Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 18:17, 17 November 2007 (UTC)[edit]
Conflict: Ambiguous Proteins (1)[edit]
Proteins without matches (11)[edit]
Proteins with a High Potential Match (3)[edit]
Redirected Proteins (10)[edit]
Manual Inspection (Page not found) (15)[edit]
Updated (10)[edit]
Protein Status Grid - Date: 18:17, 17 November 2007 (UTC)[edit]
Vebose Log - Date: 18:17, 17 November 2007 (UTC)[edit]
- INFO: Beginning work on ALOX12... {November 17, 2007 9:56:06 AM PST}
- SEARCH REDIRECT: Control Box Found: ALOX12 {November 17, 2007 9:56:39 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 9:56:42 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 9:56:42 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 9:56:42 AM PST}
- UPDATED: Updated protein page: ALOX12 {November 17, 2007 9:56:48 AM PST}
- INFO: Beginning work on ATP8... {November 17, 2007 10:04:32 AM PST}
- SEARCH REDIRECT: Control Box Found: ATP8 {November 17, 2007 10:05:01 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:05:04 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:05:04 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:05:04 AM PST}
- UPDATED: Updated protein page: ATP8 {November 17, 2007 10:05:10 AM PST}
- INFO: Beginning work on CBX5... {November 17, 2007 10:10:00 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:10:54 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
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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 = Chromobox homolog 5 (HP1 alpha homolog, Drosophila)
| HGNCid = 1555
| Symbol = CBX5
| AltSymbols =; HP1; HP1-ALPHA; HP1Hs-alpha
| OMIM = 604478
| ECnumber =
| Homologene = 7257
| MGIid = 109372
| GeneAtlas_image1 = PBB_GE_CBX5_209715_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000776 |text = kinetochore}} {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0005720 |text = nuclear heterochromatin}}
| Process = {{GNF_GO|id=GO:0006333 |text = chromatin assembly or disassembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 23468
| Hs_Ensembl = ENSG00000094916
| Hs_RefseqProtein = NP_036249
| Hs_RefseqmRNA = NM_012117
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 52921003
| Hs_GenLoc_end = 52960153
| Hs_Uniprot = P45973
| Mm_EntrezGene = 12419
| Mm_Ensembl = ENSMUSG00000009575
| Mm_RefseqmRNA = XM_001000807
| Mm_RefseqProtein = XP_001000807
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 103024721
| Mm_GenLoc_end = 103067850
| Mm_Uniprot = Q61686
}}
}}
'''Chromobox homolog 5 (HP1 alpha homolog, Drosophila)''', also known as '''CBX5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CBX5 chromobox homolog 5 (HP1 alpha homolog, Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23468| 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 = Heterochromatin protein-1 (HP1) is a methyl-lysine binding protein localized at heterochromatin sites, where it mediates gene silencing.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: CBX5 chromobox homolog 5 (HP1 alpha homolog, Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23468| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Saunders WS, Chue C, Goebl M, ''et al.'' |title=Molecular cloning of a human homologue of Drosophila heterochromatin protein HP1 using anti-centromere autoantibodies with anti-chromo specificity. |journal=J. Cell. Sci. |volume=104 ( Pt 2) |issue= |pages= 573-82 |year= 1993 |pmid= 8505380 |doi= }}
*{{cite journal | author=Ye Q, Worman HJ |title=Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 14653-6 |year= 1996 |pmid= 8663349 |doi= }}
*{{cite journal | author=Sugimoto K, Yamada T, Muro Y, Himeno M |title=Human homolog of Drosophila heterochromatin-associated protein 1 (HP1) is a DNA-binding protein which possesses a DNA-binding motif with weak similarity to that of human centromere protein C (CENP-C). |journal=J. Biochem. |volume=120 |issue= 1 |pages= 153-9 |year= 1997 |pmid= 8864858 |doi= }}
*{{cite journal | author=Ye Q, Callebaut I, Pezhman A, ''et al.'' |title=Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14983-9 |year= 1997 |pmid= 9169472 |doi= }}
*{{cite journal | author=Lessard J, Baban S, Sauvageau G |title=Stage-specific expression of polycomb group genes in human bone marrow cells. |journal=Blood |volume=91 |issue= 4 |pages= 1216-24 |year= 1998 |pmid= 9454751 |doi= }}
*{{cite journal | author=Ainsztein AM, Kandels-Lewis SE, Mackay AM, Earnshaw WC |title=INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1. |journal=J. Cell Biol. |volume=143 |issue= 7 |pages= 1763-74 |year= 1999 |pmid= 9864353 |doi= }}
*{{cite journal | author=Minc E, Allory Y, Worman HJ, ''et al.'' |title=Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells. |journal=Chromosoma |volume=108 |issue= 4 |pages= 220-34 |year= 1999 |pmid= 10460410 |doi= }}
*{{cite journal | author=Murzina N, Verreault A, Laue E, Stillman B |title=Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins. |journal=Mol. Cell |volume=4 |issue= 4 |pages= 529-40 |year= 1999 |pmid= 10549285 |doi= }}
*{{cite journal | author=Nielsen AL, Ortiz JA, You J, ''et al.'' |title=Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family. |journal=EMBO J. |volume=18 |issue= 22 |pages= 6385-95 |year= 2000 |pmid= 10562550 |doi= 10.1093/emboj/18.22.6385 }}
*{{cite journal | author=Zhao T, Heyduk T, Allis CD, Eissenberg JC |title=Heterochromatin protein 1 binds to nucleosomes and DNA in vitro. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 28332-8 |year= 2000 |pmid= 10882726 |doi= 10.1074/jbc.M003493200 }}
*{{cite journal | author=Lechner MS, Begg GE, Speicher DW, Rauscher FJ |title=Molecular determinants for targeting heterochromatin protein 1-mediated gene silencing: direct chromoshadow domain-KAP-1 corepressor interaction is essential. |journal=Mol. Cell. Biol. |volume=20 |issue= 17 |pages= 6449-65 |year= 2000 |pmid= 10938122 |doi= }}
*{{cite journal | author=Song K, Jung Y, Jung D, Lee I |title=Human Ku70 interacts with heterochromatin protein 1alpha. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 8321-7 |year= 2001 |pmid= 11112778 |doi= 10.1074/jbc.M008779200 }}
*{{cite journal | author=Lachner M, O'Carroll D, Rea S, ''et al.'' |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=Nature |volume=410 |issue= 6824 |pages= 116-20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132 }}
*{{cite journal | author=Bannister AJ, Zegerman P, Partridge JF, ''et al.'' |title=Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. |journal=Nature |volume=410 |issue= 6824 |pages= 120-4 |year= 2001 |pmid= 11242054 |doi= 10.1038/35065138 }}
*{{cite journal | author=Nielsen AL, Oulad-Abdelghani M, Ortiz JA, ''et al.'' |title=Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. |journal=Mol. Cell |volume=7 |issue= 4 |pages= 729-39 |year= 2001 |pmid= 11336697 |doi= }}
*{{cite journal | author=Wheatley SP, Carvalho A, Vagnarelli P, Earnshaw WC |title=INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis. |journal=Curr. Biol. |volume=11 |issue= 11 |pages= 886-90 |year= 2001 |pmid= 11516652 |doi= }}
*{{cite journal | author=Scholzen T, Endl E, Wohlenberg C, ''et al.'' |title=The Ki-67 protein interacts with members of the heterochromatin protein 1 (HP1) family: a potential role in the regulation of higher-order chromatin structure. |journal=J. Pathol. |volume=196 |issue= 2 |pages= 135-44 |year= 2002 |pmid= 11793364 |doi= 10.1002/path.1016 }}
*{{cite journal | author=Weinmann AS, Yan PS, Oberley MJ, ''et al.'' |title=Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis. |journal=Genes Dev. |volume=16 |issue= 2 |pages= 235-44 |year= 2002 |pmid= 11799066 |doi= 10.1101/gad.943102 }}
*{{cite journal | author=Sugimoto K, Tasaka H, Dotsu M |title=Molecular behavior in living mitotic cells of human centromere heterochromatin protein HPLalpha ectopically expressed as a fusion to red fluorescent protein. |journal=Cell Struct. Funct. |volume=26 |issue= 6 |pages= 705-18 |year= 2002 |pmid= 11942629 |doi= }}
*{{cite journal | author=Vassallo MF, Tanese N |title=Isoform-specific interaction of HP1 with human TAFII130. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 9 |pages= 5919-24 |year= 2002 |pmid= 11959914 |doi= 10.1073/pnas.092025499 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CDC20... {November 17, 2007 9:56:48 AM PST}
- SEARCH REDIRECT: Control Box Found: CDC20 {November 17, 2007 9:57:15 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 9:57:18 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 9:57:18 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 9:57:18 AM PST}
- UPDATED: Updated protein page: CDC20 {November 17, 2007 9:57:24 AM PST}
- INFO: Beginning work on COL4A4... {November 17, 2007 9:57:25 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 9:57:47 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 =
| image_source =
| PDB =
| Name = Collagen, type IV, alpha 4
| HGNCid = 2206
| Symbol = COL4A4
| AltSymbols =; CA44
| OMIM = 120131
| ECnumber =
| Homologene = 20071
| MGIid = 104687
| GeneAtlas_image1 = PBB_GE_COL4A4_214602_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005587 |text = collagen type IV}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0042062 |text = long-term strengthening of neuromuscular junction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1286
| Hs_Ensembl = ENSG00000081052
| Hs_RefseqProtein = NP_000083
| Hs_RefseqmRNA = NM_000092
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 227578177
| Hs_GenLoc_end = 227737519
| Hs_Uniprot = P53420
| Mm_EntrezGene = 12829
| Mm_Ensembl = ENSMUSG00000067158
| Mm_RefseqmRNA = NM_007735
| Mm_RefseqProtein = NP_031761
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 82331582
| Mm_GenLoc_end = 82465816
| Mm_Uniprot =
}}
}}
'''Collagen, type IV, alpha 4''', also known as '''COL4A4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COL4A4 collagen, type IV, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1286| 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 one of the six subunits of type IV collagen, the major structural component of basement membranes. This particular collagen IV subunit, however, is only found in a subset of basement membranes. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Mutations in this gene are associated with type II autosomal recessive Alport syndrome (hereditary glomerulonephropathy) and with familial benign hematuria (thin basement membrane disease). Two transcripts, differing only in their transcription start sites, have been identified for this gene and, as is common for collagen genes, multiple polyadenylation sites are found in the 3' UTR.<ref name="entrez">{{cite web | title = Entrez Gene: COL4A4 collagen, type IV, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1286| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hinek A |title=Nature and the multiple functions of the 67-kD elastin-/laminin binding protein. |journal=Cell Adhes. Commun. |volume=2 |issue= 3 |pages= 185-93 |year= 1995 |pmid= 7827955 |doi= }}
*{{cite journal | author=Hudson BG, Reeders ST, Tryggvason K |title=Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26033-6 |year= 1994 |pmid= 8253711 |doi= }}
*{{cite journal | author=Lemmink HH, Schröder CH, Monnens LA, Smeets HJ |title=The clinical spectrum of type IV collagen mutations. |journal=Hum. Mutat. |volume=9 |issue= 6 |pages= 477-99 |year= 1997 |pmid= 9195222 |doi= 10.1002/(SICI)1098-1004(1997)9:6<477::AID-HUMU1>3.0.CO;2-# }}
*{{cite journal | author=Ständer M, Naumann U, Wick W, Weller M |title=Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth. |journal=Cell Tissue Res. |volume=296 |issue= 2 |pages= 221-7 |year= 1999 |pmid= 10382266 |doi= }}
*{{cite journal | author=Kurpakus Wheater M, Kernacki KA, Hazlett LD |title=Corneal cell proteins and ocular surface pathology. |journal=Biotechnic & histochemistry : official publication of the Biological Stain Commission |volume=74 |issue= 3 |pages= 146-59 |year= 1999 |pmid= 10416788 |doi= }}
*{{cite journal | author=Pescucci C, Longo I, Bruttini M, ''et al.'' |title=Type-IV collagen related diseases. |journal=J. Nephrol. |volume=16 |issue= 2 |pages= 314-6 |year= 2003 |pmid= 12768082 |doi= }}
*{{cite journal | author=Torra R, Tazón-Vega B, Ars E, Ballarín J |title=Collagen type IV (alpha3-alpha4) nephropathy: from isolated haematuria to renal failure. |journal=Nephrol. Dial. Transplant. |volume=19 |issue= 10 |pages= 2429-32 |year= 2005 |pmid= 15280517 |doi= 10.1093/ndt/gfh435 }}
