Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 19:11, 16 November 2007 (UTC)
[edit]Proteins without matches (8)
[edit]Proteins with a High Potential Match (12)
[edit]Redirected Proteins (5)
[edit]Manual Inspection (Page not found) (20)
[edit]
Protein Status Grid - Date: 19:11, 16 November 2007 (UTC)
[edit]Vebose Log - Date: 19:11, 16 November 2007 (UTC)
[edit]- INFO: Beginning work on ABCA4... {November 16, 2007 10:50:29 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:51:16 AM 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 =
| image_source =
| PDB =
| Name = ATP-binding cassette, sub-family A (ABC1), member 4
| HGNCid = 34
| Symbol = ABCA4
| AltSymbols =; ABC10; ABCR; ARMD2; CORD3; DKFZp781N1972; FFM; RMP; RP19; STGD; STGD1
| OMIM = 601691
| ECnumber =
| Homologene = 298
| MGIid = 109424
| GeneAtlas_image1 = PBB_GE_ABCA4_210082_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042626 |text = ATPase activity, coupled to transmembrane movement of substances}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007603 |text = phototransduction, visible light}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 24
| Hs_Ensembl = ENSG00000198691
| Hs_RefseqProtein = NP_000341
| Hs_RefseqmRNA = NM_000350
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 94230981
| Hs_GenLoc_end = 94359279
| Hs_Uniprot = P78363
| Mm_EntrezGene = 11304
| Mm_Ensembl = ENSMUSG00000028125
| Mm_RefseqmRNA = NM_007378
| Mm_RefseqProtein = NP_031404
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 122036482
| Mm_GenLoc_end = 122172083
| Mm_Uniprot = Q3TLK5
}}
}}
'''ATP-binding cassette, sub-family A (ABC1), member 4''', also known as '''ABCA4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ABCA4 ATP-binding cassette, sub-family A (ABC1), member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=24| 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 membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intracellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ABC1 subfamily. Members of the ABC1 subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes. This protein is a retina-specific ABC transporter with N-retinylidene-PE as a substrate. It is expressed exclusively in retina photoreceptor cells, indicating the gene product mediates transport of an essental molecule across the photoreceptor cell membrane. Mutations in this gene are found in patients diagnosed with Stargardt disease and are associated with retinitis pigmentosa-19 and macular degeneration age-related 2.<ref name="entrez">{{cite web | title = Entrez Gene: ABCA4 ATP-binding cassette, sub-family A (ABC1), member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=24| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=MacDonald IM |title=Genetic aspects of age-related macular degeneration. |journal=Can. J. Ophthalmol. |volume=40 |issue= 3 |pages= 288-92 |year= 2006 |pmid= 15947798 |doi= 10.1139/i05-002 }}
*{{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=Allikmets R, Singh N, Sun H, ''et al.'' |title=A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy. |journal=Nat. Genet. |volume=15 |issue= 3 |pages= 236-46 |year= 1997 |pmid= 9054934 |doi= 10.1038/ng0397-236 }}
*{{cite journal | author=Martínez-Mir A, Bayés M, Vilageliu L, ''et al.'' |title=A new locus for autosomal recessive retinitis pigmentosa (RP19) maps to 1p13-1p21. |journal=Genomics |volume=40 |issue= 1 |pages= 142-6 |year= 1997 |pmid= 9070931 |doi= }}
*{{cite journal | author=Azarian SM, Travis GH |title=The photoreceptor rim protein is an ABC transporter encoded by the gene for recessive Stargardt's disease (ABCR). |journal=FEBS Lett. |volume=409 |issue= 2 |pages= 247-52 |year= 1997 |pmid= 9202155 |doi= }}
*{{cite journal | author=Sun H, Nathans J |title=Stargardt's ABCR is localized to the disc membrane of retinal rod outer segments. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 15-6 |year= 1997 |pmid= 9288089 |doi= 10.1038/ng0997-15 }}
*{{cite journal | author=Allikmets R |title=A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 122 |year= 1997 |pmid= 9288113 |doi= 10.1038/ng0997-122a }}
*{{cite journal | author=Allikmets R, Shroyer NF, Singh N, ''et al.'' |title=Mutation of the Stargardt disease gene (ABCR) in age-related macular degeneration. |journal=Science |volume=277 |issue= 5333 |pages= 1805-7 |year= 1997 |pmid= 9295268 |doi= }}
*{{cite journal | author=Martínez-Mir A, Paloma E, Allikmets R, ''et al.'' |title=Retinitis pigmentosa caused by a homozygous mutation in the Stargardt disease gene ABCR. |journal=Nat. Genet. |volume=18 |issue= 1 |pages= 11-2 |year= 1998 |pmid= 9425888 |doi= 10.1038/ng0198-11 }}
*{{cite journal | author=Cremers FP, van de Pol DJ, van Driel M, ''et al.'' |title=Autosomal recessive retinitis pigmentosa and cone-rod dystrophy caused by splice site mutations in the Stargardt's disease gene ABCR. |journal=Hum. Mol. Genet. |volume=7 |issue= 3 |pages= 355-62 |year= 1998 |pmid= 9466990 |doi= }}
*{{cite journal | author=Nasonkin I, Illing M, Koehler MR, ''et al.'' |title=Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1 and identification of novel mutations in Stargardt's disease. |journal=Hum. Genet. |volume=102 |issue= 1 |pages= 21-6 |year= 1998 |pmid= 9490294 |doi= }}
*{{cite journal | author=Gerber S, Rozet JM, van de Pol TJ, ''et al.'' |title=Complete exon-intron structure of the retina-specific ATP binding transporter gene (ABCR) allows the identification of novel mutations underlying Stargardt disease. |journal=Genomics |volume=48 |issue= 1 |pages= 139-42 |year= 1998 |pmid= 9503029 |doi= 10.1006/geno.1997.5164 }}
*{{cite journal | author=Azarian SM, Megarity CF, Weng J, ''et al.'' |title=The human photoreceptor rim protein gene (ABCR): genomic structure and primer set information for mutation analysis. |journal=Hum. Genet. |volume=102 |issue= 6 |pages= 699-705 |year= 1998 |pmid= 9703434 |doi= }}
*{{cite journal | author=Rozet JM, Gerber S, Souied E, ''et al.'' |title=Spectrum of ABCR gene mutations in autosomal recessive macular dystrophies. |journal=Eur. J. Hum. Genet. |volume=6 |issue= 3 |pages= 291-5 |year= 1998 |pmid= 9781034 |doi= 10.1038/sj.ejhg/5200221 }}
*{{cite journal | author=Lewis RA, Shroyer NF, Singh N, ''et al.'' |title=Genotype/Phenotype analysis of a photoreceptor-specific ATP-binding cassette transporter gene, ABCR, in Stargardt disease. |journal=Am. J. Hum. Genet. |volume=64 |issue= 2 |pages= 422-34 |year= 1999 |pmid= 9973280 |doi= }}
*{{cite journal | author=Sun H, Molday RS, Nathans J |title=Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt disease. |journal=J. Biol. Chem. |volume=274 |issue= 12 |pages= 8269-81 |year= 1999 |pmid= 10075733 |doi= }}
*{{cite journal | author=Maugeri A, van Driel MA, van de Pol DJ, ''et al.'' |title=The 2588G-->C mutation in the ABCR gene is a mild frequent founder mutation in the Western European population and allows the classification of ABCR mutations in patients with Stargardt disease. |journal=Am. J. Hum. Genet. |volume=64 |issue= 4 |pages= 1024-35 |year= 2000 |pmid= 10090887 |doi= }}
*{{cite journal | author=Fishman GA, Stone EM, Grover S, ''et al.'' |title=Variation of clinical expression in patients with Stargardt dystrophy and sequence variations in the ABCR gene. |journal=Arch. Ophthalmol. |volume=117 |issue= 4 |pages= 504-10 |year= 1999 |pmid= 10206579 |doi= }}
*{{cite journal | author=Körschen HG, Beyermann M, Müller F, ''et al.'' |title=Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors. |journal=Nature |volume=400 |issue= 6746 |pages= 761-6 |year= 1999 |pmid= 10466724 |doi= 10.1038/23468 }}
*{{cite journal | author=Zhang K, Garibaldi DC, Kniazeva M, ''et al.'' |title=A novel mutation in the ABCR gene in four patients with autosomal recessive Stargardt disease. |journal=Am. J. Ophthalmol. |volume=128 |issue= 6 |pages= 720-4 |year= 1999 |pmid= 10612508 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADRB1... {November 16, 2007 10:51:16 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:51:54 AM PST}
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{{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 = Adrenergic, beta-1-, receptor
| HGNCid = 285
| Symbol = ADRB1
| AltSymbols =; ADRB1R; B1AR; BETA1AR; RHR
| OMIM = 109630
| ECnumber =
| Homologene = 20171
| MGIid = 87937
| GeneAtlas_image1 = PBB_GE_ADRB1_208214_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004935 |text = adrenoceptor activity}} {{GNF_GO|id=GO:0004940 |text = beta1-adrenergic receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001996 |text = positive regulation of heart contraction rate by epinephrine-norepinephrine}} {{GNF_GO|id=GO:0001997 |text = increased strength of heart contraction by epinephrine-norepinephrine}} {{GNF_GO|id=GO:0002024 |text = diet induced thermogenesis}} {{GNF_GO|id=GO:0002025 |text = norepinephrine-epinephrine vasodilation during regulation of blood pressure}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007190 |text = adenylate cyclase activation}} {{GNF_GO|id=GO:0009409 |text = response to cold}} {{GNF_GO|id=GO:0031649 |text = heat generation}} {{GNF_GO|id=GO:0040015 |text = negative regulation of body size}} {{GNF_GO|id=GO:0042596 |text = fear response}} {{GNF_GO|id=GO:0050873 |text = brown fat cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 153
| Hs_Ensembl = ENSG00000043591
| Hs_RefseqProtein = NP_000675
| Hs_RefseqmRNA = NM_000684
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 115793796
| Hs_GenLoc_end = 115796657
| Hs_Uniprot = P08588
| Mm_EntrezGene = 11554
| Mm_Ensembl = ENSMUSG00000035283
| Mm_RefseqmRNA = NM_007419
| Mm_RefseqProtein = NP_031445
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 56775622
| Mm_GenLoc_end = 56777022
| Mm_Uniprot = Q9CRR2
}}
}}
'''Adrenergic, beta-1-, receptor''', also known as '''ADRB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADRB1 adrenergic, beta-1-, receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=153| 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 adrenergic receptors (subtypes alpha 1, alpha 2, beta 1, and beta 2) are a prototypic family of guanine nucleotide binding regulatory protein-coupled receptors that mediate the physiological effects of the hormone epinephrine and the neurotransmitter norepinephrine. Specific polymorphisms in this gene have been shown to affect the resting heart rate and can be involved in heart failure.<ref name="entrez">{{cite web | title = Entrez Gene: ADRB1 adrenergic, beta-1-, receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=153| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Frielle T, Kobilka B, Lefkowitz RJ, Caron MG |title=Human beta 1- and beta 2-adrenergic receptors: structurally and functionally related receptors derived from distinct genes. |journal=Trends Neurosci. |volume=11 |issue= 7 |pages= 321-4 |year= 1989 |pmid= 2465637 |doi= }}
*{{cite journal | author=Muszkat M |title=Interethnic differences in drug response: the contribution of genetic variability in beta adrenergic receptor and cytochrome P4502C9. |journal=Clin. Pharmacol. Ther. |volume=82 |issue= 2 |pages= 215-8 |year= 2007 |pmid= 17329986 |doi= 10.1038/sj.clpt.6100142 }}
*{{cite journal | author=Yang-Feng TL, Xue FY, Zhong WW, ''et al.'' |title=Chromosomal organization of adrenergic receptor genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 4 |pages= 1516-20 |year= 1990 |pmid= 2154750 |doi= }}
*{{cite journal | author=Forse RA, Leibel R, Gagner M |title=The effect of Escherichia coli endotoxin on the adrenergic control of lipolysis in the human adipocyte. |journal=J. Surg. Res. |volume=46 |issue= 1 |pages= 41-8 |year= 1989 |pmid= 2536864 |doi= }}
*{{cite journal | author=Frielle T, Collins S, Daniel KW, ''et al.'' |title=Cloning of the cDNA for the human beta 1-adrenergic receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 22 |pages= 7920-4 |year= 1987 |pmid= 2825170 |doi= }}
*{{cite journal | author=Stiles GL, Strasser RH, Lavin TN, ''et al.'' |title=The cardiac beta-adrenergic receptor. Structural similarities of beta 1 and beta 2 receptor subtypes demonstrated by photoaffinity labeling. |journal=J. Biol. Chem. |volume=258 |issue= 13 |pages= 8443-9 |year= 1983 |pmid= 6305985 |doi= }}
*{{cite journal | author=Hoehe MR, Otterud B, Hsieh WT, ''et al.'' |title=Genetic mapping of adrenergic receptor genes in humans. |journal=J. Mol. Med. |volume=73 |issue= 6 |pages= 299-306 |year= 1995 |pmid= 7583452 |doi= }}
*{{cite journal | author=Elies R, Ferrari I, Wallukat G, ''et al.'' |title=Structural and functional analysis of the B cell epitopes recognized by anti-receptor autoantibodies in patients with Chagas' disease. |journal=J. Immunol. |volume=157 |issue= 9 |pages= 4203-11 |year= 1996 |pmid= 8892658 |doi= }}
*{{cite journal | author=Oldenhof J, Vickery R, Anafi M, ''et al.'' |title=SH3 binding domains in the dopamine D4 receptor. |journal=Biochemistry |volume=37 |issue= 45 |pages= 15726-36 |year= 1998 |pmid= 9843378 |doi= 10.1021/bi981634+ }}
*{{cite journal | author=Mason DA, Moore JD, Green SA, Liggett SB |title=A gain-of-function polymorphism in a G-protein coupling domain of the human beta1-adrenergic receptor. |journal=J. Biol. Chem. |volume=274 |issue= 18 |pages= 12670-4 |year= 1999 |pmid= 10212248 |doi= }}
*{{cite journal | author=Moore JD, Mason DA, Green SA, ''et al.'' |title=Racial differences in the frequencies of cardiac beta(1)-adrenergic receptor polymorphisms: analysis of c145A>G and c1165G>C. |journal=Hum. Mutat. |volume=14 |issue= 3 |pages= 271 |year= 1999 |pmid= 10477438 |doi= 10.1002/(SICI)1098-1004(1999)14:3<271::AID-HUMU14>3.0.CO;2-Q }}
*{{cite journal | author=Tang Y, Hu LA, Miller WE, ''et al.'' |title=Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the beta1-adrenergic receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 22 |pages= 12559-64 |year= 1999 |pmid= 10535961 |doi= }}
*{{cite journal | author=Podlowski S, Wenzel K, Luther HP, ''et al.'' |title=Beta1-adrenoceptor gene variations: a role in idiopathic dilated cardiomyopathy? |journal=J. Mol. Med. |volume=78 |issue= 2 |pages= 87-93 |year= 2000 |pmid= 10794544 |doi= }}
*{{cite journal | author=Shiina T, Kawasaki A, Nagao T, Kurose H |title=Interaction with beta-arrestin determines the difference in internalization behavor between beta1- and beta2-adrenergic receptors. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 29082-90 |year= 2000 |pmid= 10862778 |doi= 10.1074/jbc.M909757199 }}
*{{cite journal | author=Hu LA, Tang Y, Miller WE, ''et al.'' |title=beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38659-66 |year= 2001 |pmid= 10995758 |doi= 10.1074/jbc.M005938200 }}
*{{cite journal | author=Börjesson M, Magnusson Y, Hjalmarson A, Andersson B |title=A novel polymorphism in the gene coding for the beta(1)-adrenergic receptor associated with survival in patients with heart failure. |journal=Eur. Heart J. |volume=21 |issue= 22 |pages= 1853-8 |year= 2001 |pmid= 11052857 |doi= 10.1053/euhj.1999.1994 }}
*{{cite journal | author=Xu J, Paquet M, Lau AG, ''et al.'' |title=beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 41310-7 |year= 2001 |pmid= 11526121 |doi= 10.1074/jbc.M107480200 }}
*{{cite journal | author=Hu LA, Chen W, Premont RT, ''et al.'' |title=G protein-coupled receptor kinase 5 regulates beta 1-adrenergic receptor association with PSD-95. |journal=J. Biol. Chem. |volume=277 |issue= 2 |pages= 1607-13 |year= 2002 |pmid= 11700307 |doi= 10.1074/jbc.M107297200 }}
*{{cite journal | author=Ranade K, Jorgenson E, Sheu WH, ''et al.'' |title=A polymorphism in the beta1 adrenergic receptor is associated with resting heart rate. |journal=Am. J. Hum. Genet. |volume=70 |issue= 4 |pages= 935-42 |year= 2002 |pmid= 11854867 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ARNT... {November 16, 2007 10:51:54 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:52:32 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ARNT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1x0o.
