Xu ZG, ''et al.'' |title=Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15089-94 |year= 2002 |pmid= 11752456 |doi= 10.1073/pnas.241522398 }}
*{{cite journal | author=Kuroda TS, Fukuda M, Ariga H, Mikoshiba K |title=The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9212-8 |year= 2002 |pmid= 11773082 |doi= 10.1074/jbc.M112414200 }}
*{{cite journal | author=Fukuda M, Kuroda TS, Mikoshiba K |title=Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12432-6 |year= 2002 |pmid= 11856727 |doi= 10.1074/jbc.C200005200 }}
*{{cite journal | author=Yi Z, Yokota H, Torii S, ''et al.'' |title=The Rab27a/granuphilin complex regulates the exocytosis of insulin-containing dense-core granules. |journal=Mol. Cell. Biol. |volume=22 |issue= 6 |pages= 1858-67 |year= 2002 |pmid= 11865063 |doi= }}
*{{cite journal | author=Strom M, Hume AN, Tarafder AK, ''et al.'' |title=A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25423-30 |year= 2002 |pmid= 11980908 |doi= 10.1074/jbc.M202574200 }}
*{{cite journal | author=Wu X, Wang F, Rao K, ''et al.'' |title=Rab27a is an essential component of melanosome receptor for myosin Va. |journal=Mol. Biol. Cell |volume=13 |issue= 5 |pages= 1735-49 |year= 2002 |pmid= 12006666 |doi= 10.1091/mbc.01-12-0595 }}
*{{cite journal | author=Kuroda TS, Fukuda M, Ariga H, Mikoshiba K |title=Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 3 |pages= 899-906 |year= 2002 |pmid= 12051743 |doi= 10.1016/S0006-291X(02)00320-0 }}
*{{cite journal | author=Anikster Y, Huizing M, Anderson PD, ''et al.'' |title=Evidence that Griscelli syndrome with neurological involvement is caused by mutations in RAB27A, not MYO5A. |journal=Am. J. Hum. Genet. |volume=71 |issue= 2 |pages= 407-14 |year= 2002 |pmid= 12058346 |doi= }}
*{{cite journal | author=Nagashima K, Torii S, Yi Z, ''et al.'' |title=Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. |journal=FEBS Lett. |volume=517 |issue= 1-3 |pages= 233-8 |year= 2002 |pmid= 12062444 |doi= }}
*{{cite journal | author=Torii S, Zhao S, Yi Z, ''et al.'' |title=Granuphilin modulates the exocytosis of secretory granules through interaction with syntaxin 1a. |journal=Mol. Cell. Biol. |volume=22 |issue= 15 |pages= 5518-26 |year= 2002 |pmid= 12101244 |doi= }}
*{{cite journal | author=Wistow G, Bernstein SL, Wyatt MK, ''et al.'' |title=Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants. |journal=Mol. Vis. |volume=8 |issue= |pages= 205-20 |year= 2002 |pmid= 12107410 |doi= }}
*{{cite journal | author=Barral DC, Ramalho JS, Anders R, ''et al.'' |title=Functional redundancy of Rab27 proteins and the pathogenesis of Griscelli syndrome. |journal=J. Clin. Invest. |volume=110 |issue= 2 |pages= 247-57 |year= 2002 |pmid= 12122117 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RALA... {November 17, 2007 10:45:14 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:45:50 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_RALA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1u8y.
| PDB = {{PDB2|1u8y}}, {{PDB2|1u8z}}, {{PDB2|1u90}}, {{PDB2|1uad}}, {{PDB2|1zc3}}, {{PDB2|1zc4}}, {{PDB2|2a78}}, {{PDB2|2a9k}}, {{PDB2|2bov}}
| Name = V-ral simian leukemia viral oncogene homolog A (ras related)
| HGNCid = 9839
| Symbol = RALA
| AltSymbols =; MGC48949; RAL
| OMIM = 179550
| ECnumber =
| Homologene = 3942
| MGIid = 1927243
| GeneAtlas_image1 = PBB_GE_RALA_214435_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5898
| Hs_Ensembl = ENSG00000006451
| Hs_RefseqProtein = NP_005393
| Hs_RefseqmRNA = NM_005402
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 39629687
| Hs_GenLoc_end = 39714240
| Hs_Uniprot = P11233
| Mm_EntrezGene = 56044
| Mm_Ensembl = ENSMUSG00000008859
| Mm_RefseqmRNA = XM_985790
| Mm_RefseqProtein = XP_990884
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 17665717
| Mm_GenLoc_end = 17729359
| Mm_Uniprot = Q9CXY0
}}
}}
'''V-ral simian leukemia viral oncogene homolog A (ras related)''', also known as '''RALA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RALA v-ral simian leukemia viral oncogene homolog A (ras related)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5898| 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 product of this gene belongs to the small GTPase superfamily, Ras family of proteins. GTP-binding proteins mediate the transmembrane signaling initiated by the occupancy of certain cell surface receptors. This gene encodes a low molecular mass ras-like GTP-binding protein that shares about 50% similarity with other ras proteins.<ref name="entrez">{{cite web | title = Entrez Gene: RALA v-ral simian leukemia viral oncogene homolog A (ras related)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5898| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kinsella BT, Erdman RA, Maltese WA |title=Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. |journal=J. Biol. Chem. |volume=266 |issue= 15 |pages= 9786-94 |year= 1991 |pmid= 1903399 |doi= }}
*{{cite journal | author=Polakis PG, Weber RF, Nevins B, ''et al.'' |title=Identification of the ral and rac1 gene products, low molecular mass GTP-binding proteins from human platelets. |journal=J. Biol. Chem. |volume=264 |issue= 28 |pages= 16383-9 |year= 1989 |pmid= 2550440 |doi= }}
*{{cite journal | author=Chardin P, Tavitian A |title=Coding sequences of human ralA and ralB cDNAs. |journal=Nucleic Acids Res. |volume=17 |issue= 11 |pages= 4380 |year= 1989 |pmid= 2662142 |doi= }}
*{{cite journal | author=Rousseau-Merck MF, Bernheim A, Chardin P, ''et al.'' |title=The ras-related ral gene maps to chromosome 7p15-22. |journal=Hum. Genet. |volume=79 |issue= 2 |pages= 132-6 |year= 1988 |pmid= 3292391 |doi= }}