*{{cite journal | author=Rana K, Wang YY, Buzza M, ''et al.'' |title=The genetics of thin basement membrane nephropathy. |journal=Semin. Nephrol. |volume=25 |issue= 3 |pages= 163-70 |year= 2005 |pmid= 15880327 |doi= }}
*{{cite journal | author=Maziers N, Dahan K, Pirson Y |title=[From Alport syndrome to benign familial hematuria: clinical and genetic aspect] |journal=Nephrol. Ther. |volume=1 |issue= 2 |pages= 90-100 |year= 2006 |pmid= 16895672 |doi= 10.1016/j.nephro.2005.03.005 }}
*{{cite journal | author=Kamagata Y, Mattei MG, Ninomiya Y |title=Isolation and sequencing of cDNAs and genomic DNAs encoding the alpha 4 chain of basement membrane collagen type IV and assignment of the gene to the distal long arm of human chromosome 2. |journal=J. Biol. Chem. |volume=267 |issue= 33 |pages= 23753-8 |year= 1992 |pmid= 1429714 |doi= }}
*{{cite journal | author=Mariyama M, Zheng K, Yang-Feng TL, Reeders ST |title=Colocalization of the genes for the alpha 3(IV) and alpha 4(IV) chains of type IV collagen to chromosome 2 bands q35-q37. |journal=Genomics |volume=13 |issue= 3 |pages= 809-13 |year= 1992 |pmid= 1639407 |doi= }}
*{{cite journal | author=Gupta S, Batchu RB, Datta K |title=Purification, partial characterization of rat kidney hyaluronic acid binding protein and its localization on the cell surface. |journal=Eur. J. Cell Biol. |volume=56 |issue= 1 |pages= 58-67 |year= 1992 |pmid= 1724753 |doi= }}
*{{cite journal | author=Sanes JR, Engvall E, Butkowski R, Hunter DD |title=Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere. |journal=J. Cell Biol. |volume=111 |issue= 4 |pages= 1685-99 |year= 1990 |pmid= 2211832 |doi= }}
*{{cite journal | author=Gunwar S, Saus J, Noelken ME, Hudson BG |title=Glomerular basement membrane. Identification of a fourth chain, alpha 4, of type IV collagen. |journal=J. Biol. Chem. |volume=265 |issue= 10 |pages= 5466-9 |year= 1990 |pmid= 2318822 |doi= }}
*{{cite journal | author=Hernandez MR, Igoe F, Neufeld AH |title=Extracellular matrix of the human optic nerve head. |journal=Am. J. Ophthalmol. |volume=102 |issue= 2 |pages= 139-48 |year= 1986 |pmid= 2426947 |doi= }}
*{{cite journal | author=Murata K, Motayama T, Kotake C |title=Collagen types in various layers of the human aorta and their changes with the atherosclerotic process. |journal=Atherosclerosis |volume=60 |issue= 3 |pages= 251-62 |year= 1986 |pmid= 3089234 |doi= }}
*{{cite journal | author=Glant TT, Hadházy C, Mikecz K, Sipos A |title=Appearance and persistence of fibronectin in cartilage. Specific interaction of fibronectin with collagen type II. |journal=Histochemistry |volume=82 |issue= 2 |pages= 149-58 |year= 1985 |pmid= 3997552 |doi= }}
*{{cite journal | author=Uscanga L, Kennedy RH, Stocker S, ''et al.'' |title=Immunolocalization of collagen types, laminin and fibronectin in the normal human pancreas. |journal=Digestion |volume=30 |issue= 3 |pages= 158-64 |year= 1984 |pmid= 6389236 |doi= }}
*{{cite journal | author=Sundarraj N, Willson J |title=Monoclonal antibody to human basement membrane collagen type IV. |journal=Immunology |volume=47 |issue= 1 |pages= 133-40 |year= 1982 |pmid= 6811420 |doi= }}
*{{cite journal | author=Hahn E, Wick G, Pencev D, Timpl R |title=Distribution of basement membrane proteins in normal and fibrotic human liver: collagen type IV, laminin, and fibronectin. |journal=Gut |volume=21 |issue= 1 |pages= 63-71 |year= 1980 |pmid= 6988303 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DPYD... {November 17, 2007 9:57:47 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 9:58:22 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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| update_protein_box = 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_DPYD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gt8.
| PDB = {{PDB2|1gt8}}, {{PDB2|1gte}}, {{PDB2|1gth}}, {{PDB2|1h7w}}, {{PDB2|1h7x}}
| Name = Dihydropyrimidine dehydrogenase
| HGNCid = 3012
| Symbol = DPYD
| AltSymbols =; DHP; DPD; MGC132008; MGC70799
| OMIM = 274270
| ECnumber =
| Homologene = 85
| MGIid = 2139667
| GeneAtlas_image1 = PBB_GE_DPYD_204646_at_tn.png
| Function = {{GNF_GO|id=GO:0004152 |text = dihydroorotate dehydrogenase activity}} {{GNF_GO|id=GO:0004158 |text = dihydroorotate oxidase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0015036 |text = disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0017113 |text = dihydropyrimidine dehydrogenase (NADP+) activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051539 |text = 4 iron, 4 sulfur cluster binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006207 |text = 'de novo' pyrimidine base biosynthetic process}} {{GNF_GO|id=GO:0006212 |text = uracil catabolic process}} {{GNF_GO|id=GO:0006214 |text = thymidine catabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1806
| Hs_Ensembl = ENSG00000188641
| Hs_RefseqProtein = NP_000101
| Hs_RefseqmRNA = NM_000110
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 97315887
| Hs_GenLoc_end = 98159193
| Hs_Uniprot = Q12882
| Mm_EntrezGene = 99586
| Mm_Ensembl = ENSMUSG00000033308
| Mm_RefseqmRNA = NM_170778
| Mm_RefseqProtein = NP_740748
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 118554180
| Mm_GenLoc_end = 119424922
| Mm_Uniprot =
}}
}}
'''Dihydropyrimidine dehydrogenase''', also known as '''DPYD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DPYD dihydropyrimidine dehydrogenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1806| 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 pyrimidine catabolic enzyme and the initial and rate-limiting factor in the pathway of uracil and thymidine catabolism. Genetic deficiency of this enzyme results in an error in pyrimidine metabolism associated with thymine-uraciluria and an increased risk of toxicity in cancer patients receiving 5-fluorouracil chemotherapy.<ref name="entrez">{{cite web | title = Entrez Gene: DPYD dihydropyrimidine dehydrogenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1806| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hoff PM, Royce M, Medgyesy D, ''et al.'' |title=Oral fluoropoyrimidines. |journal=Semin. Oncol. |volume=26 |issue= 6 |pages= 640-6 |year= 1999 |pmid= 10606257 |doi= }}
*{{cite journal | author=Schneider HB, Becker H |title=Impact of dihydropyrimidine dehydrogenase on 5-fluorouracil treatment in cancer patients. |journal=Eur. J. Med. Res. |volume=8 |issue= 5 |pages= 226-8 |year= 2004 |pmid= 12844478 |doi= }}
*{{cite journal | author=Omura K |title=Clinical implications of dihydropyrimidine dehydrogenase (DPD) activity in 5-FU-based chemotherapy: mutations in the DPD gene, and DPD inhibitory fluoropyrimidines. |journal=Int. J. Clin. Oncol. |volume=8 |issue= 3 |pages= 132-8 |year= 2003 |pmid= 12851836 |doi= 10.1007/s10147-003-0330-z }}
*{{cite journal | author=Lee W, Lockhart AC, Kim RB, Rothenberg ML |title=Cancer pharmacogenomics: powerful tools in cancer chemotherapy and drug development. |journal=Oncologist |volume=10 |issue= 2 |pages= 104-11 |year= 2005 |pmid= 15709212 |doi= 10.1634/theoncologist.10-2-104 }}
*{{cite journal | author=Lu ZH, Zhang R, Diasio RB |title=Purification and characterization of dihydropyrimidine dehydrogenase from human liver. |journal=J. Biol. Chem. |volume=267 |issue= 24 |pages= 17102-9 |year= 1992 |pmid= 1512248 |doi= }}
*{{cite journal | author=Porter DJ, Chestnut WG, Merrill BM, Spector T |title=Mechanism-based inactivation of dihydropyrimidine dehydrogenase by 5-ethynyluracil. |journal=J. Biol. Chem. |volume=267 |issue= 8 |pages= 5236-42 |year= 1992 |pmid= 1544906 |doi= }}
*{{cite journal | author=Dupuis A, Skehel JM, Walker JE |title=A homologue of a nuclear-coded iron-sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes. |journal=Biochemistry |volume=30 |issue= 11 |pages= 2954-60 |year= 1991 |pmid= 1901022 |doi= }}
*{{cite journal | author=Eggink G, Engel H, Vriend G, ''et al.'' |title=Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. |journal=J. Mol. Biol. |volume=212 |issue= 1 |pages= 135-42 |year= 1990 |pmid= 2319593 |doi= }}
*{{cite journal | author=Tuchman M, Roemeling RV, Hrushesky WA, ''et al.'' |title=Dihydropyrimidine dehydrogenase activity in human blood mononuclear cells. |journal=Enzyme |volume=42 |issue= 1 |pages= 15-24 |year= 1989 |pmid= 2528450 |doi= }}
*{{cite journal | author=Diasio RB, Beavers TL, Carpenter JT |title=Familial deficiency of dihydropyrimidine dehydrogenase. Biochemical basis for familial pyrimidinemia and severe 5-fluorouracil-induced toxicity. |journal=J. Clin. Invest. |volume=81 |issue= 1 |pages= 47-51 |year= 1988 |pmid= 3335642 |doi= }}
*{{cite journal | author=Takai S, Fernandez-Salguero P, Kimura S, ''et al.'' |title=Assignment of the human dihydropyrimidine dehydrogenase gene (DPYD) to chromosome region 1p22 by fluorescence in situ hybridization. |journal=Genomics |volume=24 |issue= 3 |pages= 613-4 |year= 1995 |pmid= 7713523 |doi= 10.1006/geno.1994.1680 }}
*{{cite journal | author=Yokota H, Fernandez-Salguero P, Furuya H, ''et al.'' |title=cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria. |journal=J. Biol. Chem. |volume=269 |issue= 37 |pages= 23192-6 |year= 1994 |pmid= 8083224 |doi= }}
*{{cite journal | author=Lu Z, Zhang R, Diasio RB |title=Dihydropyrimidine dehydrogenase activity in human peripheral blood mononuclear cells and liver: population characteristics, newly identified deficient patients, and clinical implication in 5-fluorouracil chemotherapy. |journal=Cancer Res. |volume=53 |issue= 22 |pages= 5433-8 |year= 1993 |pmid= 8221682 |doi= }}
*{{cite journal | author=Vreken P, Van Kuilenburg AB, Meinsma R, ''et al.'' |title=A point mutation in an invariant splice donor site leads to exon skipping in two unrelated Dutch patients with dihydropyrimidine dehydrogenase deficiency. |journal=J. Inherit. Metab. Dis. |volume=19 |issue= 5 |pages= 645-54 |year= 1997 |pmid= 8892022 |doi= }}
*{{cite journal | author=Johnson MR, Wang K, Tillmanns S, ''et al.'' |title=Structural organization of the human dihydropyrimidine dehydrogenase gene. |journal=Cancer Res. |volume=57 |issue= 9 |pages= 1660-3 |year= 1997 |pmid= 9135003 |doi= }}
*{{cite journal | author=Fernandez-Salguero PM, Sapone A, Wei X, ''et al.'' |title=Lack of correlation between phenotype and genotype for the polymorphically expressed dihydropyrimidine dehydrogenase in a family of Pakistani origin. |journal=Pharmacogenetics |volume=7 |issue= 2 |pages= 161-3 |year= 1997 |pmid= 9170156 |doi= }}
*{{cite journal | author=Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH |title=Identification of novel point mutations in the dihydropyrimidine dehydrogenase gene. |journal=J. Inherit. Metab. Dis. |volume=20 |issue= 3 |pages= 335-8 |year= 1997 |pmid= 9266349 |doi= }}
*{{cite journal | author=Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH |title=Dihydropyrimidine dehydrogenase (DPD) deficiency: identification and expression of missense mutations C29R, R886H and R235W. |journal=Hum. Genet. |volume=101 |issue= 3 |pages= 333-8 |year= 1998 |pmid= 9439663 |doi= }}
*{{cite journal | author=Ogura K, Nishiyama T, Takubo H, ''et al.'' |title=Suicidal inactivation of human dihydropyrimidine dehydrogenase by (E)-5-(2-bromovinyl)uracil derived from the antiviral, sorivudine. |journal=Cancer Lett. |volume=122 |issue= 1-2 |pages= 107-13 |year= 1998 |pmid= 9464498 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FLT4... {November 17, 2007 9:58:22 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 9:58:57 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 = Fms-related tyrosine kinase 4
| HGNCid = 3767
| Symbol = FLT4
| AltSymbols =; FLT41; PCL; VEGFR3
| OMIM = 136352
| ECnumber =
| Homologene = 7321
| MGIid = 95561
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005021 |text = vascular endothelial growth factor receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2324
| Hs_Ensembl = ENSG00000037280
| Hs_RefseqProtein = NP_002011
| Hs_RefseqmRNA = NM_002020
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 179962143
| Hs_GenLoc_end = 180009171
| Hs_Uniprot = P35916
| Mm_EntrezGene = 14257
| Mm_Ensembl = ENSMUSG00000020357
| Mm_RefseqmRNA = NM_008029
| Mm_RefseqProtein = NP_032055
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 49453150
| Mm_GenLoc_end = 49495652
| Mm_Uniprot = Q5SU94
}}
}}
'''Fms-related tyrosine kinase 4''', also known as '''FLT4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FLT4 fms-related tyrosine kinase 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2324| 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=Petrova TV, Makinen T, Alitalo K |title=Signaling via vascular endothelial growth factor receptors. |journal=Exp. Cell Res. |volume=253 |issue= 1 |pages= 117-30 |year= 1999 |pmid= 10579917 |doi= 10.1006/excr.1999.4707 }}
