- INFO: Beginning work on AGTR2... {November 16, 2007 1:15:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:15:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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 = Angiotensin II receptor, type 2
| HGNCid = 338
| Symbol = AGTR2
| AltSymbols =; AT2; ATGR2; MRX88
| OMIM = 300034
| ECnumber =
| Homologene = 20172
| MGIid = 87966
| GeneAtlas_image1 = PBB_GE_AGTR2_207294_at_tn.png
| GeneAtlas_image2 = PBB_GE_AGTR2_207293_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_AGTR2_222321_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004860 |text = protein kinase inhibitor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004945 |text = angiotensin type II receptor activity}} {{GNF_GO|id=GO:0004947 |text = bradykinin receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0002033 |text = angiotensin mediated vasodilation during regulation of blood pressure}} {{GNF_GO|id=GO:0002035 |text = brain renin-angiotensin system}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007610 |text = behavior}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 186
| Hs_Ensembl = ENSG00000180772
| Hs_RefseqProtein = NP_000677
| Hs_RefseqmRNA = NM_000686
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 115216003
| Hs_GenLoc_end = 115220253
| Hs_Uniprot = P50052
| Mm_EntrezGene = 11609
| Mm_Ensembl = ENSMUSG00000068122
| Mm_RefseqmRNA = NM_007429
| Mm_RefseqProtein = NP_031455
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 20641585
| Mm_GenLoc_end = 20646123
| Mm_Uniprot = Q3US12
}}
}}
'''Angiotensin II receptor, type 2''', also known as '''AGTR2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AGTR2 angiotensin II receptor, type 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=186| 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 = Angiotensin II is a potent pressor hormone and a primary regulator of aldosterone secretion. It is an important effector controlling blood pressure and volume in the cardiovascular system. It acts through at least two types of receptors termed AT1 and AT2. AGTR2 belongs to a family 1 of G-protein coupled receptors. It is an intergral membrane protein. It plays a role in the central nervous system and cardiovascular functions that are mediated by the renin-angiotensin system. This receptor mediates programmed cell death (apoptosis). In adults, it is highly expressed in myometrium with lower levels in adrenal gland and fallopian tube. It is highly expressed in fetal kidney and intestine. The human AGTR2 gene is composed of three exons and spans at least 5 kb. Exons 1 and 2 encode for 5' untranslated mRNA sequence and exon 3 harbors the entire uninterrupted open reading frame.<ref name="entrez">{{cite web | title = Entrez Gene: AGTR2 angiotensin II receptor, type 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=186| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Regitz-Zagrosek V, Neuss M, Warnecke C, ''et al.'' |title=Subtype 2 and atypical angiotensin receptors in the human heart. |journal=Basic Res. Cardiol. |volume=91 Suppl 2 |issue= |pages= 73-7 |year= 1997 |pmid= 8957548 |doi= }}
*{{cite journal | author=Berry C, Touyz R, Dominiczak AF, ''et al.'' |title=Angiotensin receptors: signaling, vascular pathophysiology, and interactions with ceramide. |journal=Am. J. Physiol. Heart Circ. Physiol. |volume=281 |issue= 6 |pages= H2337-65 |year= 2002 |pmid= 11709400 |doi= }}
*{{cite journal | author=Takayanagi R, Ohnaka K, Sakai Y, ''et al.'' |title=Molecular cloning, sequence analysis and expression of a cDNA encoding human type-1 angiotensin II receptor. |journal=Biochem. Biophys. Res. Commun. |volume=183 |issue= 2 |pages= 910-6 |year= 1992 |pmid= 1550596 |doi= }}
*{{cite journal | author=Hein L, Barsh GS, Pratt RE, ''et al.'' |title=Behavioural and cardiovascular effects of disrupting the angiotensin II type-2 receptor in mice. |journal=Nature |volume=377 |issue= 6551 |pages= 744-7 |year= 1995 |pmid= 7477266 |doi= 10.1038/377744a0 }}
*{{cite journal | author=Ichiki T, Labosky PA, Shiota C, ''et al.'' |title=Effects on blood pressure and exploratory behaviour of mice lacking angiotensin II type-2 receptor. |journal=Nature |volume=377 |issue= 6551 |pages= 748-50 |year= 1995 |pmid= 7477267 |doi= 10.1038/377748a0 }}
*{{cite journal | author=Lazard D, Briend-Sutren MM, Villageois P, ''et al.'' |title=Molecular characterization and chromosome localization of a human angiotensin II AT2 receptor gene highly expressed in fetal tissues. |journal=Recept. Channels |volume=2 |issue= 4 |pages= 271-80 |year= 1995 |pmid= 7719706 |doi= }}
*{{cite journal | author=Martin MM, Elton TS |title=The sequence and genomic organization of the human type 2 angiotensin II receptor. |journal=Biochem. Biophys. Res. Commun. |volume=209 |issue= 2 |pages= 554-62 |year= 1995 |pmid= 7733925 |doi= 10.1006/bbrc.1995.1537 }}
*{{cite journal | author=Chassagne C, Beatty BG, Meloche S |title=Assignment of the human angiotensin II type 2 receptor gene (AGTR2) to chromosome Xq22-q23 by fluorescence in situ hybridization. |journal=Genomics |volume=25 |issue= 2 |pages= 601-3 |year= 1995 |pmid= 7790004 |doi= }}
*{{cite journal | author=Koike G, Horiuchi M, Yamada T, ''et al.'' |title=Human type 2 angiotensin II receptor gene: cloned, mapped to the X chromosome, and its mRNA is expressed in the human lung. |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 3 |pages= 1842-50 |year= 1994 |pmid= 7945336 |doi= 10.1006/bbrc.1994.2402 }}
*{{cite journal | author=Martin MM, Su B, Elton TS |title=Molecular cloning of the human angiotensin II type 2 receptor cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 1 |pages= 645-51 |year= 1995 |pmid= 7999093 |doi= }}
*{{cite journal | author=Tsuzuki S, Ichiki T, Nakakubo H, ''et al.'' |title=Molecular cloning and expression of the gene encoding human angiotensin II type 2 receptor. |journal=Biochem. Biophys. Res. Commun. |volume=200 |issue= 3 |pages= 1449-54 |year= 1994 |pmid= 8185599 |doi= 10.1006/bbrc.1994.1613 }}
*{{cite journal | author=Servant G, Boulay G, Bossé R, ''et al.'' |title=Photoaffinity labeling of subtype 2 angiotensin receptor of human myometrium. |journal=Mol. Pharmacol. |volume=43 |issue= 5 |pages= 677-83 |year= 1993 |pmid= 8502225 |doi= }}
*{{cite journal | author=Yamada T, Horiuchi M, Dzau VJ |title=Angiotensin II type 2 receptor mediates programmed cell death. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 156-60 |year= 1996 |pmid= 8552595 |doi= }}
*{{cite journal | author=Zhang J, Pratt RE |title=The AT2 receptor selectively associates with Gialpha2 and Gialpha3 in the rat fetus. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 15026-33 |year= 1996 |pmid= 8663053 |doi= }}
*{{cite journal | author=Katsuya T, Horiuchi M, Minami S, ''et al.'' |title=Genomic organization and polymorphism of human angiotensin II type 2 receptor: no evidence for its gene mutation in two families of human premature ovarian failure syndrome. |journal=Mol. Cell. Endocrinol. |volume=127 |issue= 2 |pages= 221-8 |year= 1997 |pmid= 9099917 |doi= }}
*{{cite journal | author=Akishita M, Ito M, Lehtonen JY, ''et al.'' |title=Expression of the AT2 receptor developmentally programs extracellular signal-regulated kinase activity and influences fetal vascular growth. |journal=J. Clin. Invest. |volume=103 |issue= 1 |pages= 63-71 |year= 1999 |pmid= 9884335 |doi= }}
*{{cite journal | author=Lehtonen JY, Daviet L, Nahmias C, ''et al.'' |title=Analysis of functional domains of angiotensin II type 2 receptor involved in apoptosis. |journal=Mol. Endocrinol. |volume=13 |issue= 7 |pages= 1051-60 |year= 1999 |pmid= 10406457 |doi= }}
*{{cite journal | author=Knowle D, Ahmed S, Pulakat L |title=Identification of an interaction between the angiotensin II receptor sub-type AT2 and the ErbB3 receptor, a member of the epidermal growth factor receptor family. |journal=Regul. Pept. |volume=87 |issue= 1-3 |pages= 73-82 |year= 2000 |pmid= 10710290 |doi= }}
*{{cite journal | author=Hansen JL, Servant G, Baranski TJ, ''et al.'' |title=Functional reconstitution of the angiotensin II type 2 receptor and G(i) activation. |journal=Circ. Res. |volume=87 |issue= 9 |pages= 753-9 |year= 2000 |pmid= 11055978 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AKR1B1... {November 16, 2007 1:15:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:16:11 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_AKR1B1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1abn.
| PDB = {{PDB2|1abn}}, {{PDB2|1ads}}, {{PDB2|1az1}}, {{PDB2|1az2}}, {{PDB2|1ef3}}, {{PDB2|1el3}}, {{PDB2|1iei}}, {{PDB2|1mar}}, {{PDB2|1pwl}}, {{PDB2|1pwm}}, {{PDB2|1t40}}, {{PDB2|1t41}}, {{PDB2|1us0}}, {{PDB2|1x96}}, {{PDB2|1x97}}, {{PDB2|1x98}}, {{PDB2|1xgd}}, {{PDB2|1z3n}}, {{PDB2|1z89}}, {{PDB2|1z8a}}, {{PDB2|2acq}}, {{PDB2|2acr}}, {{PDB2|2acs}}, {{PDB2|2acu}}, {{PDB2|2agt}}, {{PDB2|2dux}}, {{PDB2|2duz}}, {{PDB2|2dv0}}, {{PDB2|2f2k}}, {{PDB2|2fz8}}, {{PDB2|2fz9}}, {{PDB2|2fzb}}, {{PDB2|2fzd}}, {{PDB2|2hv5}}, {{PDB2|2hvn}}, {{PDB2|2hvo}}, {{PDB2|2i16}}, {{PDB2|2i17}}, {{PDB2|2ikg}}, {{PDB2|2ikh}}, {{PDB2|2iki}}, {{PDB2|2ikj}}, {{PDB2|2ine}}, {{PDB2|2inz}}, {{PDB2|2ipw}}, {{PDB2|2iq0}}, {{PDB2|2iqd}}, {{PDB2|2is7}}, {{PDB2|2isf}}, {{PDB2|2j8t}}, {{PDB2|2nvc}}, {{PDB2|2nvd}}, {{PDB2|2pev}}, {{PDB2|2pf8}}, {{PDB2|2pfh}}
| Name = Aldo-keto reductase family 1, member B1 (aldose reductase)
| HGNCid = 381
| Symbol = AKR1B1
| AltSymbols =; ADR; ALDR1; AR; MGC1804
| OMIM = 103880
| ECnumber =
| Homologene = 68193
| MGIid = 1353494
| GeneAtlas_image1 = PBB_GE_AKR1B1_201272_at_tn.png
| Function = {{GNF_GO|id=GO:0004032 |text = aldehyde reductase activity}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006950 |text = response to stress}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 231
| Hs_Ensembl = ENSG00000085662
| Hs_RefseqProtein = NP_001619
| Hs_RefseqmRNA = NM_001628
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 133777649
| Hs_GenLoc_end = 133794428
| Hs_Uniprot = P15121
| Mm_EntrezGene = 11677
| Mm_Ensembl = ENSMUSG00000001642
| Mm_RefseqmRNA = NM_009658
| Mm_RefseqProtein = NP_033788
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 34234092
| Mm_GenLoc_end = 34247655
| Mm_Uniprot = Q3TCL2
}}
}}
'''Aldo-keto reductase family 1, member B1 (aldose reductase)''', also known as '''AKR1B1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AKR1B1 aldo-keto reductase family 1, member B1 (aldose reductase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=231| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member catalyzes the reduction of a number of aldehydes, including the aldehyde form of glucose, and is thereby implicated in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. There are a few putative pseudogenes for this gene, and one of them has been confirmed and mapped to chromosome 3.<ref name="entrez">{{cite web | title = Entrez Gene: AKR1B1 aldo-keto reductase family 1, member B1 (aldose reductase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=231| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Borhani DW, Harter TM, Petrash JM |title=The crystal structure of the aldose reductase.NADPH binary complex. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24841-7 |year= 1992 |pmid= 1447221 |doi= }}
*{{cite journal | author=Wilson DK, Bohren KM, Gabbay KH, Quiocho FA |title=An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. |journal=Science |volume=257 |issue= 5066 |pages= 81-4 |year= 1992 |pmid= 1621098 |doi= }}
*{{cite journal | author=Graham A, Heath P, Morten JE, Markham AF |title=The human aldose reductase gene maps to chromosome region 7q35. |journal=Hum. Genet. |volume=86 |issue= 5 |pages= 509-14 |year= 1991 |pmid= 1901827 |doi= }}
*{{cite journal | author=Graham A, Brown L, Hedge PJ, ''et al.'' |title=Structure of the human aldose reductase gene. |journal=J. Biol. Chem. |volume=266 |issue= 11 |pages= 6872-7 |year= 1991 |pmid= 1901857 |doi= }}
*{{cite journal | author=Grundmann U, Bohn H, Obermeier R, Amann E |title=Cloning and prokaryotic expression of a biologically active human placental aldose reductase. |journal=DNA Cell Biol. |volume=9 |issue= 3 |pages= 149-57 |year= 1990 |pmid= 2111143 |doi= }}