*{{cite journal | author=Cantor SB, Urano T, Feig LA |title=Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases. |journal=Mol. Cell. Biol. |volume=15 |issue= 8 |pages= 4578-84 |year= 1995 |pmid= 7623849 |doi= }}
*{{cite journal | author=Jullien-Flores V, Dorseuil O, Romero F, ''et al.'' |title=Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22473-7 |year= 1995 |pmid= 7673236 |doi= }}
*{{cite journal | author=Wang KL, Khan MT, Roufogalis BD |title=Identification and characterization of a calmodulin-binding domain in Ral-A, a Ras-related GTP-binding protein purified from human erythrocyte membrane. |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 16002-9 |year= 1997 |pmid= 9188503 |doi= }}
*{{cite journal | author=Luo JQ, Liu X, Hammond SM, ''et al.'' |title=RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 854-9 |year= 1997 |pmid= 9207251 |doi= 10.1006/bbrc.1997.6793 }}
*{{cite journal | author=Ikeda M, Ishida O, Hinoi T, ''et al.'' |title=Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral. |journal=J. Biol. Chem. |volume=273 |issue= 2 |pages= 814-21 |year= 1998 |pmid= 9422736 |doi= }}
*{{cite journal | author=Vavvas D, Li X, Avruch J, Zhang XF |title=Identification of Nore1 as a potential Ras effector. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5439-42 |year= 1998 |pmid= 9488663 |doi= }}
*{{cite journal | author=Kim JH, Lee SD, Han JM, ''et al.'' |title=Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA. |journal=FEBS Lett. |volume=430 |issue= 3 |pages= 231-5 |year= 1998 |pmid= 9688545 |doi= }}
*{{cite journal | author=Ohta Y, Suzuki N, Nakamura S, ''et al.'' |title=The small GTPase RalA targets filamin to induce filopodia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 2122-8 |year= 1999 |pmid= 10051605 |doi= }}
*{{cite journal | author=Wang KL, Roufogalis BD |title=Ca2+/calmodulin stimulates GTP binding to the ras-related protein ral-A. |journal=J. Biol. Chem. |volume=274 |issue= 21 |pages= 14525-8 |year= 1999 |pmid= 10329639 |doi= }}
*{{cite journal | author=Suzuki J, Yamazaki Y, Li G, ''et al.'' |title=Involvement of Ras and Ral in chemotactic migration of skeletal myoblasts. |journal=Mol. Cell. Biol. |volume=20 |issue= 13 |pages= 4658-65 |year= 2000 |pmid= 10848592 |doi= }}
*{{cite journal | author=de Bruyn KM, de Rooij J, Wolthuis RM, ''et al.'' |title=RalGEF2, a pleckstrin homology domain containing guanine nucleotide exchange factor for Ral. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29761-6 |year= 2000 |pmid= 10889189 |doi= 10.1074/jbc.M001160200 }}
*{{cite journal | author=Brymora A, Valova VA, Larsen MR, ''et al.'' |title=The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29792-7 |year= 2001 |pmid= 11406615 |doi= 10.1074/jbc.C100320200 }}
*{{cite journal | author=Sugihara K, Asano S, Tanaka K, ''et al.'' |title=The exocyst complex binds the small GTPase RalA to mediate filopodia formation. |journal=Nat. Cell Biol. |volume=4 |issue= 1 |pages= 73-8 |year= 2002 |pmid= 11744922 |doi= 10.1038/ncb720 }}
*{{cite journal | author=Clough RR, Sidhu RS, Bhullar RP |title=Calmodulin binds RalA and RalB and is required for the thrombin-induced activation of Ral in human platelets. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 28972-80 |year= 2002 |pmid= 12034722 |doi= 10.1074/jbc.M201504200 }}
*{{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=Xu L, Frankel P, Jackson D, ''et al.'' |title=Elevated phospholipase D activity in H-Ras- but not K-Ras-transformed cells by the synergistic action of RalA and ARF6. |journal=Mol. Cell. Biol. |volume=23 |issue= 2 |pages= 645-54 |year= 2003 |pmid= 12509462 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RBP4... {November 17, 2007 10:45:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:46:13 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_RBP4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aqb.
| PDB = {{PDB2|1aqb}}, {{PDB2|1brp}}, {{PDB2|1brq}}, {{PDB2|1erb}}, {{PDB2|1fel}}, {{PDB2|1fem}}, {{PDB2|1fen}}, {{PDB2|1hbp}}, {{PDB2|1hbq}}, {{PDB2|1jyd}}, {{PDB2|1jyj}}, {{PDB2|1kt3}}, {{PDB2|1kt4}}, {{PDB2|1kt5}}, {{PDB2|1kt6}}, {{PDB2|1kt7}}, {{PDB2|1qab}}, {{PDB2|1rbp}}, {{PDB2|1rlb}}
| Name = Retinol binding protein 4, plasma
| HGNCid = 9922
| Symbol = RBP4
| AltSymbols =;
| OMIM = 180250
| ECnumber =
| Homologene = 4908
| MGIid = 97879
| GeneAtlas_image1 = PBB_GE_RBP4_219140_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0016918 |text = retinal binding}} {{GNF_GO|id=GO:0019841 |text = retinol binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5950
| Hs_Ensembl = ENSG00000138207
| Hs_RefseqProtein = NP_006735
| Hs_RefseqmRNA = NM_006744
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 95341434
| Hs_GenLoc_end = 95351491
| Hs_Uniprot = P02753
| Mm_EntrezGene = 19662
| Mm_Ensembl = ENSMUSG00000024990
| Mm_RefseqmRNA = XM_993476
| Mm_RefseqProtein = XP_998570
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 38181773
| Mm_GenLoc_end = 38190392
| Mm_Uniprot = Q3TF08
}}
}}
'''Retinol binding protein 4, plasma''', also known as '''RBP4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RBP4 retinol binding protein 4, plasma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5950| 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 protein belongs to the lipocalin family and is the specific carrier for retinol (vitamin A alcohol) in the blood. It delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin which prevents its loss by filtration through the kidney glomeruli. A deficiency of vitamin A blocks secretion of the binding protein posttranslationally and results in defective delivery and supply to the epidermal cells.<ref name="entrez">{{cite web | title = Entrez Gene: RBP4 retinol binding protein 4, plasma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5950| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Newcomer ME, Ong DE |title=Plasma retinol binding protein: structure and function of the prototypic lipocalin. |journal=Biochim. Biophys. Acta |volume=1482 |issue= 1-2 |pages= 57-64 |year= 2000 |pmid= 11058747 |doi= }}