*{{cite journal | author=Aprelikova O, Pajusola K, Partanen J, ''et al.'' |title=FLT4, a novel class III receptor tyrosine kinase in chromosome 5q33-qter. |journal=Cancer Res. |volume=52 |issue= 3 |pages= 746-8 |year= 1992 |pmid= 1310071 |doi= }}
*{{cite journal | author=Galland F, Karamysheva A, Mattei MG, ''et al.'' |title=Chromosomal localization of FLT4, a novel receptor-type tyrosine kinase gene. |journal=Genomics |volume=13 |issue= 2 |pages= 475-8 |year= 1992 |pmid= 1319394 |doi= }}
*{{cite journal | author=Pajusola K, Aprelikova O, Korhonen J, ''et al.'' |title=FLT4 receptor tyrosine kinase contains seven immunoglobulin-like loops and is expressed in multiple human tissues and cell lines. |journal=Cancer Res. |volume=52 |issue= 20 |pages= 5738-43 |year= 1992 |pmid= 1327515 |doi= }}
*{{cite journal | author=Fournier E, Dubreuil P, Birnbaum D, Borg JP |title=Mutation at tyrosine residue 1337 abrogates ligand-dependent transforming capacity of the FLT4 receptor. |journal=Oncogene |volume=11 |issue= 5 |pages= 921-31 |year= 1995 |pmid= 7675451 |doi= }}
*{{cite journal | author=Pajusola K, Aprelikova O, Armstrong E, ''et al.'' |title=Two human FLT4 receptor tyrosine kinase isoforms with distinct carboxy terminal tails are produced by alternative processing of primary transcripts. |journal=Oncogene |volume=8 |issue= 11 |pages= 2931-7 |year= 1993 |pmid= 7692369 |doi= }}
*{{cite journal | author=Pajusola K, Aprelikova O, Pelicci G, ''et al.'' |title=Signalling properties of FLT4, a proteolytically processed receptor tyrosine kinase related to two VEGF receptors. |journal=Oncogene |volume=9 |issue= 12 |pages= 3545-55 |year= 1994 |pmid= 7970715 |doi= }}
*{{cite journal | author=Galland F, Karamysheva A, Pebusque MJ, ''et al.'' |title=The FLT4 gene encodes a transmembrane tyrosine kinase related to the vascular endothelial growth factor receptor. |journal=Oncogene |volume=8 |issue= 5 |pages= 1233-40 |year= 1993 |pmid= 8386825 |doi= }}
*{{cite journal | author=Fournier E, Rosnet O, Marchetto S, ''et al.'' |title=Interaction with the phosphotyrosine binding domain/phosphotyrosine interacting domain of SHC is required for the transforming activity of the FLT4/VEGFR3 receptor tyrosine kinase. |journal=J. Biol. Chem. |volume=271 |issue= 22 |pages= 12956-63 |year= 1996 |pmid= 8662748 |doi= }}
*{{cite journal | author=Lee J, Gray A, Yuan J, ''et al.'' |title=Vascular endothelial growth factor-related protein: a ligand and specific activator of the tyrosine kinase receptor Flt4. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 5 |pages= 1988-92 |year= 1996 |pmid= 8700872 |doi= }}
*{{cite journal | author=Kukk E, Lymboussaki A, Taira S, ''et al.'' |title=VEGF-C receptor binding and pattern of expression with VEGFR-3 suggests a role in lymphatic vascular development. |journal=Development |volume=122 |issue= 12 |pages= 3829-37 |year= 1997 |pmid= 9012504 |doi= }}
*{{cite journal | author=Achen MG, Jeltsch M, Kukk E, ''et al.'' |title=Vascular endothelial growth factor D (VEGF-D) is a ligand for the tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 2 |pages= 548-53 |year= 1998 |pmid= 9435229 |doi= }}
*{{cite journal | author=Ferrell RE, Levinson KL, Esman JH, ''et al.'' |title=Hereditary lymphedema: evidence for linkage and genetic heterogeneity. |journal=Hum. Mol. Genet. |volume=7 |issue= 13 |pages= 2073-8 |year= 1999 |pmid= 9817924 |doi= }}
*{{cite journal | author=Fournier E, Blaikie P, Rosnet O, ''et al.'' |title=Role of tyrosine residues and protein interaction domains of SHC adaptor in VEGF receptor 3 signaling. |journal=Oncogene |volume=18 |issue= 2 |pages= 507-14 |year= 1999 |pmid= 9927207 |doi= 10.1038/sj.onc.1202315 }}
*{{cite journal | author=Karkkainen MJ, Ferrell RE, Lawrence EC, ''et al.'' |title=Missense mutations interfere with VEGFR-3 signalling in primary lymphoedema. |journal=Nat. Genet. |volume=25 |issue= 2 |pages= 153-9 |year= 2000 |pmid= 10835628 |doi= 10.1038/75997 }}
*{{cite journal | author=Irrthum A, Karkkainen MJ, Devriendt K, ''et al.'' |title=Congenital hereditary lymphedema caused by a mutation that inactivates VEGFR3 tyrosine kinase. |journal=Am. J. Hum. Genet. |volume=67 |issue= 2 |pages= 295-301 |year= 2000 |pmid= 10856194 |doi= }}
*{{cite journal | author=Wang JF, Zhang XF, Groopman JE |title=Stimulation of beta 1 integrin induces tyrosine phosphorylation of vascular endothelial growth factor receptor-3 and modulates cell migration. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 41950-7 |year= 2001 |pmid= 11553610 |doi= 10.1074/jbc.M101370200 }}
*{{cite journal | author=Baldwin ME, Roufail S, Halford MM, ''et al.'' |title=Multiple forms of mouse vascular endothelial growth factor-D are generated by RNA splicing and proteolysis. |journal=J. Biol. Chem. |volume=276 |issue= 47 |pages= 44307-14 |year= 2001 |pmid= 11574540 |doi= 10.1074/jbc.M106188200 }}
*{{cite journal | author=Walter JW, North PE, Waner M, ''et al.'' |title=Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma. |journal=Genes Chromosomes Cancer |volume=33 |issue= 3 |pages= 295-303 |year= 2002 |pmid= 11807987 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GLI1... {November 17, 2007 9:58:57 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 9:59:18 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 = PBB_Protein_GLI1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2gli.
| PDB = {{PDB2|2gli}}
| Name = Glioma-associated oncogene homolog 1 (zinc finger protein)
| HGNCid = 4317
| Symbol = GLI1
| AltSymbols =; GLI
| OMIM = 165220
| ECnumber =
| Homologene = 3859
| MGIid = 95727
| GeneAtlas_image1 = PBB_GE_GLI1_206646_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008017 |text = microtubule binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0008589 |text = regulation of smoothened signaling pathway}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2735
| Hs_Ensembl = ENSG00000111087
| Hs_RefseqProtein = NP_005260
| Hs_RefseqmRNA = NM_005269
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 56140201
| Hs_GenLoc_end = 56152312
| Hs_Uniprot = P08151
| Mm_EntrezGene = 14632
| Mm_Ensembl = ENSMUSG00000025407
| Mm_RefseqmRNA = XM_989852
| Mm_RefseqProtein = XP_994946
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 126732838
| Mm_GenLoc_end = 126744538
| Mm_Uniprot = P47806
}}
}}
'''Glioma-associated oncogene homolog 1 (zinc finger protein)''', also known as '''GLI1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GLI1 glioma-associated oncogene homolog 1 (zinc finger protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2735| 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 which is a member of the Kruppel family of zinc finger proteins. The function of this gene has not been determined; however, it may play a role in normal development gene transcription. Mouse mutation studies indicate possible involvement in human foregut malformation.<ref name="entrez">{{cite web | title = Entrez Gene: GLI1 glioma-associated oncogene homolog 1 (zinc finger protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2735| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chung RY, Seizinger BR |title=Molecular genetics of neurological tumours. |journal=J. Med. Genet. |volume=29 |issue= 6 |pages= 361-7 |year= 1992 |pmid= 1320124 |doi= }}
*{{cite journal | author=Arheden K, Rønne M, Mandahl N, ''et al.'' |title=In situ hybridization localizes the human putative oncogene GLI to chromosome subbands 12q13.3-14.1. |journal=Hum. Genet. |volume=82 |issue= 1 |pages= 1-2 |year= 1989 |pmid= 2497059 |doi= }}
*{{cite journal | author=Kinzler KW, Ruppert JM, Bigner SH, Vogelstein B |title=The GLI gene is a member of the Kruppel family of zinc finger proteins. |journal=Nature |volume=332 |issue= 6162 |pages= 371-4 |year= 1988 |pmid= 2832761 |doi= 10.1038/332371a0 }}
*{{cite journal | author=Ruppert JM, Kinzler KW, Wong AJ, ''et al.'' |title=The GLI-Kruppel family of human genes. |journal=Mol. Cell. Biol. |volume=8 |issue= 8 |pages= 3104-13 |year= 1989 |pmid= 2850480 |doi= }}
*{{cite journal | author=Kinzler KW, Bigner SH, Bigner DD, ''et al.'' |title=Identification of an amplified, highly expressed gene in a human glioma. |journal=Science |volume=236 |issue= 4797 |pages= 70-3 |year= 1987 |pmid= 3563490 |doi= }}
*{{cite journal | author=Pavletich NP, Pabo CO |title=Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers. |journal=Science |volume=261 |issue= 5129 |pages= 1701-7 |year= 1993 |pmid= 8378770 |doi= }}
*{{cite journal | author=Sasaki H, Hui C, Nakafuku M, Kondoh H |title=A binding site for Gli proteins is essential for HNF-3beta floor plate enhancer activity in transgenics and can respond to Shh in vitro. |journal=Development |volume=124 |issue= 7 |pages= 1313-22 |year= 1997 |pmid= 9118802 |doi= }}
*{{cite journal | author=Liu CZ, Yang JT, Yoon JW, ''et al.'' |title=Characterization of the promoter region and genomic organization of GLI, a member of the Sonic hedgehog-Patched signaling pathway. |journal=Gene |volume=209 |issue= 1-2 |pages= 1-11 |year= 1998 |pmid= 9524201 |doi= }}
*{{cite journal | author=Motoyama J, Liu J, Mo R, ''et al.'' |title=Essential function of Gli2 and Gli3 in the formation of lung, trachea and oesophagus. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 54-7 |year= 1998 |pmid= 9731531 |doi= 10.1038/1711 }}
*{{cite journal | author=Ghali L, Wong ST, Green J, ''et al.'' |title=Gli1 protein is expressed in basal cell carcinomas, outer root sheath keratinocytes and a subpopulation of mesenchymal cells in normal human skin. |journal=J. Invest. Dermatol. |volume=113 |issue= 4 |pages= 595-9 |year= 1999 |pmid= 10504446 |doi= 10.1046/j.1523-1747.1999.00729.x }}
*{{cite journal | author=Kogerman P, Grimm T, Kogerman L, ''et al.'' |title=Mammalian suppressor-of-fused modulates nuclear-cytoplasmic shuttling of Gli-1. |journal=Nat. Cell Biol. |volume=1 |issue= 5 |pages= 312-9 |year= 1999 |pmid= 10559945 |doi= 10.1038/13031 }}
*{{cite journal | author=Stone DM, Murone M, Luoh S, ''et al.'' |title=Characterization of the human suppressor of fused, a negative regulator of the zinc-finger transcription factor Gli. |journal=J. Cell. Sci. |volume=112 ( Pt 23) |issue= |pages= 4437-48 |year= 2000 |pmid= 10564661 |doi= }}
*{{cite journal | author=Murone M, Luoh SM, Stone D, ''et al.'' |title=Gli regulation by the opposing activities of fused and suppressor of fused. |journal=Nat. Cell Biol. |volume=2 |issue= 5 |pages= 310-2 |year= 2000 |pmid= 10806483 |doi= 10.1038/35010610 }}
*{{cite journal | author=Wang XQ, Chan N, Rothnagel JA |title=Letters to the editor: identification of polymorphic variants of the GLI1 oncogene. |journal=J. Invest. Dermatol. |volume=115 |issue= 2 |pages= 328-9 |year= 2000 |pmid= 10951255 |doi= 10.1046/j.1523-1747.2000.00065.x }}
*{{cite journal | author=Wang XQ, Rothnagel JA |title=Post-transcriptional regulation of the gli1 oncogene by the expression of alternative 5' untranslated regions. |journal=J. Biol. Chem. |volume=276 |issue= 2 |pages= 1311-6 |year= 2001 |pmid= 11032829 |doi= 10.1074/jbc.M005191200 }}
*{{cite journal | author=Koyabu Y, Nakata K, Mizugishi K, ''et al.'' |title=Physical and functional interactions between Zic and Gli proteins. |journal=J. Biol. Chem. |volume=276 |issue= 10 |pages= 6889-92 |year= 2001 |pmid= 11238441 |doi= 10.1074/jbc.C000773200 }}
*{{cite journal | author=Kroft TL, Patterson J, Won Yoon J, ''et al.'' |title=GLI1 localization in the germinal epithelial cells alternates between cytoplasm and nucleus: upregulation in transgenic mice blocks spermatogenesis in pachytene. |journal=Biol. Reprod. |volume=65 |issue= 6 |pages= 1663-71 |year= 2002 |pmid= 11717126 |doi= }}
*{{cite journal | author=Villavicencio EH, Yoon JW, Frank DJ, ''et al.'' |title=Cooperative E-box regulation of human GLI1 by TWIST and USF. |journal=Genesis |volume=32 |issue= 4 |pages= 247-58 |year= 2002 |pmid= 11948912 |doi= }}
*{{cite journal | author=Mao J, Maye P, Kogerman P, ''et al.'' |title=Regulation of Gli1 transcriptional activity in the nucleus by Dyrk1. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35156-61 |year= 2002 |pmid= 12138125 |doi= 10.1074/jbc.M206743200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HNRPD... {November 17, 2007 9:59:18 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 9:59:56 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
| 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_HNRPD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hd0.