*{{cite journal | author=Nishimura C, Matsuura Y, Kokai Y, ''et al.'' |title=Cloning and expression of human aldose reductase. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 9788-92 |year= 1990 |pmid= 2112546 |doi= }}
*{{cite journal | author=Morjana NA, Lyons C, Flynn TG |title=Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. |journal=J. Biol. Chem. |volume=264 |issue= 5 |pages= 2912-9 |year= 1989 |pmid= 2492527 |doi= }}
*{{cite journal | author=Bohren KM, Bullock B, Wermuth B, Gabbay KH |title=The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. |journal=J. Biol. Chem. |volume=264 |issue= 16 |pages= 9547-51 |year= 1989 |pmid= 2498333 |doi= }}
*{{cite journal | author=Chung S, LaMendola J |title=Cloning and sequence determination of human placental aldose reductase gene. |journal=J. Biol. Chem. |volume=264 |issue= 25 |pages= 14775-7 |year= 1989 |pmid= 2504709 |doi= }}
*{{cite journal | author=Graham A, Hedge PJ, Powell SJ, ''et al.'' |title=Nucleotide sequence of cDNA for human aldose reductase. |journal=Nucleic Acids Res. |volume=17 |issue= 20 |pages= 8368 |year= 1989 |pmid= 2510130 |doi= }}
*{{cite journal | author=Akagi Y, Kador PF, Kuwabara T, Kinoshita JH |title=Aldose reductase localization in human retinal mural cells. |journal=Invest. Ophthalmol. Vis. Sci. |volume=24 |issue= 11 |pages= 1516-9 |year= 1984 |pmid= 6417042 |doi= }}
*{{cite journal | author=Ko BC, Lam KS, Wat NM, Chung SS |title=An (A-C)n dinucleotide repeat polymorphic marker at the 5' end of the aldose reductase gene is associated with early-onset diabetic retinopathy in NIDDM patients. |journal=Diabetes |volume=44 |issue= 7 |pages= 727-32 |year= 1995 |pmid= 7789640 |doi= }}
*{{cite journal | author=Wilson DK, Tarle I, Petrash JM, Quiocho FA |title=Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 21 |pages= 9847-51 |year= 1993 |pmid= 8234324 |doi= }}
*{{cite journal | author=Tarle I, Borhani DW, Wilson DK, ''et al.'' |title=Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. |journal=J. Biol. Chem. |volume=268 |issue= 34 |pages= 25687-93 |year= 1994 |pmid= 8245005 |doi= }}
*{{cite journal | author=Robinson B, Hunsaker LA, Stangebye LA, Vander Jagt DL |title=Aldose and aldehyde reductases from human kidney cortex and medulla. |journal=Biochim. Biophys. Acta |volume=1203 |issue= 2 |pages= 260-6 |year= 1994 |pmid= 8268209 |doi= }}
*{{cite journal | author=Jaquinod M, Potier N, Klarskov K, ''et al.'' |title=Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes. |journal=Eur. J. Biochem. |volume=218 |issue= 3 |pages= 893-903 |year= 1994 |pmid= 8281941 |doi= }}
*{{cite journal | author=Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK |title=Identification of the reactive cysteine residue in human placenta aldose reductase. |journal=Biochim. Biophys. Acta |volume=1164 |issue= 3 |pages= 268-72 |year= 1993 |pmid= 8343525 |doi= }}
*{{cite journal | author=Nishimura C, Furue M, Ito T, ''et al.'' |title=Quantitative determination of human aldose reductase by enzyme-linked immunosorbent assay. Immunoassay of human aldose reductase. |journal=Biochem. Pharmacol. |volume=46 |issue= 1 |pages= 21-8 |year= 1993 |pmid= 8347133 |doi= }}
*{{cite journal | author=Sato S, Lin LR, Reddy VN, Kador PF |title=Aldose reductase in human retinal pigment epithelial cells. |journal=Exp. Eye Res. |volume=57 |issue= 2 |pages= 235-41 |year= 1993 |pmid= 8405190 |doi= 10.1006/exer.1993.1119 }}
*{{cite journal | author=Ferraretto A, Negri A, Giuliani A, ''et al.'' |title=Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress. |journal=Biochim. Biophys. Acta |volume=1175 |issue= 3 |pages= 283-8 |year= 1993 |pmid= 8435445 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ALOX15... {November 16, 2007 1:16:11 PM PST}
- SEARCH REDIRECT: Control Box Found: ALOX15 {November 16, 2007 1:16:31 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:16:41 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:16:41 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:16:41 PM PST}
- UPDATED: Updated protein page: ALOX15 {November 16, 2007 1:16:48 PM PST}
- INFO: Beginning work on APOA4... {November 16, 2007 1:17:33 PM PST}
- SEARCH REDIRECT: Control Box Found: APOA4 {November 16, 2007 1:17:58 PM PST}
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- UPDATED: Updated protein page: APOA4 {November 16, 2007 1:18:06 PM PST}
- INFO: Beginning work on ATRX... {November 16, 2007 1:18:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:18:48 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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| 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 = Alpha thalassemia/mental retardation syndrome X-linked (RAD54 homolog, S. cerevisiae)
| HGNCid = 886
| Symbol = ATRX
| AltSymbols =; ATR2; MGC2094; MRXS3; RAD54; RAD54L; SHS; XH2; XNP; ZNF-HX
| OMIM = 300032
| ECnumber =
| Homologene = 416
| MGIid = 103067
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003678 |text = DNA helicase activity}} {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004386 |text = helicase activity}}
| Component = {{GNF_GO|id=GO:0000228 |text = nuclear chromosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005720 |text = nuclear heterochromatin}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006306 |text = DNA methylation}} {{GNF_GO|id=GO:0006310 |text = DNA recombination}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0030900 |text = forebrain development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 546
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000480
| Hs_RefseqmRNA = NM_000489
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 22589
| Mm_Ensembl = ENSMUSG00000031229
| Mm_RefseqmRNA = NM_009530
| Mm_RefseqProtein = NP_033556
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 102002894
| Mm_GenLoc_end = 102131271
| Mm_Uniprot = Q3TP53
}}
}}
'''Alpha thalassemia/mental retardation syndrome X-linked (RAD54 homolog, S. cerevisiae)''', also known as '''ATRX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATRX alpha thalassemia/mental retardation syndrome X-linked (RAD54 homolog, S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=546| 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 contains an ATPase/helicase domain, and thus it belongs to the SWI/SNF family of chromatin remodeling proteins. The mutations of this gene are associated with an X-linked mental retardation (XLMR) syndrome most often accompanied by alpha-thalassemia (ATRX) syndrome. These mutations have been shown to cause diverse changes in the pattern of DNA methylation, which may provide a link between chromatin remodeling, DNA methylation, and gene expression in developmental processes. This protein is found to undergo cell cycle-dependent phosphorylation, which regulates its nuclear matrix and chromatin association, and suggests its involvement in the gene regulation at interphase and chromosomal segregation in mitosis. Multiple alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: ATRX alpha thalassemia/mental retardation syndrome X-linked (RAD54 homolog, S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=546| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mulley JC, Kerr B, Stevenson R, Lubs H |title=Nomenclature guidelines for X-linked mental retardation. |journal=Am. J. Med. Genet. |volume=43 |issue= 1-2 |pages= 383-91 |year= 1992 |pmid= 1605216 |doi= }}
*{{cite journal | author=Tang P, Park DJ, Marshall Graves JA, Harley VR |title=ATRX and sex differentiation. |journal=Trends Endocrinol. Metab. |volume=15 |issue= 7 |pages= 339-44 |year= 2005 |pmid= 15350606 |doi= 10.1016/j.tem.2004.07.006 }}
*{{cite journal | author=Forget BG |title=De novo and acquired forms of alpha thalassemia. |journal=Curr. Hematol. Rep. |volume=5 |issue= 1 |pages= 11-4 |year= 2006 |pmid= 16537041 |doi= }}
*{{cite journal | author=Gibbons RJ, Suthers GK, Wilkie AO, ''et al.'' |title=X-linked alpha-thalassemia/mental retardation (ATR-X) syndrome: localization to Xq12-q21.31 by X inactivation and linkage analysis. |journal=Am. J. Hum. Genet. |volume=51 |issue= 5 |pages= 1136-49 |year= 1992 |pmid= 1415255 |doi= }}
*{{cite journal | author=Adès LC, Kerr B, Turner G, Wise G |title=Smith-Fineman-Myers syndrome in two brothers. |journal=Am. J. Med. Genet. |volume=40 |issue= 4 |pages= 467-70 |year= 1992 |pmid= 1684092 |doi= 10.1002/ajmg.1320400419 }}
*{{cite journal | author=Sutherland GR, Gedeon AK, Haan EA, ''et al.'' |title=Linkage studies with the gene for an X-linked syndrome of mental retardation, microcephaly and spastic diplegia (MRX2) |journal=Am. J. Med. Genet. |volume=30 |issue= 1-2 |pages= 493-508 |year= 1988 |pmid= 3177467 |doi= }}
*{{cite journal | author=Shapiro MB, Senapathy P |title=RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression. |journal=Nucleic Acids Res. |volume=15 |issue= 17 |pages= 7155-74 |year= 1987 |pmid= 3658675 |doi= }}
*{{cite journal | author=Gibbons RJ, Picketts DJ, Villard L, Higgs DR |title=Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome). |journal=Cell |volume=80 |issue= 6 |pages= 837-45 |year= 1995 |pmid= 7697714 |doi= }}
*{{cite journal | author=Stayton CL, Dabovic B, Gulisano M, ''et al.'' |title=Cloning and characterization of a new human Xq13 gene, encoding a putative helicase. |journal=Hum. Mol. Genet. |volume=3 |issue= 11 |pages= 1957-64 |year= 1995 |pmid= 7874112 |doi= }}
*{{cite journal | author=Wang LH, Collins A, Lawrence S, ''et al.'' |title=Integration of gene maps: chromosome X. |journal=Genomics |volume=22 |issue= 3 |pages= 590-604 |year= 1995 |pmid= 8001970 |doi= 10.1006/geno.1994.1432 }}
*{{cite journal | author=Gecz J, Pollard H, Consalez G, ''et al.'' |title=Cloning and expression of the murine homologue of a putative human X-linked nuclear protein gene closely linked to PGK1 in Xq13.3. |journal=Hum. Mol. Genet. |volume=3 |issue= 1 |pages= 39-44 |year= 1994 |pmid= 8162050 |doi= }}
*{{cite journal | author=Villard L, Gecz J, Mattéi JF, ''et al.'' |title=XNP mutation in a large family with Juberg-Marsidi syndrome. |journal=Nat. Genet. |volume=12 |issue= 4 |pages= 359-60 |year= 1996 |pmid= 8630485 |doi= 10.1038/ng0496-359 }}
*{{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=Picketts DJ, Higgs DR, Bachoo S, ''et al.'' |title=ATRX encodes a novel member of the SNF2 family of proteins: mutations point to a common mechanism underlying the ATR-X syndrome. |journal=Hum. Mol. Genet. |volume=5 |issue= 12 |pages= 1899-907 |year= 1997 |pmid= 8968741 |doi= }}
*{{cite journal | author=Villard L, Lacombe D, Fontés M |title=A point mutation in the XNP gene, associated with an ATR-X phenotype without alpha-thalassemia. |journal=Eur. J. Hum. Genet. |volume=4 |issue= 6 |pages= 316-20 |year= 1997 |pmid= 9043863 |doi= }}
*{{cite journal | author=Villard L, Lossi AM, Cardoso C, ''et al.'' |title=Determination of the genomic structure of the XNP/ATRX gene encoding a potential zinc finger helicase. |journal=Genomics |volume=43 |issue= 2 |pages= 149-55 |year= 1997 |pmid= 9244431 |doi= 10.1006/geno.1997.4793 }}
*{{cite journal | author=Golub EI, Kovalenko OV, Gupta RC, ''et al.'' |title=Interaction of human recombination proteins Rad51 and Rad54. |journal=Nucleic Acids Res. |volume=25 |issue= 20 |pages= 4106-10 |year= 1997 |pmid= 9321665 |doi= }}
*{{cite journal | author=Gibbons RJ, Bachoo S, Picketts DJ, ''et al.'' |title=Mutations in transcriptional regulator ATRX establish the functional significance of a PHD-like domain. |journal=Nat. Genet. |volume=17 |issue= 2 |pages= 146-8 |year= 1997 |pmid= 9326931 |doi= 10.1038/ng1097-146 }}
*{{cite journal | author=Cardoso C, Timsit S, Villard L, ''et al.'' |title=Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein. |journal=Hum. Mol. Genet. |volume=7 |issue= 4 |pages= 679-84 |year= 1998 |pmid= 9499421 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BGN... {November 16, 2007 1:18:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:19:21 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_BGN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ft3.