*{{cite journal | author=Fex G, Hansson B |title=Retinol-binding protein from human urine and its interaction with retinol and prealbumin. |journal=Eur. J. Biochem. |volume=94 |issue= 1 |pages= 307-13 |year= 1979 |pmid= 571335 |doi= }}
*{{cite journal | author=Rask L, Anundi H, Peterson PA |title=The primary structure of the human retinol-binding protein. |journal=FEBS Lett. |volume=104 |issue= 1 |pages= 55-8 |year= 1979 |pmid= 573217 |doi= }}
*{{cite journal | author=Fex G, Albertsson PA, Hansson B |title=Interaction between prealbumin and retinol-binding protein studied by affinity chromatography, gel filtration and two-phase partition. |journal=Eur. J. Biochem. |volume=99 |issue= 2 |pages= 353-60 |year= 1980 |pmid= 574085 |doi= }}
*{{cite journal | author=Monaco HL, Zanotti G |title=Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity. |journal=Biopolymers |volume=32 |issue= 4 |pages= 457-65 |year= 1992 |pmid= 1623143 |doi= 10.1002/bip.360320425 }}
*{{cite journal | author=Cowan SW, Newcomer ME, Jones TA |title=Crystallographic refinement of human serum retinol binding protein at 2A resolution. |journal=Proteins |volume=8 |issue= 1 |pages= 44-61 |year= 1990 |pmid= 2217163 |doi= 10.1002/prot.340080108 }}
*{{cite journal | author=Rask L, Anundi H, Fohlman J, Peterson PA |title=The complete amino acid sequence of human serum retinol-binding protein. |journal=Ups. J. Med. Sci. |volume=92 |issue= 2 |pages= 115-46 |year= 1987 |pmid= 2444024 |doi= }}
*{{cite journal | author=Rocchi M, Covone A, Romeo G, ''et al.'' |title=Regional mapping of RBP4 to 10q23----q24 and RBP1 to 3q21----q22 in man. |journal=Somat. Cell Mol. Genet. |volume=15 |issue= 2 |pages= 185-90 |year= 1989 |pmid= 2928844 |doi= }}
*{{cite journal | author=D'Onofrio C, Colantuoni V, Cortese R |title=Structure and cell-specific expression of a cloned human retinol binding protein gene: the 5'-flanking region contains hepatoma specific transcriptional signals. |journal=EMBO J. |volume=4 |issue= 8 |pages= 1981-9 |year= 1986 |pmid= 2998779 |doi= }}
*{{cite journal | author=Pfeffer BA, Clark VM, Flannery JG, Bok D |title=Membrane receptors for retinol-binding protein in cultured human retinal pigment epithelium. |journal=Invest. Ophthalmol. Vis. Sci. |volume=27 |issue= 7 |pages= 1031-40 |year= 1986 |pmid= 3013795 |doi= }}
*{{cite journal | author=Kameko M, Ichikawa M, Katsuyama T, ''et al.'' |title=Immunohistochemical localization of plasma retinol-binding protein and prealbumin in human pancreatic islets. |journal=Histochem. J. |volume=18 |issue= 4 |pages= 164-8 |year= 1986 |pmid= 3525470 |doi= }}
*{{cite journal | author=Siegenthaler G, Saurat JH |title=Loss of retinol-binding properties for plasma retinol-binding protein in normal human epidermis. |journal=J. Invest. Dermatol. |volume=88 |issue= 4 |pages= 403-8 |year= 1987 |pmid= 3559267 |doi= }}
*{{cite journal | author=Rask L, Vahlquist A, Peterson PA |title=Studies on two physiological forms of the human retinol-binding protein differing in vitamin A and arginine content. |journal=J. Biol. Chem. |volume=246 |issue= 21 |pages= 6638-46 |year= 1972 |pmid= 5132677 |doi= }}
*{{cite journal | author=Colantuoni V, Romano V, Bensi G, ''et al.'' |title=Cloning and sequencing of a full length cDNA coding for human retinol-binding protein. |journal=Nucleic Acids Res. |volume=11 |issue= 22 |pages= 7769-76 |year= 1984 |pmid= 6316270 |doi= }}
*{{cite journal | author=Newcomer ME, Jones TA, Aqvist J, ''et al.'' |title=The three-dimensional structure of retinol-binding protein. |journal=EMBO J. |volume=3 |issue= 7 |pages= 1451-4 |year= 1984 |pmid= 6540172 |doi= }}
*{{cite journal | author=Rask L, Anundi H, Böhme J, ''et al.'' |title=Structural and functional studies of vitamin A-binding proteins. |journal=Ann. N. Y. Acad. Sci. |volume=359 |issue= |pages= 79-90 |year= 1981 |pmid= 6942701 |doi= }}
*{{cite journal | author=Jaconi S, Rose K, Hughes GJ, ''et al.'' |title=Characterization of two post-translationally processed forms of human serum retinol-binding protein: altered ratios in chronic renal failure. |journal=J. Lipid Res. |volume=36 |issue= 6 |pages= 1247-53 |year= 1995 |pmid= 7666002 |doi= }}
*{{cite journal | author=Berni R, Malpeli G, Folli C, ''et al.'' |title=The Ile-84-->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein. |journal=J. Biol. Chem. |volume=269 |issue= 38 |pages= 23395-8 |year= 1994 |pmid= 8089102 |doi= }}
*{{cite journal | author=Seeliger MW, Biesalski HK, Wissinger B, ''et al.'' |title=Phenotype in retinol deficiency due to a hereditary defect in retinol binding protein synthesis. |journal=Invest. Ophthalmol. Vis. Sci. |volume=40 |issue= 1 |pages= 3-11 |year= 1999 |pmid= 9888420 |doi= }}
*{{cite journal | author=Naylor HM, Newcomer ME |title=The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP. |journal=Biochemistry |volume=38 |issue= 9 |pages= 2647-53 |year= 1999 |pmid= 10052934 |doi= 10.1021/bi982291i }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on S100A10... {November 17, 2007 10:46:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:47:07 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_S100A10_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a4p.