| PDB = {{PDB2|1hd0}}, {{PDB2|1hd1}}, {{PDB2|1iqt}}, {{PDB2|1wtb}}, {{PDB2|1x0f}}
| Name = Heterogeneous nuclear ribonucleoprotein D (AU-rich element RNA binding protein 1, 37kDa)
| HGNCid = 5036
| Symbol = HNRPD
| AltSymbols =; AUF1; AUF1A; P37; hnRNPD0
| OMIM = 601324
| ECnumber =
| Homologene = 22410
| MGIid =
| GeneAtlas_image1 = PBB_GE_HNRPD_209330_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HNRPD_221480_at_tn.png
| GeneAtlas_image3 = PBB_GE_HNRPD_221481_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0003729 |text = mRNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0000781 |text = chromosome, telomeric region}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006396 |text = RNA processing}} {{GNF_GO|id=GO:0006401 |text = RNA catabolic process}} {{GNF_GO|id=GO:0006402 |text = mRNA catabolic process}} {{GNF_GO|id=GO:0043488 |text = regulation of mRNA stability}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3184
| Hs_Ensembl = ENSG00000138668
| Hs_RefseqProtein = NP_001003810
| Hs_RefseqmRNA = NM_001003810
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 83493491
| Hs_GenLoc_end = 83514173
| Hs_Uniprot = Q14103
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Heterogeneous nuclear ribonucleoprotein D (AU-rich element RNA binding protein 1, 37kDa)''', also known as '''HNRPD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HNRPD heterogeneous nuclear ribonucleoprotein D (AU-rich element RNA binding protein 1, 37kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3184| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are nucleic acid binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind to RNAs. It localizes to both the nucleus and the cytoplasm. This protein is implicated in the regulation of mRNA stability. Alternative splicing of this gene results in four transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: HNRPD heterogeneous nuclear ribonucleoprotein D (AU-rich element RNA binding protein 1, 37kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3184| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tay N, Chan SH, Ren EC |title=Identification and cloning of a novel heterogeneous nuclear ribonucleoprotein C-like protein that functions as a transcriptional activator of the hepatitis B virus enhancer II. |journal=J. Virol. |volume=66 |issue= 12 |pages= 6841-8 |year= 1992 |pmid= 1433497 |doi= }}
*{{cite journal | author=Lahiri DK, Thomas JO |title=A cDNA clone of the hnRNP C proteins and its homology with the single-stranded DNA binding protein UP2. |journal=Nucleic Acids Res. |volume=14 |issue= 10 |pages= 4077-94 |year= 1986 |pmid= 3754960 |doi= }}
*{{cite journal | author=Kajita Y, Nakayama J, Aizawa M, Ishikawa F |title=The UUAG-specific RNA binding protein, heterogeneous nuclear ribonucleoprotein D0. Common modular structure and binding properties of the 2xRBD-Gly family. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22167-75 |year= 1995 |pmid= 7673195 |doi= }}
*{{cite journal | author=Zhang W, Wagner BJ, Ehrenman K, ''et al.'' |title=Purification, characterization, and cDNA cloning of an AU-rich element RNA-binding protein, AUF1. |journal=Mol. Cell. Biol. |volume=13 |issue= 12 |pages= 7652-65 |year= 1994 |pmid= 8246982 |doi= }}
*{{cite journal | author=Wagner BJ, Long L, Rao PN, ''et al.'' |title=Localization and physical mapping of genes encoding the A+U-rich element RNA-binding protein AUF1 to human chromosomes 4 and X. |journal=Genomics |volume=34 |issue= 2 |pages= 219-22 |year= 1997 |pmid= 8661052 |doi= 10.1006/geno.1996.0269 }}
*{{cite journal | author=Kiledjian M, DeMaria CT, Brewer G, Novick K |title=Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the alpha-globin mRNA stability complex. |journal=Mol. Cell. Biol. |volume=17 |issue= 8 |pages= 4870-6 |year= 1997 |pmid= 9234743 |doi= }}
*{{cite journal | author=Wagner BJ, DeMaria CT, Sun Y, ''et al.'' |title=Structure and genomic organization of the human AUF1 gene: alternative pre-mRNA splicing generates four protein isoforms. |journal=Genomics |volume=48 |issue= 2 |pages= 195-202 |year= 1998 |pmid= 9521873 |doi= 10.1006/geno.1997.5142 }}
*{{cite journal | author=Dempsey LA, Li MJ, DePace A, ''et al.'' |title=The human HNRPD locus maps to 4q21 and encodes a highly conserved protein. |journal=Genomics |volume=49 |issue= 3 |pages= 378-84 |year= 1998 |pmid= 9615222 |doi= 10.1006/geno.1998.5237 }}
*{{cite journal | author=Siomi MC, Fromont M, Rain JC, ''et al.'' |title=Functional conservation of the transportin nuclear import pathway in divergent organisms. |journal=Mol. Cell. Biol. |volume=18 |issue= 7 |pages= 4141-8 |year= 1998 |pmid= 9632798 |doi= }}
*{{cite journal | author=Tolnay M, Vereshchagina LA, Tsokos GC |title=Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specific DNA-binding protein. |journal=Biochem. J. |volume=338 ( Pt 2) |issue= |pages= 417-25 |year= 1999 |pmid= 10024518 |doi= }}
*{{cite journal | author=Nagata T, Kurihara Y, Matsuda G, ''et al.'' |title=Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0. |journal=J. Mol. Biol. |volume=287 |issue= 2 |pages= 221-37 |year= 1999 |pmid= 10080887 |doi= }}
*{{cite journal | author=Laroia G, Cuesta R, Brewer G, Schneider RJ |title=Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. |journal=Science |volume=284 |issue= 5413 |pages= 499-502 |year= 1999 |pmid= 10205060 |doi= }}
*{{cite journal | author=Blaxall BC, Dwyer-Nield LD, Bauer AK, ''et al.'' |title=Differential expression and localization of the mRNA binding proteins, AU-rich element mRNA binding protein (AUF1) and Hu antigen R (HuR), in neoplastic lung tissue. |journal=Mol. Carcinog. |volume=28 |issue= 2 |pages= 76-83 |year= 2000 |pmid= 10900464 |doi= }}
*{{cite journal | author=Arao Y, Kuriyama R, Kayama F, Kato S |title=A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D. |journal=Arch. Biochem. Biophys. |volume=380 |issue= 2 |pages= 228-36 |year= 2000 |pmid= 10933876 |doi= 10.1006/abbi.2000.1938 }}
*{{cite journal | author=Grosset C, Chen CY, Xu N, ''et al.'' |title=A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. |journal=Cell |volume=103 |issue= 1 |pages= 29-40 |year= 2000 |pmid= 11051545 |doi= }}
*{{cite journal | author=Katahira M, Miyanoiri Y, Enokizono Y, ''et al.'' |title=Structure of the C-terminal RNA-binding domain of hnRNP D0 (AUF1), its interactions with RNA and DNA, and change in backbone dynamics upon complex formation with DNA. |journal=J. Mol. Biol. |volume=311 |issue= 5 |pages= 973-88 |year= 2001 |pmid= 11531333 |doi= 10.1006/jmbi.2001.4862 }}
*{{cite journal | author=Lapucci A, Donnini M, Papucci L, ''et al.'' |title=AUF1 Is a bcl-2 A + U-rich element-binding protein involved in bcl-2 mRNA destabilization during apoptosis. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 16139-46 |year= 2002 |pmid= 11856759 |doi= 10.1074/jbc.M201377200 }}
*{{cite journal | author=Tolnay M, Juang YT, Tsokos GC |title=Protein kinase A enhances, whereas glycogen synthase kinase-3 beta inhibits, the activity of the exon 2-encoded transactivator domain of heterogeneous nuclear ribonucleoprotein D in a hierarchical fashion. |journal=Biochem. J. |volume=363 |issue= Pt 1 |pages= 127-36 |year= 2002 |pmid= 11903055 |doi= }}
*{{cite journal | author=Pioli PA, Hamilton BJ, Connolly JE, ''et al.'' |title=Lactate dehydrogenase is an AU-rich element-binding protein that directly interacts with AUF1. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35738-45 |year= 2002 |pmid= 12107167 |doi= 10.1074/jbc.M204002200 }}
*{{cite journal | author=Shchors K, Yehiely F, Kular RK, ''et al.'' |title=Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region binds AUF1 and heat shock protein 27. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47061-72 |year= 2003 |pmid= 12356764 |doi= 10.1074/jbc.M202272200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HOXA10... {November 17, 2007 9:59:56 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:00:37 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 =
| image_source =
| PDB =
| Name = Homeobox A10
| HGNCid = 5100
| Symbol = HOXA10
| AltSymbols =; PL; HOX1; HOX1.8; HOX1H; MGC12859
| OMIM = 142957
| ECnumber =
| Homologene = 7365
| MGIid = 96171
| GeneAtlas_image1 = PBB_GE_HOXA10_213150_at_tn.png
| GeneAtlas_image2 = PBB_GE_HOXA10_213147_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3206
| Hs_Ensembl = ENSG00000153807
| Hs_RefseqProtein = NP_061824
| Hs_RefseqmRNA = NM_018951
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 27177382
| Hs_GenLoc_end = 27180399
| Hs_Uniprot = P31260
| Mm_EntrezGene = 15395
| Mm_Ensembl = ENSMUSG00000000938
| Mm_RefseqmRNA = NM_008263
| Mm_RefseqProtein = NP_032289
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 52160780
| Mm_GenLoc_end = 52164522
| Mm_Uniprot = P31310
}}
}}
'''Homeobox A10''', also known as '''HOXA10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HOXA10 homeobox A10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3206| 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 = In vertebrates, the genes encoding the class of transcription factors called homeobox genes are found in clusters named A, B, C, and D on four separate chromosomes. Expression of these proteins is spatially and temporally regulated during embryonic development. This gene is part of the A cluster on chromosome 7 and encodes a DNA-binding transcription factor that may regulate gene expression, morphogenesis, and differentiation. More specifically, it may function in fertility, embryo viability, and regulation of hematopoietic lineage commitment. Alternatively spliced transcript variants encoding different isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: HOXA10 homeobox A10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3206| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Eun Kwon H, Taylor HS |title=The role of HOX genes in human implantation. |journal=Ann. N. Y. Acad. Sci. |volume=1034 |issue= |pages= 1-18 |year= 2005 |pmid= 15731295 |doi= 10.1196/annals.1335.001 }}
*{{cite journal | author=Scott MP |title=Vertebrate homeobox gene nomenclature. |journal=Cell |volume=71 |issue= 4 |pages= 551-3 |year= 1992 |pmid= 1358459 |doi= }}
*{{cite journal | author=Lowney P, Corral J, Detmer K, ''et al.'' |title=A human Hox 1 homeobox gene exhibits myeloid-specific expression of alternative transcripts in human hematopoietic cells. |journal=Nucleic Acids Res. |volume=19 |issue= 12 |pages= 3443-9 |year= 1991 |pmid= 1676505 |doi= }}
*{{cite journal | author=McAlpine PJ, Shows TB |title=Nomenclature for human homeobox genes. |journal=Genomics |volume=7 |issue= 3 |pages= 460 |year= 1990 |pmid= 1973146 |doi= }}