| PDB = {{PDB2|1x0o}}, {{PDB2|2a24}}, {{PDB2|2b02}}
| Name = Aryl hydrocarbon receptor nuclear translocator
| HGNCid = 700
| Symbol = ARNT
| AltSymbols =; HIF-1beta; HIF1B; HIF1BETA; TANGO
| OMIM = 126110
| ECnumber =
| Homologene = 1261
| MGIid = 88071
| GeneAtlas_image1 = PBB_GE_ARNT_218221_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARNT_210828_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ARNT_218222_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005061 |text = aryl hydrocarbon receptor nuclear translocator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000060 |text = protein import into nucleus, translocation}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 405
| Hs_Ensembl = ENSG00000143437
| Hs_RefseqProtein = NP_001659
| Hs_RefseqmRNA = NM_001668
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 149048810
| Hs_GenLoc_end = 149115837
| Hs_Uniprot = P27540
| Mm_EntrezGene = 11863
| Mm_Ensembl = ENSMUSG00000015522
| Mm_RefseqmRNA = NM_001037737
| Mm_RefseqProtein = NP_001032826
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 95519792
| Mm_GenLoc_end = 95581692
| Mm_Uniprot = Q3U7X2
}}
}}
'''Aryl hydrocarbon receptor nuclear translocator''', also known as '''ARNT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARNT aryl hydrocarbon receptor nuclear translocator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=405| 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 aryl hydrocarbon (Ah) receptor is involved in the induction of several enzymes that participate in xenobiotic metabolism. The ligand-free, cytosolic form of the Ah receptor is complexed to heat shock protein 90. Binding of ligand, which includes dioxin and polycyclic aromatic hydrocarbons, results in translocation of the ligand-binding subunit only to the nucleus. Induction of enzymes involved in xenobiotic metabolism occurs through binding of the ligand-bound Ah receptor to xenobiotic responsive elements in the promoters of genes for these enzymes. This gene encodes a protein that forms a complex with the ligand-bound Ah receptor, and is required for receptor function. The encoded protein has also been identified as the beta subunit of a heterodimeric transcription factor, hypoxia-inducible factor 1 (HIF1). A t(1;12)(q21;p13) translocation, which results in a TEL-ARNT fusion protein, is associated with acute myeloblastic leukemia. Three alternatively spliced variants encoding different isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ARNT aryl hydrocarbon receptor nuclear translocator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=405| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Haase VH |title=Hypoxia-inducible factors in the kidney. |journal=Am. J. Physiol. Renal Physiol. |volume=291 |issue= 2 |pages= F271-81 |year= 2006 |pmid= 16554418 |doi= 10.1152/ajprenal.00071.2006 }}
*{{cite journal | author=Reyes H, Reisz-Porszasz S, Hankinson O |title=Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. |journal=Science |volume=256 |issue= 5060 |pages= 1193-5 |year= 1992 |pmid= 1317062 |doi= }}
*{{cite journal | author=Hoffman EC, Reyes H, Chu FF, ''et al.'' |title=Cloning of a factor required for activity of the Ah (dioxin) receptor. |journal=Science |volume=252 |issue= 5008 |pages= 954-8 |year= 1991 |pmid= 1852076 |doi= }}
*{{cite journal | author=Yamaguchi Y, Kuo MT |title=Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system. |journal=Biochem. Pharmacol. |volume=50 |issue= 8 |pages= 1295-302 |year= 1995 |pmid= 7488247 |doi= }}
*{{cite journal | author=Wang GL, Jiang BH, Rue EA, Semenza GL |title=Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 12 |pages= 5510-4 |year= 1995 |pmid= 7539918 |doi= }}
*{{cite journal | author=Lindebro MC, Poellinger L, Whitelaw ML |title=Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex. |journal=EMBO J. |volume=14 |issue= 14 |pages= 3528-39 |year= 1995 |pmid= 7628454 |doi= }}
*{{cite journal | author=Abbott BD, Probst MR, Perdew GH |title=Immunohistochemical double-staining for Ah receptor and ARNT in human embryonic palatal shelves. |journal=Teratology |volume=50 |issue= 5 |pages= 361-6 |year= 1995 |pmid= 7716743 |doi= 10.1002/tera.1420500507 }}
*{{cite journal | author=Reisz-Porszasz S, Probst MR, Fukunaga BN, Hankinson O |title=Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT). |journal=Mol. Cell. Biol. |volume=14 |issue= 9 |pages= 6075-86 |year= 1994 |pmid= 8065341 |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=Johnson B, Brooks BA, Heinzmann C, ''et al.'' |title=The Ah receptor nuclear translocator gene (ARNT) is located on q21 of human chromosome 1 and on mouse chromosome 3 near Cf-3. |journal=Genomics |volume=17 |issue= 3 |pages= 592-8 |year= 1993 |pmid= 8244375 |doi= }}
*{{cite journal | author=Whitelaw M, Pongratz I, Wilhelmsson A, ''et al.'' |title=Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. |journal=Mol. Cell. Biol. |volume=13 |issue= 4 |pages= 2504-14 |year= 1993 |pmid= 8384309 |doi= }}
*{{cite journal | author=Jiang BH, Rue E, Wang GL, ''et al.'' |title=Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 17771-8 |year= 1996 |pmid= 8663540 |doi= }}
*{{cite journal | author=Rowlands JC, McEwan IJ, Gustafsson JA |title=Trans-activation by the human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins: direct interactions with basal transcription factors. |journal=Mol. Pharmacol. |volume=50 |issue= 3 |pages= 538-48 |year= 1996 |pmid= 8794892 |doi= }}
*{{cite journal | author=Ema M, Morita M, Ikawa S, ''et al.'' |title=Two new members of the murine Sim gene family are transcriptional repressors and show different expression patterns during mouse embryogenesis. |journal=Mol. Cell. Biol. |volume=16 |issue= 10 |pages= 5865-75 |year= 1996 |pmid= 8927054 |doi= }}
*{{cite journal | author=Swanson HI, Yang J |title=Mapping the protein/DNA contact sites of the Ah receptor and Ah receptor nuclear translocator. |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31657-65 |year= 1997 |pmid= 8940186 |doi= }}
*{{cite journal | author=Probst MR, Fan CM, Tessier-Lavigne M, Hankinson O |title=Two murine homologs of the Drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4451-7 |year= 1997 |pmid= 9020169 |doi= }}
*{{cite journal | author=Hogenesch JB, Chan WK, Jackiw VH, ''et al.'' |title=Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8581-93 |year= 1997 |pmid= 9079689 |doi= }}
*{{cite journal | author=Carver LA, Bradfield CA |title=Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11452-6 |year= 1997 |pmid= 9111057 |doi= }}
*{{cite journal | author=Ema M, Taya S, Yokotani N, ''et al.'' |title=A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 9 |pages= 4273-8 |year= 1997 |pmid= 9113979 |doi= }}
*{{cite journal | author=Moffett P, Reece M, Pelletier J |title=The murine Sim-2 gene product inhibits transcription by active repression and functional interference. |journal=Mol. Cell. Biol. |volume=17 |issue= 9 |pages= 4933-47 |year= 1997 |pmid= 9271372 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCR1... {November 16, 2007 10:52:33 AM PST}
- SEARCH REDIRECT: Control Box Found: CCR1 {November 16, 2007 10:53:06 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 10:53:09 AM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 16, 2007 10:53:09 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 10:53:09 AM PST}
- UPDATED: Updated protein page: CCR1 {November 16, 2007 10:53:17 AM PST}
- INFO: Beginning work on CSF2RB... {November 16, 2007 10:53:17 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:53:45 AM 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_CSF2RB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c8p.
| PDB = {{PDB2|1c8p}}, {{PDB2|1egj}}, {{PDB2|1gh7}}, {{PDB2|2gys}}
| Name = Colony stimulating factor 2 receptor, beta, low-affinity (granulocyte-macrophage)
| HGNCid = 2436
| Symbol = CSF2RB
| AltSymbols =; CD131; CDw131; IL3RB; IL5RB
| OMIM = 138981
| ECnumber =
| Homologene = 339
| MGIid = 1339759
| GeneAtlas_image1 = PBB_GE_CSF2RB_205159_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004912 |text = interleukin-3 receptor activity}} {{GNF_GO|id=GO:0004914 |text = interleukin-5 receptor activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030526 |text = granulocyte macrophage colony-stimulating factor receptor complex}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007585 |text = respiratory gaseous exchange}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1439
| Hs_Ensembl = ENSG00000100368
| Hs_RefseqProtein = NP_000386
| Hs_RefseqmRNA = NM_000395
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 35648168
| Hs_GenLoc_end = 35664764
| Hs_Uniprot = P32927
| Mm_EntrezGene = 12983
| Mm_Ensembl = ENSMUSG00000071713
| Mm_RefseqmRNA = NM_007780
| Mm_RefseqProtein = NP_031806
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 78153275
| Mm_GenLoc_end = 78177290
| Mm_Uniprot = Q3TB34
}}
}}
'''Colony stimulating factor 2 receptor, beta, low-affinity (granulocyte-macrophage)''', also known as '''CSF2RB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CSF2RB colony stimulating factor 2 receptor, beta, low-affinity (granulocyte-macrophage)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1439| 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 = CSF2RB is a common beta chain of the high affinity receptor for IL-3, IL-5 and CSF. Defective CSF2RB has been reported to be associated with protein alveolar proteinosis<ref name="entrez">{{cite web | title = Entrez Gene: CSF2RB colony stimulating factor 2 receptor, beta, low-affinity (granulocyte-macrophage)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1439| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Shen Y, Baker E, Callen DF, ''et al.'' |title=Localization of the human GM-CSF receptor beta chain gene (CSF2RB) to chromosome 22q12.2-->q13.1. |journal=Cytogenet. Cell Genet. |volume=61 |issue= 3 |pages= 175-7 |year= 1992 |pmid= 1424804 |doi= }}
*{{cite journal | author=Tavernier J, Tuypens T, Plaetinck G, ''et al.'' |title=Molecular basis of the membrane-anchored and two soluble isoforms of the human interleukin 5 receptor alpha subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 15 |pages= 7041-5 |year= 1992 |pmid= 1495999 |doi= }}
*{{cite journal | author=Torigoe T, O'Connor R, Santoli D, Reed JC |title=Interleukin-3 regulates the activity of the LYN protein-tyrosine kinase in myeloid-committed leukemic cell lines. |journal=Blood |volume=80 |issue= 3 |pages= 617-24 |year= 1992 |pmid= 1638019 |doi= }}
*{{cite journal | author=Hayashida K, Kitamura T, Gorman DM, ''et al.'' |title=Molecular cloning of a second subunit of the receptor for human granulocyte-macrophage colony-stimulating factor (GM-CSF): reconstitution of a high-affinity GM-CSF receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 24 |pages= 9655-9 |year= 1991 |pmid= 1702217 |doi= }}
*{{cite journal | author=Kitamura T, Sato N, Arai K, Miyajima A |title=Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors. |journal=Cell |volume=66 |issue= 6 |pages= 1165-74 |year= 1991 |pmid= 1833064 |doi= }}
*{{cite journal | author=Tavernier J, Devos R, Cornelis S, ''et al.'' |title=A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF. |journal=Cell |volume=66 |issue= 6 |pages= 1175-84 |year= 1991 |pmid= 1833065 |doi= }}
*{{cite journal | author=Chiba S, Shibuya K, Piao YF, ''et al.'' |title=Identification and cellular distribution of distinct proteins forming human GM-CSF receptor. |journal=Cell Regul. |volume=1 |issue= 4 |pages= 327-35 |year= 1991 |pmid= 2151610 |doi= }}
*{{cite journal | author=DiPersio JF, Golde DW, Gasson JD |title=GM-CSF: receptor structure and transmembrane signaling. |journal=Int. J. Cell Cloning |volume=8 Suppl 1 |issue= |pages= 63-74; discussion 74-5 |year= 1990 |pmid= 2157779 |doi= }}
*{{cite journal | author=Kaushansky K, Shoemaker SG, Alfaro S, Brown C |title=Hematopoietic activity of granulocyte/macrophage colony-stimulating factor is dependent upon two distinct regions of the molecule: functional analysis based upon the activities of interspecies hybrid growth factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 4 |pages= 1213-7 |year= 1989 |pmid= 2645577 |doi= }}
*{{cite journal | author=Jenkins BJ, D'Andrea R, Gonda TJ |title=Activating point mutations in the common beta subunit of the human GM-CSF, IL-3 and IL-5 receptors suggest the involvement of beta subunit dimerization and cell type-specific molecules in signalling. |journal=EMBO J. |volume=14 |issue= 17 |pages= 4276-87 |year= 1995 |pmid= 7556069 |doi= }}
*{{cite journal | author=Li Y, Shen BF, Karanes C, ''et al.'' |title=Association between Lyn protein tyrosine kinase (p53/56lyn) and the beta subunit of the granulocyte-macrophage colony-stimulating factor (GM-CSF) receptors in a GM-CSF-dependent human megakaryocytic leukemia cell line (M-07e). |journal=J. Immunol. |volume=155 |issue= 4 |pages= 2165-74 |year= 1995 |pmid= 7636265 |doi= }}
*{{cite journal | author=Hanazono Y, Chiba S, Sasaki K, ''et al.'' |title=c-fps/fes protein-tyrosine kinase is implicated in a signaling pathway triggered by granulocyte-macrophage colony-stimulating factor and interleukin-3. |journal=EMBO J. |volume=12 |issue= 4 |pages= 1641-6 |year= 1993 |pmid= 7682176 |doi= }}
*{{cite journal | author=Zhao Y, Wagner F, Frank SJ, Kraft AS |title=The amino-terminal portion of the JAK2 protein kinase is necessary for binding and phosphorylation of the granulocyte-macrophage colony-stimulating factor receptor beta c chain. |journal=J. Biol. Chem. |volume=270 |issue= 23 |pages= 13814-8 |year= 1995 |pmid= 7775438 |doi= }}
*{{cite journal | author=Yoshimura A, Ohkubo T, Kiguchi T, ''et al.'' |title=A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors. |journal=EMBO J. |volume=14 |issue= 12 |pages= 2816-26 |year= 1995 |pmid= 7796808 |doi= }}
*{{cite journal | author=Rao P, Mufson RA |title=A membrane proximal domain of the human interleukin-3 receptor beta c subunit that signals DNA synthesis in NIH 3T3 cells specifically binds a complex of Src and Janus family tyrosine kinases and phosphatidylinositol 3-kinase. |journal=J. Biol. Chem. |volume=270 |issue= 12 |pages= 6886-93 |year= 1995 |pmid= 7896837 |doi= }}
*{{cite journal | author=D'Andrea R, Rayner J, Moretti P, ''et al.'' |title=A mutation of the common receptor subunit for interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor, and IL-5 that leads to ligand independence and tumorigenicity. |journal=Blood |volume=83 |issue= 10 |pages= 2802-8 |year= 1994 |pmid= 8180376 |doi= }}
*{{cite journal | author=Milatovich A, Kitamura T, Miyajima A, Francke U |title=Gene for the alpha-subunit of the human interleukin-3 receptor (IL3RA) localized to the X-Y pseudoautosomal region. |journal=Am. J. Hum. Genet. |volume=53 |issue= 5 |pages= 1146-53 |year= 1993 |pmid= 8213838 |doi= }}
*{{cite journal | author=Yi T, Mui AL, Krystal G, Ihle JN |title=Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis. |journal=Mol. Cell. Biol. |volume=13 |issue= 12 |pages= 7577-86 |year= 1994 |pmid= 8246974 |doi= }}
*{{cite journal | author=Lock P, Metcalf D, Nicola NA |title=Histidine-367 of the human common beta chain of the receptor is critical for high-affinity binding of human granulocyte-macrophage colony-stimulating factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 1 |pages= 252-6 |year= 1994 |pmid= 8278375 |doi= }}
*{{cite journal | author=Brizzi MF, Aronica MG, Rosso A, ''et al.'' |title=Granulocyte-macrophage colony-stimulating factor stimulates JAK2 signaling pathway and rapidly activates p93fes, STAT1 p91, and STAT3 p92 in polymorphonuclear leukocytes. |journal=J. Biol. Chem. |volume=271 |issue= 7 |pages= 3562-7 |year= 1996 |pmid= 8631962 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CXCL1... {November 16, 2007 10:56:42 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:57:13 AM 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_CXCL1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mgs.
| PDB = {{PDB2|1mgs}}, {{PDB2|1msg}}, {{PDB2|1msh}}
| Name = Chemokine (C-X-C motif) ligand 1 (melanoma growth stimulating activity, alpha)
| HGNCid = 4602
| Symbol = CXCL1
| AltSymbols =; GRO1; GROa; MGSA; MGSA alpha; MGSA-a; NAP-3; SCYB1
| OMIM = 155730
| ECnumber =
| Homologene = 84701
| MGIid = 3037818
| Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}} {{GNF_GO|id=GO:0008047 |text = enzyme activator 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}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2919
| Hs_Ensembl = ENSG00000163739
| Hs_RefseqProtein = NP_001502
| Hs_RefseqmRNA = NM_001511
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 74953973
| Hs_GenLoc_end = 74968249
| Hs_Uniprot = P09341
| Mm_EntrezGene = 330122
| Mm_Ensembl = ENSMUSG00000029379
| Mm_RefseqmRNA = NM_203320
| Mm_RefseqProtein = NP_976065
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 91861303
| Mm_GenLoc_end = 91863293
| Mm_Uniprot =
}}
}}
'''Chemokine (C-X-C motif) ligand 1 (melanoma growth stimulating activity, alpha)''', also known as '''CXCL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CXCL1 chemokine (C-X-C motif) ligand 1 (melanoma growth stimulating activity, alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2919| 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 = Chemokines are a group of small (approximately 8 to 14 kD), mostly basic, structurally related molecules that regulate cell trafficking of various types of leukocytes through interactions with a subset of 7-transmembrane, G protein-coupled receptors. Chemokines also play fundamental roles in the development, homeostasis, and function of the immune system, and they have effects on cells of the central nervous system as well as on endothelial cells involved in angiogenesis or angiostasis. Chemokines are divided into 2 major subfamilies, CXC and CC, based on the arrangement of the first 2 of the 4 conserved cysteine residues; the 2 cysteines are separated by a single amino acid in CXC chemokines and are adjacent in CC chemokines. CXC chemokines are further subdivided into ELR and non-ELR types based on the presence or absence of a glu-leu-arg sequence adjacent and N terminal to the CXC motif.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: CXCL1 chemokine (C-X-C motif) ligand 1 (melanoma growth stimulating activity, alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2919| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lee J, Horuk R, Rice GC, ''et al.'' |title=Characterization of two high affinity human interleukin-8 receptors. |journal=J. Biol. Chem. |volume=267 |issue= 23 |pages= 16283-7 |year= 1992 |pmid= 1379593 |doi= }}
*{{cite journal | author=Anisowicz A, Messineo M, Lee SW, Sager R |title=An NF-kappa B-like transcription factor mediates IL-1/TNF-alpha induction of gro in human fibroblasts. |journal=J. Immunol. |volume=147 |issue= 2 |pages= 520-7 |year= 1991 |pmid= 1906501 |doi= }}
*{{cite journal | author=Baker NE, Kucera G, Richmond A |title=Nucleotide sequence of the human melanoma growth stimulatory activity (MGSA) gene. |journal=Nucleic Acids Res. |volume=18 |issue= 21 |pages= 6453 |year= 1991 |pmid= 2129556 |doi= }}
*{{cite journal | author=Schröder JM, Persoon NL, Christophers E |title=Lipopolysaccharide-stimulated human monocytes secrete, apart from neutrophil-activating peptide 1/interleukin 8, a second neutrophil-activating protein. NH2-terminal amino acid sequence identity with melanoma growth stimulatory activity. |journal=J. Exp. Med. |volume=171 |issue= 4 |pages= 1091-100 |year= 1990 |pmid= 2182761 |doi= }}
*{{cite journal | author=Haskill S, Peace A, Morris J, ''et al.'' |title=Identification of three related human GRO genes encoding cytokine functions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 19 |pages= 7732-6 |year= 1990 |pmid= 2217207 |doi= }}