| PDB = {{PDB2|2ft3}}
| Name = Biglycan
| HGNCid = 1044
| Symbol = BGN
| AltSymbols =; DSPG1; PG-S1; PGI; SLRR1A
| OMIM = 301870
| ECnumber =
| Homologene = 1293
| MGIid = 88158
| GeneAtlas_image1 = PBB_GE_BGN_201262_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_BGN_201261_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_BGN_213905_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0030133 |text = transport vesicle}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 633
| Hs_Ensembl = ENSG00000182492
| Hs_RefseqProtein = NP_001702
| Hs_RefseqmRNA = NM_001711
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 152413591
| Hs_GenLoc_end = 152428206
| Hs_Uniprot = P21810
| Mm_EntrezGene = 12111
| Mm_Ensembl = ENSMUSG00000031375
| Mm_RefseqmRNA = NM_007542
| Mm_RefseqProtein = NP_031568
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 69736364
| Mm_GenLoc_end = 69748653
| Mm_Uniprot = Q3TAF9
}}
}}
'''Biglycan''', also known as '''BGN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BGN biglycan| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=633| 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 small cellular or pericellular matrix proteoglycan that is closely related in structure to two other small proteoglycans, decorin and fibromodulin. The encoded protein and decorin are thought to be the result of a gene duplication. Decorin contains one attached glycosaminoglycan chain, while this protein probably contains two chains. For this reason, this protein is called biglycan. This protein is thought to function in connective tissue metabolism by binding to collagen fibrils and transfering growth factor-beta. It may promote neuronal survival. This gene is a candidate gene for the Happle syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: BGN biglycan| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=633| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Iozzo RV |title=The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins. |journal=J. Biol. Chem. |volume=274 |issue= 27 |pages= 18843-6 |year= 1999 |pmid= 10383378 |doi= }}
*{{cite journal | author=Klezovitch O, Scanu AM |title=Domains of apolipoprotein E involved in the binding to the protein core of biglycan of the vascular extracellular matrix: potential relationship between retention and anti-atherogenic properties of this apolipoprotein. |journal=Trends Cardiovasc. Med. |volume=11 |issue= 7 |pages= 263-8 |year= 2001 |pmid= 11709279 |doi= }}
*{{cite journal | author=Fujisawa R |title=[Recent advances in research on bone matrix proteins] |journal=Nippon Rinsho |volume=60 Suppl 3 |issue= |pages= 72-8 |year= 2002 |pmid= 11979972 |doi= }}
*{{cite journal | author=Traupe H, van den Ouweland AM, van Oost BA, ''et al.'' |title=Fine mapping of the human biglycan (BGN) gene within the Xq28 region employing a hybrid cell panel. |journal=Genomics |volume=13 |issue= 2 |pages= 481-3 |year= 1992 |pmid= 1612609 |doi= }}
*{{cite journal | author=Fisher LW, Heegaard AM, Vetter U, ''et al.'' |title=Human biglycan gene. Putative promoter, intron-exon junctions, and chromosomal localization. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14371-7 |year= 1991 |pmid= 1860845 |doi= }}
*{{cite journal | author=McBride OW, Fisher LW, Young MF |title=Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40) genes on human chromosomes Xq13-qter and 12q, respectively. |journal=Genomics |volume=6 |issue= 2 |pages= 219-25 |year= 1990 |pmid= 1968422 |doi= }}
*{{cite journal | author=Fleischmajer R, Fisher LW, MacDonald ED, ''et al.'' |title=Decorin interacts with fibrillar collagen of embryonic and adult human skin. |journal=J. Struct. Biol. |volume=106 |issue= 1 |pages= 82-90 |year= 1991 |pmid= 2059554 |doi= }}
*{{cite journal | author=Roughley PJ, White RJ |title=Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II. |journal=Biochem. J. |volume=262 |issue= 3 |pages= 823-7 |year= 1990 |pmid= 2590169 |doi= }}
*{{cite journal | author=Fisher LW, Termine JD, Young MF |title=Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species. |journal=J. Biol. Chem. |volume=264 |issue= 8 |pages= 4571-6 |year= 1989 |pmid= 2647739 |doi= }}
*{{cite journal | author=Fisher LW, Hawkins GR, Tuross N, Termine JD |title=Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone. |journal=J. Biol. Chem. |volume=262 |issue= 20 |pages= 9702-8 |year= 1987 |pmid= 3597437 |doi= }}
*{{cite journal | author=Geerkens C, Vetter U, Just W, ''et al.'' |title=The X-chromosomal human biglycan gene BGN is subject to X inactivation but is transcribed like an X-Y homologous gene. |journal=Hum. Genet. |volume=96 |issue= 1 |pages= 44-52 |year= 1995 |pmid= 7607653 |doi= }}
*{{cite journal | author=Snow AD, Kinsella MG, Parks E, ''et al.'' |title=Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the beta-amyloid protein of Alzheimer's disease. |journal=Arch. Biochem. Biophys. |volume=320 |issue= 1 |pages= 84-95 |year= 1995 |pmid= 7793988 |doi= 10.1006/abbi.1995.1345 }}
*{{cite journal | author=Schönherr E, Witsch-Prehm P, Harrach B, ''et al.'' |title=Interaction of biglycan with type I collagen. |journal=J. Biol. Chem. |volume=270 |issue= 6 |pages= 2776-83 |year= 1995 |pmid= 7852349 |doi= }}
*{{cite journal | author=Just W, Rau W, Müller R, ''et al.'' |title=Dinucleotide repeat polymorphism at the human biglycan (BGN) locus. |journal=Hum. Mol. Genet. |volume=3 |issue= 12 |pages= 2268 |year= 1995 |pmid= 7881444 |doi= }}
*{{cite journal | author=Hildebrand A, Romarís M, Rasmussen LM, ''et al.'' |title=Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. |journal=Biochem. J. |volume=302 ( Pt 2) |issue= |pages= 527-34 |year= 1994 |pmid= 8093006 |doi= }}
*{{cite journal | author=Chatterjee A, Faust CJ, Herman GE |title=Genetic and physical mapping of the biglycan gene on the mouse X chromosome. |journal=Mamm. Genome |volume=4 |issue= 1 |pages= 33-6 |year= 1993 |pmid= 8093671 |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=Das S, Metzenberg A, Pai GS, Gitschier J |title=Mutational analysis of the biglycan gene excludes it as a candidate for X-linked dominant chondrodysplasia punctata, dyskeratosis congenita, and incontinentia pigmenti. |journal=Am. J. Hum. Genet. |volume=54 |issue= 5 |pages= 922-5 |year= 1994 |pmid= 8178833 |doi= }}
*{{cite journal | author=Whinna HC, Choi HU, Rosenberg LC, Church FC |title=Interaction of heparin cofactor II with biglycan and decorin. |journal=J. Biol. Chem. |volume=268 |issue= 6 |pages= 3920-4 |year= 1993 |pmid= 8440685 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BIN1... {November 16, 2007 1:16:48 PM PST}
- SEARCH REDIRECT: Control Box Found: BIN1 {November 16, 2007 1:17:26 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:17:27 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:17:27 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:17:27 PM PST}
- UPDATED: Updated protein page: BIN1 {November 16, 2007 1:17:33 PM PST}
- INFO: Beginning work on CDKN1C... {November 16, 2007 1:19:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:20:13 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 =
| image_source =
| PDB =
| Name = Cyclin-dependent kinase inhibitor 1C (p57, Kip2)
| HGNCid = 1786
| Symbol = CDKN1C
| AltSymbols =; BWCR; BWS; KIP2; WBS; p57
| OMIM = 600856
| ECnumber =
| Homologene = 58
| MGIid = 104564
| GeneAtlas_image1 = PBB_GE_CDKN1C_213348_at_tn.png
| GeneAtlas_image2 = PBB_GE_CDKN1C_213182_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CDKN1C_216894_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004861 |text = cyclin-dependent protein kinase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0000080 |text = G1 phase of mitotic cell cycle}} {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0042551 |text = neuron maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1028
| Hs_Ensembl = ENSG00000129757
| Hs_RefseqProtein = NP_000067
| Hs_RefseqmRNA = NM_000076
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 2861019
| Hs_GenLoc_end = 2863577
| Hs_Uniprot = P49918
| Mm_EntrezGene = 12577
| Mm_Ensembl = ENSMUSG00000037664
| Mm_RefseqmRNA = NM_009876
| Mm_RefseqProtein = NP_034006
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 143267730
| Mm_GenLoc_end = 143270386
| Mm_Uniprot = Q791X1
}}
}}
'''Cyclin-dependent kinase inhibitor 1C (p57, Kip2)''', also known as '''CDKN1C''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDKN1C cyclin-dependent kinase inhibitor 1C (p57, Kip2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1028| 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 = Cyclin-dependent kinase inhibitor 1C is a tight-binding inhibitor of several G1 cyclin/Cdk complexes and a negative regulator of cell proliferation. Mutations of CDKN1C are implicated in sporadic cancers and Beckwith-Wiedemann syndorome suggesting that it is a tumor suppressor candidate.<ref name="entrez">{{cite web | title = Entrez Gene: CDKN1C cyclin-dependent kinase inhibitor 1C (p57, Kip2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1028| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Seizinger BR |title=Genes associated with tumor suppression and growth control in the human nervous system. |journal=Cancer Metastasis Rev. |volume=10 |issue= 4 |pages= 281-7 |year= 1992 |pmid= 1786629 |doi= }}
*{{cite journal | author=Lee MH, Reynisdóttir I, Massagué J |title=Cloning of p57KIP2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution. |journal=Genes Dev. |volume=9 |issue= 6 |pages= 639-49 |year= 1995 |pmid= 7729683 |doi= }}
*{{cite journal | author=Matsuoka S, Edwards MC, Bai C, ''et al.'' |title=p57KIP2, a structurally distinct member of the p21CIP1 Cdk inhibitor family, is a candidate tumor suppressor gene. |journal=Genes Dev. |volume=9 |issue= 6 |pages= 650-62 |year= 1995 |pmid= 7729684 |doi= }}
*{{cite journal | author=Matsuoka S, Thompson JS, Edwards MC, ''et al.'' |title=Imprinting of the gene encoding a human cyclin-dependent kinase inhibitor, p57KIP2, on chromosome 11p15. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 7 |pages= 3026-30 |year= 1996 |pmid= 8610162 |doi= }}
*{{cite journal | author=Reid LH, Crider-Miller SJ, West A, ''et al.'' |title=Genomic organization of the human p57KIP2 gene and its analysis in the G401 Wilms' tumor assay. |journal=Cancer Res. |volume=56 |issue= 6 |pages= 1214-8 |year= 1996 |pmid= 8640800 |doi= }}
*{{cite journal | author=Tokino T, Urano T, Furuhata T, ''et al.'' |title=Characterization of the human p57KIP2 gene: alternative splicing, insertion/deletion polymorphisms in VNTR sequences in the coding region, and mutational analysis. |journal=Hum. Genet. |volume=97 |issue= 5 |pages= 625-31 |year= 1996 |pmid= 8655143 |doi= }}
*{{cite journal | author=Hatada I, Ohashi H, Fukushima Y, ''et al.'' |title=An imprinted gene p57KIP2 is mutated in Beckwith-Wiedemann syndrome. |journal=Nat. Genet. |volume=14 |issue= 2 |pages= 171-3 |year= 1996 |pmid= 8841187 |doi= 10.1038/ng1096-171 }}
*{{cite journal | author=Furuhata T, Tokino T, Urano T, Nakamura Y |title=Isolation of a novel GPI-anchored gene specifically regulated by p53; correlation between its expression and anti-cancer drug sensitivity. |journal=Oncogene |volume=13 |issue= 9 |pages= 1965-70 |year= 1997 |pmid= 8934543 |doi= }}
*{{cite journal | author=LaBaer J, Garrett MD, Stevenson LF, ''et al.'' |title=New functional activities for the p21 family of CDK inhibitors. |journal=Genes Dev. |volume=11 |issue= 7 |pages= 847-62 |year= 1997 |pmid= 9106657 |doi= }}
*{{cite journal | author=Watanabe H, Pan ZQ, Schreiber-Agus N, ''et al.'' |title=Suppression of cell transformation by the cyclin-dependent kinase inhibitor p57KIP2 requires binding to proliferating cell nuclear antigen. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 4 |pages= 1392-7 |year= 1998 |pmid= 9465025 |doi= }}
*{{cite journal | author=Bhuiyan ZA, Yatsuki H, Sasaguri T, ''et al.'' |title=Functional analysis of the p57KIP2 gene mutation in Beckwith-Wiedemann syndrome. |journal=Hum. Genet. |volume=104 |issue= 3 |pages= 205-10 |year= 1999 |pmid= 10323243 |doi= }}
*{{cite journal | author=Lam WW, Hatada I, Ohishi S, ''et al.'' |title=Analysis of germline CDKN1C (p57KIP2) mutations in familial and sporadic Beckwith-Wiedemann syndrome (BWS) provides a novel genotype-phenotype correlation. |journal=J. Med. Genet. |volume=36 |issue= 7 |pages= 518-23 |year= 1999 |pmid= 10424811 |doi= }}
*{{cite journal | author=Reynaud EG, Leibovitch MP, Tintignac LA, ''et al.'' |title=Stabilization of MyoD by direct binding to p57(Kip2). |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 18767-76 |year= 2000 |pmid= 10764802 |doi= 10.1074/jbc.M907412199 }}
*{{cite journal | author=Fink JR, LeBien TW |title=Novel expression of cyclin-dependent kinase inhibitors in human B-cell precursors. |journal=Exp. Hematol. |volume=29 |issue= 4 |pages= 490-8 |year= 2001 |pmid= 11301189 |doi= }}
*{{cite journal | author=Kido K, Doerks A, Lochelt M, Flügel RM |title=Identification and functional characterization of an intragenic DNA binding site for the spumaretroviral trans-activator in the human p57Kip2 gene. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12032-9 |year= 2002 |pmid= 11815601 |doi= 10.1074/jbc.M108747200 }}
*{{cite journal | author=Blint E, Phillips AC, Kozlov S, ''et al.'' |title=Induction of p57(KIP2) expression by p73beta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 6 |pages= 3529-34 |year= 2002 |pmid= 11891335 |doi= 10.1073/pnas.062491899 }}
*{{cite journal | author=Ito Y, Yoshida H, Nakano K, ''et al.'' |title=Expression of p57/Kip2 protein in normal and neoplastic thyroid tissues. |journal=Int. J. Mol. Med. |volume=9 |issue= 4 |pages= 373-6 |year= 2002 |pmid= 11891530 |doi= }}
*{{cite journal | author=Kikuchi T, Toyota M, Itoh F, ''et al.'' |title=Inactivation of p57KIP2 by regional promoter hypermethylation and histone deacetylation in human tumors. |journal=Oncogene |volume=21 |issue= 17 |pages= 2741-9 |year= 2002 |pmid= 11965547 |doi= 10.1038/sj.onc.1205376 }}
*{{cite journal | author=Li Y, Nagai H, Ohno T, ''et al.'' |title=Aberrant DNA methylation of p57(KIP2) gene in the promoter region in lymphoid malignancies of B-cell phenotype. |journal=Blood |volume=100 |issue= 7 |pages= 2572-7 |year= 2002 |pmid= 12239171 |doi= 10.1182/blood-2001-11-0026 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYR61... {November 16, 2007 1:51:53 PM PST}