| PDB = {{PDB2|1a4p}}, {{PDB2|1bt6}}
| Name = S100 calcium binding protein A10
| HGNCid = 10487
| Symbol = S100A10
| AltSymbols =; 42C; ANX2L; ANX2LG; CAL1L; CLP11; Ca[1]; GP11; MGC111133; P11; p10
| OMIM = 114085
| ECnumber =
| Homologene = 2228
| MGIid = 1339468
| GeneAtlas_image1 = PBB_GE_S100A10_200872_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6281
| Hs_Ensembl = ENSG00000197747
| Hs_RefseqProtein = NP_002957
| Hs_RefseqmRNA = NM_002966
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 150222015
| Hs_GenLoc_end = 150233490
| Hs_Uniprot = P60903
| Mm_EntrezGene = 20194
| Mm_Ensembl = ENSMUSG00000041959
| Mm_RefseqmRNA = NM_009112
| Mm_RefseqProtein = NP_033138
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 93640568
| Mm_GenLoc_end = 93650047
| Mm_Uniprot = Q3TC45
}}
}}
'''S100 calcium binding protein A10''', also known as '''S100A10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: S100A10 S100 calcium binding protein A10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6281| 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 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in exocytosis and endocytosis.<ref name="entrez">{{cite web | title = Entrez Gene: S100A10 S100 calcium binding protein A10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6281| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schäfer BW, Heizmann CW |title=The S100 family of EF-hand calcium-binding proteins: functions and pathology. |journal=Trends Biochem. Sci. |volume=21 |issue= 4 |pages= 134-40 |year= 1996 |pmid= 8701470 |doi= }}
*{{cite journal | author=Kwon M, MacLeod TJ, Zhang Y, Waisman DM |title=S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors. |journal=Front. Biosci. |volume=10 |issue= |pages= 300-25 |year= 2006 |pmid= 15574370 |doi= }}
*{{cite journal | author=Dooley TP, Weiland KL, Simon M |title=cDNA sequence of human p11 calpactin I light chain. |journal=Genomics |volume=13 |issue= 3 |pages= 866-8 |year= 1992 |pmid= 1386341 |doi= }}
*{{cite journal | author=Creutz CE, Moss S, Edwardson JM, ''et al.'' |title=Differential recognition of secretory vesicles by annexins. European Molecular Biology Organization Course "Advanced Techniques for Studying Secretion". |journal=Biochem. Biophys. Res. Commun. |volume=184 |issue= 1 |pages= 347-52 |year= 1992 |pmid= 1533123 |doi= }}
*{{cite journal | author=Harder T, Kube E, Gerke V |title=Cloning and characterization of the human gene encoding p11: structural similarity to other members of the S-100 gene family. |journal=Gene |volume=113 |issue= 2 |pages= 269-74 |year= 1992 |pmid= 1533380 |doi= }}
*{{cite journal | author=Kube E, Weber K, Gerke V |title=Primary structure of human, chicken, and Xenopus laevis p11, a cellular ligand of the Src-kinase substrate, annexin II. |journal=Gene |volume=102 |issue= 2 |pages= 255-9 |year= 1991 |pmid= 1831433 |doi= }}
*{{cite journal | author=Becker T, Weber K, Johnsson N |title=Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11. |journal=EMBO J. |volume=9 |issue= 13 |pages= 4207-13 |year= 1991 |pmid= 2148288 |doi= }}
*{{cite journal | author=Schäfer BW, Wicki R, Engelkamp D, ''et al.'' |title=Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family. |journal=Genomics |volume=25 |issue= 3 |pages= 638-43 |year= 1995 |pmid= 7759097 |doi= }}
*{{cite journal | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi= }}
*{{cite journal | author=Volz A, Korge BP, Compton JG, ''et al.'' |title=Physical mapping of a functional cluster of epidermal differentiation genes on chromosome 1q21. |journal=Genomics |volume=18 |issue= 1 |pages= 92-9 |year= 1994 |pmid= 8276421 |doi= 10.1006/geno.1993.1430 }}
*{{cite journal | author=Engelkamp D, Schäfer BW, Mattei MG, ''et al.'' |title=Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6547-51 |year= 1993 |pmid= 8341667 |doi= }}
*{{cite journal | author=Jost M, Gerke V |title=Mapping of a regulatory important site for protein kinase C phosphorylation in the N-terminal domain of annexin II. |journal=Biochim. Biophys. Acta |volume=1313 |issue= 3 |pages= 283-9 |year= 1996 |pmid= 8898866 |doi= }}
*{{cite journal | author=Munz B, Gerke V, Gillitzer R, Werner S |title=Differential expression of the calpactin I subunits annexin II and p11 in cultured keratinocytes and during wound repair. |journal=J. Invest. Dermatol. |volume=108 |issue= 3 |pages= 307-12 |year= 1997 |pmid= 9036930 |doi= }}
*{{cite journal | author=Kang HM, Kassam G, Jarvis SE, ''et al.'' |title=Characterization of human recombinant annexin II tetramer purified from bacteria: role of N-terminal acetylation. |journal=Biochemistry |volume=36 |issue= 8 |pages= 2041-50 |year= 1997 |pmid= 9047302 |doi= 10.1021/bi962569b }}
*{{cite journal | author=Wu T, Angus CW, Yao XL, ''et al.'' |title=P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2. |journal=J. Biol. Chem. |volume=272 |issue= 27 |pages= 17145-53 |year= 1997 |pmid= 9202034 |doi= }}
*{{cite journal | author=Hsu SY, Kaipia A, Zhu L, Hsueh AJ |title=Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11. |journal=Mol. Endocrinol. |volume=11 |issue= 12 |pages= 1858-67 |year= 1997 |pmid= 9369453 |doi= }}
*{{cite journal | author=Réty S, Sopkova J, Renouard M, ''et al.'' |title=The crystal structure of a complex of p11 with the annexin II N-terminal peptide. |journal=Nat. Struct. Biol. |volume=6 |issue= 1 |pages= 89-95 |year= 1999 |pmid= 9886297 |doi= 10.1038/4965 }}
*{{cite journal | author=Ramalingam R, Rafii S, Worgall S, ''et al.'' |title=Induction of endogenous genes following infection of human endothelial cells with an E1(-) E4(+) adenovirus gene transfer vector. |journal=J. Virol. |volume=73 |issue= 12 |pages= 10183-90 |year= 1999 |pmid= 10559334 |doi= }}
*{{cite journal | author=Mai J, Finley RL, Waisman DM, Sloane BF |title=Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12806-12 |year= 2000 |pmid= 10777578 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SCNN1A... {November 17, 2007 10:47:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:47:41 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 = Sodium channel, nonvoltage-gated 1 alpha