*{{cite journal | author=Golds EE, Mason P, Nyirkos P |title=Inflammatory cytokines induce synthesis and secretion of gro protein and a neutrophil chemotactic factor but not beta 2-microglobulin in human synovial cells and fibroblasts. |journal=Biochem. J. |volume=259 |issue= 2 |pages= 585-8 |year= 1989 |pmid= 2655583 |doi= }}
*{{cite journal | author=Wen DZ, Rowland A, Derynck R |title=Expression and secretion of gro/MGSA by stimulated human endothelial cells. |journal=EMBO J. |volume=8 |issue= 6 |pages= 1761-6 |year= 1989 |pmid= 2670560 |doi= }}
*{{cite journal | author=Anisowicz A, Bardwell L, Sager R |title=Constitutive overexpression of a growth-regulated gene in transformed Chinese hamster and human cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 20 |pages= 7188-92 |year= 1987 |pmid= 2890161 |doi= }}
*{{cite journal | author=Richmond A, Balentien E, Thomas HG, ''et al.'' |title=Molecular characterization and chromosomal mapping of melanoma growth stimulatory activity, a growth factor structurally related to beta-thromboglobulin. |journal=EMBO J. |volume=7 |issue= 7 |pages= 2025-33 |year= 1988 |pmid= 2970963 |doi= }}
*{{cite journal | author=Anisowicz A, Zajchowski D, Stenman G, Sager R |title=Functional diversity of gro gene expression in human fibroblasts and mammary epithelial cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 24 |pages= 9645-9 |year= 1989 |pmid= 3264403 |doi= }}
*{{cite journal | author=Koch AE, Kunkel SL, Shah MR, ''et al.'' |title=Growth-related gene product alpha. A chemotactic cytokine for neutrophils in rheumatoid arthritis. |journal=J. Immunol. |volume=155 |issue= 7 |pages= 3660-6 |year= 1995 |pmid= 7561066 |doi= }}
*{{cite journal | author=Lu ZH, Wang ZX, Horuk R, ''et al.'' |title=The promiscuous chemokine binding profile of the Duffy antigen/receptor for chemokines is primarily localized to sequences in the amino-terminal domain. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26239-45 |year= 1995 |pmid= 7592830 |doi= }}
*{{cite journal | author=Kim KS, Clark-Lewis I, Sykes BD |title=Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy. |journal=J. Biol. Chem. |volume=269 |issue= 52 |pages= 32909-15 |year= 1995 |pmid= 7806518 |doi= }}
*{{cite journal | author=Fairbrother WJ, Reilly D, Colby TJ, ''et al.'' |title=The solution structure of melanoma growth stimulating activity. |journal=J. Mol. Biol. |volume=242 |issue= 3 |pages= 252-70 |year= 1994 |pmid= 8089846 |doi= 10.1006/jmbi.1994.1577 }}
*{{cite journal | author=Horuk R, Yansura DG, Reilly D, ''et al.'' |title=Purification, receptor binding analysis, and biological characterization of human melanoma growth stimulating activity (MGSA). Evidence for a novel MGSA receptor. |journal=J. Biol. Chem. |volume=268 |issue= 1 |pages= 541-6 |year= 1993 |pmid= 8380167 |doi= }}
*{{cite journal | author=Fairbrother WJ, Reilly D, Colby T, Horuk R |title=1H assignment and secondary structure determination of human melanoma growth stimulating activity (MGSA) by NMR spectroscopy. |journal=FEBS Lett. |volume=330 |issue= 3 |pages= 302-6 |year= 1993 |pmid= 8397104 |doi= }}
*{{cite journal | author=Ahuja SK, Lee JC, Murphy PM |title=CXC chemokines bind to unique sets of selectivity determinants that can function independently and are broadly distributed on multiple domains of human interleukin-8 receptor B. Determinants of high affinity binding and receptor activation are distinct. |journal=J. Biol. Chem. |volume=271 |issue= 1 |pages= 225-32 |year= 1996 |pmid= 8550564 |doi= }}
*{{cite journal | author=Gasperini S, Calzetti F, Russo MP, ''et al.'' |title=Regulation of GRO alpha production in human granulocytes. |journal=J. Inflamm. |volume=45 |issue= 3 |pages= 143-51 |year= 1996 |pmid= 8597869 |doi= }}
*{{cite journal | author=Ahuja SK, Murphy PM |title=The CXC chemokines growth-regulated oncogene (GRO) alpha, GRObeta, GROgamma, neutrophil-activating peptide-2, and epithelial cell-derived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20545-50 |year= 1996 |pmid= 8702798 |doi= }}
*{{cite journal | author=Wu L, Ruffing N, Shi X, ''et al.'' |title=Discrete steps in binding and signaling of interleukin-8 with its receptor. |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31202-9 |year= 1997 |pmid= 8940121 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DRD3... {November 16, 2007 10:53:45 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:54:22 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Dopamine receptor D3
| HGNCid = 3024
| Symbol = DRD3
| AltSymbols =; D3DR; ETM1; FET1; MGC149204; MGC149205
| OMIM = 126451
| ECnumber =
| Homologene = 623
| MGIid = 94925
| GeneAtlas_image1 = PBB_GE_DRD3_211625_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DRD3_214559_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004952 |text = dopamine receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007212 |text = dopamine receptor signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007610 |text = behavior}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1814
| Hs_Ensembl = ENSG00000151577
| Hs_RefseqProtein = NP_000787
| Hs_RefseqmRNA = NM_000796
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 115330247
| Hs_GenLoc_end = 115380446
| Hs_Uniprot = P35462
| Mm_EntrezGene = 13490
| Mm_Ensembl = ENSMUSG00000022705
| Mm_RefseqmRNA = NM_007877
| Mm_RefseqProtein = NP_031903
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 43681574
| Mm_GenLoc_end = 43742171
| Mm_Uniprot = Q0VEC4
}}
}}
'''Dopamine receptor D3''', also known as '''DRD3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DRD3 dopamine receptor D3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1814| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the D3 subtype of the dopamine receptor. The D3 subtype inhibits adenylyl cyclase through inhibitory G-proteins. This receptor is expressed in phylogenetically older regions of the brain, suggesting that this receptor plays a role in cognitive and emotional functions. It is a target for drugs which treat schizophrenia, drug addiction, and Parkinson disease. Alternative splicing of this gene results in multiple transcript variants that would encode different isoforms, although some variants may be subject to nonsense-mediated decay (NMD).<ref name="entrez">{{cite web | title = Entrez Gene: DRD3 dopamine receptor D3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1814| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Missale C, Nash SR, Robinson SW, ''et al.'' |title=Dopamine receptors: from structure to function. |journal=Physiol. Rev. |volume=78 |issue= 1 |pages= 189-225 |year= 1998 |pmid= 9457173 |doi= }}
*{{cite journal | author=Sidhu A, Niznik HB |title=Coupling of dopamine receptor subtypes to multiple and diverse G proteins. |journal=Int. J. Dev. Neurosci. |volume=18 |issue= 7 |pages= 669-77 |year= 2000 |pmid= 10978845 |doi= }}
*{{cite journal | author=Le Coniat M, Sokoloff P, Hillion J, ''et al.'' |title=Chromosomal localization of the human D3 dopamine receptor gene. |journal=Hum. Genet. |volume=87 |issue= 5 |pages= 618-20 |year= 1991 |pmid= 1916765 |doi= }}
*{{cite journal | author=Sokoloff P, Giros B, Martres MP, ''et al.'' |title=Molecular cloning and characterization of a novel dopamine receptor (D3) as a target for neuroleptics. |journal=Nature |volume=347 |issue= 6289 |pages= 146-51 |year= 1990 |pmid= 1975644 |doi= 10.1038/347146a0 }}
*{{cite journal | author=Giros B, Martres MP, Sokoloff P, Schwartz JC |title=[Gene cloning of human dopaminergic D3 receptor and identification of its chromosome] |journal=C. R. Acad. Sci. III, Sci. Vie |volume=311 |issue= 13 |pages= 501-8 |year= 1991 |pmid= 2129115 |doi= }}
*{{cite journal | author=Liu K, Bergson C, Levenson R, Schmauss C |title=On the origin of mRNA encoding the truncated dopamine D3-type receptor D3nf and detection of D3nf-like immunoreactivity in human brain. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 29220-6 |year= 1994 |pmid= 7961889 |doi= }}
*{{cite journal | author=Schmauss C, Haroutunian V, Davis KL, Davidson M |title=Selective loss of dopamine D3-type receptor mRNA expression in parietal and motor cortices of patients with chronic schizophrenia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 19 |pages= 8942-6 |year= 1993 |pmid= 8415635 |doi= }}
*{{cite journal | author=Griffon N, Crocq MA, Pilon C, ''et al.'' |title=Dopamine D3 receptor gene: organization, transcript variants, and polymorphism associated with schizophrenia. |journal=Am. J. Med. Genet. |volume=67 |issue= 1 |pages= 63-70 |year= 1996 |pmid= 8678117 |doi= 10.1002/(SICI)1096-8628(19960216)67:1<63::AID-AJMG11>3.0.CO;2-N }}
*{{cite journal | author=Staley JK, Mash DC |title=Adaptive increase in D3 dopamine receptors in the brain reward circuits of human cocaine fatalities. |journal=J. Neurosci. |volume=16 |issue= 19 |pages= 6100-6 |year= 1996 |pmid= 8815892 |doi= }}
*{{cite journal | author=Chen CH, Liu MY, Wei FC, ''et al.'' |title=Further evidence of no association between Ser9Gly polymorphism of dopamine D3 receptor gene and schizophrenia. |journal=Am. J. Med. Genet. |volume=74 |issue= 1 |pages= 40-3 |year= 1997 |pmid= 9034004 |doi= }}
*{{cite journal | author=Gulcher JR, Jónsson P, Kong A, ''et al.'' |title=Mapping of a familial essential tremor gene, FET1, to chromosome 3q13. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 84-7 |year= 1997 |pmid= 9288103 |doi= 10.1038/ng0997-84 }}
*{{cite journal | author=Oldenhof J, Vickery R, Anafi M, ''et al.'' |title=SH3 binding domains in the dopamine D4 receptor. |journal=Biochemistry |volume=37 |issue= 45 |pages= 15726-36 |year= 1998 |pmid= 9843378 |doi= 10.1021/bi981634+ }}
*{{cite journal | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal | author=Pilla M, Perachon S, Sautel F, ''et al.'' |title=Selective inhibition of cocaine-seeking behaviour by a partial dopamine D3 receptor agonist. |journal=Nature |volume=400 |issue= 6742 |pages= 371-5 |year= 1999 |pmid= 10432116 |doi= 10.1038/22560 }}
*{{cite journal | author=Ilani T, Ben-Shachar D, Strous RD, ''et al.'' |title=A peripheral marker for schizophrenia: Increased levels of D3 dopamine receptor mRNA in blood lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 2 |pages= 625-8 |year= 2001 |pmid= 11149951 |doi= 10.1073/pnas.021535398 }}
*{{cite journal | author=Lin R, Karpa K, Kabbani N, ''et al.'' |title=Dopamine D2 and D3 receptors are linked to the actin cytoskeleton via interaction with filamin A. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 9 |pages= 5258-63 |year= 2001 |pmid= 11320256 |doi= 10.1073/pnas.011538198 }}
*{{cite journal | author=Oldenhof J, Ray A, Vickery R, Van Tol HH |title=SH3 ligands in the dopamine D3 receptor. |journal=Cell. Signal. |volume=13 |issue= 6 |pages= 411-6 |year= 2001 |pmid= 11384839 |doi= }}
*{{cite journal | author=Soma M, Nakayama K, Rahmutula D, ''et al.'' |title=Ser9Gly polymorphism in the dopamine D3 receptor gene is not associated with essential hypertension in the Japanese. |journal=Med. Sci. Monit. |volume=8 |issue= 1 |pages= CR1-4 |year= 2002 |pmid= 11796958 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on E2F4... {November 16, 2007 10:54:22 AM PST}
- SEARCH REDIRECT: Control Box Found: E2F4 {November 16, 2007 10:54:51 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 10:54:52 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 10:54:52 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 10:54:52 AM PST}
- UPDATED: Updated protein page: E2F4 {November 16, 2007 10:54:58 AM PST}
- INFO: Beginning work on EDNRA... {November 16, 2007 10:54:58 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:55:22 AM 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
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Endothelin receptor type A
| HGNCid = 3179
| Symbol = EDNRA
| AltSymbols =; ETA; ETRA
| OMIM = 131243
| ECnumber =
| Homologene = 1478
| MGIid = 105923
| GeneAtlas_image1 = PBB_GE_EDNRA_204464_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_EDNRA_204463_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_EDNRA_216235_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0001599 |text = endothelin-A receptor activity}} {{GNF_GO|id=GO:0004435 |text = phosphoinositide phospholipase C activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001569 |text = patterning of blood vessels}} {{GNF_GO|id=GO:0001666 |text = response to hypoxia}} {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0006939 |text = smooth muscle contraction}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007190 |text = adenylate cyclase activation}} {{GNF_GO|id=GO:0007202 |text = phospholipase C activation}} {{GNF_GO|id=GO:0007204 |text = elevation of cytosolic calcium ion concentration}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0007585 |text = respiratory gaseous exchange}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0014032 |text = neural crest cell development}} {{GNF_GO|id=GO:0015758 |text = glucose transport}} {{GNF_GO|id=GO:0030818 |text = negative regulation of cAMP biosynthetic process}} {{GNF_GO|id=GO:0042310 |text = vasoconstriction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1909
| Hs_Ensembl = ENSG00000151617
| Hs_RefseqProtein = NP_001948
| Hs_RefseqmRNA = NM_001957
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 148621575
| Hs_GenLoc_end = 148685555
| Hs_Uniprot = P25101
| Mm_EntrezGene = 13617
| Mm_Ensembl = ENSMUSG00000031616
| Mm_RefseqmRNA = NM_010332
| Mm_RefseqProtein = NP_034462
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 80559103
| Mm_GenLoc_end = 80620420
| Mm_Uniprot = Q61614
}}
}}
'''Endothelin receptor type A''', also known as '''EDNRA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EDNRA endothelin receptor type A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1909| 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=Arai H, Nakao K, Hosoda K, ''et al.'' |title=[Molecular cloning of human endothelin receptors and their expression in vascular endothelial cells and smooth muscle cells] |journal=Jpn. Circ. J. |volume=56 Suppl 5 |issue= |pages= 1303-7 |year= 1993 |pmid= 1291713 |doi= }}
*{{cite journal | author=Hosoda K, Nakao K, Tamura N, ''et al.'' |title=Organization, structure, chromosomal assignment, and expression of the gene encoding the human endothelin-A receptor. |journal=J. Biol. Chem. |volume=267 |issue= 26 |pages= 18797-804 |year= 1992 |pmid= 1326535 |doi= }}
*{{cite journal | author=Hayzer DJ, Rose PM, Lynch JS, ''et al.'' |title=Cloning and expression of a human endothelin receptor: subtype A. |journal=Am. J. Med. Sci. |volume=304 |issue= 4 |pages= 231-8 |year= 1992 |pmid= 1415318 |doi= }}
*{{cite journal | author=Hosoda K, Nakao K, Hiroshi-Arai, ''et al.'' |title=Cloning and expression of human endothelin-1 receptor cDNA. |journal=FEBS Lett. |volume=287 |issue= 1-2 |pages= 23-6 |year= 1991 |pmid= 1652463 |doi= }}
*{{cite journal | author=Cyr C, Huebner K, Druck T, Kris R |title=Cloning and chromosomal localization of a human endothelin ETA receptor. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 1 |pages= 184-90 |year= 1992 |pmid= 1659806 |doi= }}
*{{cite journal | author=Adachi M, Yang YY, Furuichi Y, Miyamoto C |title=Cloning and characterization of cDNA encoding human A-type endothelin receptor. |journal=Biochem. Biophys. Res. Commun. |volume=180 |issue= 3 |pages= 1265-72 |year= 1991 |pmid= 1719979 |doi= }}
*{{cite journal | author=Lin HY, Kaji EH, Winkel GK, ''et al.'' |title=Cloning and functional expression of a vascular smooth muscle endothelin 1 receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 8 |pages= 3185-9 |year= 1991 |pmid= 1849646 |doi= }}
*{{cite journal | author=Takigawa M, Sakurai T, Kasuya Y, ''et al.'' |title=Molecular identification of guanine-nucleotide-binding regulatory proteins which couple to endothelin receptors. |journal=Eur. J. Biochem. |volume=228 |issue= 1 |pages= 102-8 |year= 1995 |pmid= 7882989 |doi= }}
*{{cite journal | author=Kobayashi S, Tang R, Wang B, ''et al.'' |title=Binding and functional properties of endothelin receptor subtypes in the human prostate. |journal=Mol. Pharmacol. |volume=45 |issue= 2 |pages= 306-11 |year= 1994 |pmid= 8114678 |doi= }}
*{{cite journal | author=Yang H, Tabuchi H, Furuichi Y, Miyamoto C |title=Molecular characterization of the 5'-flanking region of human genomic ETA gene. |journal=Biochem. Biophys. Res. Commun. |volume=190 |issue= 2 |pages= 332-9 |year= 1993 |pmid= 8427579 |doi= 10.1006/bbrc.1993.1052 }}
*{{cite journal | author=Elshourbagy NA, Korman DR, Wu HL, ''et al.'' |title=Molecular characterization and regulation of the human endothelin receptors. |journal=J. Biol. Chem. |volume=268 |issue= 6 |pages= 3873-9 |year= 1993 |pmid= 8440682 |doi= }}
*{{cite journal | author=Miyamoto Y, Yoshimasa T, Arai H, ''et al.'' |title=Alternative RNA splicing of the human endothelin-A receptor generates multiple transcripts. |journal=Biochem. J. |volume=313 ( Pt 3) |issue= |pages= 795-801 |year= 1996 |pmid= 8611157 |doi= }}
*{{cite journal | author=Horstmeyer A, Cramer H, Sauer T, ''et al.'' |title=Palmitoylation of endothelin receptor A. Differential modulation of signal transduction activity by post-translational modification. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20811-9 |year= 1996 |pmid= 8702836 |doi= }}
*{{cite journal | author=Freedman NJ, Ament AS, Oppermann M, ''et al.'' |title=Phosphorylation and desensitization of human endothelin A and B receptors. Evidence for G protein-coupled receptor kinase specificity. |journal=J. Biol. Chem. |volume=272 |issue= 28 |pages= 17734-43 |year= 1997 |pmid= 9211925 |doi= }}
*{{cite journal | author=Bourgeois C, Robert B, Rebourcet R, ''et al.'' |title=Endothelin-1 and ETA receptor expression in vascular smooth muscle cells from human placenta: a new ETA receptor messenger ribonucleic acid is generated by alternative splicing of exon 3. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 9 |pages= 3116-23 |year= 1997 |pmid= 9284755 |doi= }}
*{{cite journal | author=Mao XQ, Gao PS, Roberts MH, ''et al.'' |title=Variants of endothelin-1 and its receptors in atopic asthma. |journal=Biochem. Biophys. Res. Commun. |volume=262 |issue= 1 |pages= 259-62 |year= 1999 |pmid= 10448102 |doi= 10.1006/bbrc.1999.1158 }}
*{{cite journal | author=Maggi M, Barni T, Fantoni G, ''et al.'' |title=Expression and biological effects of endothelin-1 in human gonadotropin-releasing hormone-secreting neurons. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 4 |pages= 1658-65 |year= 2000 |pmid= 10770212 |doi= }}
*{{cite journal | author=Shraga-Levine Z, Sokolovsky M |title=Functional coupling of G proteins to endothelin receptors is ligand and receptor subtype specific. |journal=Cell. Mol. Neurobiol. |volume=20 |issue= 3 |pages= 305-17 |year= 2000 |pmid= 10789830 |doi= }}
*{{cite journal | author=Lee HJ, Chun M, Kandror KV |title=Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 16597-600 |year= 2001 |pmid= 11262386 |doi= 10.1074/jbc.C000909200 }}
*{{cite journal | author=Paasche JD, Attramadal T, Sandberg C, ''et al.'' |title=Mechanisms of endothelin receptor subtype-specific targeting to distinct intracellular trafficking pathways. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 34041-50 |year= 2001 |pmid= 11382773 |doi= 10.1074/jbc.M103243200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EMD... {November 16, 2007 10:55:22 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:55:43 AM 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_EMD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jei.