- SEARCH REDIRECT: Control Box Found: CYR61 {November 16, 2007 1:52:20 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:52:23 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:52:23 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:52:23 PM PST}
- UPDATED: Updated protein page: CYR61 {November 16, 2007 1:52:30 PM PST}
- INFO: Beginning work on EFNB2... {November 16, 2007 1:20:13 PM PST}
- SEARCH REDIRECT: Control Box Found: EFNB2 {November 16, 2007 1:49:27 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:49:28 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:49:28 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:49:28 PM PST}
- UPDATED: Updated protein page: EFNB2 {November 16, 2007 1:49:33 PM PST}
- INFO: Beginning work on EPHX1... {November 16, 2007 1:49:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:50:02 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Epoxide hydrolase 1, microsomal (xenobiotic)
| HGNCid = 3401
| Symbol = EPHX1
| AltSymbols =; EPHX; EPOX; MEH
| OMIM = 132810
| ECnumber =
| Homologene = 94
| MGIid = 95405
| GeneAtlas_image1 = PBB_GE_EPHX1_202017_at_tn.png
| Function = {{GNF_GO|id=GO:0004301 |text = epoxide hydrolase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0009636 |text = response to toxin}} {{GNF_GO|id=GO:0019439 |text = aromatic compound catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2052
| Hs_Ensembl = ENSG00000143819
| Hs_RefseqProtein = NP_000111
| Hs_RefseqmRNA = NM_000120
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 224064459
| Hs_GenLoc_end = 224099883
| Hs_Uniprot = P07099
| Mm_EntrezGene = 13849
| Mm_Ensembl = ENSMUSG00000038776
| Mm_RefseqmRNA = NM_010145
| Mm_RefseqProtein = NP_034275
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 182826233
| Mm_GenLoc_end = 182854196
| Mm_Uniprot = P97869
}}
}}
'''Epoxide hydrolase 1, microsomal (xenobiotic)''', also known as '''EPHX1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPHX1 epoxide hydrolase 1, microsomal (xenobiotic)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2052| 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 = Epoxide hydrolase plays an important role in both the activation and detoxification of exogenous chemicals such as polycyclic aromatic hydrocarbons.<ref name="entrez">{{cite web | title = Entrez Gene: EPHX1 epoxide hydrolase 1, microsomal (xenobiotic)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2052| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Seidegård J, Ekström G |title=The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics. |journal=Environ. Health Perspect. |volume=105 Suppl 4 |issue= |pages= 791-9 |year= 1997 |pmid= 9255563 |doi= }}
*{{cite journal | author=Wormhoudt LW, Commandeur JN, Vermeulen NP |title=Genetic polymorphisms of human N-acetyltransferase, cytochrome P450, glutathione-S-transferase, and epoxide hydrolase enzymes: relevance to xenobiotic metabolism and toxicity. |journal=Crit. Rev. Toxicol. |volume=29 |issue= 1 |pages= 59-124 |year= 1999 |pmid= 10066160 |doi= }}
*{{cite journal | author=Wilson NM, Omiecinski CJ |title=Xenobiotic microsomal epoxide hydrolase: 5' sequence of the human gene. |journal=Biochim. Biophys. Acta |volume=1008 |issue= 3 |pages= 357-8 |year= 1989 |pmid= 2758034 |doi= }}
*{{cite journal | author=Strickler SM, Dansky LV, Miller MA, ''et al.'' |title=Genetic predisposition to phenytoin-induced birth defects. |journal=Lancet |volume=2 |issue= 8458 |pages= 746-9 |year= 1985 |pmid= 2864485 |doi= }}
*{{cite journal | author=Skoda RC, Demierre A, McBride OW, ''et al.'' |title=Human microsomal xenobiotic epoxide hydrolase. Complementary DNA sequence, complementary DNA-directed expression in COS-1 cells, and chromosomal localization. |journal=J. Biol. Chem. |volume=263 |issue= 3 |pages= 1549-54 |year= 1988 |pmid= 2891713 |doi= }}
*{{cite journal | author=Jackson MR, Craft JA, Burchell B |title=Nucleotide and deduced amino acid sequence of human liver microsomal epoxide hydrolase. |journal=Nucleic Acids Res. |volume=15 |issue= 17 |pages= 7188 |year= 1987 |pmid= 3502697 |doi= }}
*{{cite journal | author=Hassett C, Aicher L, Sidhu JS, Omiecinski CJ |title=Human microsomal epoxide hydrolase: genetic polymorphism and functional expression in vitro of amino acid variants. |journal=Hum. Mol. Genet. |volume=3 |issue= 3 |pages= 421-8 |year= 1994 |pmid= 7516776 |doi= }}
*{{cite journal | author=Hassett C, Robinson KB, Beck NB, Omiecinski CJ |title=The human microsomal epoxide hydrolase gene (EPHX1): complete nucleotide sequence and structural characterization. |journal=Genomics |volume=23 |issue= 2 |pages= 433-42 |year= 1995 |pmid= 7835893 |doi= 10.1006/geno.1994.1520 }}
*{{cite journal | author=McGlynn KA, Rosvold EA, Lustbader ED, ''et al.'' |title=Susceptibility to hepatocellular carcinoma is associated with genetic variation in the enzymatic detoxification of aflatoxin B1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 6 |pages= 2384-7 |year= 1995 |pmid= 7892276 |doi= }}
*{{cite journal | author=Gaedigk A, Spielberg SP, Grant DM |title=Characterization of the microsomal epoxide hydrolase gene in patients with anticonvulsant adverse drug reactions. |journal=Pharmacogenetics |volume=4 |issue= 3 |pages= 142-53 |year= 1994 |pmid= 7920694 |doi= }}
*{{cite journal | author=Hartsfield JK, Sutcliffe MJ, Everett ET, ''et al.'' |title=Assignment1 of microsomal epoxide hydrolase (EPHX1) to human chromosome 1q42.1 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=83 |issue= 1-2 |pages= 44-5 |year= 1999 |pmid= 9925921 |doi= }}
*{{cite journal | author=Krovat BC, Tracy JH, Omiecinski CJ |title=Fingerprinting of cytochrome P450 and microsomal epoxide hydrolase gene expression in human blood cells. |journal=Toxicol. Sci. |volume=55 |issue= 2 |pages= 352-60 |year= 2000 |pmid= 10828267 |doi= }}
*{{cite journal | author=Hattori N, Fujiwara H, Maeda M, ''et al.'' |title=Epoxide hydrolase affects estrogen production in the human ovary. |journal=Endocrinology |volume=141 |issue= 9 |pages= 3353-65 |year= 2000 |pmid= 10965908 |doi= }}
*{{cite journal | author=Belmahdi F, Chevalier D, Lo-Guidice JM, ''et al.'' |title=Identification of 6 new polymorphisms, g.11177G>A, g.14622C>T (R49C), g.17540T>C, g.17639T>C, g.30929T>C, g.31074G>A (R454Q), in the human microsomal epoxide hydrolase gene (EPHX1) in a French population. |journal=Hum. Mutat. |volume=16 |issue= 5 |pages= 450 |year= 2000 |pmid= 11058921 |doi= 10.1002/1098-1004(200011)16:5<450::AID-HUMU28>3.0.CO;2-1 }}
*{{cite journal | author=Zusterzeel PL, Peters WH, Visser W, ''et al.'' |title=A polymorphism in the gene for microsomal epoxide hydrolase is associated with pre-eclampsia. |journal=J. Med. Genet. |volume=38 |issue= 4 |pages= 234-7 |year= 2001 |pmid= 11283205 |doi= }}
*{{cite journal | author=Sarmanová J, Benesová K, Gut I, ''et al.'' |title=Genetic polymorphisms of biotransformation enzymes in patients with Hodgkin's and non-Hodgkin's lymphomas. |journal=Hum. Mol. Genet. |volume=10 |issue= 12 |pages= 1265-73 |year= 2001 |pmid= 11406608 |doi= }}
*{{cite journal | author=Farin FM, Janssen P, Quigley S, ''et al.'' |title=Genetic polymorphisms of microsomal and soluble epoxide hydrolase and the risk of Parkinson's disease. |journal=Pharmacogenetics |volume=11 |issue= 8 |pages= 703-8 |year= 2002 |pmid= 11692079 |doi= }}
*{{cite journal | author=Coller JK, Fritz P, Zanger UM, ''et al.'' |title=Distribution of microsomal epoxide hydrolase in humans: an immunohistochemical study in normal tissues, and benign and malignant tumours. |journal=Histochem. J. |volume=33 |issue= 6 |pages= 329-36 |year= 2002 |pmid= 11758809 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FGR... {November 16, 2007 1:50:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:50:32 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
}}
<!-- 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 = Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog
| HGNCid = 3697
| Symbol = FGR
| AltSymbols =; FLJ43153; MGC75096; SRC2; c-fgr; c-src2; p55c-fgr; p58c-fgr
| OMIM = 164940
| ECnumber =
| Homologene = 3842
| MGIid = 95527
| GeneAtlas_image1 = PBB_GE_FGR_208438_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{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}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2268
| Hs_Ensembl = ENSG00000000938
| Hs_RefseqProtein = NP_001036194
| Hs_RefseqmRNA = NM_001042729
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 27811162
| Hs_GenLoc_end = 27834375
| Hs_Uniprot = P09769
| Mm_EntrezGene = 14191
| Mm_Ensembl = ENSMUSG00000028874
| Mm_RefseqmRNA = NM_010208
| Mm_RefseqProtein = NP_034338
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 132246266
| Mm_GenLoc_end = 132273953
| Mm_Uniprot = Q6GTF2
}}
}}
'''Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog''', also known as '''FGR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FGR Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2268| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to plasma membrane ruffles, and functions as a negative regulator of cell migration and adhesion triggered by the beta-2 integrin signal transduction pathway. Infection with Epstein-Barr virus results in the overexpression of this gene. Multiple alternatively spliced variants, encoding the same protein, have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: FGR Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2268| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Patel M, Faulkner L, Katz DR, Brickell PM |title=The c-fgr proto-oncogene: expression in Epstein-Barr-virus-infected B lymphocytes and in cells of the myelomonocytic and granulocytic lineages. |journal=Pathobiology |volume=59 |issue= 4 |pages= 289-92 |year= 1991 |pmid= 1652975 |doi= }}
*{{cite journal | author=Resh MD |title=Myristylation and palmitylation of Src family members: the fats of the matter. |journal=Cell |volume=76 |issue= 3 |pages= 411-3 |year= 1994 |pmid= 8313462 |doi= }}
*{{cite journal | author=Lowell CA, Berton G |title=Integrin signal transduction in myeloid leukocytes. |journal=J. Leukoc. Biol. |volume=65 |issue= 3 |pages= 313-20 |year= 1999 |pmid= 10080533 |doi= }}
*{{cite journal | author=Snapper SB, Rosen FS |title=The Wiskott-Aldrich syndrome protein (WASP): roles in signaling and cytoskeletal organization. |journal=Annu. Rev. Immunol. |volume=17 |issue= |pages= 905-29 |year= 1999 |pmid= 10358777 |doi= 10.1146/annurev.immunol.17.1.905 }}
*{{cite journal | author=Tatosyan AG, Mizenina OA |title=Kinases of the Src family: structure and functions. |journal=Biochemistry Mosc. |volume=65 |issue= 1 |pages= 49-58 |year= 2000 |pmid= 10702640 |doi= }}
*{{cite journal | author=Patel MS, Mankoo BS, Brickell PM |title=A polymorphic microsatellite repeat is located close to the promoter region of the c-fgr proto-oncogene (FGR) at chromosome 1p36.2-p36.1. |journal=Hum. Mol. Genet. |volume=1 |issue= 1 |pages= 65 |year= 1993 |pmid= 1339476 |doi= }}
*{{cite journal | author=Link DC, Gutkind SJ, Robbins KC, Ley TJ |title=Characterization of the 5' untranslated region of the human c-fgr gene and identification of the major myelomonocytic c-fgr promoter. |journal=Oncogene |volume=7 |issue= 5 |pages= 877-84 |year= 1992 |pmid= 1373875 |doi= }}
*{{cite journal | author=Patel M, Leevers SJ, Brickell PM |title=Structure of the complete human c-fgr proto-oncogene and identification of multiple transcriptional start sites. |journal=Oncogene |volume=5 |issue= 2 |pages= 201-6 |year= 1990 |pmid= 1690869 |doi= }}
*{{cite journal | author=Biondi A, Paganin C, Rossi V, ''et al.'' |title=Expression of lineage-restricted protein tyrosine kinase genes in human natural killer cells. |journal=Eur. J. Immunol. |volume=21 |issue= 3 |pages= 843-6 |year= 1991 |pmid= 1826268 |doi= }}
*{{cite journal | author=Gutkind JS, Link DC, Katamine S, ''et al.'' |title=A novel c-fgr exon utilized in Epstein-Barr virus-infected B lymphocytes but not in normal monocytes. |journal=Mol. Cell. Biol. |volume=11 |issue= 3 |pages= 1500-7 |year= 1991 |pmid= 1847500 |doi= }}
*{{cite journal | author=Patel M, Leevers SJ, Brickell PM |title=Regulation of c-fgr proto-oncogene expression in Epstein-Barr virus infected B-cell lines. |journal=Int. J. Cancer |volume=45 |issue= 2 |pages= 342-6 |year= 1990 |pmid= 2154410 |doi= }}
*{{cite journal | author=Parker RC, Mardon G, Lebo RV, ''et al.'' |title=Isolation of duplicated human c-src genes located on chromosomes 1 and 20. |journal=Mol. Cell. Biol. |volume=5 |issue= 4 |pages= 831-8 |year= 1985 |pmid= 2581127 |doi= }}
*{{cite journal | author=Brickell PM, Patel M |title=Structure and expression of c-fgr protooncogene mRNA in Epstein-Barr virus converted cell lines. |journal=Br. J. Cancer |volume=58 |issue= 6 |pages= 704-9 |year= 1989 |pmid= 2852026 |doi= }}
*{{cite journal | author=Tronick SR, Popescu NC, Cheah MS, ''et al.'' |title=Isolation and chromosomal localization of the human fgr protooncogene, a distinct member of the tyrosine kinase gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 19 |pages= 6595-9 |year= 1985 |pmid= 2995972 |doi= }}
*{{cite journal | author=Cheah MS, Ley TJ, Tronick SR, Robbins KC |title=fgr proto-oncogene mRNA induced in B lymphocytes by Epstein-Barr virus infection. |journal=Nature |volume=319 |issue= 6050 |pages= 238-40 |year= 1986 |pmid= 3003578 |doi= 10.1038/319238a0 }}
*{{cite journal | author=Nishizawa M, Semba K, Yoshida MC, ''et al.'' |title=Structure, expression, and chromosomal location of the human c-fgr gene. |journal=Mol. Cell. Biol. |volume=6 |issue= 2 |pages= 511-7 |year= 1987 |pmid= 3023853 |doi= }}
*{{cite journal | author=Katamine S, Notario V, Rao CD, ''et al.'' |title=Primary structure of the human fgr proto-oncogene product p55c-fgr. |journal=Mol. Cell. Biol. |volume=8 |issue= 1 |pages= 259-66 |year= 1988 |pmid= 3275868 |doi= }}
*{{cite journal | author=Inoue K, Ikawa S, Semba K, ''et al.'' |title=Isolation and sequencing of cDNA clones homologous to the v-fgr oncogene from a human B lymphocyte cell line, IM-9. |journal=Oncogene |volume=1 |issue= 3 |pages= 301-4 |year= 1988 |pmid= 3330776 |doi= }}
*{{cite journal | author=Nishizawa M, Semba K, Yamamoto T, Toyoshima K |title=Human c-f gr gene does not contain coding sequence for actin-like protein. |journal=Jpn. J. Cancer Res. |volume=76 |issue= 3 |pages= 155-9 |year= 1985 |pmid= 3922831 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GRN... {November 16, 2007 1:50:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:51:18 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_GRN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1g26.