| HGNCid = 10599
| Symbol = SCNN1A
| AltSymbols =; ENaCa; ENaCalpha; FLJ21883; SCNEA; SCNN1
| OMIM = 600228
| ECnumber =
| Homologene = 811
| MGIid = 101782
| GeneAtlas_image1 = PBB_GE_SCNN1A_203453_at_tn.png
| GeneAtlas_image2 = PBB_GE_SCNN1A_215026_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015280 |text = amiloride-sensitive sodium channel activity}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}} {{GNF_GO|id=GO:0007588 |text = excretion}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6337
| Hs_Ensembl = ENSG00000111319
| Hs_RefseqProtein = NP_001029
| Hs_RefseqmRNA = NM_001038
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 6326276
| Hs_GenLoc_end = 6354976
| Hs_Uniprot = P37088
| Mm_EntrezGene = 20276
| Mm_Ensembl = ENSMUSG00000030340
| Mm_RefseqmRNA = XM_982260
| Mm_RefseqProtein = XP_987354
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 125287329
| Mm_GenLoc_end = 125310559
| Mm_Uniprot = Q3USG4
}}
}}
'''Sodium channel, nonvoltage-gated 1 alpha''', also known as '''SCNN1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SCNN1A sodium channel, nonvoltage-gated 1 alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6337| 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=Edelheit O, Hanukoglu I, Gizewska M, ''et al.'' |title=Novel mutations in epithelial sodium channel (ENaC) subunit genes and phenotypic expression of multisystem pseudohypoaldosteronism. |journal=Clin. Endocrinol. (Oxf) |volume=62 |issue= 5 |pages= 547-53 |year= 2005 |pmid= 15853823 |doi= 10.1111/j.1365-2265.2005.02255.x }}
*{{cite journal | author=Meisler MH, Barrow LL, Canessa CM, Rossier BC |title=SCNN1, an epithelial cell sodium channel gene in the conserved linkage group on mouse chromosome 6 and human chromosome 12. |journal=Genomics |volume=24 |issue= 1 |pages= 185-6 |year= 1995 |pmid= 7896277 |doi= 10.1006/geno.1994.1599 }}
*{{cite journal | author=McDonald FJ, Snyder PM, McCray PB, Welsh MJ |title=Cloning, expression, and tissue distribution of a human amiloride-sensitive Na+ channel. |journal=Am. J. Physiol. |volume=266 |issue= 6 Pt 1 |pages= L728-34 |year= 1994 |pmid= 8023962 |doi= }}
*{{cite journal | author=Voilley N, Lingueglia E, Champigny G, ''et al.'' |title=The lung amiloride-sensitive Na+ channel: biophysical properties, pharmacology, ontogenesis, and molecular cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 1 |pages= 247-51 |year= 1994 |pmid= 8278374 |doi= }}
*{{cite journal | author=Chang SS, Grunder S, Hanukoglu A, ''et al.'' |title=Mutations in subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1. |journal=Nat. Genet. |volume=12 |issue= 3 |pages= 248-53 |year= 1996 |pmid= 8589714 |doi= 10.1038/ng0396-248 }}
*{{cite journal | author=Firsov D, Schild L, Gautschi I, ''et al.'' |title=Cell surface expression of the epithelial Na channel and a mutant causing Liddle syndrome: a quantitative approach. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 26 |pages= 15370-5 |year= 1997 |pmid= 8986818 |doi= }}
*{{cite journal | author=Pirozzi G, McConnell SJ, Uveges AJ, ''et al.'' |title=Identification of novel human WW domain-containing proteins by cloning of ligand targets. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14611-6 |year= 1997 |pmid= 9169421 |doi= }}
*{{cite journal | author=Tucker JK, Tamba K, Lee YJ, ''et al.'' |title=Cloning and functional studies of splice variants of the alpha-subunit of the amiloride-sensitive Na+ channel. |journal=Am. J. Physiol. |volume=274 |issue= 4 Pt 1 |pages= C1081-9 |year= 1998 |pmid= 9575806 |doi= }}
*{{cite journal | author=Thomas CP, Auerbach S, Stokes JB, Volk KA |title=5' heterogeneity in epithelial sodium channel alpha-subunit mRNA leads to distinct NH2-terminal variant proteins. |journal=Am. J. Physiol. |volume=274 |issue= 5 Pt 1 |pages= C1312-23 |year= 1998 |pmid= 9612219 |doi= }}
*{{cite journal | author=Ludwig M, Bolkenius U, Wickert L, ''et al.'' |title=Structural organisation of the gene encoding the alpha-subunit of the human amiloride-sensitive epithelial sodium channel. |journal=Hum. Genet. |volume=102 |issue= 5 |pages= 576-81 |year= 1998 |pmid= 9654208 |doi= }}
*{{cite journal | author=Harvey KF, Dinudom A, Komwatana P, ''et al.'' |title=All three WW domains of murine Nedd4 are involved in the regulation of epithelial sodium channels by intracellular Na+. |journal=J. Biol. Chem. |volume=274 |issue= 18 |pages= 12525-30 |year= 1999 |pmid= 10212229 |doi= }}
*{{cite journal | author=Arai K, Zachman K, Shibasaki T, Chrousos GP |title=Polymorphisms of amiloride-sensitive sodium channel subunits in five sporadic cases of pseudohypoaldosteronism: do they have pathologic potential? |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 7 |pages= 2434-7 |year= 1999 |pmid= 10404817 |doi= }}
*{{cite journal | author=Saxena S, Quick MW, Tousson A, ''et al.'' |title=Interaction of syntaxins with the amiloride-sensitive epithelial sodium channel. |journal=J. Biol. Chem. |volume=274 |issue= 30 |pages= 20812-7 |year= 1999 |pmid= 10409621 |doi= }}
*{{cite journal | author=Chow YH, Wang Y, Plumb J, ''et al.'' |title=Hormonal regulation and genomic organization of the human amiloride-sensitive epithelial sodium channel alpha subunit gene. |journal=Pediatr. Res. |volume=46 |issue= 2 |pages= 208-14 |year= 1999 |pmid= 10447117 |doi= }}
*{{cite journal | author=Schaedel C, Marthinsen L, Kristoffersson AC, ''et al.'' |title=Lung symptoms in pseudohypoaldosteronism type 1 are associated with deficiency of the alpha-subunit of the epithelial sodium channel. |journal=J. Pediatr. |volume=135 |issue= 6 |pages= 739-45 |year= 1999 |pmid= 10586178 |doi= }}
*{{cite journal | author=Farr TJ, Coddington-Lawson SJ, Snyder PM, McDonald FJ |title=Human Nedd4 interacts with the human epithelial Na+ channel: WW3 but not WW1 binds to Na+-channel subunits. |journal=Biochem. J. |volume=345 Pt 3 |issue= |pages= 503-9 |year= 2000 |pmid= 10642508 |doi= }}