| PDB = {{PDB2|1jei}}, {{PDB2|2odc}}, {{PDB2|2odg}}
| Name = Emerin (Emery-Dreifuss muscular dystrophy)
| HGNCid = 3331
| Symbol = EMD
| AltSymbols =; EDMD; STA
| OMIM = 300384
| ECnumber =
| Homologene = 91
| MGIid = 108117
| GeneAtlas_image1 = PBB_GE_EMD_209477_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007517 |text = muscle development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2010
| Hs_Ensembl = ENSG00000102119
| Hs_RefseqProtein = NP_000108
| Hs_RefseqmRNA = NM_000117
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 153260751
| Hs_GenLoc_end = 153263077
| Hs_Uniprot = P50402
| Mm_EntrezGene = 13726
| Mm_Ensembl = ENSMUSG00000001964
| Mm_RefseqmRNA = NM_007927
| Mm_RefseqProtein = NP_031953
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 70507559
| Mm_GenLoc_end = 70513529
| Mm_Uniprot = Q3TIH6
}}
}}
'''Emerin (Emery-Dreifuss muscular dystrophy)''', also known as '''EMD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EMD emerin (Emery-Dreifuss muscular dystrophy)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2010| 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 = Emerin is a serine-rich nuclear membrane protein and a member of the nuclear lamina-associated protein family. It mediates membrane anchorage to the cytoskeleton. Dreifuss-Emery muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the emerin gene.<ref name="entrez">{{cite web | title = Entrez Gene: EMD emerin (Emery-Dreifuss muscular dystrophy)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2010| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gant TM, Wilson KL |title=Nuclear assembly. |journal=Annu. Rev. Cell Dev. Biol. |volume=13 |issue= |pages= 669-95 |year= 1998 |pmid= 9442884 |doi= 10.1146/annurev.cellbio.13.1.669 }}
*{{cite journal | author=Helbling-Leclerc A, Bonne G, Schwartz K |title=Emery-Dreifuss muscular dystrophy. |journal=Eur. J. Hum. Genet. |volume=10 |issue= 3 |pages= 157-61 |year= 2002 |pmid= 11973618 |doi= 10.1038/sj.ejhg.5200744 }}
*{{cite journal | author=Holaska JM, Wilson KL |title=Multiple roles for emerin: implications for Emery-Dreifuss muscular dystrophy. |journal=The anatomical record. Part A, Discoveries in molecular, cellular, and evolutionary biology |volume=288 |issue= 7 |pages= 676-80 |year= 2006 |pmid= 16761279 |doi= 10.1002/ar.a.20334 }}
*{{cite journal | author=Bione S, Maestrini E, Rivella S, ''et al.'' |title=Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. |journal=Nat. Genet. |volume=8 |issue= 4 |pages= 323-7 |year= 1995 |pmid= 7894480 |doi= 10.1038/ng1294-323 }}
*{{cite journal | author=Bione S, Tamanini F, Maestrini E, ''et al.'' |title=Transcriptional organization of a 450-kb region of the human X chromosome in Xq28. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 23 |pages= 10977-81 |year= 1994 |pmid= 8248200 |doi= }}
*{{cite journal | author=Nagano A, Koga R, Ogawa M, ''et al.'' |title=Emerin deficiency at the nuclear membrane in patients with Emery-Dreifuss muscular dystrophy. |journal=Nat. Genet. |volume=12 |issue= 3 |pages= 254-9 |year= 1996 |pmid= 8589715 |doi= 10.1038/ng0396-254 }}
*{{cite journal | author=Bione S, Small K, Aksmanovic VM, ''et al.'' |title=Identification of new mutations in the Emery-Dreifuss muscular dystrophy gene and evidence for genetic heterogeneity of the disease. |journal=Hum. Mol. Genet. |volume=4 |issue= 10 |pages= 1859-63 |year= 1996 |pmid= 8595407 |doi= }}
*{{cite journal | author=Yamada T, Kobayashi T |title=A novel emerin mutation in a Japanese patient with Emery-Dreifuss muscular dystrophy. |journal=Hum. Genet. |volume=97 |issue= 5 |pages= 693-4 |year= 1996 |pmid= 8655156 |doi= }}
*{{cite journal | author=Chen EY, Zollo M, Mazzarella R, ''et al.'' |title=Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci. |journal=Hum. Mol. Genet. |volume=5 |issue= 5 |pages= 659-68 |year= 1997 |pmid= 8733135 |doi= }}
*{{cite journal | author=Cartegni L, di Barletta MR, Barresi R, ''et al.'' |title=Heart-specific localization of emerin: new insights into Emery-Dreifuss muscular dystrophy. |journal=Hum. Mol. Genet. |volume=6 |issue= 13 |pages= 2257-64 |year= 1998 |pmid= 9361031 |doi= }}
*{{cite journal | author=Ellis JA, Craxton M, Yates JR, Kendrick-Jones J |title=Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype. |journal=J. Cell. Sci. |volume=111 ( Pt 6) |issue= |pages= 781-92 |year= 1998 |pmid= 9472006 |doi= }}
*{{cite journal | author=Squarzoni S, Sabatelli P, Ognibene A, ''et al.'' |title=Immunocytochemical detection of emerin within the nuclear matrix. |journal=Neuromuscul. Disord. |volume=8 |issue= 5 |pages= 338-44 |year= 1998 |pmid= 9673989 |doi= }}
*{{cite journal | author=Ellis JA, Yates JR, Kendrick-Jones J, Brown CA |title=Changes at P183 of emerin weaken its protein-protein interactions resulting in X-linked Emery-Dreifuss muscular dystrophy. |journal=Hum. Genet. |volume=104 |issue= 3 |pages= 262-8 |year= 1999 |pmid= 10323252 |doi= }}
*{{cite journal | author=Clements L, Manilal S, Love DR, Morris GE |title=Direct interaction between emerin and lamin A. |journal=Biochem. Biophys. Res. Commun. |volume=267 |issue= 3 |pages= 709-14 |year= 2000 |pmid= 10673356 |doi= 10.1006/bbrc.1999.2023 }}
*{{cite journal | author=Squarzoni S, Sabatelli P, Capanni C, ''et al.'' |title=Emerin presence in platelets. |journal=Acta Neuropathol. |volume=100 |issue= 3 |pages= 291-8 |year= 2001 |pmid= 10965799 |doi= }}
*{{cite journal | author=Martins SB, Eide T, Steen RL, ''et al.'' |title=HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics. |journal=J. Cell. Sci. |volume=113 Pt 21 |issue= |pages= 3703-13 |year= 2001 |pmid= 11034899 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Sakaki M, Koike H, Takahashi N, ''et al.'' |title=Interaction between emerin and nuclear lamins. |journal=J. Biochem. |volume=129 |issue= 2 |pages= 321-7 |year= 2001 |pmid= 11173535 |doi= }}
*{{cite journal | author=Laguri C, Gilquin B, Wolff N, ''et al.'' |title=Structural characterization of the LEM motif common to three human inner nuclear membrane proteins. |journal=Structure |volume=9 |issue= 6 |pages= 503-11 |year= 2001 |pmid= 11435115 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FXN... {November 16, 2007 10:55:43 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:56:16 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FXN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ekg.
| PDB = {{PDB2|1ekg}}, {{PDB2|1ly7}}
| Name = Frataxin
| HGNCid = 3951
| Symbol = FXN
| AltSymbols =; FA; CyaY; FARR; FRDA; MGC57199; X25
| OMIM = 606829
| ECnumber =
| Homologene = 47908
| MGIid = 1096879
| GeneAtlas_image1 = PBB_GE_FXN_205565_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004428 |text = inositol or phosphatidylinositol kinase activity}} {{GNF_GO|id=GO:0005381 |text = iron ion transmembrane transporter activity}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0016192 |text = vesicle-mediated transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2395
| Hs_Ensembl = ENSG00000165060
| Hs_RefseqProtein = NP_000135
| Hs_RefseqmRNA = NM_000144
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 70839995
| Hs_GenLoc_end = 70878949
| Hs_Uniprot = Q16595
| Mm_EntrezGene = 14297
| Mm_Ensembl = ENSMUSG00000059363
| Mm_RefseqmRNA = XM_989030
| Mm_RefseqProtein = XP_994124
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 24328550
| Mm_GenLoc_end = 24347683
| Mm_Uniprot = Q3TV21
}}
}}
'''Frataxin''', also known as '''FXN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FXN frataxin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2395| 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 nuclear gene encodes a mitochondrial protein which belongs to FRATAXIN family. The protein functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: FXN frataxin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2395| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Montermini L, Rodius F, Pianese L, ''et al.'' |title=The Friedreich ataxia critical region spans a 150-kb interval on chromosome 9q13. |journal=Am. J. Hum. Genet. |volume=57 |issue= 5 |pages= 1061-7 |year= 1995 |pmid= 7485155 |doi= }}
*{{cite journal | author=Campuzano V, Montermini L, Moltò MD, ''et al.'' |title=Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. |journal=Science |volume=271 |issue= 5254 |pages= 1423-7 |year= 1996 |pmid= 8596916 |doi= }}
*{{cite journal | author=Carvajal JJ, Pook MA, dos Santos M, ''et al.'' |title=The Friedreich's ataxia gene encodes a novel phosphatidylinositol-4- phosphate 5-kinase. |journal=Nat. Genet. |volume=14 |issue= 2 |pages= 157-62 |year= 1996 |pmid= 8841185 |doi= 10.1038/ng1096-157 }}
*{{cite journal | author=Bidichandani SI, Ashizawa T, Patel PI |title=Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion. |journal=Am. J. Hum. Genet. |volume=60 |issue= 5 |pages= 1251-6 |year= 1997 |pmid= 9150176 |doi= }}
*{{cite journal | author=Babcock M, de Silva D, Oaks R, ''et al.'' |title=Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin. |journal=Science |volume=276 |issue= 5319 |pages= 1709-12 |year= 1997 |pmid= 9180083 |doi= }}
*{{cite journal | author=Koutnikova H, Campuzano V, Foury F, ''et al.'' |title=Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. |journal=Nat. Genet. |volume=16 |issue= 4 |pages= 345-51 |year= 1997 |pmid= 9241270 |doi= 10.1038/ng0897-345 }}
*{{cite journal | author=Wilson RB, Roof DM |title=Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue. |journal=Nat. Genet. |volume=16 |issue= 4 |pages= 352-7 |year= 1997 |pmid= 9241271 |doi= 10.1038/ng0897-352 }}
*{{cite journal | author=Campuzano V, Montermini L, Lutz Y, ''et al.'' |title=Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1771-80 |year= 1998 |pmid= 9302253 |doi= }}
*{{cite journal | author=Rötig A, de Lonlay P, Chretien D, ''et al.'' |title=Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. |journal=Nat. Genet. |volume=17 |issue= 2 |pages= 215-7 |year= 1997 |pmid= 9326946 |doi= 10.1038/ng1097-215 }}
*{{cite journal | author=Jiralerspong S, Liu Y, Montermini L, ''et al.'' |title=Frataxin shows developmentally regulated tissue-specific expression in the mouse embryo. |journal=Neurobiol. Dis. |volume=4 |issue= 2 |pages= 103-13 |year= 1997 |pmid= 9331900 |doi= 10.1006/nbdi.1997.0139 }}
*{{cite journal | author=Koutnikova H, Campuzano V, Koenig M |title=Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase. |journal=Hum. Mol. Genet. |volume=7 |issue= 9 |pages= 1485-9 |year= 1998 |pmid= 9700204 |doi= }}
*{{cite journal | author=Zühlke C, Laccone F, Cossée M, ''et al.'' |title=Mutation of the start codon in the FRDA1 gene: linkage analysis of three pedigrees with the ATG to ATT transversion points to a unique common ancestor. |journal=Hum. Genet. |volume=103 |issue= 1 |pages= 102-5 |year= 1998 |pmid= 9737785 |doi= }}
*{{cite journal | author=Bartolo C, Mendell JR, Prior TW |title=Identification of a missense mutation in a Friedreich's ataxia patient: implications for diagnosis and carrier studies. |journal=Am. J. Med. Genet. |volume=79 |issue= 5 |pages= 396-9 |year= 1999 |pmid= 9779809 |doi= }}
*{{cite journal | author=Cossée M, Dürr A, Schmitt M, ''et al.'' |title=Friedreich's ataxia: point mutations and clinical presentation of compound heterozygotes. |journal=Ann. Neurol. |volume=45 |issue= 2 |pages= 200-6 |year= 1999 |pmid= 9989622 |doi= }}
*{{cite journal | author=Coppola G, De Michele G, Cavalcanti F, ''et al.'' |title=Why do some Friedreich's ataxia patients retain tendon reflexes? A clinical, neurophysiological and molecular study. |journal=J. Neurol. |volume=246 |issue= 5 |pages= 353-7 |year= 1999 |pmid= 10399865 |doi= }}
*{{cite journal | author=Branda SS, Cavadini P, Adamec J, ''et al.'' |title=Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase. |journal=J. Biol. Chem. |volume=274 |issue= 32 |pages= 22763-9 |year= 1999 |pmid= 10428860 |doi= }}
*{{cite journal | author=Gordon DM, Shi Q, Dancis A, Pain D |title=Maturation of frataxin within mammalian and yeast mitochondria: one-step processing by matrix processing peptidase. |journal=Hum. Mol. Genet. |volume=8 |issue= 12 |pages= 2255-62 |year= 1999 |pmid= 10545606 |doi= }}
*{{cite journal | author=Forrest SM, Knight M, Delatycki MB, ''et al.'' |title=The correlation of clinical phenotype in Friedreich ataxia with the site of point mutations in the FRDA gene. |journal=Neurogenetics |volume=1 |issue= 4 |pages= 253-7 |year= 2000 |pmid= 10732799 |doi= }}
*{{cite journal | author=Al-Mahdawi S, Pook M, Chamberlain S |title=A novel missense mutation (L198R) in the Friedreich's ataxia gene. |journal=Hum. Mutat. |volume=16 |issue= 1 |pages= 95 |year= 2000 |pmid= 10874325 |doi= 10.1002/1098-1004(200007)16:1<95::AID-HUMU29>3.0.CO;2-E }}
*{{cite journal | author=Dhe-Paganon S, Shigeta R, Chi YI, ''et al.'' |title=Crystal structure of human frataxin. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 30753-6 |year= 2000 |pmid= 10900192 |doi= 10.1074/jbc.C000407200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GC... {November 16, 2007 10:56:16 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:56:42 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1j78.
| PDB = {{PDB2|1j78}}, {{PDB2|1j7e}}, {{PDB2|1kw2}}, {{PDB2|1kxp}}, {{PDB2|1lot}}, {{PDB2|1ma9}}
| Name = Group-specific component (vitamin D binding protein)
| HGNCid = 4187
| Symbol = GC
| AltSymbols =; DBP; DBP/GC; VDBG; VDBP
| OMIM = 139200
| ECnumber =
| Homologene = 486
| MGIid = 95669
| GeneAtlas_image1 = PBB_GE_GC_204965_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005386 |text = transmembrane transporter activity}} {{GNF_GO|id=GO:0005499 |text = vitamin D binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0051183 |text = vitamin transporter activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0042359 |text = vitamin D metabolic process}} {{GNF_GO|id=GO:0051180 |text = vitamin transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2638
| Hs_Ensembl = ENSG00000145321
| Hs_RefseqProtein = NP_000574
| Hs_RefseqmRNA = NM_000583
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 72826296
| Hs_GenLoc_end = 72868798
| Hs_Uniprot = P02774
| Mm_EntrezGene = 14473
| Mm_Ensembl = ENSMUSG00000035540
| Mm_RefseqmRNA = XM_904856
| Mm_RefseqProtein = XP_909949
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 90492721
| Mm_GenLoc_end = 90532964
| Mm_Uniprot = P21614
}}
}}
'''Group-specific component (vitamin D binding protein)''', also known as '''GC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GC group-specific component (vitamin D binding protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2638| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the albumin gene family. It is a multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid and on the surface of many cell types. It binds to vitamin D and its plasma metabolites and transports them to target tissues.<ref name="entrez">{{cite web | title = Entrez Gene: GC group-specific component (vitamin D binding protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2638| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Svasti J, Kurosky A, Bennett A, Bowman BH |title=Molecular basis for the three major forms of human serum vitamin D binding protein (group-specific component). |journal=Biochemistry |volume=18 |issue= 8 |pages= 1611-7 |year= 1979 |pmid= 218624 |doi= }}
*{{cite journal | author=Mikkelsen M, Jacobsen P, Henningsen K |title=Possible localization of Gc-System on chromosome 4. Loss of long arm 4 material associated with father-child incompatibility within the Gc-System. |journal=Hum. Hered. |volume=27 |issue= 2 |pages= 105-7 |year= 1977 |pmid= 558959 |doi= }}
*{{cite journal | author=Braun A, Bichlmaier R, Cleve H |title=Molecular analysis of the gene for the human vitamin-D-binding protein (group-specific component): allelic differences of the common genetic GC types. |journal=Hum. Genet. |volume=89 |issue= 4 |pages= 401-6 |year= 1992 |pmid= 1352271 |doi= }}
*{{cite journal | author=Esteban C, Geuskens M, Ena JM, ''et al.'' |title=Receptor-mediated uptake and processing of vitamin D-binding protein in human B-lymphoid cells. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 10177-83 |year= 1992 |pmid= 1374401 |doi= }}
*{{cite journal | author=Szpirer C, Riviere M, Cortese R, ''et al.'' |title=Chromosomal localization in man and rat of the genes encoding the liver-enriched transcription factors C/EBP, DBP, and HNF1/LFB-1 (CEBP, DBP, and transcription factor 1, TCF1, respectively) and of the hepatocyte growth factor/scatter factor gene (HGF). |journal=Genomics |volume=13 |issue= 2 |pages= 293-300 |year= 1992 |pmid= 1535333 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Yang F, Bergeron JM, Linehan LA, ''et al.'' |title=Mapping and conservation of the group-specific component gene in mouse. |journal=Genomics |volume=7 |issue= 4 |pages= 509-16 |year= 1990 |pmid= 1696927 |doi= }}
*{{cite journal | author=Yang F, Luna VJ, McAnelly RD, ''et al.'' |title=Evolutionary and structural relationships among the group-specific component, albumin and alpha-fetoprotein. |journal=Nucleic Acids Res. |volume=13 |issue= 22 |pages= 8007-17 |year= 1986 |pmid= 2415926 |doi= }}
*{{cite journal | author=Yang F, Brune JL, Naylor SL, ''et al.'' |title=Human group-specific component (Gc) is a member of the albumin family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 23 |pages= 7994-8 |year= 1986 |pmid= 2415977 |doi= }}
*{{cite journal | author=Cooke NE, David EV |title=Serum vitamin D-binding protein is a third member of the albumin and alpha fetoprotein gene family. |journal=J. Clin. Invest. |volume=76 |issue= 6 |pages= 2420-4 |year= 1986 |pmid= 2416779 |doi= }}
*{{cite journal | author=Schoentgen F, Metz-Boutigue MH, Jollès J, ''et al.'' |title=Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein. |journal=Biochim. Biophys. Acta |volume=871 |issue= 2 |pages= 189-98 |year= 1986 |pmid= 2423133 |doi= }}
*{{cite journal | author=McNearney TA, Odell C, Holers VM, ''et al.'' |title=Herpes simplex virus glycoproteins gC-1 and gC-2 bind to the third component of complement and provide protection against complement-mediated neutralization of viral infectivity. |journal=J. Exp. Med. |volume=166 |issue= 5 |pages= 1525-35 |year= 1987 |pmid= 2824652 |doi= }}
*{{cite journal | author=Yang F, Naberhaus KH, Adrian GS, ''et al.'' |title=The vitamin D-binding protein gene contains conserved nucleotide sequences that respond to heavy metal, adipocyte and mitotic signals. |journal=Gene |volume=54 |issue= 2-3 |pages= 285-90 |year= 1987 |pmid= 2958390 |doi= }}
*{{cite journal | author=Cooke NE, Willard HF, David EV, George DL |title=Direct regional assignment of the gene for vitamin D binding protein (Gc-globulin) to human chromosome 4q11-q13 and identification of an associated DNA polymorphism. |journal=Hum. Genet. |volume=73 |issue= 3 |pages= 225-9 |year= 1986 |pmid= 3015768 |doi= }}
*{{cite journal | author=Nestler JE, McLeod JF, Kowalski MA, ''et al.'' |title=Detection of vitamin D binding protein on the surface of cytotrophoblasts isolated from human placentae. |journal=Endocrinology |volume=120 |issue= 5 |pages= 1996-2002 |year= 1987 |pmid= 3552627 |doi= }}
*{{cite journal | author=Pierce EA, Dame MC, Bouillon R, ''et al.'' |title=Monoclonal antibodies to human vitamin D-binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 24 |pages= 8429-33 |year= 1986 |pmid= 3936035 |doi= }}
*{{cite journal | author=Wooten MW, Nel AE, Goldschmidt-Clermont PJ, ''et al.'' |title=Identification of a major endogenous substrate for phospholipid/Ca2+-dependent kinase in pancreatic acini as Gc (vitamin D-binding protein). |journal=FEBS Lett. |volume=191 |issue= 1 |pages= 97-101 |year= 1985 |pmid= 4054306 |doi= }}
*{{cite journal | author=Constans J, Oksman F, Viau M |title=Binding of the apo and holo forms of the serum vitamin D-binding protein to human lymphocyte cytoplasm and membrane by indirect immunofluorescence. |journal=Immunol. Lett. |volume=3 |issue= 3 |pages= 159-62 |year= 1981 |pmid= 7026425 |doi= }}
*{{cite journal | author=Braun A, Kofler A, Morawietz S, Cleve H |title=Sequence and organization of the human vitamin D-binding protein gene. |journal=Biochim. Biophys. Acta |volume=1216 |issue= 3 |pages= 385-94 |year= 1994 |pmid= 7505619 |doi= }}
*{{cite journal | author=Swamy N, Roy A, Chang R, ''et al.'' |title=Affinity purification of human plasma vitamin D-binding protein. |journal=Protein Expr. Purif. |volume=6 |issue= 2 |pages= 185-8 |year= 1995 |pmid= 7606167 |doi= 10.1006/prep.1995.1023 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GTF2H1... {November 16, 2007 10:57:58 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:58:27 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GTF2H1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1pfj.