| PDB = {{PDB2|1g26}}
| Name = Granulin
| HGNCid = 4601
| Symbol = GRN
| AltSymbols =; GEP; GP88; PCDGF; PEPI; PGRN
| OMIM = 138945
| ECnumber =
| Homologene = 1577
| MGIid = 95832
| GeneAtlas_image1 = PBB_GE_GRN_211284_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GRN_200678_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_GRN_216041_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0001835 |text = blastocyst hatching}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007566 |text = embryo implantation}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0050679 |text = positive regulation of epithelial cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2896
| Hs_Ensembl = ENSG00000030582
| Hs_RefseqProtein = NP_001012497
| Hs_RefseqmRNA = NM_001012479
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 39778017
| Hs_GenLoc_end = 39785996
| Hs_Uniprot = P28799
| Mm_EntrezGene = 14824
| Mm_Ensembl = ENSMUSG00000034708
| Mm_RefseqmRNA = XM_984981
| Mm_RefseqProtein = XP_990075
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 102246571
| Mm_GenLoc_end = 102252895
| Mm_Uniprot = Q3TVQ3
}}
}}
'''Granulin''', also known as '''GRN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GRN granulin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2896| 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 = Granulins are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. The 88 kDa precursor protein, progranulin, is also called proepithelin and PC cell-derived growth factor. Cleavage of the signal peptide produces mature granulin which can be further cleaved into a variety of active, 6 kDa peptides. These smaller cleavage products are named granulin A, granulin B, granulin C, etc. Epithelins 1 and 2 are synonymous with granulins A and B, respectively. Both the peptides and intact granulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis.<ref name="entrez">{{cite web | title = Entrez Gene: GRN granulin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2896| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Serrero G |title=Autocrine growth factor revisited: PC-cell-derived growth factor (progranulin), a critical player in breast cancer tumorigenesis. |journal=Biochem. Biophys. Res. Commun. |volume=308 |issue= 3 |pages= 409-13 |year= 2003 |pmid= 12914763 |doi= }}
*{{cite journal | author=Ahmed Z, Mackenzie IR, Hutton ML, Dickson DW |title=Progranulin in frontotemporal lobar degeneration and neuroinflammation. |journal=Journal of neuroinflammation |volume=4 |issue= |pages= 7 |year= 2007 |pmid= 17291356 |doi= 10.1186/1742-2094-4-7 }}
*{{cite journal | author=Bhandari V, Bateman A |title=Structure and chromosomal location of the human granulin gene. |journal=Biochem. Biophys. Res. Commun. |volume=188 |issue= 1 |pages= 57-63 |year= 1992 |pmid= 1417868 |doi= }}
*{{cite journal | author=Bhandari V, Palfree RG, Bateman A |title=Isolation and sequence of the granulin precursor cDNA from human bone marrow reveals tandem cysteine-rich granulin domains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1715-9 |year= 1992 |pmid= 1542665 |doi= }}
*{{cite journal | author=Plowman GD, Green JM, Neubauer MG, ''et al.'' |title=The epithelin precursor encodes two proteins with opposing activities on epithelial cell growth. |journal=J. Biol. Chem. |volume=267 |issue= 18 |pages= 13073-8 |year= 1992 |pmid= 1618805 |doi= }}
*{{cite journal | author=Bateman A, Belcourt D, Bennett H, ''et al.'' |title=Granulins, a novel class of peptide from leukocytes. |journal=Biochem. Biophys. Res. Commun. |volume=173 |issue= 3 |pages= 1161-8 |year= 1991 |pmid= 2268320 |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=Baba T, Hoff HB, Nemoto H, ''et al.'' |title=Acrogranin, an acrosomal cysteine-rich glycoprotein, is the precursor of the growth-modulating peptides, granulins, and epithelins, and is expressed in somatic as well as male germ cells. |journal=Mol. Reprod. Dev. |volume=34 |issue= 3 |pages= 233-43 |year= 1993 |pmid= 8471244 |doi= 10.1002/mrd.1080340302 }}
*{{cite journal | author=Kardana A, Bagshawe KD, Coles B, ''et al.'' |title=Characterisation of UGP and its relationship with beta-core fragment. |journal=Br. J. Cancer |volume=67 |issue= 4 |pages= 686-92 |year= 1993 |pmid= 8471426 |doi= }}
*{{cite journal | author=Zhou J, Gao G, Crabb JW, Serrero G |title=Purification of an autocrine growth factor homologous with mouse epithelin precursor from a highly tumorigenic cell line. |journal=J. Biol. Chem. |volume=268 |issue= 15 |pages= 10863-9 |year= 1993 |pmid= 8496151 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Bhandari V, Daniel R, Lim PS, Bateman A |title=Structural and functional analysis of a promoter of the human granulin/epithelin gene. |journal=Biochem. J. |volume=319 ( Pt 2) |issue= |pages= 441-7 |year= 1996 |pmid= 8912679 |doi= }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |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=Zhang H, Serrero G |title=Inhibition of tumorigenicity of the teratoma PC cell line by transfection with antisense cDNA for PC cell-derived growth factor (PCDGF, epithelin/granulin precursor). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 24 |pages= 14202-7 |year= 1998 |pmid= 9826678 |doi= }}
*{{cite journal | author=Trinh DP, Brown KM, Jeang KT |title=Epithelin/granulin growth factors: extracellular cofactors for HIV-1 and HIV-2 Tat proteins. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 2 |pages= 299-306 |year= 1999 |pmid= 10079180 |doi= 10.1006/bbrc.1999.0317 }}
*{{cite journal | author=He Z, Bateman A |title=Progranulin gene expression regulates epithelial cell growth and promotes tumor growth in vivo. |journal=Cancer Res. |volume=59 |issue= 13 |pages= 3222-9 |year= 1999 |pmid= 10397269 |doi= }}
*{{cite journal | author=Thornton MA, Poncz M, Korostishevsky M, ''et al.'' |title=The human platelet alphaIIb gene is not closely linked to its integrin partner beta3. |journal=Blood |volume=94 |issue= 6 |pages= 2039-47 |year= 1999 |pmid= 10477733 |doi= }}
*{{cite journal | author=Tolkatchev D, Ng A, Vranken W, Ni F |title=Design and solution structure of a well-folded stack of two beta-hairpins based on the amino-terminal fragment of human granulin A. |journal=Biochemistry |volume=39 |issue= 11 |pages= 2878-86 |year= 2000 |pmid= 10715107 |doi= }}
*{{cite journal | author=Liau LM, Lallone RL, Seitz RS, ''et al.'' |title=Identification of a human glioma-associated growth factor gene, granulin, using differential immuno-absorption. |journal=Cancer Res. |volume=60 |issue= 5 |pages= 1353-60 |year= 2000 |pmid= 10728698 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HGS... {November 16, 2007 1:57:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:58:09 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 = Hepatocyte growth factor-regulated tyrosine kinase substrate
| HGNCid = 4897
| Symbol = HGS
| AltSymbols =; HRS; ZFYVE8
| OMIM = 604375
| ECnumber =
| Homologene = 37954
| MGIid = 104681
| GeneAtlas_image1 = PBB_GE_HGS_210428_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0016197 |text = endosome transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9146
| Hs_Ensembl = ENSG00000185359
| Hs_RefseqProtein = NP_004703
| Hs_RefseqmRNA = NM_004712
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 77261425
| Hs_GenLoc_end = 77279548
| Hs_Uniprot = O14964
| Mm_EntrezGene = 15239
| Mm_Ensembl = ENSMUSG00000025793
| Mm_RefseqmRNA = NM_008244
| Mm_RefseqProtein = NP_032270
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 120283765
| Mm_GenLoc_end = 120300065
| Mm_Uniprot = Q3TLL4
}}
}}
'''Hepatocyte growth factor-regulated tyrosine kinase substrate''', also known as '''HGS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HGS hepatocyte growth factor-regulated tyrosine kinase substrate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9146| 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=Comoglio PM |title=Structure, biosynthesis and biochemical properties of the HGF receptor in normal and malignant cells. |journal=EXS |volume=65 |issue= |pages= 131-65 |year= 1993 |pmid= 8380735 |doi= }}
*{{cite journal | author=Komada M, Masaki R, Yamamoto A, Kitamura N |title=Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes. |journal=J. Biol. Chem. |volume=272 |issue= 33 |pages= 20538-44 |year= 1997 |pmid= 9252367 |doi= }}
*{{cite journal | author=Asao H, Sasaki Y, Arita T, ''et al.'' |title=Hrs is associated with STAM, a signal-transducing adaptor molecule. Its suppressive effect on cytokine-induced cell growth. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 32785-91 |year= 1998 |pmid= 9407053 |doi= }}
*{{cite journal | author=Lu L, Komada M, Kitamura N |title=Human Hrs, a tyrosine kinase substrate in growth factor-stimulated cells: cDNA cloning and mapping of the gene to chromosome 17. |journal=Gene |volume=213 |issue= 1-2 |pages= 125-32 |year= 1998 |pmid= 9630564 |doi= }}
*{{cite journal | author=Stephens DJ, Banting G |title=Direct interaction of the trans-Golgi network membrane protein, TGN38, with the F-actin binding protein, neurabin. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 30080-6 |year= 1999 |pmid= 10514494 |doi= }}
*{{cite journal | author=Bean AJ, Davanger S, Chou MF, ''et al.'' |title=Hrs-2 regulates receptor-mediated endocytosis via interactions with Eps15. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15271-8 |year= 2000 |pmid= 10809762 |doi= }}
*{{cite journal | author=Kwong J, Roundabush FL, Hutton Moore P, ''et al.'' |title=Hrs interacts with SNAP-25 and regulates Ca(2+)-dependent exocytosis. |journal=J. Cell. Sci. |volume=113 ( Pt 12) |issue= |pages= 2273-84 |year= 2000 |pmid= 10825299 |doi= }}
*{{cite journal | author=Scoles DR, Huynh DP, Chen MS, ''et al.'' |title=The neurofibromatosis 2 tumor suppressor protein interacts with hepatocyte growth factor-regulated tyrosine kinase substrate. |journal=Hum. Mol. Genet. |volume=9 |issue= 11 |pages= 1567-74 |year= 2000 |pmid= 10861283 |doi= }}
*{{cite journal | author=Gillooly DJ, Morrow IC, Lindsay M, ''et al.'' |title=Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. |journal=EMBO J. |volume=19 |issue= 17 |pages= 4577-88 |year= 2000 |pmid= 10970851 |doi= 10.1093/emboj/19.17.4577 }}
*{{cite journal | author=Miura S, Takeshita T, Asao H, ''et al.'' |title=Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through cooperation with SARA. |journal=Mol. Cell. Biol. |volume=20 |issue= 24 |pages= 9346-55 |year= 2001 |pmid= 11094085 |doi= }}
*{{cite journal | author=Chin LS, Raynor MC, Wei X, ''et al.'' |title=Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor. |journal=J. Biol. Chem. |volume=276 |issue= 10 |pages= 7069-78 |year= 2001 |pmid= 11110793 |doi= 10.1074/jbc.M004129200 }}
*{{cite journal | author=Gutmann DH, Haipek CA, Burke SP, ''et al.'' |title=The NF2 interactor, hepatocyte growth factor-regulated tyrosine kinase substrate (HRS), associates with merlin in the "open" conformation and suppresses cell growth and motility. |journal=Hum. Mol. Genet. |volume=10 |issue= 8 |pages= 825-34 |year= 2001 |pmid= 11285248 |doi= }}
*{{cite journal | author=Sasaki Y, Sugamura K |title=Involvement of Hgs/Hrs in signaling for cytokine-mediated c-fos induction through interaction with TAK1 and Pak1. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29943-52 |year= 2001 |pmid= 11397816 |doi= 10.1074/jbc.M104230200 }}
*{{cite journal | author=Raiborg C, Bremnes B, Mehlum A, ''et al.'' |title=FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes. |journal=J. Cell. Sci. |volume=114 |issue= Pt 12 |pages= 2255-63 |year= 2001 |pmid= 11493665 |doi= }}
*{{cite journal | author=Raiborg C, Bache KG, Mehlum A, ''et al.'' |title=Hrs recruits clathrin to early endosomes. |journal=EMBO J. |volume=20 |issue= 17 |pages= 5008-21 |year= 2001 |pmid= 11532964 |doi= 10.1093/emboj/20.17.5008 }}
*{{cite journal | author=Steen H, Kuster B, Fernandez M, ''et al.'' |title=Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. |journal=J. Biol. Chem. |volume=277 |issue= 2 |pages= 1031-9 |year= 2002 |pmid= 11687594 |doi= 10.1074/jbc.M109992200 }}
*{{cite journal | author=Bishop N, Horman A, Woodman P |title=Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. |journal=J. Cell Biol. |volume=157 |issue= 1 |pages= 91-101 |year= 2002 |pmid= 11916981 |doi= 10.1083/jcb.200112080 }}
*{{cite journal | author=Tchernev VT, Mansfield TA, Giot L, ''et al.'' |title=The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins. |journal=Mol. Med. |volume=8 |issue= 1 |pages= 56-64 |year= 2002 |pmid= 11984006 |doi= }}
*{{cite journal | author=Li Y, Chin LS, Levey AI, Li L |title=Huntingtin-associated protein 1 interacts with hepatocyte growth factor-regulated tyrosine kinase substrate and functions in endosomal trafficking. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 28212-21 |year= 2002 |pmid= 12021262 |doi= 10.1074/jbc.M111612200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HTR2C... {November 16, 2007 1:51:18 PM PST}
- SEARCH REDIRECT: Control Box Found: HTR2C {November 16, 2007 1:51:45 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:51:47 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:51:47 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:51:47 PM PST}
- UPDATED: Updated protein page: HTR2C {November 16, 2007 1:51:53 PM PST}
- INFO: Beginning work on MAP3K1... {November 16, 2007 1:52:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:53:07 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 =
| image_source =
| PDB =
| Name = Mitogen-activated protein kinase kinase kinase 1
| HGNCid = 6848
| Symbol = MAP3K1
| AltSymbols =; MAPKKK1; MEKK; MEKK1
| OMIM = 600982
| ECnumber =
| Homologene = 8056
| MGIid = 1346872
| GeneAtlas_image1 = PBB_GE_MAP3K1_214786_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004709 |text = MAP kinase kinase kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007179 |text = transforming growth factor beta receptor signaling pathway}} {{GNF_GO|id=GO:0008637 |text = apoptotic mitochondrial changes}} {{GNF_GO|id=GO:0030334 |text = regulation of cell migration}} {{GNF_GO|id=GO:0030838 |text = positive regulation of actin filament polymerization}} {{GNF_GO|id=GO:0042060 |text = wound healing}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4214