*{{cite journal | author=Shen WF, Largman C, Lowney P, ''et al.'' |title=Lineage-restricted expression of homeobox-containing genes in human hematopoietic cell lines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 21 |pages= 8536-40 |year= 1989 |pmid= 2573064 |doi= }}
*{{cite journal | author=Acampora D, D'Esposito M, Faiella A, ''et al.'' |title=The human HOX gene family. |journal=Nucleic Acids Res. |volume=17 |issue= 24 |pages= 10385-402 |year= 1990 |pmid= 2574852 |doi= }}
*{{cite journal | author=Sauvageau G, Lansdorp PM, Eaves CJ, ''et al.'' |title=Differential expression of homeobox genes in functionally distinct CD34+ subpopulations of human bone marrow cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 12223-7 |year= 1995 |pmid= 7527557 |doi= }}
*{{cite journal | author=Lawrence HJ, Sauvageau G, Ahmadi N, ''et al.'' |title=Stage- and lineage-specific expression of the HOXA10 homeobox gene in normal and leukemic hematopoietic cells. |journal=Exp. Hematol. |volume=23 |issue= 11 |pages= 1160-6 |year= 1995 |pmid= 7556525 |doi= }}
*{{cite journal | author=Satokata I, Benson G, Maas R |title=Sexually dimorphic sterility phenotypes in Hoxa10-deficient mice. |journal=Nature |volume=374 |issue= 6521 |pages= 460-3 |year= 1995 |pmid= 7700356 |doi= 10.1038/374460a0 }}
*{{cite journal | author=Castronovo V, Kusaka M, Chariot A, ''et al.'' |title=Homeobox genes: potential candidates for the transcriptional control of the transformed and invasive phenotype. |journal=Biochem. Pharmacol. |volume=47 |issue= 1 |pages= 137-43 |year= 1994 |pmid= 7906121 |doi= }}
*{{cite journal | author=Apiou F, Flagiello D, Cillo C, ''et al.'' |title=Fine mapping of human HOX gene clusters. |journal=Cytogenet. Cell Genet. |volume=73 |issue= 1-2 |pages= 114-5 |year= 1996 |pmid= 8646877 |doi= }}
*{{cite journal | author=Thorsteinsdottir U, Sauvageau G, Hough MR, ''et al.'' |title=Overexpression of HOXA10 in murine hematopoietic cells perturbs both myeloid and lymphoid differentiation and leads to acute myeloid leukemia. |journal=Mol. Cell. Biol. |volume=17 |issue= 1 |pages= 495-505 |year= 1997 |pmid= 8972230 |doi= }}
*{{cite journal | author=Shen WF, Montgomery JC, Rozenfeld S, ''et al.'' |title=AbdB-like Hox proteins stabilize DNA binding by the Meis1 homeodomain proteins. |journal=Mol. Cell. Biol. |volume=17 |issue= 11 |pages= 6448-58 |year= 1997 |pmid= 9343407 |doi= }}
*{{cite journal | author=Taylor HS, Vanden Heuvel GB, Igarashi P |title=A conserved Hox axis in the mouse and human female reproductive system: late establishment and persistent adult expression of the Hoxa cluster genes. |journal=Biol. Reprod. |volume=57 |issue= 6 |pages= 1338-45 |year= 1998 |pmid= 9408238 |doi= }}
*{{cite journal | author=Taylor HS, Arici A, Olive D, Igarashi P |title=HOXA10 is expressed in response to sex steroids at the time of implantation in the human endometrium. |journal=J. Clin. Invest. |volume=101 |issue= 7 |pages= 1379-84 |year= 1998 |pmid= 9525980 |doi= }}
*{{cite journal | author=Kawagoe H, Humphries RK, Blair A, ''et al.'' |title=Expression of HOX genes, HOX cofactors, and MLL in phenotypically and functionally defined subpopulations of leukemic and normal human hematopoietic cells. |journal=Leukemia |volume=13 |issue= 5 |pages= 687-98 |year= 1999 |pmid= 10374871 |doi= }}
*{{cite journal | author=Eklund EA, Jalava A, Kakar R |title=Tyrosine phosphorylation of HoxA10 decreases DNA binding and transcriptional repression during interferon gamma -induced differentiation of myeloid leukemia cell lines. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 20117-26 |year= 2000 |pmid= 10766757 |doi= 10.1074/jbc.M907915199 }}
*{{cite journal | author=Buske C, Feuring-Buske M, Antonchuk J, ''et al.'' |title=Overexpression of HOXA10 perturbs human lymphomyelopoiesis in vitro and in vivo. |journal=Blood |volume=97 |issue= 8 |pages= 2286-92 |year= 2001 |pmid= 11290589 |doi= }}
*{{cite journal | author=Cermik D, Karaca M, Taylor HS |title=HOXA10 expression is repressed by progesterone in the myometrium: differential tissue-specific regulation of HOX gene expression in the reproductive tract. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 7 |pages= 3387-92 |year= 2001 |pmid= 11443215 |doi= }}
*{{cite journal | author=Shen WF, Krishnan K, Lawrence HJ, Largman C |title=The HOX homeodomain proteins block CBP histone acetyltransferase activity. |journal=Mol. Cell. Biol. |volume=21 |issue= 21 |pages= 7509-22 |year= 2001 |pmid= 11585930 |doi= 10.1128/MCB.21.21.7509-7522.2001 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IGFBP4... {November 17, 2007 10:00:37 AM PST}
- SEARCH REDIRECT: Control Box Found: IGFBP4 {November 17, 2007 10:01:10 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:01:11 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:01:11 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:01:11 AM PST}
- UPDATED: Updated protein page: IGFBP4 {November 17, 2007 10:01:17 AM PST}
- INFO: Beginning work on INSL3... {November 17, 2007 10:01:17 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:01:45 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_INSL3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2h8b.
| PDB = {{PDB2|2h8b}}
| Name = Insulin-like 3 (Leydig cell)
| HGNCid = 6086
| Symbol = INSL3
| AltSymbols =; MGC119818; MGC119819; RLF; RLNL
| OMIM = 146738
| ECnumber =
| Homologene = 4048
| MGIid = 108427
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005158 |text = insulin receptor binding}} {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3640
| Hs_Ensembl =
| Hs_RefseqProtein = NP_005534
| Hs_RefseqmRNA = NM_005543
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 16336
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_013564
| Mm_RefseqProtein = NP_038592
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Insulin-like 3 (Leydig cell)''', also known as '''INSL3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: INSL3 insulin-like 3 (Leydig cell)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3640| 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 an insulin like hormone produced mainly in gonadal tissues in males and females. Studies of the mouse counterpart suggest that this gene may be involved in the development of urogenital tract and female fertility. It may also act as a hormone to regulate growth and differentiation of gubernaculum, and thus mediating intra-abdominal testicular descent. The mutations in this gene may lead to, but not a frequent cause of, cryptorchidism.<ref name="entrez">{{cite web | title = Entrez Gene: INSL3 insulin-like 3 (Leydig cell)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3640| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lai KS, Jin Y, Graham DK, ''et al.'' |title=A kinase-deficient splice variant of the human JAK3 is expressed in hematopoietic and epithelial cancer cells. |journal=J. Biol. Chem. |volume=270 |issue= 42 |pages= 25028-36 |year= 1995 |pmid= 7559633 |doi= }}
*{{cite journal | author=Macchi P, Villa A, Giliani S, ''et al.'' |title=Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). |journal=Nature |volume=377 |issue= 6544 |pages= 65-8 |year= 1995 |pmid= 7659163 |doi= 10.1038/377065a0 }}
*{{cite journal | author=Tashima LS, Hieber AD, Greenwood FC, Bryant-Greenwood GD |title=The human Leydig insulin-like (hLEY I-L) gene is expressed in the corpus luteum and trophoblast. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 2 |pages= 707-10 |year= 1995 |pmid= 7852540 |doi= }}
*{{cite journal | author=Burkhardt E, Adham IM, Brosig B, ''et al.'' |title=Structural organization of the porcine and human genes coding for a Leydig cell-specific insulin-like peptide (LEY I-L) and chromosomal localization of the human gene (INSL3). |journal=Genomics |volume=20 |issue= 1 |pages= 13-9 |year= 1994 |pmid= 8020942 |doi= 10.1006/geno.1994.1121 }}
*{{cite journal | author=Witthuhn BA, Silvennoinen O, Miura O, ''et al.'' |title=Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells. |journal=Nature |volume=370 |issue= 6485 |pages= 153-7 |year= 1994 |pmid= 8022486 |doi= 10.1038/370153a0 }}
*{{cite journal | author=Kawamura M, McVicar DW, Johnston JA, ''et al.'' |title=Molecular cloning of L-JAK, a Janus family protein-tyrosine kinase expressed in natural killer cells and activated leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6374-8 |year= 1994 |pmid= 8022790 |doi= }}
*{{cite journal | author=Burkhardt E, Adham IM, Hobohm U, ''et al.'' |title=A human cDNA coding for the Leydig insulin-like peptide (Ley I-L). |journal=Hum. Genet. |volume=94 |issue= 1 |pages= 91-4 |year= 1994 |pmid= 8034302 |doi= }}
*{{cite journal | author=Adham IM, Burkhardt E, Benahmed M, Engel W |title=Cloning of a cDNA for a novel insulin-like peptide of the testicular Leydig cells. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26668-72 |year= 1994 |pmid= 8253799 |doi= }}
*{{cite journal | author=Verbsky JW, Bach EA, Fang YF, ''et al.'' |title=Expression of Janus kinase 3 in human endothelial and other non-lymphoid and non-myeloid cells. |journal=J. Biol. Chem. |volume=271 |issue= 24 |pages= 13976-80 |year= 1996 |pmid= 8662778 |doi= }}
*{{cite journal | author=Candotti F, Oakes SA, Johnston JA, ''et al.'' |title=Structural and functional basis for JAK3-deficient severe combined immunodeficiency. |journal=Blood |volume=90 |issue= 10 |pages= 3996-4003 |year= 1997 |pmid= 9354668 |doi= }}
*{{cite journal | author=Bozzi F, Lefranc G, Villa A, ''et al.'' |title=Molecular and biochemical characterization of JAK3 deficiency in a patient with severe combined immunodeficiency over 20 years after bone marrow transplantation: implications for treatment. |journal=Br. J. Haematol. |volume=102 |issue= 5 |pages= 1363-6 |year= 1998 |pmid= 9753072 |doi= }}
*{{cite journal | author=Nef S, Parada LF |title=Cryptorchidism in mice mutant for Insl3. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 295-9 |year= 1999 |pmid= 10391220 |doi= 10.1038/10364 }}
*{{cite journal | author=Büllesbach EE, Rhodes R, Rembiesa B, Schwabe C |title=The relaxin-like factor is a hormone. |journal=Endocrine |volume=10 |issue= 2 |pages= 167-9 |year= 1999 |pmid= 10451226 |doi= }}
*{{cite journal | author=Krausz C, Quintana-Murci L, Fellous M, ''et al.'' |title=Absence of mutations involving the INSL3 gene in human idiopathic cryptorchidism. |journal=Mol. Hum. Reprod. |volume=6 |issue= 4 |pages= 298-302 |year= 2000 |pmid= 10729310 |doi= }}