| PDB = {{PDB2|1pfj}}, {{PDB2|2dii}}
| Name = General transcription factor IIH, polypeptide 1, 62kDa
| HGNCid = 4655
| Symbol = GTF2H1
| AltSymbols =; BTF2; TFIIH
| OMIM = 189972
| ECnumber =
| Homologene = 3885
| MGIid = 1277216
| GeneAtlas_image1 = PBB_GE_GTF2H1_202451_at_tn.png
| GeneAtlas_image2 = PBB_GE_GTF2H1_202453_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008353 |text = RNA polymerase subunit kinase activity}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005675 |text = holo TFIIH complex}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2965
| Hs_Ensembl = ENSG00000110768
| Hs_RefseqProtein = NP_005307
| Hs_RefseqmRNA = NM_005316
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 18300719
| Hs_GenLoc_end = 18345152
| Hs_Uniprot = P32780
| Mm_EntrezGene = 14884
| Mm_Ensembl = ENSMUSG00000006599
| Mm_RefseqmRNA = NM_008186
| Mm_RefseqProtein = NP_032212
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 46664145
| Mm_GenLoc_end = 46691839
| Mm_Uniprot = Q7TPY0
}}
}}
'''General transcription factor IIH, polypeptide 1, 62kDa''', also known as '''GTF2H1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GTF2H1 general transcription factor IIH, polypeptide 1, 62kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2965| 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=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24-7 |year= 1998 |pmid= 9570510 |doi= }}
*{{cite journal | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447-9 |year= 1998 |pmid= 9651670 |doi= }}
*{{cite journal | author=Fischer L, Gerard M, Chalut C, ''et al.'' |title=Cloning of the 62-kilodalton component of basic transcription factor BTF2. |journal=Science |volume=257 |issue= 5075 |pages= 1392-5 |year= 1992 |pmid= 1529339 |doi= }}
*{{cite journal | author=Shiekhattar R, Mermelstein F, Fisher RP, ''et al.'' |title=Cdk-activating kinase complex is a component of human transcription factor TFIIH. |journal=Nature |volume=374 |issue= 6519 |pages= 283-7 |year= 1995 |pmid= 7533895 |doi= 10.1038/374283a0 }}
*{{cite journal | author=Tong X, Drapkin R, Reinberg D, Kieff E |title=The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 8 |pages= 3259-63 |year= 1995 |pmid= 7724549 |doi= }}
*{{cite journal | author=Fantes JA, Oghene K, Boyle S, ''et al.'' |title=A high-resolution integrated physical, cytogenetic, and genetic map of human chromosome 11: distal p13 to proximal p15.1. |journal=Genomics |volume=25 |issue= 2 |pages= 447-61 |year= 1995 |pmid= 7789978 |doi= }}
*{{cite journal | author=Xiao H, Pearson A, Coulombe B, ''et al.'' |title=Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53. |journal=Mol. Cell. Biol. |volume=14 |issue= 10 |pages= 7013-24 |year= 1994 |pmid= 7935417 |doi= }}
*{{cite journal | author=Heng HH, Xiao H, Shi XM, ''et al.'' |title=Genes encoding general initiation factors for RNA polymerase II transcription are dispersed in the human genome. |journal=Hum. Mol. Genet. |volume=3 |issue= 1 |pages= 61-4 |year= 1994 |pmid= 8162052 |doi= }}
*{{cite journal | author=Schaeffer L, Moncollin V, Roy R, ''et al.'' |title=The ERCC2/DNA repair protein is associated with the class II BTF2/TFIIH transcription factor. |journal=EMBO J. |volume=13 |issue= 10 |pages= 2388-92 |year= 1994 |pmid= 8194528 |doi= }}
*{{cite journal | author=Blau J, Xiao H, McCracken S, ''et al.'' |title=Three functional classes of transcriptional activation domain. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 2044-55 |year= 1996 |pmid= 8628270 |doi= }}
*{{cite journal | author=Iyer N, Reagan MS, Wu KJ, ''et al.'' |title=Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. |journal=Biochemistry |volume=35 |issue= 7 |pages= 2157-67 |year= 1996 |pmid= 8652557 |doi= 10.1021/bi9524124 }}
*{{cite journal | author=Reardon JT, Ge H, Gibbs E, ''et al.'' |title=Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6482-7 |year= 1996 |pmid= 8692841 |doi= }}
*{{cite journal | author=Drapkin R, Le Roy G, Cho H, ''et al.'' |title=Human cyclin-dependent kinase-activating kinase exists in three distinct complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6488-93 |year= 1996 |pmid= 8692842 |doi= }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi= }}
*{{cite journal | author=Marinoni JC, Roy R, Vermeulen W, ''et al.'' |title=Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH. |journal=EMBO J. |volume=16 |issue= 5 |pages= 1093-102 |year= 1997 |pmid= 9118947 |doi= 10.1093/emboj/16.5.1093 }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi= }}
*{{cite journal | author=Rossignol M, Kolb-Cheynel I, Egly JM |title=Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH. |journal=EMBO J. |volume=16 |issue= 7 |pages= 1628-37 |year= 1997 |pmid= 9130708 |doi= 10.1093/emboj/16.7.1628 }}
*{{cite journal | author=García-Martínez LF, Mavankal G, Neveu JM, ''et al.'' |title=Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription. |journal=EMBO J. |volume=16 |issue= 10 |pages= 2836-50 |year= 1997 |pmid= 9184228 |doi= 10.1093/emboj/16.10.2836 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HEXB... {November 16, 2007 10:58:27 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:58:53 AM 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_HEXB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nou.
| PDB = {{PDB2|1nou}}, {{PDB2|1now}}, {{PDB2|1np0}}, {{PDB2|1o7a}}, {{PDB2|2gjx}}, {{PDB2|2gk1}}
| Name = Hexosaminidase B (beta polypeptide)
| HGNCid = 4879
| Symbol = HEXB
| AltSymbols =; ENC-1AS
| OMIM = 606873
| ECnumber =
| Homologene = 437
| MGIid = 96074
| GeneAtlas_image1 = PBB_GE_HEXB_201944_at_tn.png
| Function = {{GNF_GO|id=GO:0004563 |text = beta-N-acetylhexosaminidase activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0043169 |text = cation binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0001669 |text = acrosome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006687 |text = glycosphingolipid metabolic process}} {{GNF_GO|id=GO:0006689 |text = ganglioside catabolic process}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0007040 |text = lysosome organization and biogenesis}} {{GNF_GO|id=GO:0007341 |text = penetration of zona pellucida}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0007626 |text = locomotory behavior}} {{GNF_GO|id=GO:0008049 |text = male courtship behavior}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008654 |text = phospholipid biosynthetic process}} {{GNF_GO|id=GO:0009313 |text = oligosaccharide catabolic process}} {{GNF_GO|id=GO:0019915 |text = sequestering of lipid}} {{GNF_GO|id=GO:0019953 |text = sexual reproduction}} {{GNF_GO|id=GO:0030203 |text = glycosaminoglycan metabolic process}} {{GNF_GO|id=GO:0031323 |text = regulation of cellular metabolic process}} {{GNF_GO|id=GO:0042552 |text = myelination}} {{GNF_GO|id=GO:0044267 |text = cellular protein metabolic process}} {{GNF_GO|id=GO:0048157 |text = oogenesis}} {{GNF_GO|id=GO:0050885 |text = regulation of balance}} {{GNF_GO|id=GO:0050905 |text = neuromuscular process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3074
| Hs_Ensembl = ENSG00000049860
| Hs_RefseqProtein = NP_000512
| Hs_RefseqmRNA = NM_000521
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 74016725
| Hs_GenLoc_end = 74052869
| Hs_Uniprot = P07686
| Mm_EntrezGene = 15212
| Mm_Ensembl = ENSMUSG00000021665
| Mm_RefseqmRNA = NM_010422
| Mm_RefseqProtein = NP_034552
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 98277106
| Mm_GenLoc_end = 98298969
| Mm_Uniprot = Q3TXR9
}}
}}
'''Hexosaminidase B (beta polypeptide)''', also known as '''HEXB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HEXB hexosaminidase B (beta polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3074| 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 = Hexosaminidase B is the beta subunit of the lysosomal enzyme beta-hexosaminidase that, together with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. Beta-hexosaminidase is composed of two subunits, alpha and beta, which are encoded by separate genes. Both beta-hexosaminidase alpha and beta subunits are members of family 20 of glycosyl hydrolases. Mutations in the alpha or beta subunit genes lead to an accumulation of GM2 ganglioside in neurons and neurodegenerative disorders termed the GM2 gangliosidoses. Beta subunit gene mutations lead to Sandhoff disease (GM2-gangliosidosis type II).<ref name="entrez">{{cite web | title = Entrez Gene: HEXB hexosaminidase B (beta polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3074| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mahuran DJ |title=The biochemistry of HEXA and HEXB gene mutations causing GM2 gangliosidosis. |journal=Biochim. Biophys. Acta |volume=1096 |issue= 2 |pages= 87-94 |year= 1991 |pmid= 1825792 |doi= }}
*{{cite journal | author=Mahuran DJ |title=Biochemical consequences of mutations causing the GM2 gangliosidoses. |journal=Biochim. Biophys. Acta |volume=1455 |issue= 2-3 |pages= 105-38 |year= 1999 |pmid= 10571007 |doi= }}
*{{cite journal | author=Gilbert F, Kucherlapati R, Creagan RP, ''et al.'' |title=Tay-Sachs' and Sandhoff's diseases: the assignment of genes for hexosaminidase A and B to individual human chromosomes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=72 |issue= 1 |pages= 263-7 |year= 1975 |pmid= 1054503 |doi= }}
*{{cite journal | author=McInnes B, Potier M, Wakamatsu N, ''et al.'' |title=An unusual splicing mutation in the HEXB gene is associated with dramatically different phenotypes in patients from different racial backgrounds. |journal=J. Clin. Invest. |volume=90 |issue= 2 |pages= 306-14 |year= 1992 |pmid= 1386607 |doi= }}
*{{cite journal | author=Bolhuis PA, Bikker H |title=Deletion of the 5'-region in one or two alleles of HEXB in 15 out of 30 patients with Sandhoff disease. |journal=Hum. Genet. |volume=90 |issue= 3 |pages= 328-9 |year= 1993 |pmid= 1487253 |doi= }}
*{{cite journal | author=Wakamatsu N, Kobayashi H, Miyatake T, Tsuji S |title=A novel exon mutation in the human beta-hexosaminidase beta subunit gene affects 3' splice site selection. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2406-13 |year= 1992 |pmid= 1531140 |doi= }}
*{{cite journal | author=Banerjee P, Siciliano L, Oliveri D, ''et al.'' |title=Molecular basis of an adult form of beta-hexosaminidase B deficiency with motor neuron disease. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 1 |pages= 108-15 |year= 1992 |pmid= 1720305 |doi= }}
*{{cite journal | author=Boose JA, Tifft CJ, Proia RL, Myerowitz R |title=Synthesis of a human lysosomal enzyme, beta-hexosaminidase B, using the baculovirus expression system. |journal=Protein Expr. Purif. |volume=1 |issue= 2 |pages= 111-20 |year= 1992 |pmid= 1967020 |doi= }}
*{{cite journal | author=Mahuran DJ |title=Characterization of human placental beta-hexosaminidase I2. Proteolytic processing intermediates of hexosaminidase A. |journal=J. Biol. Chem. |volume=265 |issue= 12 |pages= 6794-9 |year= 1990 |pmid= 2139028 |doi= }}
*{{cite journal | author=Neote K, McInnes B, Mahuran DJ, Gravel RA |title=Structure and distribution of an Alu-type deletion mutation in Sandhoff disease. |journal=J. Clin. Invest. |volume=86 |issue= 5 |pages= 1524-31 |year= 1990 |pmid= 2147027 |doi= }}
*{{cite journal | author=Neote K, Brown CA, Mahuran DJ, Gravel RA |title=Translation initiation in the HEXB gene encoding the beta-subunit of human beta-hexosaminidase. |journal=J. Biol. Chem. |volume=265 |issue= 34 |pages= 20799-806 |year= 1991 |pmid= 2147427 |doi= }}
*{{cite journal | author=Dlott B, d'Azzo A, Quon DV, Neufeld EF |title=Two mutations produce intron insertion in mRNA and elongated beta-subunit of human beta-hexosaminidase. |journal=J. Biol. Chem. |volume=265 |issue= 29 |pages= 17921-7 |year= 1990 |pmid= 2170400 |doi= }}
*{{cite journal | author=Nakano T, Suzuki K |title=Genetic cause of a juvenile form of Sandhoff disease. Abnormal splicing of beta-hexosaminidase beta chain gene transcript due to a point mutation within intron 12. |journal=J. Biol. Chem. |volume=264 |issue= 9 |pages= 5155-8 |year= 1989 |pmid= 2522450 |doi= }}
*{{cite journal | author=Hubbes M, Callahan J, Gravel R, Mahuran D |title=The amino-terminal sequences in the pro-alpha and -beta polypeptides of human lysosomal beta-hexosaminidase A and B are retained in the mature isozymes. |journal=FEBS Lett. |volume=249 |issue= 2 |pages= 316-20 |year= 1989 |pmid= 2525487 |doi= }}
*{{cite journal | author=O'Dowd BF, Quan F, Willard HF, ''et al.'' |title=Isolation of cDNA clones coding for the beta subunit of human beta-hexosaminidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 4 |pages= 1184-8 |year= 1985 |pmid= 2579389 |doi= }}
*{{cite journal | author=Bikker H, van den Berg FM, Wolterman RA, ''et al.'' |title=Demonstration of a Sandhoff disease-associated autosomal 50-kb deletion by field inversion gel electrophoresis. |journal=Hum. Genet. |volume=81 |issue= 3 |pages= 287-8 |year= 1989 |pmid= 2921040 |doi= }}
*{{cite journal | author=Bolhuis PA, Oonk JG, Kamp PE, ''et al.'' |title=Ganglioside storage, hexosaminidase lability, and urinary oligosaccharides in adult Sandhoff's disease. |journal=Neurology |volume=37 |issue= 1 |pages= 75-81 |year= 1987 |pmid= 2948136 |doi= }}
*{{cite journal | author=Proia RL |title=Gene encoding the human beta-hexosaminidase beta chain: extensive homology of intron placement in the alpha- and beta-chain genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 6 |pages= 1883-7 |year= 1988 |pmid= 2964638 |doi= }}
*{{cite journal | author=Mahuran DJ, Neote K, Klavins MH, ''et al.'' |title=Proteolytic processing of pro-alpha and pro-beta precursors from human beta-hexosaminidase. Generation of the mature alpha and beta a beta b subunits. |journal=J. Biol. Chem. |volume=263 |issue= 10 |pages= 4612-8 |year= 1988 |pmid= 2965147 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HSD11B1... {November 16, 2007 10:58:53 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:59:44 AM 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_HSD11B1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xu7.