| Hs_Ensembl = ENSG00000095015
| Hs_RefseqProtein = XP_001128827
| Hs_RefseqmRNA = XM_001128827
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 56147216
| Hs_GenLoc_end = 56225472
| Hs_Uniprot = Q13233
| Mm_EntrezGene = 26401
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011945
| Mm_RefseqProtein = NP_036075
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Mitogen-activated protein kinase kinase kinase 1''', also known as '''MAP3K1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAP3K1 mitogen-activated protein kinase kinase kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4214| 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 = MAP3K, or MEK kinase, is a serine/threonine kinase that occupies a pivotal role in a network of phosphorylating enzymes integrating cellular responses to a number of mitogenic and metabolic stimuli, including insulin (MIM 176730) and many growth factors.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: MAP3K1 mitogen-activated protein kinase kinase kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4214| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vinik BS, Kay ES, Fiedorek FT |title=Mapping of the MEK kinase gene (Mekk) to mouse chromosome 13 and human chromosome 5. |journal=Mamm. Genome |volume=6 |issue= 11 |pages= 782-3 |year= 1996 |pmid= 8597633 |doi= }}
*{{cite journal | author=Lee FS, Hagler J, Chen ZJ, Maniatis T |title=Activation of the IkappaB alpha kinase complex by MEKK1, a kinase of the JNK pathway. |journal=Cell |volume=88 |issue= 2 |pages= 213-22 |year= 1997 |pmid= 9008162 |doi= }}
*{{cite journal | author=Siow YL, Kalmar GB, Sanghera JS, ''et al.'' |title=Identification of two essential phosphorylated threonine residues in the catalytic domain of Mekk1. Indirect activation by Pak3 and protein kinase C. |journal=J. Biol. Chem. |volume=272 |issue= 12 |pages= 7586-94 |year= 1997 |pmid= 9065412 |doi= }}
*{{cite journal | author=Su YC, Han J, Xu S, ''et al.'' |title=NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain. |journal=EMBO J. |volume=16 |issue= 6 |pages= 1279-90 |year= 1997 |pmid= 9135144 |doi= 10.1093/emboj/16.6.1279 }}
*{{cite journal | author=Wu Z, Wu J, Jacinto E, Karin M |title=Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7407-16 |year= 1997 |pmid= 9372971 |doi= }}
*{{cite journal | author=Xu S, Cobb MH |title=MEKK1 binds directly to the c-Jun N-terminal kinases/stress-activated protein kinases. |journal=J. Biol. Chem. |volume=272 |issue= 51 |pages= 32056-60 |year= 1998 |pmid= 9405400 |doi= }}
*{{cite journal | author=Fanger GR, Widmann C, Porter AC, ''et al.'' |title=14-3-3 proteins interact with specific MEK kinases. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3476-83 |year= 1998 |pmid= 9452471 |doi= }}
*{{cite journal | author=Hirai S, Noda K, Moriguchi T, ''et al.'' |title=Differential activation of two JNK activators, MKK7 and SEK1, by MKN28-derived nonreceptor serine/threonine kinase/mixed lineage kinase 2. |journal=J. Biol. Chem. |volume=273 |issue= 13 |pages= 7406-12 |year= 1998 |pmid= 9516438 |doi= }}
*{{cite journal | author=Saltzman A, Searfoss G, Marcireau C, ''et al.'' |title=hUBC9 associates with MEKK1 and type I TNF-alpha receptor and stimulates NFkappaB activity. |journal=FEBS Lett. |volume=425 |issue= 3 |pages= 431-5 |year= 1998 |pmid= 9563508 |doi= }}
*{{cite journal | author=Guan Z, Buckman SY, Pentland AP, ''et al.'' |title=Induction of cyclooxygenase-2 by the activated MEKK1 --> SEK1/MKK4 --> p38 mitogen-activated protein kinase pathway. |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 12901-8 |year= 1998 |pmid= 9582321 |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=Yuasa T, Ohno S, Kehrl JH, Kyriakis JM |title=Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase (JNK) and p38. Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/ERK kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38. |journal=J. Biol. Chem. |volume=273 |issue= 35 |pages= 22681-92 |year= 1998 |pmid= 9712898 |doi= }}
*{{cite journal | author=Pomérance M, Multon MC, Parker F, ''et al.'' |title=Grb2 interaction with MEK-kinase 1 is involved in regulation of Jun-kinase activities in response to epidermal growth factor. |journal=J. Biol. Chem. |volume=273 |issue= 38 |pages= 24301-4 |year= 1998 |pmid= 9733714 |doi= }}
*{{cite journal | author=Xia Y, Wu Z, Su B, ''et al.'' |title=JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension. |journal=Genes Dev. |volume=12 |issue= 21 |pages= 3369-81 |year= 1998 |pmid= 9808624 |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=Yujiri T, Sather S, Fanger GR, Johnson GL |title=Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption. |journal=Science |volume=282 |issue= 5395 |pages= 1911-4 |year= 1998 |pmid= 9836645 |doi= }}
*{{cite journal | author=Baud V, Liu ZG, Bennett B, ''et al.'' |title=Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain. |journal=Genes Dev. |volume=13 |issue= 10 |pages= 1297-308 |year= 1999 |pmid= 10346818 |doi= }}
*{{cite journal | author=Kopp E, Medzhitov R, Carothers J, ''et al.'' |title=ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway. |journal=Genes Dev. |volume=13 |issue= 16 |pages= 2059-71 |year= 1999 |pmid= 10465784 |doi= }}
*{{cite journal | author=Ito M, Yoshioka K, Akechi M, ''et al.'' |title=JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway. |journal=Mol. Cell. Biol. |volume=19 |issue= 11 |pages= 7539-48 |year= 1999 |pmid= 10523642 |doi= }}
*{{cite journal | author=Minamino T, Yujiri T, Papst PJ, ''et al.'' |title=MEKK1 suppresses oxidative stress-induced apoptosis of embryonic stem cell-derived cardiac myocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 26 |pages= 15127-32 |year= 2000 |pmid= 10611349 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAPKAPK2... {November 16, 2007 1:58:09 PM PST}
- SEARCH REDIRECT: Control Box Found: MAPKAPK2 {November 16, 2007 1:58:37 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:58:38 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:58:38 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:58:38 PM PST}
- UPDATED: Updated protein page: MAPKAPK2 {November 16, 2007 1:58:44 PM PST}
- INFO: Beginning work on ND4L... {November 16, 2007 1:53:07 PM PST}
- SEARCH REDIRECT: Control Box Found: ND4L {November 16, 2007 1:53:27 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:53:30 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:53:30 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:53:30 PM PST}
- UPDATED: Updated protein page: ND4L {November 16, 2007 1:53:35 PM PST}
- INFO: Beginning work on PTBP1... {November 16, 2007 1:53:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:54:31 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_PTBP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qm9.
| PDB = {{PDB2|1qm9}}, {{PDB2|1sjq}}, {{PDB2|1sjr}}, {{PDB2|2ad9}}, {{PDB2|2adb}}, {{PDB2|2adc}}, {{PDB2|2evz}}
| Name = Polypyrimidine tract binding protein 1
| HGNCid = 9583
| Symbol = PTBP1
| AltSymbols =; HNRNPI; HNRPI; MGC10830; MGC8461; PTB; PTB-1; PTB-T; PTB2; PTB3; PTB4; pPTB
| OMIM = 600693
| ECnumber =
| Homologene = 49188
| MGIid = 97791
| GeneAtlas_image1 = PBB_GE_PTBP1_212016_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTBP1_202189_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTBP1_211270_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008187 |text = poly-pyrimidine tract binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0030530 |text = heterogeneous nuclear ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5725
| Hs_Ensembl = ENSG00000011304
| Hs_RefseqProtein = NP_002810
| Hs_RefseqmRNA = NM_002819
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 748411
| Hs_GenLoc_end = 763327
| Hs_Uniprot = P26599
| Mm_EntrezGene = 19205
| Mm_Ensembl = ENSMUSG00000006498
| Mm_RefseqmRNA = NM_001077363
| Mm_RefseqProtein = NP_001070831
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 79257797
| Mm_GenLoc_end = 79267561
| Mm_Uniprot = Q8C2R5
}}
}}
'''Polypyrimidine tract binding protein 1''', also known as '''PTBP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTBP1 polypyrimidine tract binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5725| 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 belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has four repeats of quasi-RNA recognition motif (RRM) domains that bind RNAs. This protein binds to the intronic polypyrimidine tracts that requires pre-mRNA splicing and acts via the protein degradation ubiquitin-proteasome pathway. It may also promote the binding of U2 snRNP to pre-mRNAs. This protein is localized in the nucleoplasm and it is also detected in the perinucleolar structure. Alternatively spliced transcript variants encoding different isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: PTBP1 polypyrimidine tract binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5725| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{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=Ghetti A, Piñol-Roma S, Michael WM, ''et al.'' |title=hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear localization and association with hnRNAs. |journal=Nucleic Acids Res. |volume=20 |issue= 14 |pages= 3671-8 |year= 1992 |pmid= 1641332 |doi= }}
*{{cite journal | author=Gil A, Sharp PA, Jamison SF, Garcia-Blanco MA |title=Characterization of cDNAs encoding the polypyrimidine tract-binding protein. |journal=Genes Dev. |volume=5 |issue= 7 |pages= 1224-36 |year= 1991 |pmid= 1906035 |doi= }}
*{{cite journal | author=Patton JG, Mayer SA, Tempst P, Nadal-Ginard B |title=Characterization and molecular cloning of polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing. |journal=Genes Dev. |volume=5 |issue= 7 |pages= 1237-51 |year= 1991 |pmid= 1906036 |doi= }}
*{{cite journal | author=Raimondi E, Romanelli MG, Moralli D, ''et al.'' |title=Assignment of the human gene encoding heterogeneous nuclear RNA ribonucleoprotein I (PTB) to chromosome 14q23-q24.1. |journal=Genomics |volume=27 |issue= 3 |pages= 553-5 |year= 1995 |pmid= 7558043 |doi= 10.1006/geno.1995.1093 }}
*{{cite journal | author=Patton JG, Porro EB, Galceran J, ''et al.'' |title=Cloning and characterization of PSF, a novel pre-mRNA splicing factor. |journal=Genes Dev. |volume=7 |issue= 3 |pages= 393-406 |year= 1993 |pmid= 8449401 |doi= }}
*{{cite journal | author=Wu-Baer F, Lane WS, Gaynor RB |title=Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA. |journal=J. Biol. Chem. |volume=271 |issue= 8 |pages= 4201-8 |year= 1996 |pmid= 8626763 |doi= }}
*{{cite journal | author=Black AC, Luo J, Chun S, ''et al.'' |title=Specific binding of polypyrimidine tract binding protein and hnRNP A1 to HIV-1 CRS elements. |journal=Virus Genes |volume=12 |issue= 3 |pages= 275-85 |year= 1997 |pmid= 8883365 |doi= }}
*{{cite journal | author=Huang S, Deerinck TJ, Ellisman MH, Spector DL |title=The dynamic organization of the perinucleolar compartment in the cell nucleus. |journal=J. Cell Biol. |volume=137 |issue= 5 |pages= 965-74 |year= 1997 |pmid= 9166399 |doi= }}
*{{cite journal | author=Oh YL, Hahm B, Kim YK, ''et al.'' |title=Determination of functional domains in polypyrimidine-tract-binding protein. |journal=Biochem. J. |volume=331 ( Pt 1) |issue= |pages= 169-75 |year= 1998 |pmid= 9512476 |doi= }}
*{{cite journal | author=Hahm B, Cho OH, Kim JE, ''et al.'' |title=Polypyrimidine tract-binding protein interacts with HnRNP L. |journal=FEBS Lett. |volume=425 |issue= 3 |pages= 401-6 |year= 1998 |pmid= 9563502 |doi= }}
*{{cite journal | author=Meissner M, Dechat T, Gerner C, ''et al.'' |title=Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB. |journal=J. Cell. Biochem. |volume=76 |issue= 4 |pages= 559-66 |year= 2000 |pmid= 10653975 |doi= }}
*{{cite journal | author=Kim JH, Hahm B, Kim YK, ''et al.'' |title=Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm. |journal=J. Mol. Biol. |volume=298 |issue= 3 |pages= 395-405 |year= 2000 |pmid= 10772858 |doi= 10.1006/jmbi.2000.3687 }}
*{{cite journal | author=Conte MR, Grüne T, Ghuman J, ''et al.'' |title=Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold. |journal=EMBO J. |volume=19 |issue= 12 |pages= 3132-41 |year= 2000 |pmid= 10856256 |doi= 10.1093/emboj/19.12.3132 }}
*{{cite journal | author=Markovtsov V, Nikolic JM, Goldman JA, ''et al.'' |title=Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein. |journal=Mol. Cell. Biol. |volume=20 |issue= 20 |pages= 7463-79 |year= 2000 |pmid= 11003644 |doi= }}
*{{cite journal | author=Romanelli MG, Lorenzi P, Morandi C |title=Organization of the human gene encoding heterogeneous nuclear ribonucleoprotein type I (hnRNP I) and characterization of hnRNP I related pseudogene. |journal=Gene |volume=255 |issue= 2 |pages= 267-72 |year= 2000 |pmid= 11024286 |doi= }}
*{{cite journal | author=de Vries H, Rüegsegger U, Hübner W, ''et al.'' |title=Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. |journal=EMBO J. |volume=19 |issue= 21 |pages= 5895-904 |year= 2000 |pmid= 11060040 |doi= 10.1093/emboj/19.21.5895 }}
*{{cite journal | author=Zang WQ, Li B, Huang PY, ''et al.'' |title=Role of polypyrimidine tract binding protein in the function of the hepatitis B virus posttranscriptional regulatory element. |journal=J. Virol. |volume=75 |issue= 22 |pages= 10779-86 |year= 2001 |pmid= 11602719 |doi= 10.1128/JVI.75.22.10779-10786.2001 }}
*{{cite journal | author=Hüttelmaier S, Illenberger S, Grosheva I, ''et al.'' |title=Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins. |journal=J. Cell Biol. |volume=155 |issue= 5 |pages= 775-86 |year= 2002 |pmid= 11724819 |doi= 10.1083/jcb.200105044 }}
*{{cite journal | author=Kamath RV, Leary DJ, Huang S |title=Nucleocytoplasmic shuttling of polypyrimidine tract-binding protein is uncoupled from RNA export. |journal=Mol. Biol. Cell |volume=12 |issue= 12 |pages= 3808-20 |year= 2002 |pmid= 11739782 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SCN1A... {November 16, 2007 1:54:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:55:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SCN1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1byy.