*{{cite journal | author=Koskimies P, Virtanen H, Lindström M, ''et al.'' |title=A common polymorphism in the human relaxin-like factor (RLF) gene: no relationship with cryptorchidism. |journal=Pediatr. Res. |volume=47 |issue= 4 Pt 1 |pages= 538-41 |year= 2000 |pmid= 10759163 |doi= }}
*{{cite journal | author=Endo K, Takeshita T, Kasai H, ''et al.'' |title=STAM2, a new member of the STAM family, binding to the Janus kinases. |journal=FEBS Lett. |volume=477 |issue= 1-2 |pages= 55-61 |year= 2000 |pmid= 10899310 |doi= }}
*{{cite journal | author=Schumacher RF, Mella P, Badolato R, ''et al.'' |title=Complete genomic organization of the human JAK3 gene and mutation analysis in severe combined immunodeficiency by single-strand conformation polymorphism. |journal=Hum. Genet. |volume=106 |issue= 1 |pages= 73-9 |year= 2000 |pmid= 10982185 |doi= }}
*{{cite journal | author=Tomboc M, Lee PA, Mitwally MF, ''et al.'' |title=Insulin-like 3/relaxin-like factor gene mutations are associated with cryptorchidism. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 11 |pages= 4013-8 |year= 2000 |pmid= 11095425 |doi= }}
*{{cite journal | author=Hombach-Klonisch S, Buchmann J, Sarun S, ''et al.'' |title=Relaxin-like factor (RLF) is differentially expressed in the normal and neoplastic human mammary gland. |journal=Cancer |volume=89 |issue= 11 |pages= 2161-8 |year= 2001 |pmid= 11147585 |doi= }}
*{{cite journal | author=Lim HN, Raipert-de Meyts E, Skakkebaek NE, ''et al.'' |title=Genetic analysis of the INSL3 gene in patients with maldescent of the testis. |journal=Eur. J. Endocrinol. |volume=144 |issue= 2 |pages= 129-37 |year= 2001 |pmid= 11182749 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on JUND... {November 17, 2007 10:01:45 AM PST}
- SEARCH REDIRECT: Control Box Found: JUND {November 17, 2007 10:02:16 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:02:19 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:02:19 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:02:19 AM PST}
- UPDATED: Updated protein page: JUND {November 17, 2007 10:02:25 AM PST}
- INFO: Beginning work on KLK1... {November 17, 2007 10:02:25 AM PST}
- SEARCH REDIRECT: Control Box Found: KLK1 {November 17, 2007 10:02:50 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:02:51 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:02:51 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:02:51 AM PST}
- UPDATED: Updated protein page: KLK1 {November 17, 2007 10:02:59 AM PST}
- INFO: Beginning work on MCM2... {November 17, 2007 10:03:46 AM PST}
- SEARCH REDIRECT: Control Box Found: MCM2 {November 17, 2007 10:04:23 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:04:26 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:04:26 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:04:26 AM PST}
- UPDATED: Updated protein page: MCM2 {November 17, 2007 10:04:32 AM PST}
- INFO: Beginning work on NCSTN... {November 17, 2007 10:09:34 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:10:00 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 =
| image_source =
| PDB =
| Name = Nicastrin
| HGNCid = 17091
| Symbol = NCSTN
| AltSymbols =; APH2; KIAA0253; RP11-517F10.1
| OMIM = 605254
| ECnumber =
| Homologene = 41029
| MGIid = 1891700
| GeneAtlas_image1 = PBB_GE_NCSTN_208759_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006509 |text = membrane protein ectodomain proteolysis}} {{GNF_GO|id=GO:0007220 |text = Notch receptor processing}} {{GNF_GO|id=GO:0016485 |text = protein processing}} {{GNF_GO|id=GO:0042987 |text = amyloid precursor protein catabolic process}} {{GNF_GO|id=GO:0043085 |text = positive regulation of enzyme activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 23385
| Hs_Ensembl = ENSG00000162736
| Hs_RefseqProtein = NP_056146
| Hs_RefseqmRNA = NM_015331
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 158579678
| Hs_GenLoc_end = 158595366
| Hs_Uniprot = Q92542
| Mm_EntrezGene = 59287
| Mm_Ensembl = ENSMUSG00000003458
| Mm_RefseqmRNA = NM_021607
| Mm_RefseqProtein = NP_067620
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 173902696
| Mm_GenLoc_end = 173919424
| Mm_Uniprot = Q3T9E5
}}
}}
'''Nicastrin''', also known as '''NCSTN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NCSTN nicastrin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23385| 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 Type I transmembrane glycoprotein that is an integral component of the multimeric gamma-secretase complex. The encoded protein cleaves integral membrane proteins, including Notch receptors and beta-amyloid precursor protein, and may be a stabilizing cofactor required for gamma-secretase complex assembly. The cleavage of beta-amyloid precursor protein yields amyloid beta peptide, the main component of the neuritic plaque and the hallmark lesion in the brains of patients with Alzheimer's disease; however, the nature of the encoded protein's role in Alzheimer's disease is not known for certain. Alternatively spliced transcript variants have been described, but their full-length nature has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: NCSTN nicastrin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23385| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nagase T, Seki N, Ishikawa K, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. |journal=DNA Res. |volume=3 |issue= 5 |pages= 321-9, 341-54 |year= 1997 |pmid= 9039502 |doi= }}
*{{cite journal | author=Yu G, Nishimura M, Arawaka S, ''et al.'' |title=Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing. |journal=Nature |volume=407 |issue= 6800 |pages= 48-54 |year= 2000 |pmid= 10993067 |doi= 10.1038/35024009 }}
*{{cite journal | author=Fagan R, Swindells M, Overington J, Weir M |title=Nicastrin, a presenilin-interacting protein, contains an aminopeptidase/transferrin receptor superfamily domain. |journal=Trends Biochem. Sci. |volume=26 |issue= 4 |pages= 213-4 |year= 2001 |pmid= 11295540 |doi= }}
*{{cite journal | author=Satoh J, Kuroda Y |title=Nicastrin, a key regulator of presenilin function, is expressed constitutively in human neural cell lines. |journal=Neuropathology : official journal of the Japanese Society of Neuropathology |volume=21 |issue= 2 |pages= 115-22 |year= 2001 |pmid= 11396676 |doi= }}
*{{cite journal | author=Chen F, Yu G, Arawaka S, ''et al.'' |title=Nicastrin binds to membrane-tethered Notch. |journal=Nat. Cell Biol. |volume=3 |issue= 8 |pages= 751-4 |year= 2001 |pmid= 11483961 |doi= 10.1038/35087069 }}
*{{cite journal | author=Fergani A, Yu G, St George-Hyslop P, Checler F |title=Wild-type and mutated nicastrins do not display aminopeptidase M- and B-like activities. |journal=Biochem. Biophys. Res. Commun. |volume=289 |issue= 3 |pages= 678-80 |year= 2002 |pmid= 11726200 |doi= 10.1006/bbrc.2001.6030 }}
*{{cite journal | author=Leem JY, Vijayan S, Han P, ''et al.'' |title=Presenilin 1 is required for maturation and cell surface accumulation of nicastrin. |journal=J. Biol. Chem. |volume=277 |issue= 21 |pages= 19236-40 |year= 2002 |pmid= 11943765 |doi= 10.1074/jbc.C200148200 }}
*{{cite journal | author=Dermaut B, Theuns J, Sleegers K, ''et al.'' |title=The gene encoding nicastrin, a major gamma-secretase component, modifies risk for familial early-onset Alzheimer disease in a Dutch population-based sample. |journal=Am. J. Hum. Genet. |volume=70 |issue= 6 |pages= 1568-74 |year= 2002 |pmid= 11992262 |doi= }}
*{{cite journal | author=Li B, Cong F, Tan CP, ''et al.'' |title=Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-apoptotic activity. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 28870-6 |year= 2002 |pmid= 12021275 |doi= 10.1074/jbc.M202388200 }}
*{{cite journal | author=Yang DS, Tandon A, Chen F, ''et al.'' |title=Mature glycosylation and trafficking of nicastrin modulate its binding to presenilins. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 28135-42 |year= 2002 |pmid= 12032140 |doi= 10.1074/jbc.M110871200 }}
*{{cite journal | author=Tomita T, Katayama R, Takikawa R, Iwatsubo T |title=Complex N-glycosylated form of nicastrin is stabilized and selectively bound to presenilin fragments. |journal=FEBS Lett. |volume=520 |issue= 1-3 |pages= 117-21 |year= 2002 |pmid= 12044882 |doi= }}
*{{cite journal | author=Edbauer D, Winkler E, Haass C, Steiner H |title=Presenilin and nicastrin regulate each other and determine amyloid beta-peptide production via complex formation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 13 |pages= 8666-71 |year= 2002 |pmid= 12048259 |doi= 10.1073/pnas.132277899 }}
*{{cite journal | author=Hattori C, Asai M, Oma Y, ''et al.'' |title=BACE1 interacts with nicastrin. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 4 |pages= 1228-32 |year= 2002 |pmid= 12054507 |doi= 10.1016/S0006-291X(02)00351-0 }}
*{{cite journal | author=Kimberly WT, LaVoie MJ, Ostaszewski BL, ''et al.'' |title=Complex N-linked glycosylated nicastrin associates with active gamma-secretase and undergoes tight cellular regulation. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35113-7 |year= 2002 |pmid= 12130643 |doi= 10.1074/jbc.M204446200 }}
*{{cite journal | author=Steiner H, Winkler E, Edbauer D, ''et al.'' |title=PEN-2 is an integral component of the gamma-secretase complex required for coordinated expression of presenilin and nicastrin. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39062-5 |year= 2002 |pmid= 12198112 |doi= 10.1074/jbc.C200469200 }}
*{{cite journal | author=Lee SF, Shah S, Li H, ''et al.'' |title=Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 45013-9 |year= 2003 |pmid= 12297508 |doi= 10.1074/jbc.M208164200 }}
*{{cite journal | author=Gu Y, Chen F, Sanjo N, ''et al.'' |title=APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin.nicastrin complexes. |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7374-80 |year= 2003 |pmid= 12471034 |doi= 10.1074/jbc.M209499200 }}
*{{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=Siman R, Velji J |title=Localization of presenilin-nicastrin complexes and gamma-secretase activity to the trans-Golgi network. |journal=J. Neurochem. |volume=84 |issue= 5 |pages= 1143-53 |year= 2003 |pmid= 12603837 |doi= }}
*{{cite journal | author=Basrur V, Yang F, Kushimoto T, ''et al.'' |title=Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. |journal=J. Proteome Res. |volume=2 |issue= 1 |pages= 69-79 |year= 2003 |pmid= 12643545 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PROCR... {November 17, 2007 10:08:51 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:09:34 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_PROCR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1l8j.