| PDB = {{PDB2|1xu7}}, {{PDB2|1xu9}}, {{PDB2|2bel}}, {{PDB2|2ilt}}, {{PDB2|2irw}}
| Name = Hydroxysteroid (11-beta) dehydrogenase 1
| HGNCid = 5208
| Symbol = HSD11B1
| AltSymbols =; 11-DH; 11-beta-HSD1; HDL; HSD11; HSD11B; HSD11L; MGC13539
| OMIM = 600713
| ECnumber =
| Homologene = 68471
| MGIid = 103562
| GeneAtlas_image1 = PBB_GE_HSD11B1_205404_at_tn.png
| Function = {{GNF_GO|id=GO:0003845 |text = 11-beta-hydroxysteroid dehydrogenase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005789 |text = endoplasmic reticulum membrane}} {{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:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008211 |text = glucocorticoid metabolic process}} {{GNF_GO|id=GO:0030324 |text = lung development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3290
| Hs_Ensembl = ENSG00000117594
| Hs_RefseqProtein = NP_005516
| Hs_RefseqmRNA = NM_005525
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 207926133
| Hs_GenLoc_end = 207974918
| Hs_Uniprot = P28845
| Mm_EntrezGene = 15483
| Mm_Ensembl = ENSMUSG00000016194
| Mm_RefseqmRNA = NM_001044751
| Mm_RefseqProtein = NP_001038216
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 194922413
| Mm_GenLoc_end = 194964769
| Mm_Uniprot = Q3TJI8
}}
}}
'''Hydroxysteroid (11-beta) dehydrogenase 1''', also known as '''HSD11B1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSD11B1 hydroxysteroid (11-beta) dehydrogenase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3290| 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 microsomal enzyme that catalyzes the conversion of the stress hormone cortisol to the inactive metabolite cortisone. In addition, the encoded protein can catalyze the reverse reaction, the conversion of cortisone to cortisol. Too much cortisol can lead to central obesity, and a particular variation in this gene has been associated with obesity and insulin resistance in children. Two transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: HSD11B1 hydroxysteroid (11-beta) dehydrogenase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3290| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=White PC, Mune T, Agarwal AK |title=11 beta-Hydroxysteroid dehydrogenase and the syndrome of apparent mineralocorticoid excess. |journal=Endocr. Rev. |volume=18 |issue= 1 |pages= 135-56 |year= 1997 |pmid= 9034789 |doi= }}
*{{cite journal | author=Agarwal AK |title=Cortisol metabolism and visceral obesity: role of 11beta-hydroxysteroid dehydrogenase type I enzyme and reduced co-factor NADPH. |journal=Endocr. Res. |volume=29 |issue= 4 |pages= 411-8 |year= 2004 |pmid= 14682470 |doi= }}
*{{cite journal | author=Tomlinson JW, Walker EA, Bujalska IJ, ''et al.'' |title=11beta-hydroxysteroid dehydrogenase type 1: a tissue-specific regulator of glucocorticoid response. |journal=Endocr. Rev. |volume=25 |issue= 5 |pages= 831-66 |year= 2005 |pmid= 15466942 |doi= 10.1210/er.2003-0031 }}
*{{cite journal | author=Odermatt A, Atanasov AG, Balazs Z, ''et al.'' |title=Why is 11beta-hydroxysteroid dehydrogenase type 1 facing the endoplasmic reticulum lumen? Physiological relevance of the membrane topology of 11beta-HSD1. |journal=Mol. Cell. Endocrinol. |volume=248 |issue= 1-2 |pages= 15-23 |year= 2006 |pmid= 16412558 |doi= 10.1016/j.mce.2005.11.040 }}
*{{cite journal | author=Wake DJ, Walker BR |title=Inhibition of 11beta-hydroxysteroid dehydrogenase type 1 in obesity. |journal=Endocrine |volume=29 |issue= 1 |pages= 101-8 |year= 2006 |pmid= 16622297 |doi= }}
*{{cite journal | author=Tannin GM, Agarwal AK, Monder C, ''et al.'' |title=The human gene for 11 beta-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization. |journal=J. Biol. Chem. |volume=266 |issue= 25 |pages= 16653-8 |year= 1991 |pmid= 1885595 |doi= }}
*{{cite journal | author=Graham DL, Oram JF |title=Identification and characterization of a high density lipoprotein-binding protein in cell membranes by ligand blotting. |journal=J. Biol. Chem. |volume=262 |issue= 16 |pages= 7439-42 |year= 1987 |pmid= 3034894 |doi= }}
*{{cite journal | author=Whorwood CB, Mason JI, Ricketts ML, ''et al.'' |title=Detection of human 11 beta-hydroxysteroid dehydrogenase isoforms using reverse-transcriptase-polymerase chain reaction and localization of the type 2 isoform to renal collecting ducts. |journal=Mol. Cell. Endocrinol. |volume=110 |issue= 1-2 |pages= R7-12 |year= 1995 |pmid= 7545619 |doi= }}
*{{cite journal | author=Mune T, Rogerson FM, Nikkilä H, ''et al.'' |title=Human hypertension caused by mutations in the kidney isozyme of 11 beta-hydroxysteroid dehydrogenase. |journal=Nat. Genet. |volume=10 |issue= 4 |pages= 394-9 |year= 1995 |pmid= 7670488 |doi= 10.1038/ng0895-394 }}
*{{cite journal | author=Ricketts ML, Verhaeg JM, Bujalska I, ''et al.'' |title=Immunohistochemical localization of type 1 11beta-hydroxysteroid dehydrogenase in human tissues. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 4 |pages= 1325-35 |year= 1998 |pmid= 9543163 |doi= }}
*{{cite journal | author=Calvo D, Gómez-Coronado D, Suárez Y, ''et al.'' |title=Human CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, and VLDL. |journal=J. Lipid Res. |volume=39 |issue= 4 |pages= 777-88 |year= 1998 |pmid= 9555943 |doi= }}
*{{cite journal | author=Odermatt A, Arnold P, Stauffer A, ''et al.'' |title=The N-terminal anchor sequences of 11beta-hydroxysteroid dehydrogenases determine their orientation in the endoplasmic reticulum membrane. |journal=J. Biol. Chem. |volume=274 |issue= 40 |pages= 28762-70 |year= 1999 |pmid= 10497248 |doi= }}
*{{cite journal | author=Sriskanda V, Schwer B, Ho CK, Shuman S |title=Mutational analysis of Escherichia coli DNA ligase identifies amino acids required for nick-ligation in vitro and for in vivo complementation of the growth of yeast cells deleted for CDC9 and LIG4. |journal=Nucleic Acids Res. |volume=27 |issue= 20 |pages= 3953-63 |year= 1999 |pmid= 10497258 |doi= }}
*{{cite journal | author=Schutte BC, Bjork BC, Coppage KB, ''et al.'' |title=A preliminary gene map for the Van der Woude syndrome critical region derived from 900 kb of genomic sequence at 1q32-q41. |journal=Genome Res. |volume=10 |issue= 1 |pages= 81-94 |year= 2000 |pmid= 10645953 |doi= }}
*{{cite journal | author=Cooper MS, Walker EA, Bland R, ''et al.'' |title=Expression and functional consequences of 11beta-hydroxysteroid dehydrogenase activity in human bone. |journal=Bone |volume=27 |issue= 3 |pages= 375-81 |year= 2000 |pmid= 10962348 |doi= }}
*{{cite journal | author=Reddy ST, Wadleigh DJ, Grijalva V, ''et al.'' |title=Human paraoxonase-3 is an HDL-associated enzyme with biological activity similar to paraoxonase-1 protein but is not regulated by oxidized lipids. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=21 |issue= 4 |pages= 542-7 |year= 2001 |pmid= 11304470 |doi= }}
*{{cite journal | author=Pácha J, Lisá V, Miksík I |title=Effect of cellular differentiation on 11beta-hydroxysteroid dehydrogenase activity in the intestine. |journal=Steroids |volume=67 |issue= 2 |pages= 119-26 |year= 2002 |pmid= 11755176 |doi= }}
*{{cite journal | author=Albertin G, Tortorella C, Malendowicz LK, ''et al.'' |title=Human adrenal cortex and aldosterone secreting adenomas express both 11beta-hydroxysteroid dehydrogenase type 1 and type 2 genes. |journal=Int. J. Mol. Med. |volume=9 |issue= 5 |pages= 495-8 |year= 2002 |pmid= 11956655 |doi= }}
*{{cite journal | author=Mazzocchi G, Malendowicz LK, Aragona F, ''et al.'' |title=11beta-Hydroxysteroid dehydrogenase types 1 and 2 are up- and downregulated in cortisol-secreting adrenal adenomas. |journal=J. Investig. Med. |volume=50 |issue= 4 |pages= 288-92 |year= 2002 |pmid= 12109593 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL2RB... {November 16, 2007 10:59:44 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:00:09 AM 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_IL2RB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2b5i.
| PDB = {{PDB2|2b5i}}, {{PDB2|2erj}}
| Name = Interleukin 2 receptor, beta
| HGNCid = 6009
| Symbol = IL2RB
| AltSymbols =; CD122; P70-75
| OMIM = 146710
| ECnumber =
| Homologene = 47955
| MGIid = 96550
| GeneAtlas_image1 = PBB_GE_IL2RB_205291_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004896 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor activity}} {{GNF_GO|id=GO:0004911 |text = interleukin-2 receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}} {{GNF_GO|id=GO:0045885 |text = positive regulation of survival gene product activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3560
| Hs_Ensembl = ENSG00000100385
| Hs_RefseqProtein = NP_000869
| Hs_RefseqmRNA = NM_000878
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 35851824
| Hs_GenLoc_end = 35875908
| Hs_Uniprot = P14784
| Mm_EntrezGene = 16185
| Mm_Ensembl = ENSMUSG00000068227
| Mm_RefseqmRNA = NM_008368
| Mm_RefseqProtein = NP_032394
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 78307808
| Mm_GenLoc_end = 78322321
| Mm_Uniprot = Q3TEQ2
}}
}}
'''Interleukin 2 receptor, beta''', also known as '''IL2RB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL2RB interleukin 2 receptor, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3560| 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 interleukin 2 receptor, which is involved in T cell-mediated immune responses, is present in 3 forms with respect to ability to bind interleukin 2. The low affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. The protein encoded by this gene represents the beta subunit and is a type I membrane protein.<ref name="entrez">{{cite web | title = Entrez Gene: IL2RB interleukin 2 receptor, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3560| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ellery JM, Nicholls PJ |title=Alternate signalling pathways from the interleukin-2 receptor. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 1 |pages= 27-40 |year= 2002 |pmid= 11750878 |doi= }}
*{{cite journal | author=Purvis SF, Georges DL, Williams TM, Lederman MM |title=Suppression of interleukin-2 and interleukin-2 receptor expression in Jurkat cells stably expressing the human immunodeficiency virus Tat protein. |journal=Cell. Immunol. |volume=144 |issue= 1 |pages= 32-42 |year= 1992 |pmid= 1394441 |doi= }}
*{{cite journal | author=Torigoe T, Saragovi HU, Reed JC |title=Interleukin 2 regulates the activity of the lyn protein-tyrosine kinase in a B-cell line. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 7 |pages= 2674-8 |year= 1992 |pmid= 1557373 |doi= }}
*{{cite journal | author=Maslinski W, Remillard B, Tsudo M, Strom TB |title=Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol. |journal=J. Biol. Chem. |volume=267 |issue= 22 |pages= 15281-4 |year= 1992 |pmid= 1639773 |doi= }}
*{{cite journal | author=Miyazaki T, Maruyama M, Yamada G, ''et al.'' |title=The integrity of the conserved 'WS motif' common to IL-2 and other cytokine receptors is essential for ligand binding and signal transduction. |journal=EMBO J. |volume=10 |issue= 11 |pages= 3191-7 |year= 1991 |pmid= 1915291 |doi= }}
*{{cite journal | author=Shibuya H, Yoneyama M, Nakamura Y, ''et al.'' |title=The human interleukin-2 receptor beta-chain gene: genomic organization, promoter analysis and chromosomal assignment. |journal=Nucleic Acids Res. |volume=18 |issue= 13 |pages= 3697-703 |year= 1990 |pmid= 1973832 |doi= }}
*{{cite journal | author=Hatakeyama M, Kono T, Kobayashi N, ''et al.'' |title=Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association. |journal=Science |volume=252 |issue= 5012 |pages= 1523-8 |year= 1991 |pmid= 2047859 |doi= }}
*{{cite journal | author=Mills GB, May C, McGill M, ''et al.'' |title=Interleukin 2-induced tyrosine phosphorylation. Interleukin 2 receptor beta is tyrosine phosphorylated. |journal=J. Biol. Chem. |volume=265 |issue= 6 |pages= 3561-7 |year= 1990 |pmid= 2303462 |doi= }}
*{{cite journal | author=Oyaizu N, Chirmule N, Kalyanaraman VS, ''et al.'' |title=Human immunodeficiency virus type 1 envelope glycoprotein gp120 produces immune defects in CD4+ T lymphocytes by inhibiting interleukin 2 mRNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 6 |pages= 2379-83 |year= 1990 |pmid= 2315327 |doi= }}
*{{cite journal | author=Gnarra JR, Otani H, Wang MG, ''et al.'' |title=Human interleukin 2 receptor beta-chain gene: chromosomal localization and identification of 5' regulatory sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 9 |pages= 3440-4 |year= 1990 |pmid= 2333293 |doi= }}
*{{cite journal | author=Tsudo M, Kitamura F, Miyasaka M |title=Characterization of the interleukin 2 receptor beta chain using three distinct monoclonal antibodies. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 6 |pages= 1982-6 |year= 1989 |pmid= 2467293 |doi= }}
*{{cite journal | author=Hatakeyama M, Tsudo M, Minamoto S, ''et al.'' |title=Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's. |journal=Science |volume=244 |issue= 4904 |pages= 551-6 |year= 1989 |pmid= 2785715 |doi= }}
*{{cite journal | author=Kornfeld H, Cruikshank WW, Pyle SW, ''et al.'' |title=Lymphocyte activation by HIV-1 envelope glycoprotein. |journal=Nature |volume=335 |issue= 6189 |pages= 445-8 |year= 1988 |pmid= 2843775 |doi= 10.1038/335445a0 }}
*{{cite journal | author=Leonard WJ, Donlon TA, Lebo RV, Greene WC |title=Localization of the gene encoding the human interleukin-2 receptor on chromosome 10. |journal=Science |volume=228 |issue= 4707 |pages= 1547-9 |year= 1985 |pmid= 3925551 |doi= }}
*{{cite journal | author=Bamborough P, Hedgecock CJ, Richards WG |title=The interleukin-2 and interleukin-4 receptors studied by molecular modelling. |journal=Structure |volume=2 |issue= 9 |pages= 839-51 |year= 1995 |pmid= 7529123 |doi= }}
*{{cite journal | author=Minami Y, Nakagawa Y, Kawahara A, ''et al.'' |title=Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: possible link with the c-myc induction pathway. |journal=Immunity |volume=2 |issue= 1 |pages= 89-100 |year= 1995 |pmid= 7600304 |doi= }}
*{{cite journal | author=Giri JG, Kumaki S, Ahdieh M, ''et al.'' |title=Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor. |journal=EMBO J. |volume=14 |issue= 15 |pages= 3654-63 |year= 1995 |pmid= 7641685 |doi= }}
*{{cite journal | author=Kirken RA, Rui H, Evans GA, Farrar WL |title=Characterization of an interleukin-2 (IL-2)-induced tyrosine phosphorylated 116-kDa protein associated with the IL-2 receptor beta-subunit. |journal=J. Biol. Chem. |volume=268 |issue= 30 |pages= 22765-70 |year= 1993 |pmid= 7693677 |doi= }}
*{{cite journal | author=Puri RK, Leland P, Aggarwal BB |title=Constitutive expression of human immunodeficiency virus type 1 tat gene inhibits interleukin 2 and interleukin 2 receptor expression in a human CD4+ T lymphoid (H9) cell line. |journal=AIDS Res. Hum. Retroviruses |volume=11 |issue= 1 |pages= 31-40 |year= 1995 |pmid= 7734194 |doi= }}
*{{cite journal | author=Miyazaki T, Liu ZJ, Kawahara A, ''et al.'' |title=Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. |journal=Cell |volume=81 |issue= 2 |pages= 223-31 |year= 1995 |pmid= 7736574 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ITGA1... {November 16, 2007 11:00:09 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:00:32 AM 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_ITGA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ck4.
| PDB = {{PDB2|1ck4}}, {{PDB2|1mhp}}, {{PDB2|1pt6}}, {{PDB2|1qc5}}, {{PDB2|1qcy}}, {{PDB2|2b2x}}
| Name = Integrin, alpha 1
| HGNCid = 6134
| Symbol = ITGA1
| AltSymbols =; CD49a; VLA1
| OMIM = 192968
| ECnumber =
| Homologene = 57137
| MGIid = 96599
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005518 |text = collagen binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3672
| Hs_Ensembl =
| Hs_RefseqProtein = NP_852478
| Hs_RefseqmRNA = NM_181501
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 109700
| Mm_Ensembl = ENSMUSG00000042284
| Mm_RefseqmRNA = NM_001033228
| Mm_RefseqProtein = NP_001028400
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 116080957
| Mm_GenLoc_end = 116222842
| Mm_Uniprot = Q05DI0
}}
}}
'''Integrin, alpha 1''', also known as '''ITGA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ITGA1 integrin, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3672| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the alpha 1 subunit of integrin receptors. This protein heterodimerizes with the beta 1 subunit to form a cell-surface receptor for collagen and laminin. The heterodimeric receptor is involved in cell-cell adhesion and may play a role in inflammation and fibrosis. The alpha 1 subunit contains an inserted (I) von Willebrand factor type I domain which is thought to be involved in collagen binding.<ref name="entrez">{{cite web | title = Entrez Gene: ITGA1 integrin, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3672| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Virtanen I, Korhonen M, Kariniemi AL, ''et al.'' |title=Integrins in human cells and tumors. |journal=Cell Differ. Dev. |volume=32 |issue= 3 |pages= 215-27 |year= 1991 |pmid= 2099238 |doi= }}
*{{cite journal | author=Plenz GA, Deng MC, Robenek H, Völker W |title=Vascular collagens: spotlight on the role of type VIII collagen in atherogenesis. |journal=Atherosclerosis |volume=166 |issue= 1 |pages= 1-11 |year= 2003 |pmid= 12482545 |doi= }}
*{{cite journal | author=Clover J, Dodds RA, Gowen M |title=Integrin subunit expression by human osteoblasts and osteoclasts in situ and in culture. |journal=J. Cell. Sci. |volume=103 ( Pt 1) |issue= |pages= 267-71 |year= 1992 |pmid= 1429908 |doi= }}
*{{cite journal | author=Bodary SC, McLean JW |title=The integrin beta 1 subunit associates with the vitronectin receptor alpha v subunit to form a novel vitronectin receptor in a human embryonic kidney cell line. |journal=J. Biol. Chem. |volume=265 |issue= 11 |pages= 5938-41 |year= 1990 |pmid= 1690718 |doi= }}
*{{cite journal | author=Sonnenberg A, Linders CJ, Modderman PW, ''et al.'' |title=Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that alpha 6 beta 1 but not alpha 6 beta 4 functions as a major receptor for fragment E8. |journal=J. Cell Biol. |volume=110 |issue= 6 |pages= 2145-55 |year= 1990 |pmid= 1693624 |doi= }}
*{{cite journal | author=Belkin VM, Belkin AM, Dol'nikova AE, ''et al.'' |title=[Isolation and characteristics of ligand specificity of VLA-1 integrin from human smooth muscles] |journal=Biokhimiia |volume=56 |issue= 12 |pages= 2198-206 |year= 1992 |pmid= 1807406 |doi= }}
*{{cite journal | author=Bank I, Roth D, Book M, ''et al.'' |title=Expression and functions of very late antigen 1 in inflammatory joint diseases. |journal=J. Clin. Immunol. |volume=11 |issue= 1 |pages= 29-38 |year= 1991 |pmid= 1827128 |doi= }}
*{{cite journal | author=Tabibzadeh S |title=Evidence of T-cell activation and potential cytokine action in human endometrium. |journal=J. Clin. Endocrinol. Metab. |volume=71 |issue= 3 |pages= 645-9 |year= 1990 |pmid= 2144294 |doi= }}
*{{cite journal | author=Tawil NJ, Houde M, Blacher R, ''et al.'' |title=Alpha 1 beta 1 integrin heterodimer functions as a dual laminin/collagen receptor in neural cells. |journal=Biochemistry |volume=29 |issue= 27 |pages= 6540-4 |year= 1990 |pmid= 2169872 |doi= }}
*{{cite journal | author=Belkin VM, Belkin AM, Koteliansky VE |title=Human smooth muscle VLA-1 integrin: purification, substrate specificity, localization in aorta, and expression during development. |journal=J. Cell Biol. |volume=111 |issue= 5 Pt 1 |pages= 2159-70 |year= 1990 |pmid= 2229189 |doi= }}
*{{cite journal | author=MacDonald TT, Horton MA, Choy MY, Richman PI |title=Increased expression of laminin/collagen receptor (VLA-1) on epithelium of inflamed human intestine. |journal=J. Clin. Pathol. |volume=43 |issue= 4 |pages= 313-5 |year= 1990 |pmid= 2341567 |doi= }}
*{{cite journal | author=Takada Y, Strominger JL, Hemler ME |title=The very late antigen family of heterodimers is part of a superfamily of molecules involved in adhesion and embryogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 10 |pages= 3239-43 |year= 1987 |pmid= 3033641 |doi= }}
*{{cite journal | author=Hemler ME, Huang C, Schwarz L |title=The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight beta subunit. |journal=J. Biol. Chem. |volume=262 |issue= 7 |pages= 3300-9 |year= 1987 |pmid= 3546305 |doi= }}
*{{cite journal | author=Kono Y, Yang S, Letarte M, Roberts EA |title=Establishment of a human hepatocyte line derived from primary culture in a collagen gel sandwich culture system. |journal=Exp. Cell Res. |volume=221 |issue= 2 |pages= 478-85 |year= 1996 |pmid= 7493648 |doi= 10.1006/excr.1995.1399 }}
*{{cite journal | author=Eglinton BA, Roberton DM, Cummins AG |title=Phenotype of T cells, their soluble receptor levels, and cytokine profile of human breast milk. |journal=Immunol. Cell Biol. |volume=72 |issue= 4 |pages= 306-13 |year= 1995 |pmid= 7806264 |doi= }}
*{{cite journal | author=Salter DM, Godolphin JL, Gourlay MS |title=Chondrocyte heterogeneity: immunohistologically defined variation of integrin expression at different sites in human fetal knees. |journal=J. Histochem. Cytochem. |volume=43 |issue= 4 |pages= 447-57 |year= 1995 |pmid= 7897185 |doi= }}
*{{cite journal | author=Pfaff M, Aumailley M, Specks U, ''et al.'' |title=Integrin and Arg-Gly-Asp dependence of cell adhesion to the native and unfolded triple helix of collagen type VI. |journal=Exp. Cell Res. |volume=206 |issue= 1 |pages= 167-76 |year= 1993 |pmid= 8387021 |doi= 10.1006/excr.1993.1134 }}
*{{cite journal | author=Briesewitz R, Epstein MR, Marcantonio EE |title=Expression of native and truncated forms of the human integrin alpha 1 subunit. |journal=J. Biol. Chem. |volume=268 |issue= 4 |pages= 2989-96 |year= 1993 |pmid= 8428973 |doi= }}
*{{cite journal | author=Langholz O, Röckel D, Mauch C, ''et al.'' |title=Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by alpha 1 beta 1 and alpha 2 beta 1 integrins. |journal=J. Cell Biol. |volume=131 |issue= 6 Pt 2 |pages= 1903-15 |year= 1996 |pmid= 8557756 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KPNA3... {November 16, 2007 11:00:32 AM PST}
- SEARCH REDIRECT: Control Box Found: KPNA3 {November 16, 2007 11:01:05 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:01:08 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:01:08 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:01:08 AM PST}
- UPDATED: Updated protein page: KPNA3 {November 16, 2007 11:01:13 AM PST}
- INFO: Beginning work on MAOB... {November 16, 2007 11:01:13 AM PST}
- SEARCH REDIRECT: Control Box Found: Monoamine oxidase B {November 16, 2007 11:01:36 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:01:37 AM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 16, 2007 11:01:37 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:01:37 AM PST}
- UPDATED: Updated protein page: Monoamine oxidase B {November 16, 2007 11:01:42 AM PST}
- INFO: Beginning work on ND4... {November 16, 2007 11:01:42 AM PST}
- SEARCH REDIRECT: Control Box Found: ND4 {November 16, 2007 11:02:02 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:02:15 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:02:15 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:02:15 AM PST}
- UPDATED: Updated protein page: ND4 {November 16, 2007 11:02:22 AM PST}
- INFO: Beginning work on NGFB... {November 16, 2007 11:02:22 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:02:54 AM 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_NGFB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bet.