*{{cite journal | author=Harvey KF, Dinudom A, Cook DI, Kumar S |title=The Nedd4-like protein KIAA0439 is a potential regulator of the epithelial sodium channel. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 8597-601 |year= 2001 |pmid= 11244092 |doi= 10.1074/jbc.C000906200 }}
*{{cite journal | author=Mick VE, Itani OA, Loftus RW, ''et al.'' |title=The alpha-subunit of the epithelial sodium channel is an aldosterone-induced transcript in mammalian collecting ducts, and this transcriptional response is mediated via distinct cis-elements in the 5'-flanking region of the gene. |journal=Mol. Endocrinol. |volume=15 |issue= 4 |pages= 575-88 |year= 2001 |pmid= 11266509 |doi= }}
*{{cite journal | author=Snyder PM, Olson DR, McDonald FJ, Bucher DB |title=Multiple WW domains, but not the C2 domain, are required for inhibition of the epithelial Na+ channel by human Nedd4. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28321-6 |year= 2001 |pmid= 11359767 |doi= 10.1074/jbc.M011487200 }}
*{{cite journal | author=Snyder PM, Olson DR, Thomas BC |title=Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 5-8 |year= 2002 |pmid= 11696533 |doi= 10.1074/jbc.C100623200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SPRY2... {November 17, 2007 10:51:11 PM PST}
- SEARCH REDIRECT: Control Box Found: SPRY2 {November 17, 2007 10:51:39 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:51:43 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:51:43 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:51:43 PM PST}
- UPDATED: Updated protein page: SPRY2 {November 17, 2007 10:51:50 PM PST}
- INFO: Beginning work on STUB1... {November 17, 2007 10:51:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:53:15 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_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_STUB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2c2l.
| PDB = {{PDB2|2c2l}}, {{PDB2|2c2v}}
| Name = STIP1 homology and U-box containing protein 1
| HGNCid = 11427
| Symbol = STUB1
| AltSymbols =; CHIP; HSPABP2; NY-CO-7; SDCCAG7; UBOX1
| OMIM = 607207
| ECnumber =
| Homologene = 4281
| MGIid = 1891731
| GeneAtlas_image1 = PBB_GE_STUB1_217934_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0030544 |text = Hsp70 protein binding}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0046332 |text = SMAD binding}} {{GNF_GO|id=GO:0051879 |text = Hsp90 protein binding}}
| Component = {{GNF_GO|id=GO:0000151 |text = ubiquitin ligase complex}} {{GNF_GO|id=GO:0031371 |text = ubiquitin conjugating enzyme complex}}
| Process = {{GNF_GO|id=GO:0000209 |text = protein polyubiquitination}} {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0030579 |text = ubiquitin-dependent SMAD protein catabolic process}} {{GNF_GO|id=GO:0043161 |text = proteasomal ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0051604 |text = protein maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10273
| Hs_Ensembl = ENSG00000103266
| Hs_RefseqProtein = NP_005852
| Hs_RefseqmRNA = NM_005861
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 670116
| Hs_GenLoc_end = 672768
| Hs_Uniprot = Q9UNE7
| Mm_EntrezGene = 56424
| Mm_Ensembl = ENSMUSG00000039615
| Mm_RefseqmRNA = NM_019719
| Mm_RefseqProtein = NP_062693
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 25558234
| Mm_GenLoc_end = 25560961
| Mm_Uniprot = Q3TYJ0
}}
}}
'''STIP1 homology and U-box containing protein 1''', also known as '''STUB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: STUB1 STIP1 homology and U-box containing protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10273| 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=Patterson C |title=A new gun in town: the U box is a ubiquitin ligase domain. |journal=Sci. STKE |volume=2002 |issue= 116 |pages= PE4 |year= 2002 |pmid= 11805346 |doi= 10.1126/stke.2002.116.pe4 }}
*{{cite journal | author=Scanlan MJ, Chen YT, Williamson B, ''et al.'' |title=Characterization of human colon cancer antigens recognized by autologous antibodies. |journal=Int. J. Cancer |volume=76 |issue= 5 |pages= 652-8 |year= 1998 |pmid= 9610721 |doi= }}
*{{cite journal | author=Ballinger CA, Connell P, Wu Y, ''et al.'' |title=Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. |journal=Mol. Cell. Biol. |volume=19 |issue= 6 |pages= 4535-45 |year= 1999 |pmid= 10330192 |doi= }}
*{{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=Daniels RJ, Peden JF, Lloyd C, ''et al.'' |title=Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. |journal=Hum. Mol. Genet. |volume=10 |issue= 4 |pages= 339-52 |year= 2001 |pmid= 11157797 |doi= }}
*{{cite journal | author=Jiang J, Ballinger CA, Wu Y, ''et al.'' |title=CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. |journal=J. Biol. Chem. |volume=276 |issue= 46 |pages= 42938-44 |year= 2001 |pmid= 11557750 |doi= 10.1074/jbc.M101968200 }}
*{{cite journal | author=Demand J, Alberti S, Patterson C, Höhfeld J |title=Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. |journal=Curr. Biol. |volume=11 |issue= 20 |pages= 1569-77 |year= 2002 |pmid= 11676916 |doi= }}
*{{cite journal | author=Imai Y, Soda M, Hatakeyama S, ''et al.'' |title=CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. |journal=Mol. Cell |volume=10 |issue= 1 |pages= 55-67 |year= 2002 |pmid= 12150907 |doi= }}
*{{cite journal | author=Krackhardt AM, Witzens M, Harig S, ''et al.'' |title=Identification of tumor-associated antigens in chronic lymphocytic leukemia by SEREX. |journal=Blood |volume=100 |issue= 6 |pages= 2123-31 |year= 2002 |pmid= 12200376 |doi= 10.1182/blood-2002-02-0513 }}
*{{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=Cardozo CP, Michaud C, Ost MC, ''et al.'' |title=C-terminal Hsp-interacting protein slows androgen receptor synthesis and reduces its rate of degradation. |journal=Arch. Biochem. Biophys. |volume=410 |issue= 1 |pages= 134-40 |year= 2003 |pmid= 12559985 |doi= }}