| PDB = {{PDB2|1byy}}
| Name = Sodium channel, voltage-gated, type I, alpha subunit
| HGNCid = 10585
| Symbol = SCN1A
| AltSymbols =; FEB3; GEFSP2; HBSCI; NAC1; Nav1.1; SCN1; SMEI
| OMIM = 182389
| ECnumber =
| Homologene = 21375
| MGIid = 98246
| GeneAtlas_image1 = PBB_GE_SCN1A_210383_at_tn.png
| Function = {{GNF_GO|id=GO:0005248 |text = voltage-gated sodium channel activity}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0001518 |text = voltage-gated sodium channel complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6323
| Hs_Ensembl = ENSG00000144285
| Hs_RefseqProtein = NP_008851
| Hs_RefseqmRNA = NM_006920
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 166553919
| Hs_GenLoc_end = 166638395
| Hs_Uniprot = P35498
| Mm_EntrezGene = 20265
| Mm_Ensembl = ENSMUSG00000064329
| Mm_RefseqmRNA = XM_001001733
| Mm_RefseqProtein = XP_001001733
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 66073727
| Mm_GenLoc_end = 66119125
| Mm_Uniprot =
}}
}}
'''Sodium channel, voltage-gated, type I, alpha subunit''', also known as '''SCN1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SCN1A sodium channel, voltage-gated, type I, alpha subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6323| 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 vertebrate sodium channel is a voltage-gated ion channel essential for the generation and propagation of action potentials, chiefly in nerve and muscle. Voltage-sensitive sodium channels are heteromeric complexes consisting of a large central pore-forming glycosylated alpha subunit and 2 smaller auxiliary beta subunits. Functional studies have indicated that the transmembrane alpha subunit of the brain sodium channels is sufficient for expression of functional sodium channels (Goldin et al., 1986; Isom, 2002). Brain sodium channel alpha subunits form a gene subfamily with several structurally distinct isoforms clustering on chromosome 2, types I, II (SCN2A1, MIM 182390; SCN2A2, MIM 601219); and III (SCN3A, MIM 182391). There are also several distinct sodium channel alpha subunit isoforms in skeletal and cardiac muscle (SCN4A, MIM 603967; SCN5A, MIM 600163; SCN7A, MIM 182392).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SCN1A sodium channel, voltage-gated, type I, alpha subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6323| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lerche H, Jurkat-Rott K, Lehmann-Horn F |title=Ion channels and epilepsy. |journal=Am. J. Med. Genet. |volume=106 |issue= 2 |pages= 146-59 |year= 2001 |pmid= 11579435 |doi= 10.1002/ajmg.1582 }}
*{{cite journal | author=Isom LL |title=The role of sodium channels in cell adhesion. |journal=Front. Biosci. |volume=7 |issue= |pages= 12-23 |year= 2002 |pmid= 11779698 |doi= }}
*{{cite journal | author=Kanai K, Hirose S, Oguni H, ''et al.'' |title=Effect of localization of missense mutations in SCN1A on epilepsy phenotype severity. |journal=Neurology |volume=63 |issue= 2 |pages= 329-34 |year= 2005 |pmid= 15277629 |doi= }}
*{{cite journal | author=Oguni H, Hayashi K, Osawa M, ''et al.'' |title=Severe myoclonic epilepsy in infancy: clinical analysis and relation to SCN1A mutations in a Japanese cohort. |journal=Advances in neurology |volume=95 |issue= |pages= 103-17 |year= 2004 |pmid= 15508916 |doi= }}
*{{cite journal | author=Mulley JC, Scheffer IE, Petrou S, ''et al.'' |title=SCN1A mutations and epilepsy. |journal=Hum. Mutat. |volume=25 |issue= 6 |pages= 535-42 |year= 2006 |pmid= 15880351 |doi= 10.1002/humu.20178 }}
*{{cite journal | author=Catterall WA, Goldin AL, Waxman SG |title=International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 397-409 |year= 2006 |pmid= 16382098 |doi= 10.1124/pr.57.4.4 }}
*{{cite journal | author=Lu CM, Han J, Rado TA, Brown GB |title=Differential expression of two sodium channel subtypes in human brain. |journal=FEBS Lett. |volume=303 |issue= 1 |pages= 53-8 |year= 1992 |pmid= 1317301 |doi= }}
*{{cite journal | author=Goldin AL, Snutch T, Lübbert H, ''et al.'' |title=Messenger RNA coding for only the alpha subunit of the rat brain Na channel is sufficient for expression of functional channels in Xenopus oocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 19 |pages= 7503-7 |year= 1986 |pmid= 2429308 |doi= }}
*{{cite journal | author=Malo MS, Blanchard BJ, Andresen JM, ''et al.'' |title=Localization of a putative human brain sodium channel gene (SCN1A) to chromosome band 2q24. |journal=Cytogenet. Cell Genet. |volume=67 |issue= 3 |pages= 178-86 |year= 1994 |pmid= 8062593 |doi= }}
*{{cite journal | author=Peiffer A, Thompson J, Charlier C, ''et al.'' |title=A locus for febrile seizures (FEB3) maps to chromosome 2q23-24. |journal=Ann. Neurol. |volume=46 |issue= 4 |pages= 671-8 |year= 1999 |pmid= 10514109 |doi= }}
*{{cite journal | author=Escayg A, MacDonald BT, Meisler MH, ''et al.'' |title=Mutations of SCN1A, encoding a neuronal sodium channel, in two families with GEFS+2. |journal=Nat. Genet. |volume=24 |issue= 4 |pages= 343-5 |year= 2000 |pmid= 10742094 |doi= 10.1038/74159 }}
*{{cite journal | author=Wallace RH, Scheffer IE, Barnett S, ''et al.'' |title=Neuronal sodium-channel alpha1-subunit mutations in generalized epilepsy with febrile seizures plus. |journal=Am. J. Hum. Genet. |volume=68 |issue= 4 |pages= 859-65 |year= 2001 |pmid= 11254444 |doi= }}
*{{cite journal | author=Escayg A, Heils A, MacDonald BT, ''et al.'' |title=A novel SCN1A mutation associated with generalized epilepsy with febrile seizures plus--and prevalence of variants in patients with epilepsy. |journal=Am. J. Hum. Genet. |volume=68 |issue= 4 |pages= 866-73 |year= 2001 |pmid= 11254445 |doi= }}
*{{cite journal | author=Whitaker WR, Faull RL, Waldvogel HJ, ''et al.'' |title=Comparative distribution of voltage-gated sodium channel proteins in human brain. |journal=Brain Res. Mol. Brain Res. |volume=88 |issue= 1-2 |pages= 37-53 |year= 2001 |pmid= 11295230 |doi= }}
*{{cite journal | author=Claes L, Del-Favero J, Ceulemans B, ''et al.'' |title=De novo mutations in the sodium-channel gene SCN1A cause severe myoclonic epilepsy of infancy. |journal=Am. J. Hum. Genet. |volume=68 |issue= 6 |pages= 1327-32 |year= 2001 |pmid= 11359211 |doi= }}
*{{cite journal | author=Sugawara T, Mazaki-Miyazaki E, Ito M, ''et al.'' |title=Nav1.1 mutations cause febrile seizures associated with afebrile partial seizures. |journal=Neurology |volume=57 |issue= 4 |pages= 703-5 |year= 2001 |pmid= 11524484 |doi= }}
*{{cite journal | author=Abou-Khalil B, Ge Q, Desai R, ''et al.'' |title=Partial and generalized epilepsy with febrile seizures plus and a novel SCN1A mutation. |journal=Neurology |volume=57 |issue= 12 |pages= 2265-72 |year= 2003 |pmid= 11756608 |doi= }}
*{{cite journal | author=Ito M, Nagafuji H, Okazawa H, ''et al.'' |title=Autosomal dominant epilepsy with febrile seizures plus with missense mutations of the (Na+)-channel alpha 1 subunit gene, SCN1A. |journal=Epilepsy Res. |volume=48 |issue= 1-2 |pages= 15-23 |year= 2002 |pmid= 11823106 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SDC2... {November 16, 2007 1:55:03 PM PST}
- SEARCH REDIRECT: Control Box Found: SDC2 {November 16, 2007 1:55:32 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:55:36 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:55:36 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:55:36 PM PST}
- UPDATED: Updated protein page: SDC2 {November 16, 2007 1:55:41 PM PST}
- INFO: Beginning work on SLC5A5... {November 16, 2007 1:55:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:56:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 5 (sodium iodide symporter), member 5
| HGNCid = 11040
| Symbol = SLC5A5
| AltSymbols =; NIS
| OMIM = 601843
| ECnumber =
| Homologene = 37311
| MGIid = 2149330
| GeneAtlas_image1 = PBB_GE_SLC5A5_211123_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0008507 |text = sodium:iodide symporter activity}} {{GNF_GO|id=GO:0015111 |text = iodide transmembrane transporter activity}} {{GNF_GO|id=GO:0015293 |text = symporter activity}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6528
| Hs_Ensembl = ENSG00000105641
| Hs_RefseqProtein = NP_000444
| Hs_RefseqmRNA = NM_000453
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 17843782
| Hs_GenLoc_end = 17865897
| Hs_Uniprot = Q92911
| Mm_EntrezGene = 114479
| Mm_Ensembl = ENSMUSG00000000792
| Mm_RefseqmRNA = NM_053248
| Mm_RefseqProtein = NP_444478
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 73811881
| Mm_GenLoc_end = 73821746
| Mm_Uniprot = Q99PN0
}}
}}
'''Solute carrier family 5 (sodium iodide symporter), member 5''', also known as '''SLC5A5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC5A5 solute carrier family 5 (sodium iodide symporter), member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6528| 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 sodium-iodide symporter (NIS), a member of the sodium/solute symporter family, actively transports iodide across the basolateral plasma membrane of the thyroid follicular cells.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SLC5A5 solute carrier family 5 (sodium iodide symporter), member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6528| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Fukushima K, Kaneko CR, Fuchs AF |title=The neuronal substrate of integration in the oculomotor system. |journal=Prog. Neurobiol. |volume=39 |issue= 6 |pages= 609-39 |year= 1992 |pmid= 1410443 |doi= }}
*{{cite journal | author=De La Vieja A, Dohan O, Levy O, Carrasco N |title=Molecular analysis of the sodium/iodide symporter: impact on thyroid and extrathyroid pathophysiology. |journal=Physiol. Rev. |volume=80 |issue= 3 |pages= 1083-105 |year= 2000 |pmid= 10893432 |doi= }}
*{{cite journal | author=Dohán O, De la Vieja A, Paroder V, ''et al.'' |title=The sodium/iodide Symporter (NIS): characterization, regulation, and medical significance. |journal=Endocr. Rev. |volume=24 |issue= 1 |pages= 48-77 |year= 2003 |pmid= 12588808 |doi= }}
*{{cite journal | author=Kogai T, Taki K, Brent GA |title=Enhancement of sodium/iodide symporter expression in thyroid and breast cancer. |journal=Endocr. Relat. Cancer |volume=13 |issue= 3 |pages= 797-826 |year= 2007 |pmid= 16954431 |doi= 10.1677/erc.1.01143 }}
*{{cite journal | author=Riesco-Eizaguirre G, Santisteban P |title=A perspective view of sodium iodide symporter research and its clinical implications. |journal=Eur. J. Endocrinol. |volume=155 |issue= 4 |pages= 495-512 |year= 2006 |pmid= 16990649 |doi= 10.1530/eje.1.02257 }}
*{{cite journal | author=Libert F, Passage E, Lefort A, ''et al.'' |title=Localization of human thyrotropin receptor gene to chromosome region 14q3 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=54 |issue= 1-2 |pages= 82-3 |year= 1991 |pmid= 2249482 |doi= }}
*{{cite journal | author=Albero R, Cerdan A, Sanchez Franco F |title=Congenital hypothyroidism from complete iodide transport defect: long-term evolution with iodide treatment. |journal=Postgraduate medical journal |volume=63 |issue= 746 |pages= 1043-7 |year= 1988 |pmid= 3451231 |doi= }}
*{{cite journal | author=Couch RM, Dean HJ, Winter JS |title=Congenital hypothyroidism caused by defective iodide transport. |journal=J. Pediatr. |volume=106 |issue= 6 |pages= 950-3 |year= 1985 |pmid= 3998954 |doi= }}
*{{cite journal | author=Smanik PA, Liu Q, Furminger TL, ''et al.'' |title=Cloning of the human sodium lodide symporter. |journal=Biochem. Biophys. Res. Commun. |volume=226 |issue= 2 |pages= 339-45 |year= 1996 |pmid= 8806637 |doi= }}
*{{cite journal | author=Fujiwara H, Tatsumi K, Miki K, ''et al.'' |title=Congenital hypothyroidism caused by a mutation in the Na+/I- symporter. |journal=Nat. Genet. |volume=16 |issue= 2 |pages= 124-5 |year= 1997 |pmid= 9171822 |doi= 10.1038/ng0697-124 }}
*{{cite journal | author=Smanik PA, Ryu KY, Theil KS, ''et al.'' |title=Expression, exon-intron organization, and chromosome mapping of the human sodium iodide symporter. |journal=Endocrinology |volume=138 |issue= 8 |pages= 3555-8 |year= 1997 |pmid= 9231811 |doi= }}
*{{cite journal | author=Saito T, Endo T, Kawaguchi A, ''et al.'' |title=Increased expression of the Na+/I- symporter in cultured human thyroid cells exposed to thyrotropin and in Graves' thyroid tissue. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 10 |pages= 3331-6 |year= 1997 |pmid= 9329364 |doi= }}
*{{cite journal | author=Pohlenz J, Medeiros-Neto G, Gross JL, ''et al.'' |title=Hypothyroidism in a Brazilian kindred due to iodide trapping defect caused by a homozygous mutation in the sodium/iodide symporter gene. |journal=Biochem. Biophys. Res. Commun. |volume=240 |issue= 2 |pages= 488-91 |year= 1997 |pmid= 9388506 |doi= 10.1006/bbrc.1997.7594 }}
*{{cite journal | author=Matsuda A, Kosugi S |title=A homozygous missense mutation of the sodium/iodide symporter gene causing iodide transport defect. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 12 |pages= 3966-71 |year= 1998 |pmid= 9398697 |doi= }}
*{{cite journal | author=Pohlenz J, Rosenthal IM, Weiss RE, ''et al.'' |title=Congenital hypothyroidism due to mutations in the sodium/iodide symporter. Identification of a nonsense mutation producing a downstream cryptic 3' splice site. |journal=J. Clin. Invest. |volume=101 |issue= 5 |pages= 1028-35 |year= 1998 |pmid= 9486973 |doi= }}
*{{cite journal | author=Venkataraman GM, Yatin M, Ain KB |title=Cloning of the human sodium-iodide symporter promoter and characterization in a differentiated human thyroid cell line, KAT-50. |journal=Thyroid |volume=8 |issue= 1 |pages= 63-9 |year= 1998 |pmid= 9492156 |doi= }}
*{{cite journal | author=Levy O, Ginter CS, De la Vieja A, ''et al.'' |title=Identification of a structural requirement for thyroid Na+/I- symporter (NIS) function from analysis of a mutation that causes human congenital hypothyroidism. |journal=FEBS Lett. |volume=429 |issue= 1 |pages= 36-40 |year= 1998 |pmid= 9657379 |doi= }}
*{{cite journal | author=Fujiwara H, Tatsumi K, Miki K, ''et al.'' |title=Recurrent T354P mutation of the Na+/I- symporter in patients with iodide transport defect. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 8 |pages= 2940-3 |year= 1998 |pmid= 9709973 |doi= }}
*{{cite journal | author=Kosugi S, Inoue S, Matsuda A, Jhiang SM |title=Novel, missense and loss-of-function mutations in the sodium/iodide symporter gene causing iodide transport defect in three Japanese patients. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 9 |pages= 3373-6 |year= 1998 |pmid= 9745458 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SSB... {November 16, 2007 1:56:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:56:25 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SSB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1owx.