| PDB = {{PDB2|1bet}}, {{PDB2|1btg}}, {{PDB2|1sg1}}, {{PDB2|1www}}, {{PDB2|2ifg}}
| Name = Nerve growth factor, beta polypeptide
| HGNCid = 7808
| Symbol = NGFB
| AltSymbols =; Beta-NGF; HSAN5; MGC161426; MGC161428; NGF
| OMIM = 162030
| ECnumber =
| Homologene = 1876
| MGIid = 97321
| GeneAtlas_image1 = PBB_GE_NGFB_206814_at_tn.png
| Function = {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component =
| Process = {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007422 |text = peripheral nervous system development}} {{GNF_GO|id=GO:0019233 |text = sensory perception of pain}} {{GNF_GO|id=GO:0045664 |text = regulation of neuron differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4803
| Hs_Ensembl = ENSG00000134259
| Hs_RefseqProtein = NP_002497
| Hs_RefseqmRNA = NM_002506
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 115630060
| Hs_GenLoc_end = 115682380
| Hs_Uniprot = P01138
| Mm_EntrezGene = 18049
| Mm_Ensembl = ENSMUSG00000027859
| Mm_RefseqmRNA = NM_013609
| Mm_RefseqProtein = NP_038637
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 102598989
| Mm_GenLoc_end = 102650066
| Mm_Uniprot = Q6LDU8
}}
}}
'''Nerve growth factor, beta polypeptide''', also known as '''NGFB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NGFB nerve growth factor, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4803| 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 NGF-beta family and encodes a secreted protein which homodimerizes and is incorporated into a larger complex. This protein has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.<ref name="entrez">{{cite web | title = Entrez Gene: NGFB nerve growth factor, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4803| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=MacGrogan D, Saint-André JP, Dicou E |title=Expression of nerve growth factor and nerve growth factor receptor genes in human tissues and in prostatic adenocarcinoma cell lines. |journal=J. Neurochem. |volume=59 |issue= 4 |pages= 1381-91 |year= 1992 |pmid= 1383421 |doi= }}
*{{cite journal | author=Dracopoli NC, Meisler MH |title=Mapping the human amylase gene cluster on the proximal short arm of chromosome 1 using a highly informative (CA)n repeat. |journal=Genomics |volume=7 |issue= 1 |pages= 97-102 |year= 1990 |pmid= 1692298 |doi= }}
*{{cite journal | author=Hallböök F, Ibáñez CF, Persson H |title=Evolutionary studies of the nerve growth factor family reveal a novel member abundantly expressed in Xenopus ovary. |journal=Neuron |volume=6 |issue= 5 |pages= 845-58 |year= 1991 |pmid= 2025430 |doi= }}
*{{cite journal | author=Borsani G, Pizzuti A, Rugarli EI, ''et al.'' |title=cDNA sequence of human beta-NGF. |journal=Nucleic Acids Res. |volume=18 |issue= 13 |pages= 4020 |year= 1990 |pmid= 2374737 |doi= }}
*{{cite journal | author=Dracopoli NC, Rose E, Whitfield GK, ''et al.'' |title=Two thyroid hormone regulated genes, the beta-subunits of nerve growth factor (NGFB) and thyroid stimulating hormone (TSHB), are located less than 310 kb apart in both human and mouse genomes. |journal=Genomics |volume=3 |issue= 2 |pages= 161-7 |year= 1989 |pmid= 2906326 |doi= }}
*{{cite journal | author=Zabel BU, Eddy RL, Lalley PA, ''et al.'' |title=Chromosomal locations of the human and mouse genes for precursors of epidermal growth factor and the beta subunit of nerve growth factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 2 |pages= 469-73 |year= 1985 |pmid= 3871525 |doi= }}
*{{cite journal | author=Ullrich A, Gray A, Berman C, ''et al.'' |title=Sequence homology of human and mouse beta-NGF subunit genes. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=48 Pt 1 |issue= |pages= 435-42 |year= 1984 |pmid= 6327169 |doi= }}
*{{cite journal | author=Breakefield XO, Orloff G, Castiglione C, ''et al.'' |title=Structural gene for beta-nerve growth factor not defective in familial dysautonomia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 13 |pages= 4213-6 |year= 1984 |pmid= 6330750 |doi= }}
*{{cite journal | author=Francke U, de Martinville B, Coussens L, Ullrich A |title=The human gene for the beta subunit of nerve growth factor is located on the proximal short arm of chromosome 1. |journal=Science |volume=222 |issue= 4629 |pages= 1248-51 |year= 1984 |pmid= 6648531 |doi= }}
*{{cite journal | author=Ullrich A, Gray A, Berman C, Dull TJ |title=Human beta-nerve growth factor gene sequence highly homologous to that of mouse. |journal=Nature |volume=303 |issue= 5920 |pages= 821-5 |year= 1983 |pmid= 6688123 |doi= }}
*{{cite journal | author=Mitchell EL, Jones D, White GR, ''et al.'' |title=Determination of the gene order of the three loci CD2, NGFB, and NRAS at human chromosome band 1p13 and refinement of their localisation at the subband level by fluorescence in situ hybridisation. |journal=Cytogenet. Cell Genet. |volume=70 |issue= 3-4 |pages= 183-5 |year= 1995 |pmid= 7789166 |doi= }}
*{{cite journal | author=Ensoli F, Ensoli B, Thiele CJ |title=HIV-1 gene expression and replication in neuronal and glial cell lines with immature phenotype: effects of nerve growth factor. |journal=Virology |volume=200 |issue= 2 |pages= 668-76 |year= 1994 |pmid= 8178451 |doi= 10.1006/viro.1994.1230 }}
*{{cite journal | author=Carrier A, Rosier MF, Guillemot F, ''et al.'' |title=Integrated physical, genetic, and genic map covering 3 Mb around the human NGF gene (NGFB) at 1p13. |journal=Genomics |volume=31 |issue= 1 |pages= 80-9 |year= 1996 |pmid= 8808283 |doi= 10.1006/geno.1996.0012 }}
*{{cite journal | author=Yamamoto M, Sobue G, Yamamoto K, ''et al.'' |title=Expression of mRNAs for neurotrophic factors (NGF, BDNF, NT-3, and GDNF) and their receptors (p75NGFR, trkA, trkB, and trkC) in the adult human peripheral nervous system and nonneural tissues. |journal=Neurochem. Res. |volume=21 |issue= 8 |pages= 929-38 |year= 1997 |pmid= 8895847 |doi= }}
*{{cite journal | author=Bax B, Blundell TL, Murray-Rust J, McDonald NQ |title=Structure of mouse 7S NGF: a complex of nerve growth factor with four binding proteins. |journal=Structure |volume=5 |issue= 10 |pages= 1275-85 |year= 1998 |pmid= 9351801 |doi= }}
*{{cite journal | author=Tong Y, Wang H, Chen W |title=[Cloning and sequencing of the gene for premature beta nerve growth factor] |journal=Zhongguo Ying Yong Sheng Li Xue Za Zhi |volume=13 |issue= 4 |pages= 316-8 |year= 1999 |pmid= 10322959 |doi= }}
*{{cite journal | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal | author=Wiesmann C, Ultsch MH, Bass SH, de Vos AM |title=Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor. |journal=Nature |volume=401 |issue= 6749 |pages= 184-8 |year= 1999 |pmid= 10490030 |doi= 10.1038/43705 }}
*{{cite journal | author=Gonias SL, Carmichael A, Mettenburg JM, ''et al.'' |title=Identical or overlapping sequences in the primary structure of human alpha(2)-macroglobulin are responsible for the binding of nerve growth factor-beta, platelet-derived growth factor-BB, and transforming growth factor-beta. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5826-31 |year= 2000 |pmid= 10681572 |doi= }}
*{{cite journal | author=Yarski MA, Bax BD, Hogue-Angeletti RA, Bradshaw RA |title=Nerve growth factor alpha subunit: effect of site-directed mutations on catalytic activity and 7S NGF complex formation. |journal=Biochim. Biophys. Acta |volume=1477 |issue= 1-2 |pages= 253-66 |year= 2000 |pmid= 10708862 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NPPA... {November 16, 2007 11:02:54 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:03:25 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Natriuretic peptide precursor A
| HGNCid = 7939
| Symbol = NPPA
| AltSymbols =; ANF; ANP; CDD-ANF; PND
| OMIM = 108780
| ECnumber =
| Homologene = 4498
| MGIid = 97367
| GeneAtlas_image1 = PBB_GE_NPPA_209957_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0050880 |text = regulation of blood vessel size}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4878
| Hs_Ensembl = ENSG00000175206
| Hs_RefseqProtein = NP_006163
| Hs_RefseqmRNA = NM_006172
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 11828353
| Hs_GenLoc_end = 11830989
| Hs_Uniprot = P01160
| Mm_EntrezGene = 230899
| Mm_Ensembl = ENSMUSG00000041616
| Mm_RefseqmRNA = NM_008725
| Mm_RefseqProtein = NP_032751
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 146844522
| Mm_GenLoc_end = 146845879
| Mm_Uniprot = O55083
}}
}}
'''Natriuretic peptide precursor A''', also known as '''NPPA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NPPA natriuretic peptide precursor A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4878| 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=Vesely DL |title=Atrial natriuretic peptide prohormone gene expression: hormones and diseases that upregulate its expression. |journal=IUBMB Life |volume=53 |issue= 3 |pages= 153-9 |year= 2002 |pmid= 12102171 |doi= }}
*{{cite journal | author=Suga S, Nakao K, Hosoda K, ''et al.'' |title=Receptor selectivity of natriuretic peptide family, atrial natriuretic peptide, brain natriuretic peptide, and C-type natriuretic peptide. |journal=Endocrinology |volume=130 |issue= 1 |pages= 229-39 |year= 1992 |pmid= 1309330 |doi= }}
*{{cite journal | author=Vanneste Y, Michel A, Deschodt-Lanckman M |title=Hydrolysis of intact and Cys-Phe-cleaved human atrial natriuretic peptide in vitro by human tissue kallikrein. |journal=Eur. J. Biochem. |volume=196 |issue= 2 |pages= 281-6 |year= 1991 |pmid= 1826098 |doi= }}
*{{cite journal | author=Porter JG, Arfsten A, Fuller F, ''et al.'' |title=Isolation and functional expression of the human atrial natriuretic peptide clearance receptor cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=171 |issue= 2 |pages= 796-803 |year= 1990 |pmid= 2169733 |doi= }}
*{{cite journal | author=Yandle TG, Brennan SO, Espiner EA, ''et al.'' |title=Endopeptidase-24.11 in human plasma degrades atrial natriuretic factor (ANF) to ANF(99-105/106-126). |journal=Peptides |volume=10 |issue= 4 |pages= 891-4 |year= 1989 |pmid= 2531377 |doi= }}
*{{cite journal | author=Yang-Feng TL, Floyd-Smith G, Nemer M, ''et al.'' |title=The pronatriodilatin gene is located on the distal short arm of human chromosome 1 and on mouse chromosome 4. |journal=Am. J. Hum. Genet. |volume=37 |issue= 6 |pages= 1117-28 |year= 1986 |pmid= 2934979 |doi= }}
*{{cite journal | author=Vanneste Y, Michel A, Dimaline R, ''et al.'' |title=Hydrolysis of alpha-human atrial natriuretic peptide in vitro by human kidney membranes and purified endopeptidase-24.11. Evidence for a novel cleavage site. |journal=Biochem. J. |volume=254 |issue= 2 |pages= 531-7 |year= 1988 |pmid= 2972276 |doi= }}
*{{cite journal | author=Seidman CE, Bloch KD, Zisfein J, ''et al.'' |title=Molecular studies of the atrial natriuretic factor gene. |journal=Hypertension |volume=7 |issue= 3 Pt 2 |pages= I31-4 |year= 1985 |pmid= 3158606 |doi= }}
*{{cite journal | author=Nemer M, Chamberland M, Sirois D, ''et al.'' |title=Gene structure of human cardiac hormone precursor, pronatriodilatin. |journal=Nature |volume=312 |issue= 5995 |pages= 654-6 |year= 1985 |pmid= 6095118 |doi= }}
*{{cite journal | author=Greenberg BD, Bencen GH, Seilhamer JJ, ''et al.'' |title=Nucleotide sequence of the gene encoding human atrial natriuretic factor precursor. |journal=Nature |volume=312 |issue= 5995 |pages= 656-8 |year= 1985 |pmid= 6095119 |doi= }}
*{{cite journal | author=Maki M, Parmentier M, Inagami T |title=Cloning of genomic DNA for human atrial natriuretic factor. |journal=Biochem. Biophys. Res. Commun. |volume=125 |issue= 2 |pages= 797-802 |year= 1985 |pmid= 6097248 |doi= }}
*{{cite journal | author=Oikawa S, Imai M, Ueno A, ''et al.'' |title=Cloning and sequence analysis of cDNA encoding a precursor for human atrial natriuretic polypeptide. |journal=Nature |volume=309 |issue= 5970 |pages= 724-6 |year= 1984 |pmid= 6203042 |doi= }}
*{{cite journal | author=Kangawa K, Matsuo H |title=Purification and complete amino acid sequence of alpha-human atrial natriuretic polypeptide (alpha-hANP). |journal=Biochem. Biophys. Res. Commun. |volume=118 |issue= 1 |pages= 131-9 |year= 1984 |pmid= 6230082 |doi= }}
*{{cite journal | author=Zivin RA, Condra JH, Dixon RA, ''et al.'' |title=Molecular cloning and characterization of DNA sequences encoding rat and human atrial natriuretic factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 20 |pages= 6325-9 |year= 1984 |pmid= 6238331 |doi= }}
*{{cite journal | author=Seidman CE, Bloch KD, Klein KA, ''et al.'' |title=Nucleotide sequences of the human and mouse atrial natriuretic factor genes. |journal=Science |volume=226 |issue= 4679 |pages= 1206-9 |year= 1985 |pmid= 6542248 |doi= }}
*{{cite journal | author=Nakayama K, Ohkubo H, Hirose T, ''et al.'' |title=mRNA sequence for human cardiodilatin-atrial natriuretic factor precursor and regulation of precursor mRNA in rat atria. |journal=Nature |volume=310 |issue= 5979 |pages= 699-701 |year= 1984 |pmid= 6547996 |doi= }}
*{{cite journal | author=Rondeau JJ, McNicoll N, Gagnon J, ''et al.'' |title=Stoichiometry of the atrial natriuretic factor-R1 receptor complex in the bovine zona glomerulosa. |journal=Biochemistry |volume=34 |issue= 7 |pages= 2130-6 |year= 1995 |pmid= 7857923 |doi= }}
*{{cite journal | author=Fairbrother WJ, McDowell RS, Cunningham BC |title=Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor. |journal=Biochemistry |volume=33 |issue= 30 |pages= 8897-904 |year= 1994 |pmid= 8043577 |doi= }}
*{{cite journal | author=Watanabe Y, Nakajima K, Shimamori Y, Fujimoto Y |title=Comparison of the hydrolysis of the three types of natriuretic peptides by human kidney neutral endopeptidase 24.11. |journal=Biochem. Mol. Med. |volume=61 |issue= 1 |pages= 47-51 |year= 1997 |pmid= 9232196 |doi= }}
*{{cite journal | author=Yan W, Wu F, Morser J, Wu Q |title=Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 15 |pages= 8525-9 |year= 2000 |pmid= 10880574 |doi= 10.1073/pnas.150149097 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PAEP... {November 16, 2007 11:03:25 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:04:14 AM 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
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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 = Progestagen-associated endometrial protein (placental protein 14, pregnancy-associated endometrial alpha-2-globulin, alpha uterine protein)
| HGNCid = 8573
| Symbol = PAEP
| AltSymbols =; GD; GdA; GdF; GdS; MGC138509; MGC142288; PAEG; PEP; PP14
| OMIM = 173310
| ECnumber =
| Homologene = 83207
| MGIid =
| GeneAtlas_image1 = PBB_GE_PAEP_206859_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005488 |text = binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5047
| Hs_Ensembl = ENSG00000122133
| Hs_RefseqProtein = NP_001018059
| Hs_RefseqmRNA = NM_001018049
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 137593423
| Hs_GenLoc_end = 137598622
| Hs_Uniprot = P09466
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Progestagen-associated endometrial protein (placental protein 14, pregnancy-associated endometrial alpha-2-globulin, alpha uterine protein)''', also known as '''PAEP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PAEP progestagen-associated endometrial protein (placental protein 14, pregnancy-associated endometrial alpha-2-globulin, alpha uterine protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5047| 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 kernel lipocalin superfamily whose members share relatively low sequence similarity but have highly conserved exon/intron structure and three-dimensional protein folding. Most lipocalins are clustered on the long arm of chromosome 9. The encoded glycoprotein has been previously referred to as pregnancy-associated endometrial alpha-2-globulin, placental protein 14, and glycodelin, but has been officially named progestagen-associated endometrial protein. Three distinct forms, with identical protein backbones but different glycosylation profiles, are found in amniotic fluid, follicular fluid and seminal plasma of the reproductive system. These glycoproteins have distinct and essential roles in regulating a uterine environment suitable for pregnancy and in the timing and occurrence of the appropriate sequence of events in the fertilization process. A number of alternatively spliced transcript variants have been observed at this locus, but the full-length nature of only two, each encoding the same protein, has been determined.<ref name="entrez">{{cite web | title = Entrez Gene: PAEP progestagen-associated endometrial protein (placental protein 14, pregnancy-associated endometrial alpha-2-globulin, alpha uterine protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5047| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rutanen EM, Koistinen R, Seppälä M, ''et al.'' |title=Progesterone-associated proteins PP12 and PP14 in the human endometrium. |journal=J. Steroid Biochem. |volume=27 |issue= 1-3 |pages= 25-31 |year= 1988 |pmid= 3320533 |doi= }}
*{{cite journal | author=Seppälä M, Bohn H, Tatarinov Y |title=Glycodelins. |journal=Tumour Biol. |volume=19 |issue= 3 |pages= 213-20 |year= 1998 |pmid= 9591048 |doi= }}
*{{cite journal | author=Salier JP |title=Chromosomal location, exon/intron organization and evolution of lipocalin genes. |journal=Biochim. Biophys. Acta |volume=1482 |issue= 1-2 |pages= 25-34 |year= 2000 |pmid= 11058744 |doi= }}
*{{cite journal | author=Halttunen M, Kämäräinen M, Koistinen H |title=Glycodelin: a reproduction-related lipocalin. |journal=Biochim. Biophys. Acta |volume=1482 |issue= 1-2 |pages= 149-56 |year= 2000 |pmid= 11058757 |doi= }}