*{{cite journal | author=Zhou P, Fernandes N, Dodge IL, ''et al.'' |title=ErbB2 degradation mediated by the co-chaperone protein CHIP. |journal=J. Biol. Chem. |volume=278 |issue= 16 |pages= 13829-37 |year= 2003 |pmid= 12574167 |doi= 10.1074/jbc.M209640200 }}
*{{cite journal | author=Shimura H, Schwartz D, Gygi SP, Kosik KS |title=CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. |journal=J. Biol. Chem. |volume=279 |issue= 6 |pages= 4869-76 |year= 2004 |pmid= 14612456 |doi= 10.1074/jbc.M305838200 }}
*{{cite journal | author=Li L, Xin H, Xu X, ''et al.'' |title=CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription. |journal=Mol. Cell. Biol. |volume=24 |issue= 2 |pages= 856-64 |year= 2004 |pmid= 14701756 |doi= }}
*{{cite journal | author=Petrucelli L, Dickson D, Kehoe K, ''et al.'' |title=CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. |journal=Hum. Mol. Genet. |volume=13 |issue= 7 |pages= 703-14 |year= 2004 |pmid= 14962978 |doi= 10.1093/hmg/ddh083 }}
*{{cite journal | author=Galigniana MD, Harrell JM, Housley PR, ''et al.'' |title=Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation. |journal=Brain Res. Mol. Brain Res. |volume=123 |issue= 1-2 |pages= 27-36 |year= 2004 |pmid= 15046863 |doi= 10.1016/j.molbrainres.2003.12.015 }}
*{{cite journal | author=He B, Bai S, Hnat AT, ''et al.'' |title=An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP). |journal=J. Biol. Chem. |volume=279 |issue= 29 |pages= 30643-53 |year= 2004 |pmid= 15107424 |doi= 10.1074/jbc.M403117200 }}
*{{cite journal | author=Alberti S, Böhse K, Arndt V, ''et al.'' |title=The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. |journal=Mol. Biol. Cell |volume=15 |issue= 9 |pages= 4003-10 |year= 2005 |pmid= 15215316 |doi= 10.1091/mbc.E04-04-0293 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNFSF13... {November 17, 2007 10:49:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:50:00 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 = Tumor necrosis factor (ligand) superfamily, member 13
| HGNCid = 11928
| Symbol = TNFSF13
| AltSymbols =; APRIL; CD256; TALL2; TRDL-1; UNQ383/PRO715; ligand
| OMIM = 604472
| ECnumber =
| Homologene = 56971
| MGIid = 1916833
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005164 |text = tumor necrosis factor receptor binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0048298 |text = positive regulation of isotype switching to IgA isotypes}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8741
| Hs_Ensembl =
| Hs_RefseqProtein = NP_003799
| Hs_RefseqmRNA = NM_003808
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 69583
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_023517
| Mm_RefseqProtein = NP_076006
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Tumor necrosis factor (ligand) superfamily, member 13''', also known as '''TNFSF13''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNFSF13 tumor necrosis factor (ligand) superfamily, member 13| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8741| 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 is a member of the tumor necrosis factor (TNF) ligand family. This protein is a ligand for TNFRSF17/BCMA, a member of the TNF receptor family. This protein and its receptor are both found to be important for B cell development. In vitro experiments suggested that this protein may be able to induce apoptosis through its interaction with other TNF receptor family proteins such as TNFRSF6/FAS and TNFRSF14/HVEM. Three alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: TNFSF13 tumor necrosis factor (ligand) superfamily, member 13| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8741| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bossen C, Schneider P |title=BAFF, APRIL and their receptors: structure, function and signaling. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 263-75 |year= 2007 |pmid= 16914324 |doi= 10.1016/j.smim.2006.04.006 }}
*{{cite journal | author=Tangye SG, Bryant VL, Cuss AK, Good KL |title=BAFF, APRIL and human B cell disorders. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 305-17 |year= 2007 |pmid= 16916610 |doi= 10.1016/j.smim.2006.04.004 }}
*{{cite journal | author=Treml LS, Crowley JE, Cancro MP |title=BLyS receptor signatures resolve homeostatically independent compartments among naïve and antigen-experienced B cells. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 297-304 |year= 2007 |pmid= 16919470 |doi= 10.1016/j.smim.2006.07.001 }}
*{{cite journal | author=Mackay F, Leung H |title=The role of the BAFF/APRIL system on T cell function. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 284-9 |year= 2007 |pmid= 16931039 |doi= 10.1016/j.smim.2006.04.005 }}
*{{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=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=Hahne M, Kataoka T, Schröter M, ''et al.'' |title=APRIL, a new ligand of the tumor necrosis factor family, stimulates tumor cell growth. |journal=J. Exp. Med. |volume=188 |issue= 6 |pages= 1185-90 |year= 1998 |pmid= 9743536 |doi= }}
*{{cite journal | author=Shu HB, Hu WH, Johnson H |title=TALL-1 is a novel member of the TNF family that is down-regulated by mitogens. |journal=J. Leukoc. Biol. |volume=65 |issue= 5 |pages= 680-3 |year= 1999 |pmid= 10331498 |doi= }}
*{{cite journal | author=Cousin P, Billotte J, Chaubert P, Shaw P |title=Physical map of 17p13 and the genes adjacent to p53. |journal=Genomics |volume=63 |issue= 1 |pages= 60-8 |year= 2000 |pmid= 10662545 |doi= 10.1006/geno.1999.6062 }}
*{{cite journal | author=Kelly K, Manos E, Jensen G, ''et al.'' |title=APRIL/TRDL-1, a tumor necrosis factor-like ligand, stimulates cell death. |journal=Cancer Res. |volume=60 |issue= 4 |pages= 1021-7 |year= 2000 |pmid= 10706119 |doi= }}
*{{cite journal | author=Wu Y, Bressette D, Carrell JA, ''et al.'' |title=Tumor necrosis factor (TNF) receptor superfamily member TACI is a high affinity receptor for TNF family members APRIL and BLyS. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 35478-85 |year= 2001 |pmid= 10956646 |doi= 10.1074/jbc.M005224200 }}