| PDB = {{PDB2|1owx}}, {{PDB2|1s79}}, {{PDB2|1s7a}}, {{PDB2|1yty}}, {{PDB2|1zh5}}
| Name = Sjogren syndrome antigen B (autoantigen La)
| HGNCid = 11316
| Symbol = SSB
| AltSymbols =; LARP3; La
| OMIM = 109090
| ECnumber =
| Homologene = 2366
| MGIid = 98423
| GeneAtlas_image1 = PBB_GE_SSB_201138_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SSB_201139_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000049 |text = tRNA binding}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003729 |text = mRNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0006383 |text = transcription from RNA polymerase III promoter}} {{GNF_GO|id=GO:0006396 |text = RNA processing}} {{GNF_GO|id=GO:0006400 |text = tRNA modification}} {{GNF_GO|id=GO:0008334 |text = histone mRNA metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6741
| Hs_Ensembl = ENSG00000138385
| Hs_RefseqProtein = NP_003133
| Hs_RefseqmRNA = NM_003142
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 170363605
| Hs_GenLoc_end = 170376797
| Hs_Uniprot = P05455
| Mm_EntrezGene = 20823
| Mm_Ensembl = ENSMUSG00000068882
| Mm_RefseqmRNA = NM_009278
| Mm_RefseqProtein = NP_033304
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 69662419
| Mm_GenLoc_end = 69672625
| Mm_Uniprot = Q3TG93
}}
}}
'''Sjogren syndrome antigen B (autoantigen La)''', also known as '''SSB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SSB Sjogren syndrome antigen B (autoantigen La)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6741| 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 = La is involved in diverse aspects of RNA metabolism, including binding and protecting 3-prime UUU(OH) elements of newly RNA polymerase III (see MIM 606007)-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs associated with hepatitis C virus. La protein was originally defined by its reactivity with autoantibodies from patients with Sjogren syndrome (MIM 270150) and systemic lupus erythematosus (SLE; MIM 152700) (Teplova et al., 2006).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SSB Sjogren syndrome antigen B (autoantigen La)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6741| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kohsaka H, Yamamoto K, Fujii H, ''et al.'' |title=Fine epitope mapping of the human SS-B/La protein. Identification of a distinct autoepitope homologous to a viral gag polyprotein. |journal=J. Clin. Invest. |volume=85 |issue= 5 |pages= 1566-74 |year= 1990 |pmid= 1692037 |doi= }}
*{{cite journal | author=Sturgess AD, Peterson MG, McNeilage LJ, ''et al.'' |title=Characteristics and epitope mapping of a cloned human autoantigen La. |journal=J. Immunol. |volume=140 |issue= 9 |pages= 3212-8 |year= 1988 |pmid= 2452201 |doi= }}
*{{cite journal | author=Rauh AJ, Hornig H, Lührmann R |title=At least three distinct B cell epitopes reside in the C-terminal half of La protein, as determined by a recombinant DNA approach. |journal=Eur. J. Immunol. |volume=18 |issue= 12 |pages= 2049-57 |year= 1989 |pmid= 2464497 |doi= }}
*{{cite journal | author=Chan EK, Sullivan KF, Tan EM |title=Ribonucleoprotein SS-B/La belongs to a protein family with consensus sequences for RNA-binding. |journal=Nucleic Acids Res. |volume=17 |issue= 6 |pages= 2233-44 |year= 1989 |pmid= 2468131 |doi= }}
*{{cite journal | author=Gottlieb E, Steitz JA |title=Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III. |journal=EMBO J. |volume=8 |issue= 3 |pages= 851-61 |year= 1989 |pmid= 2470590 |doi= }}
*{{cite journal | author=Chambers JC, Kenan D, Martin BJ, Keene JD |title=Genomic structure and amino acid sequence domains of the human La autoantigen. |journal=J. Biol. Chem. |volume=263 |issue= 34 |pages= 18043-51 |year= 1989 |pmid= 3192525 |doi= }}
*{{cite journal | author=Chambers JC, Keene JD |title=Isolation and analysis of cDNA clones expressing human lupus La antigen. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 7 |pages= 2115-9 |year= 1985 |pmid= 3856888 |doi= }}
*{{cite journal | author=Svitkin YV, Pause A, Sonenberg N |title=La autoantigen alleviates translational repression by the 5' leader sequence of the human immunodeficiency virus type 1 mRNA. |journal=J. Virol. |volume=68 |issue= 11 |pages= 7001-7 |year= 1994 |pmid= 7933082 |doi= }}
*{{cite journal | author=Tröster H, Metzger TE, Semsei I, ''et al.'' |title=One gene, two transcripts: isolation of an alternative transcript encoding for the autoantigen La/SS-B from a cDNA library of a patient with primary Sjögrens' syndrome. |journal=J. Exp. Med. |volume=180 |issue= 6 |pages= 2059-67 |year= 1994 |pmid= 7964483 |doi= }}
*{{cite journal | author=Fan H, Sakulich AL, Goodier JL, ''et al.'' |title=Phosphorylation of the human La antigen on serine 366 can regulate recycling of RNA polymerase III transcription complexes. |journal=Cell |volume=88 |issue= 5 |pages= 707-15 |year= 1997 |pmid= 9054510 |doi= }}
*{{cite journal | author=McLaren RS, Caruccio N, Ross J |title=Human La protein: a stabilizer of histone mRNA. |journal=Mol. Cell. Biol. |volume=17 |issue= 6 |pages= 3028-36 |year= 1997 |pmid= 9154801 |doi= }}
*{{cite journal | author=Grölz D, Bachmann M |title=The nuclear autoantigen La/SS-associated antigen B: one gene, three functional mRNAs. |journal=Biochem. J. |volume=323 ( Pt 1) |issue= |pages= 151-8 |year= 1997 |pmid= 9173875 |doi= }}
*{{cite journal | author=Helsloot J, Sturgess A |title=T cell reactivity to Sjögren's syndrome related antigen La(SSB). |journal=J. Rheumatol. |volume=24 |issue= 12 |pages= 2340-7 |year= 1998 |pmid= 9415639 |doi= }}
*{{cite journal | author=Broekhuis CH, Neubauer G, van der Heijden A, ''et al.'' |title=Detailed analysis of the phosphorylation of the human La (SS-B) autoantigen. (De)phosphorylation does not affect its subcellular distribution. |journal=Biochemistry |volume=39 |issue= 11 |pages= 3023-33 |year= 2000 |pmid= 10715123 |doi= }}
*{{cite journal | author=Spångberg K, Wiklund L, Schwartz S |title=HuR, a protein implicated in oncogene and growth factor mRNA decay, binds to the 3' ends of hepatitis C virus RNA of both polarities. |journal=Virology |volume=274 |issue= 2 |pages= 378-90 |year= 2000 |pmid= 10964780 |doi= 10.1006/viro.2000.0461 }}
*{{cite journal | author=Intine RV, Sakulich AL, Koduru SB, ''et al.'' |title=Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366. |journal=Mol. Cell |volume=6 |issue= 2 |pages= 339-48 |year= 2000 |pmid= 10983981 |doi= }}
*{{cite journal | author=Nashimoto M, Nashimoto C, Tamura M, ''et al.'' |title=The inhibitory effect of the autoantigen La on in vitro 3' processing of mammalian precursor tRNAs. |journal=J. Mol. Biol. |volume=312 |issue= 5 |pages= 975-84 |year= 2001 |pmid= 11580243 |doi= 10.1006/jmbi.2001.5026 }}
*{{cite journal | author=De Nova-Ocampo M, Villegas-Sepúlveda N, del Angel RM |title=Translation elongation factor-1alpha, La, and PTB interact with the 3' untranslated region of dengue 4 virus RNA. |journal=Virology |volume=295 |issue= 2 |pages= 337-47 |year= 2002 |pmid= 12033793 |doi= 10.1006/viro.2002.1407 }}
*{{cite journal | author=Intine RV, Dundr M, Misteli T, Maraia RJ |title=Aberrant nuclear trafficking of La protein leads to disordered processing of associated precursor tRNAs. |journal=Mol. Cell |volume=9 |issue= 5 |pages= 1113-23 |year= 2002 |pmid= 12049746 |doi= }}
*{{cite journal | author=Fouraux MA, Bouvet P, Verkaart S, ''et al.'' |title=Nucleolin associates with a subset of the human Ro ribonucleoprotein complexes. |journal=J. Mol. Biol. |volume=320 |issue= 3 |pages= 475-88 |year= 2002 |pmid= 12096904 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SSTR2... {November 16, 2007 1:56:25 PM PST}
- SEARCH REDIRECT: Control Box Found: SSTR2 {November 16, 2007 1:56:48 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:56:50 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:56:50 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:56:50 PM PST}
- UPDATED: Updated protein page: SSTR2 {November 16, 2007 1:56:57 PM PST}
- INFO: Beginning work on SULT1A1... {November 16, 2007 1:56:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 1:57:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SULT1A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cjm.
| PDB = {{PDB2|1cjm}}, {{PDB2|1ls6}}, {{PDB2|1z28}}, {{PDB2|1z29}}, {{PDB2|2a3r}}, {{PDB2|2d06}}
| Name = Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1
| HGNCid = 11453
| Symbol = SULT1A1
| AltSymbols =; P-PST; HAST1/HAST2; MGC131921; MGC5163; PST; ST1A3; STP; STP1; TSPST1
| OMIM = 171150
| ECnumber =
| Homologene = 68152
| MGIid = 102896
| GeneAtlas_image1 = PBB_GE_SULT1A1_203615_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_SULT1A1_207122_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_SULT1A1_209607_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004062 |text = aryl sulfotransferase activity}} {{GNF_GO|id=GO:0008146 |text = sulfotransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006584 |text = catecholamine metabolic process}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0009308 |text = amine metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6817
| Hs_Ensembl = ENSG00000196502
| Hs_RefseqProtein = NP_001046
| Hs_RefseqmRNA = NM_001055
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 28524450
| Hs_GenLoc_end = 28542447
| Hs_Uniprot = P50225
| Mm_EntrezGene = 20887
| Mm_Ensembl = ENSMUSG00000030711
| Mm_RefseqmRNA = NM_133670
| Mm_RefseqProtein = NP_598431
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126464291
| Mm_GenLoc_end = 126467505
| Mm_Uniprot = Q91W19
}}
}}
'''Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1''', also known as '''SULT1A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SULT1A1 sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6817| 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 = Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes one of two phenol sulfotransferases with thermostable enzyme activity. Multiple alternatively spliced variants that encode two isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: SULT1A1 sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6817| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Weinshilboum RM, Otterness DM, Aksoy IA, ''et al.'' |title=Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes. |journal=FASEB J. |volume=11 |issue= 1 |pages= 3-14 |year= 1997 |pmid= 9034160 |doi= }}
*{{cite journal | author=Windmill KF, Christiansen A, Teusner JT, ''et al.'' |title=Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and immunohistochemistry. |journal=Chem. Biol. Interact. |volume=109 |issue= 1-3 |pages= 341-6 |year= 1998 |pmid= 9566757 |doi= }}
*{{cite journal | author=Glatt H, Engelke CE, Pabel U, ''et al.'' |title=Sulfotransferases: genetics and role in toxicology. |journal=Toxicol. Lett. |volume=112-113 |issue= |pages= 341-8 |year= 2000 |pmid= 10720750 |doi= }}
*{{cite journal | author=Glatt H |title=Sulfotransferases in the bioactivation of xenobiotics. |journal=Chem. Biol. Interact. |volume=129 |issue= 1-2 |pages= 141-70 |year= 2001 |pmid= 11154739 |doi= }}
*{{cite journal | author=Glatt H, Boeing H, Engelke CE, ''et al.'' |title=Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects. |journal=Mutat. Res. |volume=482 |issue= 1-2 |pages= 27-40 |year= 2001 |pmid= 11535246 |doi= }}
*{{cite journal | author=Ozawa S, Nagata K, Shimada M, ''et al.'' |title=Primary structures and properties of two related forms of aryl sulfotransferases in human liver. |journal=Pharmacogenetics |volume=5 Spec No |issue= |pages= S135-40 |year= 1995 |pmid= 7581483 |doi= }}
*{{cite journal | author=Jones AL, Hagen M, Coughtrie MW, ''et al.'' |title=Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 2 |pages= 855-62 |year= 1995 |pmid= 7695643 |doi= 10.1006/bbrc.1995.1414 }}
*{{cite journal | author=Hwang SR, Kohn AB, Hook VY |title=Molecular cloning of an isoform of phenol sulfotransferase from human brain hippocampus. |journal=Biochem. Biophys. Res. Commun. |volume=207 |issue= 2 |pages= 701-7 |year= 1995 |pmid= 7864863 |doi= }}
*{{cite journal | author=Yamazoe Y, Nagata K, Ozawa S, Kato R |title=Structural similarity and diversity of sulfotransferases. |journal=Chem. Biol. Interact. |volume=92 |issue= 1-3 |pages= 107-17 |year= 1994 |pmid= 8033246 |doi= }}
*{{cite journal | author=Falany CN, Zhuang W, Falany JL |title=Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability. |journal=Chem. Biol. Interact. |volume=92 |issue= 1-3 |pages= 57-66 |year= 1994 |pmid= 8033270 |doi= }}
*{{cite journal | author=Veronese ME, Burgess W, Zhu X, McManus ME |title=Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies. |journal=Biochem. J. |volume=302 ( Pt 2) |issue= |pages= 497-502 |year= 1994 |pmid= 8093002 |doi= }}
*{{cite journal | author=Dooley TP, Obermoeller RD, Leiter EH, ''et al.'' |title=Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2 and to mouse chromosome 7. |journal=Genomics |volume=18 |issue= 2 |pages= 440-3 |year= 1994 |pmid= 8288252 |doi= 10.1006/geno.1993.1494 }}
*{{cite journal | author=Zhu X, Veronese ME, Bernard CC, ''et al.'' |title=Identification of two human brain aryl sulfotransferase cDNAs. |journal=Biochem. Biophys. Res. Commun. |volume=195 |issue= 1 |pages= 120-7 |year= 1993 |pmid= 8363592 |doi= }}
*{{cite journal | author=Wilborn TW, Comer KA, Dooley TP, ''et al.'' |title=Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase. |journal=Mol. Pharmacol. |volume=43 |issue= 1 |pages= 70-7 |year= 1993 |pmid= 8423770 |doi= }}
*{{cite journal | author=Zhu X, Veronese ME, Sansom LN, McManus ME |title=Molecular characterisation of a human aryl sulfotransferase cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=192 |issue= 2 |pages= 671-6 |year= 1993 |pmid= 8484775 |doi= }}
*{{cite journal | author=Her C, Raftogianis R, Weinshilboum RM |title=Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization. |journal=Genomics |volume=33 |issue= 3 |pages= 409-20 |year= 1996 |pmid= 8661000 |doi= 10.1006/geno.1996.0216 }}
*{{cite journal | author=Dooley TP, Huang Z |title=Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16. |journal=Biochem. Biophys. Res. Commun. |volume=228 |issue= 1 |pages= 134-40 |year= 1996 |pmid= 8912648 |doi= 10.1006/bbrc.1996.1628 }}
*{{cite journal | author=Bernier F, Soucy P, Luu-The V |title=Human phenol sulfotransferase gene contains two alternative promoters: Structure and expression of the gene. |journal=DNA Cell Biol. |volume=15 |issue= 5 |pages= 367-75 |year= 1996 |pmid= 8924211 |doi= }}
*{{cite journal | author=Raftogianis RB, Her C, Weinshilboum RM |title=Human phenol sulfotransferase pharmacogenetics: STP1 gene cloning and structural characterization. |journal=Pharmacogenetics |volume=6 |issue= 6 |pages= 473-87 |year= 1997 |pmid= 9014197 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