*{{cite journal | author=Seppälä M, Taylor RN, Koistinen H, ''et al.'' |title=Glycodelin: a major lipocalin protein of the reproductive axis with diverse actions in cell recognition and differentiation. |journal=Endocr. Rev. |volume=23 |issue= 4 |pages= 401-30 |year= 2003 |pmid= 12202458 |doi= }}
*{{cite journal | author=Seppälä M, Koistinen H, Koistinen R, ''et al.'' |title=Glycosylation related actions of glycodelin: gamete, cumulus cell, immune cell and clinical associations. |journal=Hum. Reprod. Update |volume=13 |issue= 3 |pages= 275-87 |year= 2007 |pmid= 17329396 |doi= 10.1093/humupd/dmm004 }}
*{{cite journal | author=Garde J, Bell SC, Eperon IC |title=Multiple forms of mRNA encoding human pregnancy-associated endometrial alpha 2-globulin, a beta-lactoglobulin homologue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 6 |pages= 2456-60 |year= 1991 |pmid= 2006183 |doi= }}
*{{cite journal | author=Van Cong N, Vaisse C, Gross MS, ''et al.'' |title=The human placental protein 14 (PP14) gene is localized on chromosome 9q34. |journal=Hum. Genet. |volume=86 |issue= 5 |pages= 515-8 |year= 1991 |pmid= 2016092 |doi= }}
*{{cite journal | author=Wood PL, Iffland CA, Allen E, ''et al.'' |title=Serum levels of pregnancy-associated endometrial alpha 2-globulin (alpha 2-PEG), a glycosylated beta-lactoglobulin homologue, in successful and unsuccessful assisted conception. |journal=Hum. Reprod. |volume=5 |issue= 4 |pages= 421-6 |year= 1990 |pmid= 2113930 |doi= }}
*{{cite journal | author=Vaisse C, Atger M, Potier B, Milgrom E |title=Human placental protein 14 gene: sequence and characterization of a short duplication. |journal=DNA Cell Biol. |volume=9 |issue= 6 |pages= 401-13 |year= 1990 |pmid= 2206398 |doi= }}
*{{cite journal | author=Check JH, Nowroozi K, Chase JS, ''et al.'' |title=Serum progestagen-associated endometrial protein (PEP) levels in conception versus nonconception cycles following in vitro fertilization-embryo transfer. |journal=Journal of in vitro fertilization and embryo transfer : IVF |volume=7 |issue= 3 |pages= 134-6 |year= 1990 |pmid= 2380618 |doi= }}
*{{cite journal | author=Wood PL, Waites GT, MacVicar J, ''et al.'' |title=Immunohistological localization of pregnancy-associated endometrial alpha 2-globulin (alpha 2-PEG) in endometrial adenocarcinoma and effect of medroxyprogesterone acetate. |journal=British journal of obstetrics and gynaecology |volume=95 |issue= 12 |pages= 1292-8 |year= 1989 |pmid= 2975952 |doi= }}
*{{cite journal | author=Joshi SG |title=Progestin-dependent human endometrial protein: a marker for monitoring human endometrial function. |journal=Adv. Exp. Med. Biol. |volume=230 |issue= |pages= 167-86 |year= 1988 |pmid= 3135704 |doi= }}
*{{cite journal | author=Julkunen M, Seppälä M, Jänne OA |title=Complete amino acid sequence of human placental protein 14: a progesterone-regulated uterine protein homologous to beta-lactoglobulins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 8845-9 |year= 1988 |pmid= 3194393 |doi= }}
*{{cite journal | author=Huhtala ML, Seppälä M, Närvänen A, ''et al.'' |title=Amino acid sequence homology between human placental protein 14 and beta-lactoglobulins from various species. |journal=Endocrinology |volume=120 |issue= 6 |pages= 2620-2 |year= 1987 |pmid= 3569148 |doi= }}
*{{cite journal | author=Bell SC, Keyte JW, Waites GT |title=Pregnancy-associated endometrial alpha 2-globulin, the major secretory protein of the luteal phase and first trimester pregnancy endometrium, is not glycosylated prolactin but related to beta-lactoglobulins. |journal=J. Clin. Endocrinol. Metab. |volume=65 |issue= 5 |pages= 1067-71 |year= 1987 |pmid= 3667877 |doi= }}
*{{cite journal | author=Bell SC, Hales MW, Patel SR, ''et al.'' |title=Amniotic fluid concentrations of secreted pregnancy-associated endometrial alpha 1- and alpha 2-globulins (alpha 1- and alpha 2-PEG). |journal=British journal of obstetrics and gynaecology |volume=93 |issue= 9 |pages= 909-15 |year= 1986 |pmid= 3768286 |doi= }}
*{{cite journal | author=Joshi SG, Smith RA, Stokes DK |title=A progestagen-dependent endometrial protein in human amniotic fluid. |journal=J. Reprod. Fertil. |volume=60 |issue= 2 |pages= 317-21 |year= 1981 |pmid= 6776278 |doi= }}
*{{cite journal | author=Horne CH, Paterson WF, Sutcliffe RG |title=Localization of alpha-uterine protein in human endometrium. |journal=J. Reprod. Fertil. |volume=65 |issue= 2 |pages= 447-50 |year= 1982 |pmid= 7047733 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PDIA3... {November 16, 2007 10:57:13 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 10:57:58 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
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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 = PBB_Protein_PDIA3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2alb.
| PDB = {{PDB2|2alb}}, {{PDB2|2dmm}}, {{PDB2|2h8l}}
| Name = Protein disulfide isomerase family A, member 3
| HGNCid = 4606
| Symbol = PDIA3
| AltSymbols =; ERp57; ERp60; ERp61; GRP57; GRP58; HsT17083; P58; PI-PLC
| OMIM = 602046
| ECnumber =
| Homologene = 68454
| MGIid = 95834
| GeneAtlas_image1 = PBB_GE_PDIA3_208612_at_tn.png
| Function = {{GNF_GO|id=GO:0003756 |text = protein disulfide isomerase activity}} {{GNF_GO|id=GO:0004197 |text = cysteine-type endopeptidase activity}} {{GNF_GO|id=GO:0004629 |text = phospholipase C activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0015035 |text = protein disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0006606 |text = protein import into nucleus}} {{GNF_GO|id=GO:0006621 |text = protein retention in ER}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}} {{GNF_GO|id=GO:0045454 |text = cell redox homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2923
| Hs_Ensembl = ENSG00000167004
| Hs_RefseqProtein = NP_005304
| Hs_RefseqmRNA = NM_005313
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 41825882
| Hs_GenLoc_end = 41851035
| Hs_Uniprot = P30101
| Mm_EntrezGene = 14827
| Mm_Ensembl = ENSMUSG00000027248
| Mm_RefseqmRNA = NM_007952
| Mm_RefseqProtein = NP_031978
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 121105386
| Mm_GenLoc_end = 121129419
| Mm_Uniprot = Q3TEI9
}}
}}
'''Protein disulfide isomerase family A, member 3''', also known as '''PDIA3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PDIA3 protein disulfide isomerase family A, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2923| 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 protein of the endoplasmic reticulum that interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. The protein was once thought to be a phospholipase; however, it has been demonstrated that the protein actually has protein disulfide isomerase activity. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.<ref name="entrez">{{cite web | title = Entrez Gene: PDIA3 protein disulfide isomerase family A, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2923| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ryser HJ, Flückiger R |title=Progress in targeting HIV-1 entry. |journal=Drug Discov. Today |volume=10 |issue= 16 |pages= 1085-94 |year= 2005 |pmid= 16182193 |doi= 10.1016/S1359-6446(05)03550-6 }}
*{{cite journal | author=Garbi N, Hämmerling G, Tanaka S |title=Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes. |journal=Curr. Opin. Immunol. |volume=19 |issue= 1 |pages= 99-105 |year= 2007 |pmid= 17150345 |doi= 10.1016/j.coi.2006.11.013 }}
*{{cite journal | author=Khanal RC, Nemere I |title=The ERp57/GRp58/1,25D3-MARRS receptor: multiple functional roles in diverse cell systems. |journal=Curr. Med. Chem. |volume=14 |issue= 10 |pages= 1087-93 |year= 2007 |pmid= 17456022 |doi= }}
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Bennett CF, Balcarek JM, Varrichio A, Crooke ST |title=Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. |journal=Nature |volume=334 |issue= 6179 |pages= 268-70 |year= 1988 |pmid= 3398923 |doi= 10.1038/334268a0 }}
*{{cite journal | author=Bourdi M, Demady D, Martin JL, ''et al.'' |title=cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase. |journal=Arch. Biochem. Biophys. |volume=323 |issue= 2 |pages= 397-403 |year= 1995 |pmid= 7487104 |doi= 10.1006/abbi.1995.0060 }}
*{{cite journal | author=Hirano N, Shibasaki F, Sakai R, ''et al.'' |title=Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation. |journal=Eur. J. Biochem. |volume=234 |issue= 1 |pages= 336-42 |year= 1996 |pmid= 8529662 |doi= }}
*{{cite journal | author=Charnock-Jones DS, Day K, Smith SK |title=Cloning, expression and genomic organization of human placental protein disulfide isomerase (previously identified as phospholipase C alpha). |journal=Int. J. Biochem. Cell Biol. |volume=28 |issue= 1 |pages= 81-9 |year= 1996 |pmid= 8624847 |doi= }}
*{{cite journal | author=Koivunen P, Helaakoski T, Annunen P, ''et al.'' |title=ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase. |journal=Biochem. J. |volume=316 ( Pt 2) |issue= |pages= 599-605 |year= 1996 |pmid= 8687406 |doi= }}
*{{cite journal | author=Lewis JW, Neisig A, Neefjes J, Elliott T |title=Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP. |journal=Curr. Biol. |volume=6 |issue= 7 |pages= 873-83 |year= 1997 |pmid= 8805302 |doi= }}
*{{cite journal | author=Oliver JD, van der Wal FJ, Bulleid NJ, High S |title=Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. |journal=Science |volume=275 |issue= 5296 |pages= 86-8 |year= 1997 |pmid= 8974399 |doi= }}
*{{cite journal | author=Rasmussen RK, Ji H, Eddes JS, ''et al.'' |title=Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 588-98 |year= 1997 |pmid= 9150946 |doi= 10.1002/elps.1150180342 }}
*{{cite journal | author=Ji H, Reid GE, Moritz RL, ''et al.'' |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605-13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344 }}
*{{cite journal | author=Elliott JG, Oliver JD, High S |title=The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13849-55 |year= 1997 |pmid= 9153243 |doi= }}
*{{cite journal | author=Koivunen P, Horelli-Kuitunen N, Helaakoski T, ''et al.'' |title=Structures of the human gene for the protein disulfide isomerase-related polypeptide ERp60 and a processed gene and assignment of these genes to 15q15 and 1q21. |journal=Genomics |volume=42 |issue= 3 |pages= 397-404 |year= 1997 |pmid= 9205111 |doi= 10.1006/geno.1997.4750 }}
*{{cite journal | author=Urade R, Oda T, Ito H, ''et al.'' |title=Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease. |journal=J. Biochem. |volume=122 |issue= 4 |pages= 834-42 |year= 1998 |pmid= 9399589 |doi= }}
*{{cite journal | author=Lindquist JA, Jensen ON, Mann M, Hämmerling GJ |title=ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. |journal=EMBO J. |volume=17 |issue= 8 |pages= 2186-95 |year= 1998 |pmid= 9545232 |doi= 10.1093/emboj/17.8.2186 }}
*{{cite journal | author=Oliver JD, Roderick HL, Llewellyn DH, High S |title=ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. |journal=Mol. Biol. Cell |volume=10 |issue= 8 |pages= 2573-82 |year= 1999 |pmid= 10436013 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINF1... {November 16, 2007 11:04:14 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:04:46 AM 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_SERPINF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1imv.
| PDB = {{PDB2|1imv}}
| Name = Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1
| HGNCid = 8824
| Symbol = SERPINF1
| AltSymbols =; EPC-1; PEDF; PIG35
| OMIM = 172860
| ECnumber =
| Homologene = 1965
| MGIid = 108080
| GeneAtlas_image1 = PBB_GE_SERPINF1_202283_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0016525 |text = negative regulation of angiogenesis}} {{GNF_GO|id=GO:0050769 |text = positive regulation of neurogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5176
| Hs_Ensembl = ENSG00000132386
| Hs_RefseqProtein = NP_002606
| Hs_RefseqmRNA = NM_002615
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 1612003
| Hs_GenLoc_end = 1627618
| Hs_Uniprot = P36955
| Mm_EntrezGene = 20317
| Mm_Ensembl = ENSMUSG00000000753
| Mm_RefseqmRNA = NM_011340
| Mm_RefseqProtein = NP_035470
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 75225964
| Mm_GenLoc_end = 75238728
| Mm_Uniprot = Q5ND38
}}
}}
'''Serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1''', also known as '''SERPINF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SERPINF1 serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epithelium derived factor), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5176| 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=Tong JP, Yao YF |title=Contribution of VEGF and PEDF to choroidal angiogenesis: a need for balanced expressions. |journal=Clin. Biochem. |volume=39 |issue= 3 |pages= 267-76 |year= 2006 |pmid= 16409998 |doi= 10.1016/j.clinbiochem.2005.11.013 }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal | author=Becerra SP, Sagasti A, Spinella P, Notario V |title=Pigment epithelium-derived factor behaves like a noninhibitory serpin. Neurotrophic activity does not require the serpin reactive loop. |journal=J. Biol. Chem. |volume=270 |issue= 43 |pages= 25992-9 |year= 1995 |pmid= 7592790 |doi= }}
*{{cite journal | author=Tombran-Tink J, Pawar H, Swaroop A, ''et al.'' |title=Localization of the gene for pigment epithelium-derived factor (PEDF) to chromosome 17p13.1 and expression in cultured human retinoblastoma cells. |journal=Genomics |volume=19 |issue= 2 |pages= 266-72 |year= 1994 |pmid= 8188257 |doi= 10.1006/geno.1994.1057 }}
*{{cite journal | author=Becerra SP, Palmer I, Kumar A, ''et al.'' |title=Overexpression of fetal human pigment epithelium-derived factor in Escherichia coli. A functionally active neurotrophic factor. |journal=J. Biol. Chem. |volume=268 |issue= 31 |pages= 23148-56 |year= 1993 |pmid= 8226833 |doi= }}
*{{cite journal | author=Steele FR, Chader GJ, Johnson LV, Tombran-Tink J |title=Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine protease inhibitor gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 4 |pages= 1526-30 |year= 1993 |pmid= 8434014 |doi= }}
*{{cite journal | author=Pignolo RJ, Cristofalo VJ, Rotenberg MO |title=Senescent WI-38 cells fail to express EPC-1, a gene induced in young cells upon entry into the G0 state. |journal=J. Biol. Chem. |volume=268 |issue= 12 |pages= 8949-57 |year= 1993 |pmid= 8473338 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Ortego J, Escribano J, Becerra SP, Coca-Prados M |title=Gene expression of the neurotrophic pigment epithelium-derived factor in the human ciliary epithelium. Synthesis and secretion into the aqueous humor. |journal=Invest. Ophthalmol. Vis. Sci. |volume=37 |issue= 13 |pages= 2759-67 |year= 1997 |pmid= 8977492 |doi= }}
*{{cite journal | author=Tombran-Tink J, Mazuruk K, Rodriguez IR, ''et al.'' |title=Organization, evolutionary conservation, expression and unusual Alu density of the human gene for pigment epithelium-derived factor, a unique neurotrophic serpin. |journal=Mol. Vis. |volume=2 |issue= |pages= 11 |year= 1998 |pmid= 9238088 |doi= }}
*{{cite journal | author=Alberdi E, Hyde CC, Becerra SP |title=Pigment epithelium-derived factor (PEDF) binds to glycosaminoglycans: analysis of the binding site. |journal=Biochemistry |volume=37 |issue= 30 |pages= 10643-52 |year= 1998 |pmid= 9692954 |doi= 10.1021/bi9802317 }}
*{{cite journal | author=Dawson DW, Volpert OV, Gillis P, ''et al.'' |title=Pigment epithelium-derived factor: a potent inhibitor of angiogenesis. |journal=Science |volume=285 |issue= 5425 |pages= 245-8 |year= 1999 |pmid= 10398599 |doi= }}
*{{cite journal | author=Koenekoop R, Pina AL, Loyer M, ''et al.'' |title=Four polymorphic variations in the PEDF gene identified during the mutation screening of patients with Leber congenital amaurosis. |journal=Mol. Vis. |volume=5 |issue= |pages= 10 |year= 1999 |pmid= 10398730 |doi= }}
*{{cite journal | author=Alberdi E, Aymerich MS, Becerra SP |title=Binding of pigment epithelium-derived factor (PEDF) to retinoblastoma cells and cerebellar granule neurons. Evidence for a PEDF receptor. |journal=J. Biol. Chem. |volume=274 |issue= 44 |pages= 31605-12 |year= 1999 |pmid= 10531367 |doi= }}
*{{cite journal | author=Karakousis PC, John SK, Behling KC, ''et al.'' |title=Localization of pigment epithelium derived factor (PEDF) in developing and adult human ocular tissues. |journal=Mol. Vis. |volume=7 |issue= |pages= 154-63 |year= 2001 |pmid= 11438800 |doi= }}
*{{cite journal | author=Simonovic M, Gettins PG, Volz K |title=Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 20 |pages= 11131-5 |year= 2001 |pmid= 11562499 |doi= 10.1073/pnas.211268598 }}
*{{cite journal | author=Yamagishi S, Inagaki Y, Amano S, ''et al.'' |title=Pigment epithelium-derived factor protects cultured retinal pericytes from advanced glycation end product-induced injury through its antioxidative properties. |journal=Biochem. Biophys. Res. Commun. |volume=296 |issue= 4 |pages= 877-82 |year= 2002 |pmid= 12200129 |doi= }}
*{{cite journal | author=Meyer C, Notari L, Becerra SP |title=Mapping the type I collagen-binding site on pigment epithelium-derived factor. Implications for its antiangiogenic activity. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 45400-7 |year= 2003 |pmid= 12237317 |doi= 10.1074/jbc.M208339200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Pignolo RJ, Francis MK, Rotenberg MO, Cristofalo VJ |title=Putative role for EPC-1/PEDF in the G0 growth arrest of human diploid fibroblasts. |journal=J. Cell. Physiol. |volume=195 |issue= 1 |pages= 12-20 |year= 2003 |pmid= 12599204 |doi= 10.1002/jcp.10212 }}
}}
{{refend}}
{{protein-stub}}
end log.