*{{cite journal | author=Yu G, Boone T, Delaney J, ''et al.'' |title=APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity. |journal=Nat. Immunol. |volume=1 |issue= 3 |pages= 252-6 |year= 2001 |pmid= 10973284 |doi= 10.1038/79802 }}
*{{cite journal | author=Gallouzi IE, Brennan CM, Steitz JA |title=Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock. |journal=RNA |volume=7 |issue= 9 |pages= 1348-61 |year= 2001 |pmid= 11565755 |doi= }}
*{{cite journal | author=López-Fraga M, Fernández R, Albar JP, Hahne M |title=Biologically active APRIL is secreted following intracellular processing in the Golgi apparatus by furin convertase. |journal=EMBO Rep. |volume=2 |issue= 10 |pages= 945-51 |year= 2002 |pmid= 11571266 |doi= 10.1093/embo-reports/kve198 }}
*{{cite journal | author=Stein JV, López-Fraga M, Elustondo FA, ''et al.'' |title=APRIL modulates B and T cell immunity. |journal=J. Clin. Invest. |volume=109 |issue= 12 |pages= 1587-98 |year= 2002 |pmid= 12070306 |doi= }}
*{{cite journal | author=Litinskiy MB, Nardelli B, Hilbert DM, ''et al.'' |title=DCs induce CD40-independent immunoglobulin class switching through BLyS and APRIL. |journal=Nat. Immunol. |volume=3 |issue= 9 |pages= 822-9 |year= 2002 |pmid= 12154359 |doi= 10.1038/ni829 }}
*{{cite journal | author=Roschke V, Sosnovtseva S, Ward CD, ''et al.'' |title=BLyS and APRIL form biologically active heterotrimers that are expressed in patients with systemic immune-based rheumatic diseases. |journal=J. Immunol. |volume=169 |issue= 8 |pages= 4314-21 |year= 2002 |pmid= 12370363 |doi= }}
*{{cite journal | author=Pradet-Balade B, Medema JP, López-Fraga M, ''et al.'' |title=An endogenous hybrid mRNA encodes TWE-PRIL, a functional cell surface TWEAK-APRIL fusion protein. |journal=EMBO J. |volume=21 |issue= 21 |pages= 5711-20 |year= 2002 |pmid= 12411489 |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=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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TRIM28... {November 17, 2007 10:50:29 PM PST}
- SEARCH REDIRECT: Control Box Found: TRIM28 {November 17, 2007 10:51:02 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:51:05 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:51:05 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:51:05 PM PST}
- UPDATED: Updated protein page: TRIM28 {November 17, 2007 10:51:11 PM PST}
- INFO: Beginning work on XRCC4... {November 17, 2007 10:48:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:48:49 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_XRCC4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fu1.
| PDB = {{PDB2|1fu1}}, {{PDB2|1ik9}}
| Name = X-ray repair complementing defective repair in Chinese hamster cells 4
| HGNCid = 12831
| Symbol = XRCC4
| AltSymbols =;
| OMIM = 194363
| ECnumber =
| Homologene = 2555
| MGIid = 1333799
| GeneAtlas_image1 = PBB_GE_XRCC4_205072_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_XRCC4_205071_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_XRCC4_210813_s_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:0006303 |text = double-strand break repair via nonhomologous end joining}} {{GNF_GO|id=GO:0006310 |text = DNA recombination}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7518
| Hs_Ensembl = ENSG00000152422
| Hs_RefseqProtein = NP_003392
| Hs_RefseqmRNA = NM_003401
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 82409073
| Hs_GenLoc_end = 82685333
| Hs_Uniprot = Q13426
| Mm_EntrezGene = 108138
| Mm_Ensembl = ENSMUSG00000021615
| Mm_RefseqmRNA = NM_028012
| Mm_RefseqProtein = NP_082288
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 90323160
| Mm_GenLoc_end = 90563768
| Mm_Uniprot = Q924T3
}}
}}
'''X-ray repair complementing defective repair in Chinese hamster cells 4''', also known as '''XRCC4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: XRCC4 X-ray repair complementing defective repair in Chinese hamster cells 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7518| 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 functions together with DNA ligase IV and the DNA-dependent protein kinase in the repair of DNA double-strand break by non-homologous end joining and the completion of V(D)J recombination events. The non-homologous end-joining pathway is required both for normal development and for suppression of tumors. This gene functionally complements XR-1 Chinese hamster ovary cell mutant, which is impaired in DNA double-strand breaks produced by ionizing radiation and restriction enzymes. This gene contains 8 exons, and alternative transcription initiation and alternative splicing generates several transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: XRCC4 X-ray repair complementing defective repair in Chinese hamster cells 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7518| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lieber MR |title=The biochemistry and biological significance of nonhomologous DNA end joining: an essential repair process in multicellular eukaryotes. |journal=Genes Cells |volume=4 |issue= 2 |pages= 77-85 |year= 1999 |pmid= 10320474 |doi= }}
*{{cite journal | author=Giaccia AJ, Denko N, MacLaren R, ''et al.'' |title=Human chromosome 5 complements the DNA double-strand break-repair deficiency and gamma-ray sensitivity of the XR-1 hamster variant. |journal=Am. J. Hum. Genet. |volume=47 |issue= 3 |pages= 459-69 |year= 1990 |pmid= 1697445 |doi= }}
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}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on YWHAG... {November 17, 2007 10:48:49 PM PST}
- SEARCH REDIRECT: Control Box Found: YWHAG {November 17, 2007 10:49:23 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:49:24 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:49:24 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:49:24 PM PST}
- UPDATED: Updated protein page: YWHAG {November 17, 2007 10:49:30 PM PST}
end log.