| PDB = {{PDB2|1l8j}}, {{PDB2|1lqv}}
| Name = Protein C receptor, endothelial (EPCR)
| HGNCid = 9452
| Symbol = PROCR
| AltSymbols =; CCCA; CCD41; CD201; EPCR; MGC23024; bA42O4.2
| OMIM = 600646
| ECnumber =
| Homologene = 4670
| MGIid = 104596
| GeneAtlas_image1 = PBB_GE_PROCR_203650_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}}
| Component = {{GNF_GO|id=GO:0005813 |text = centrosome}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10544
| Hs_Ensembl = ENSG00000101000
| Hs_RefseqProtein = NP_006395
| Hs_RefseqmRNA = NM_006404
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 33212131
| Hs_GenLoc_end = 33228826
| Hs_Uniprot = Q9UNN8
| Mm_EntrezGene = 19124
| Mm_Ensembl = ENSMUSG00000027611
| Mm_RefseqmRNA = NM_011171
| Mm_RefseqProtein = NP_035301
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 155442784
| Mm_GenLoc_end = 155446899
| Mm_Uniprot = Q4FK76
}}
}}
'''Protein C receptor, endothelial (EPCR)''', also known as '''PROCR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PROCR protein C receptor, endothelial (EPCR)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10544| 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 receptor for activated protein C, a serine protease activated by and involved in the blood coagulation pathway. The encoded protein is an N-glycosylated type I membrane protein that enhances the activation of protein C. Mutations in this gene have been associated with venous thromboembolism and myocardial infarction, as well as with late fetal loss during pregnancy.<ref name="entrez">{{cite web | title = Entrez Gene: PROCR protein C receptor, endothelial (EPCR)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10544| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Esmon CT |title=Coagulation and inflammation. |journal=J. Endotoxin Res. |volume=9 |issue= 3 |pages= 192-8 |year= 2004 |pmid= 12831462 |doi= 10.1179/096805103125001603 }}
*{{cite journal | author=Ruf W, Dorfleutner A, Riewald M |title=Specificity of coagulation factor signaling. |journal=J. Thromb. Haemost. |volume=1 |issue= 7 |pages= 1495-503 |year= 2003 |pmid= 12871285 |doi= }}
*{{cite journal | author=Van de Wouwer M, Collen D, Conway EM |title=Thrombomodulin-protein C-EPCR system: integrated to regulate coagulation and inflammation. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 8 |pages= 1374-83 |year= 2005 |pmid= 15178554 |doi= 10.1161/01.ATV.0000134298.25489.92 }}
*{{cite journal | author=Medina P, Navarro S, Estellés A, España F |title=Polymorphisms in the endothelial protein C receptor gene and thrombophilia. |journal=Thromb. Haemost. |volume=98 |issue= 3 |pages= 564-9 |year= 2007 |pmid= 17849044 |doi= }}
*{{cite journal | author=Raheja KK |title=Nursing in transition. |journal=Nursing forum |volume=15 |issue= 4 |pages= 413-7 |year= 1977 |pmid= 1051893 |doi= }}
*{{cite journal | author=Fukudome K, Esmon CT |title=Identification, cloning, and regulation of a novel endothelial cell protein C/activated protein C receptor. |journal=J. Biol. Chem. |volume=269 |issue= 42 |pages= 26486-91 |year= 1994 |pmid= 7929370 |doi= }}
*{{cite journal | author=Laszik Z, Mitro A, Taylor FB, ''et al.'' |title=Human protein C receptor is present primarily on endothelium of large blood vessels: implications for the control of the protein C pathway. |journal=Circulation |volume=96 |issue= 10 |pages= 3633-40 |year= 1998 |pmid= 9396465 |doi= }}
*{{cite journal | author=Ye X, Fukudome K, Tsuneyoshi N, ''et al.'' |title=The endothelial cell protein C receptor (EPCR) functions as a primary receptor for protein C activation on endothelial cells in arteries, veins, and capillaries. |journal=Biochem. Biophys. Res. Commun. |volume=259 |issue= 3 |pages= 671-7 |year= 1999 |pmid= 10364477 |doi= 10.1006/bbrc.1999.0846 }}
*{{cite journal | author=Simmonds RE, Lane DA |title=Structural and functional implications of the intron/exon organization of the human endothelial cell protein C/activated protein C receptor (EPCR) gene: comparison with the structure of CD1/major histocompatibility complex alpha1 and alpha2 domains. |journal=Blood |volume=94 |issue= 2 |pages= 632-41 |year= 1999 |pmid= 10397730 |doi= }}
*{{cite journal | author=Rothbarth K, Dabaghian AR, Stammer H, Werner D |title=One single mRNA encodes the centrosomal protein CCD41 and the endothelial cell protein C receptor (EPCR). |journal=FEBS Lett. |volume=458 |issue= 1 |pages= 77-80 |year= 1999 |pmid= 10518938 |doi= }}
*{{cite journal | author=Hayashi T, Nakamura H, Okada A, ''et al.'' |title=Organization and chromosomal localization of the human endothelial protein C receptor gene. |journal=Gene |volume=238 |issue= 2 |pages= 367-73 |year= 1999 |pmid= 10570964 |doi= }}
*{{cite journal | author=Liaw PC, Neuenschwander PF, Smirnov MD, Esmon CT |title=Mechanisms by which soluble endothelial cell protein C receptor modulates protein C and activated protein C function. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5447-52 |year= 2000 |pmid= 10681521 |doi= }}
*{{cite journal | author=Xu J, Qu D, Esmon NL, Esmon CT |title=Metalloproteolytic release of endothelial cell protein C receptor. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 6038-44 |year= 2000 |pmid= 10681599 |doi= }}
*{{cite journal | author=Liaw PC, Mather T, Oganesyan N, ''et al.'' |title=Identification of the protein C/activated protein C binding sites on the endothelial cell protein C receptor. Implications for a novel mode of ligand recognition by a major histocompatibility complex class 1-type receptor. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 8364-70 |year= 2001 |pmid= 11099506 |doi= 10.1074/jbc.M010572200 }}
*{{cite journal | author=Biguzzi E, Merati G, Liaw PC, ''et al.'' |title=A 23bp insertion in the endothelial protein C receptor (EPCR) gene impairs EPCR function. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 945-8 |year= 2002 |pmid= 11686350 |doi= }}
*{{cite journal | author=Galligan L, Livingstone W, Volkov Y, ''et al.'' |title=Characterization of protein C receptor expression in monocytes. |journal=Br. J. Haematol. |volume=115 |issue= 2 |pages= 408-14 |year= 2001 |pmid= 11703343 |doi= }}
*{{cite journal | author=von Depka M, Czwalinna A, Eisert R, ''et al.'' |title=Prevalence of a 23bp insertion in exon 3 of the endothelial cell protein C receptor gene in venous thrombophilia. |journal=Thromb. Haemost. |volume=86 |issue= 6 |pages= 1360-2 |year= 2002 |pmid= 11776299 |doi= }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Oganesyan V, Oganesyan N, Terzyan S, ''et al.'' |title=The crystal structure of the endothelial protein C receptor and a bound phospholipid. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 24851-4 |year= 2002 |pmid= 12034704 |doi= 10.1074/jbc.C200163200 }}
*{{cite journal | author=Riewald M, Petrovan RJ, Donner A, ''et al.'' |title=Activation of endothelial cell protease activated receptor 1 by the protein C pathway. |journal=Science |volume=296 |issue= 5574 |pages= 1880-2 |year= 2002 |pmid= 12052963 |doi= 10.1126/science.1071699 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMC2... {November 17, 2007 10:05:10 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:05:43 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 =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) 26S subunit, ATPase, 2
| HGNCid = 9548
| Symbol = PSMC2
| AltSymbols =; S7; MGC3004; MSS1; Nbla10058
| OMIM = 154365
| ECnumber =
| Homologene = 2096
| MGIid = 109555
| GeneAtlas_image1 = PBB_GE_PSMC2_201068_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMC2_201067_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0017111 |text = nucleoside-triphosphatase activity}}
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5701
| Hs_Ensembl = ENSG00000161057
| Hs_RefseqProtein = NP_002794
| Hs_RefseqmRNA = NM_002803
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 102775325
| Hs_GenLoc_end = 102795891
| Hs_Uniprot = P35998
| Mm_EntrezGene = 19181
| Mm_Ensembl = ENSMUSG00000028932
| Mm_RefseqmRNA = NM_011188
| Mm_RefseqProtein = NP_035318
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 21297107
| Mm_GenLoc_end = 21315608
| Mm_Uniprot = Q3U5V3
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, ATPase, 2''', also known as '''PSMC2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMC2 proteasome (prosome, macropain) 26S subunit, ATPase, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5701| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. This subunit has been shown to interact with several of the basal transcription factors so, in addition to participation in proteasome functions, this subunit may participate in the regulation of transcription. This subunit may also compete with PSMC3 for binding to the HIV tat protein to regulate the interaction between the viral protein and the transcription complex.<ref name="entrez">{{cite web | title = Entrez Gene: PSMC2 proteasome (prosome, macropain) 26S subunit, ATPase, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5701| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Shibuya H, Irie K, Ninomiya-Tsuji J, ''et al.'' |title=New human gene encoding a positive modulator of HIV Tat-mediated transactivation. |journal=Nature |volume=357 |issue= 6380 |pages= 700-2 |year= 1992 |pmid= 1377363 |doi= 10.1038/357700a0 }}
*{{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=Nacken W, Kingsman AJ, Kingsman SM, ''et al.'' |title=A homologue of the human MSS1 gene, a positive modulator of HIV-1 gene expression, is massively expressed in Xenopus oocytes. |journal=Biochim. Biophys. Acta |volume=1261 |issue= 2 |pages= 293-5 |year= 1995 |pmid= 7711076 |doi= }}
*{{cite journal | author=Ghislain M, Udvardy A, Mann C |title=S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. |journal=Nature |volume=366 |issue= 6453 |pages= 358-62 |year= 1993 |pmid= 8247132 |doi= 10.1038/366358a0 }}
*{{cite journal | author=Dubiel W, Ferrell K, Rechsteiner M |title=Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease. |journal=FEBS Lett. |volume=323 |issue= 3 |pages= 276-8 |year= 1993 |pmid= 8500623 |doi= }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Chen Y, Sharp ZD, Lee WH |title=HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 24081-7 |year= 1997 |pmid= 9295362 |doi= }}
*{{cite journal | author=Tanahashi N, Suzuki M, Fujiwara T, ''et al.'' |title=Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 229-32 |year= 1998 |pmid= 9473509 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Zheng L, Chen Y, Lee WH |title=Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 8 |pages= 5417-28 |year= 1999 |pmid= 10409732 |doi= }}
*{{cite journal | author=Gorbea C, Taillandier D, Rechsteiner M |title=Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7. |journal=J. Biol. Chem. |volume=275 |issue= 2 |pages= 875-82 |year= 2000 |pmid= 10625621 |doi= }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Hwang J, Fauzi H, Fukuda K, ''et al.'' |title=The RNA aptamer-binding site of hepatitis C virus NS3 protease. |journal=Biochem. Biophys. Res. Commun. |volume=279 |issue= 2 |pages= 557-62 |year= 2001 |pmid= 11118325 |doi= 10.1006/bbrc.2000.4007 }}
*{{cite journal | author=Yanagi S, Shimbara N, Tamura T |title=Tissue and cell distribution of a mammalian proteasomal ATPase, MSS1, and its complex formation with the basal transcription factors. |journal=Biochem. Biophys. Res. Commun. |volume=279 |issue= 2 |pages= 568-73 |year= 2001 |pmid= 11118327 |doi= 10.1006/bbrc.2000.3969 }}
*{{cite journal | author=Hartmann-Petersen R, Tanaka K, Hendil KB |title=Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 89-94 |year= 2001 |pmid= 11361004 |doi= 10.1006/abbi.2000.2178 }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMC3... {November 17, 2007 10:05:43 AM PST}
- SEARCH REDIRECT: Control Box Found: PSMC3 {November 17, 2007 10:06:09 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:06:12 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:06:12 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:06:12 AM PST}
- UPDATED: Updated protein page: PSMC3 {November 17, 2007 10:06:18 AM PST}
- INFO: Beginning work on PTPN12... {November 17, 2007 10:06:18 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:06:44 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 =
| image_source =
| PDB =
| Name = Protein tyrosine phosphatase, non-receptor type 12
| HGNCid = 9645
| Symbol = PTPN12
| AltSymbols =; PTP-PEST; PTPG1
| OMIM = 600079
| ECnumber =
| Homologene = 37691
| MGIid = 104673
| GeneAtlas_image1 = PBB_GE_PTPN12_202006_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTPN12_216915_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004726 |text = non-membrane spanning protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0017124 |text = SH3 domain binding}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5782
| Hs_Ensembl = ENSG00000127947
| Hs_RefseqProtein = NP_002826
| Hs_RefseqmRNA = NM_002835
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 77004351
| Hs_GenLoc_end = 77107324
| Hs_Uniprot = Q05209
| Mm_EntrezGene = 19248
| Mm_Ensembl = ENSMUSG00000028771
| Mm_RefseqmRNA = NM_011203
| Mm_RefseqProtein = NP_035333
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 20498465
| Mm_GenLoc_end = 20567621
| Mm_Uniprot = Q3TVC3
}}
}}
'''Protein tyrosine phosphatase, non-receptor type 12''', also known as '''PTPN12''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPN12 protein tyrosine phosphatase, non-receptor type 12| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5782| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains a C-terminal PEST motif, which serves as a protein-protein interaction domain, and may be related to protein intracellular half-life. This PTP was found to bind and dephosphorylate the product of oncogene c-ABL, thus may play a role in oncogenesis. This PTP was shown to interact with, and dephosphorylate, various of cytoskeleton and cell adhesion molecules, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin, which suggested its regulatory roles in controlling cell shape and mobility.<ref name="entrez">{{cite web | title = Entrez Gene: PTPN12 protein tyrosine phosphatase, non-receptor type 12| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5782| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Takekawa M, Itoh F, Hinoda Y, ''et al.'' |title=Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 2 |pages= 1223-30 |year= 1993 |pmid= 1472029 |doi= }}
*{{cite journal | author=Yi T, Cleveland JL, Ihle JN |title=Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification. |journal=Blood |volume=78 |issue= 9 |pages= 2222-8 |year= 1991 |pmid= 1932742 |doi= }}
*{{cite journal | author=Takekawa M, Itoh F, Hinoda Y, ''et al.'' |title=Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells. |journal=FEBS Lett. |volume=339 |issue= 3 |pages= 222-8 |year= 1994 |pmid= 7509295 |doi= }}
*{{cite journal | author=Garton AJ, Tonks NK |title=PTP-PEST: a protein tyrosine phosphatase regulated by serine phosphorylation. |journal=EMBO J. |volume=13 |issue= 16 |pages= 3763-71 |year= 1994 |pmid= 7520867 |doi= }}
*{{cite journal | author=Habib T, Herrera R, Decker SJ |title=Activators of protein kinase C stimulate association of Shc and the PEST tyrosine phosphatase. |journal=J. Biol. Chem. |volume=269 |issue= 41 |pages= 25243-6 |year= 1994 |pmid= 7929214 |doi= }}
*{{cite journal | author=Yang Q, Co D, Sommercorn J, Tonks NK |title=Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase. |journal=J. Biol. Chem. |volume=268 |issue= 23 |pages= 17650 |year= 1993 |pmid= 8349645 |doi= }}
*{{cite journal | author=Yang Q, Co D, Sommercorn J, Tonks NK |title=Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase. |journal=J. Biol. Chem. |volume=268 |issue= 9 |pages= 6622-8 |year= 1993 |pmid= 8454633 |doi= }}
*{{cite journal | author=Charest A, Wagner J, Jacob S, ''et al.'' |title=Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8424-9 |year= 1996 |pmid= 8626541 |doi= }}
*{{cite journal | author=Garton AJ, Flint AJ, Tonks NK |title=Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6408-18 |year= 1996 |pmid= 8887669 |doi= }}
*{{cite journal | author=Charest A, Wagner J, Kwan M, Tremblay ML |title=Coupling of the murine protein tyrosine phosphatase PEST to the epidermal growth factor (EGF) receptor through a Src homology 3 (SH3) domain-mediated association with Grb2. |journal=Oncogene |volume=14 |issue= 14 |pages= 1643-51 |year= 1997 |pmid= 9135065 |doi= 10.1038/sj.onc.1201008 }}
*{{cite journal | author=Garton AJ, Burnham MR, Bouton AH, Tonks NK |title=Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition. |journal=Oncogene |volume=15 |issue= 8 |pages= 877-85 |year= 1997 |pmid= 9285683 |doi= 10.1038/sj.onc.1201279 }}
*{{cite journal | author=Dowbenko D, Spencer S, Quan C, Lasky LA |title=Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein. |journal=J. Biol. Chem. |volume=273 |issue= 2 |pages= 989-96 |year= 1998 |pmid= 9422760 |doi= }}
*{{cite journal | author=Shen Y, Schneider G, Cloutier JF, ''et al.'' |title=Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin. |journal=J. Biol. Chem. |volume=273 |issue= 11 |pages= 6474-81 |year= 1998 |pmid= 9497381 |doi= }}
*{{cite journal | author=Côté JF, Charest A, Wagner J, Tremblay ML |title=Combination of gene targeting and substrate trapping to identify substrates of protein tyrosine phosphatases using PTP-PEST as a model. |journal=Biochemistry |volume=37 |issue= 38 |pages= 13128-37 |year= 1998 |pmid= 9748319 |doi= 10.1021/bi981259l }}
*{{cite journal | author=Wu Y, Dowbenko D, Lasky LA |title=PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30487-96 |year= 1998 |pmid= 9804817 |doi= }}
*{{cite journal | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi= }}
*{{cite journal | author=Li J, Nishizawa K, An W, ''et al.'' |title=A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion. |journal=EMBO J. |volume=17 |issue= 24 |pages= 7320-36 |year= 1999 |pmid= 9857189 |doi= 10.1093/emboj/17.24.7320 }}
*{{cite journal | author=Garton AJ, Tonks NK |title=Regulation of fibroblast motility by the protein tyrosine phosphatase PTP-PEST. |journal=J. Biol. Chem. |volume=274 |issue= 6 |pages= 3811-8 |year= 1999 |pmid= 9920935 |doi= }}
*{{cite journal | author=Angers-Loustau A, Côté JF, Charest A, ''et al.'' |title=Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts. |journal=J. Cell Biol. |volume=144 |issue= 5 |pages= 1019-31 |year= 1999 |pmid= 10085298 |doi= }}
*{{cite journal | author=Nishiya N, Iwabuchi Y, Shibanuma M, ''et al.'' |title=Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9847-53 |year= 1999 |pmid= 10092676 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAB7A... {November 17, 2007 10:07:45 AM PST}
- SEARCH: Multiple Conflicting Pages. Need Resolution. {November 17, 2007 10:08:16 AM PST}
- AMBIGUITY: More than one potential page found for updating, RAB7A RAB7A {November 17, 2007 10:08:16 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_RAB7A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1t91.
| PDB = {{PDB2|1t91}}, {{PDB2|1vg0}}, {{PDB2|1vg1}}, {{PDB2|1vg8}}, {{PDB2|1vg9}}, {{PDB2|1yhn}}
| Name = RAB7A, member RAS oncogene family
| HGNCid = 9788
| Symbol = RAB7A
| AltSymbols =; FLJ20819; PRO2706; RAB7
| OMIM = 602298
| ECnumber =
| Homologene = 3408
| MGIid = 105068
| GeneAtlas_image1 = PBB_GE_RAB7A_211960_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005770 |text = late endosome}}
| Process = {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7879
| Hs_Ensembl = ENSG00000075785
| Hs_RefseqProtein = NP_004628
| Hs_RefseqmRNA = NM_004637
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 129927669
| Hs_GenLoc_end = 130016329
| Hs_Uniprot = P51149
| Mm_EntrezGene = 19349
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009005
| Mm_RefseqProtein = NP_033031
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''RAB7A, member RAS oncogene family''', also known as '''RAB7A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAB7A RAB7A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7879| 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 = Members of the RAB family of RAS-related GTP-binding proteins are important regulators of vesicular transport and are located in specific intracellular compartments. RAB7 has been localized to late endosomes and shown to be important in the late endocytic pathway. In addition, it has been shown to have a fundamental role in the cellular vacuolation induced by the cytotoxin VacA of Helicobacter pylori.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: RAB7A RAB7A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7879| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chavrier P, Parton RG, Hauri HP, ''et al.'' |title=Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. |journal=Cell |volume=62 |issue= 2 |pages= 317-29 |year= 1990 |pmid= 2115402 |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=Simon I, Zerial M, Goody RS |title=Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20470-8 |year= 1996 |pmid= 8702787 |doi= }}
*{{cite journal | author=Bottger G, Nagelkerken B, van der Sluijs P |title=Rab4 and Rab7 define distinct nonoverlapping endosomal compartments. |journal=J. Biol. Chem. |volume=271 |issue= 46 |pages= 29191-7 |year= 1997 |pmid= 8910576 |doi= }}
*{{cite journal | author=Vitelli R, Chiariello M, Lattero D, ''et al.'' |title=Molecular cloning and expression analysis of the human Rab7 GTP-ase complementary deoxyribonucleic acid. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 3 |pages= 887-90 |year= 1997 |pmid= 8954989 |doi= 10.1006/bbrc.1996.1897 }}
*{{cite journal | author=Davies JP, Cotter PD, Ioannou YA |title=Cloning and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene. |journal=Genomics |volume=41 |issue= 1 |pages= 131-4 |year= 1997 |pmid= 9126495 |doi= 10.1006/geno.1997.4644 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Kashuba VI, Gizatullin RZ, Protopopov AI, ''et al.'' |title=NotI linking/jumping clones of human chromosome 3: mapping of the TFRC, RAB7 and HAUSP genes to regions rearranged in leukemia and deleted in solid tumors. |journal=FEBS Lett. |volume=419 |issue= 2-3 |pages= 181-5 |year= 1998 |pmid= 9428630 |doi= }}
*{{cite journal | author=Alexandrov K, Simon I, Iakovenko A, ''et al.'' |title=Moderate discrimination of REP-1 between Rab7 x GDP and Rab7 x GTP arises from a difference of an order of magnitude in dissociation rates. |journal=FEBS Lett. |volume=425 |issue= 3 |pages= 460-4 |year= 1998 |pmid= 9563513 |doi= }}
*{{cite journal | author=Chiariello M, De Gregorio L, Vitelli R, ''et al.'' |title=Genetic mapping of the mouse Rab7 gene and pseudogene and of the human RAB7 homolog. |journal=Mamm. Genome |volume=9 |issue= 6 |pages= 448-52 |year= 1998 |pmid= 9585432 |doi= }}
*{{cite journal | author=de Leeuw HP, Koster PM, Calafat J, ''et al.'' |title=Small GTP-binding proteins in human endothelial cells. |journal=Br. J. Haematol. |volume=103 |issue= 1 |pages= 15-9 |year= 1998 |pmid= 9792283 |doi= }}
*{{cite journal | author=Bao S, Zhu J, Garvey WT |title=Cloning of Rab GTPases expressed in human skeletal muscle: studies in insulin-resistant subjects. |journal=Horm. Metab. Res. |volume=30 |issue= 11 |pages= 656-62 |year= 1999 |pmid= 9918381 |doi= }}
*{{cite journal | author=Bucci C, Chiariello M, Lattero D, ''et al.'' |title=Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1). |journal=Biochem. Biophys. Res. Commun. |volume=258 |issue= 3 |pages= 657-62 |year= 1999 |pmid= 10329441 |doi= 10.1006/bbrc.1999.0651 }}
*{{cite journal | author=Alexandrov K, Simon I, Yurchenko V, ''et al.'' |title=Characterization of the ternary complex between Rab7, REP-1 and Rab geranylgeranyl transferase. |journal=Eur. J. Biochem. |volume=265 |issue= 1 |pages= 160-70 |year= 1999 |pmid= 10491170 |doi= }}
*{{cite journal | author=Bucci C, Thomsen P, Nicoziani P, ''et al.'' |title=Rab7: a key to lysosome biogenesis. |journal=Mol. Biol. Cell |volume=11 |issue= 2 |pages= 467-80 |year= 2000 |pmid= 10679007 |doi= }}
*{{cite journal | author=Thomä NH, Iakovenko A, Kalinin A, ''et al.'' |title=Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II. |journal=Biochemistry |volume=40 |issue= 1 |pages= 268-74 |year= 2001 |pmid= 11141079 |doi= }}
*{{cite journal | author=Cantalupo G, Alifano P, Roberti V, ''et al.'' |title=Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. |journal=EMBO J. |volume=20 |issue= 4 |pages= 683-93 |year= 2001 |pmid= 11179213 |doi= 10.1093/emboj/20.4.683 }}
*{{cite journal | author=Thomä NH, Niculae A, Goody RS, Alexandrov K |title=Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate. |journal=J. Biol. Chem. |volume=276 |issue= 52 |pages= 48631-6 |year= 2002 |pmid= 11591706 |doi= 10.1074/jbc.M106470200 }}
*{{cite journal | author=Thomä NH, Iakovenko A, Goody RS, Alexandrov K |title=Phosphoisoprenoids modulate association of Rab geranylgeranyltransferase with REP-1. |journal=J. Biol. Chem. |volume=276 |issue= 52 |pages= 48637-43 |year= 2002 |pmid= 11675392 |doi= 10.1074/jbc.M108241200 }}
*{{cite journal | author=Croizet-Berger K, Daumerie C, Couvreur M, ''et al.'' |title=The endocytic catalysts, Rab5a and Rab7, are tandem regulators of thyroid hormone production. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 8277-82 |year= 2002 |pmid= 12034881 |doi= 10.1073/pnas.122187699 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TFPI2... {November 17, 2007 10:08:16 AM PST}
- SEARCH REDIRECT: Control Box Found: TFPI2 {November 17, 2007 10:08:44 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:08:45 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:08:45 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:08:45 AM PST}
- UPDATED: Updated protein page: TFPI2 {November 17, 2007 10:08:51 AM PST}
- INFO: Beginning work on TNPO1... {November 17, 2007 10:02:59 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:03:46 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TNPO1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qbk.
| PDB = {{PDB2|1qbk}}, {{PDB2|2h4m}}, {{PDB2|2ot8}}
| Name = Transportin 1
| HGNCid = 6401
| Symbol = TNPO1
| AltSymbols =; IPO2; KPNB2; MIP; MIP1; TRN
| OMIM = 602901
| ECnumber =
| Homologene = 5358
| MGIid = 2681523
| GeneAtlas_image1 = PBB_GE_TNPO1_221829_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TNPO1_207657_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_TNPO1_209225_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008139 |text = nuclear localization sequence binding}} {{GNF_GO|id=GO:0008565 |text = protein transporter activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005643 |text = nuclear pore}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000059 |text = protein import into nucleus, docking}} {{GNF_GO|id=GO:0000060 |text = protein import into nucleus, translocation}} {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3842
| Hs_Ensembl = ENSG00000083312
| Hs_RefseqProtein = NP_002261
| Hs_RefseqmRNA = NM_002270
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 72148171
| Hs_GenLoc_end = 72248316
| Hs_Uniprot = Q92973
| Mm_EntrezGene = 238799
| Mm_Ensembl = ENSMUSG00000009470
| Mm_RefseqmRNA = NM_001048267
| Mm_RefseqProtein = NP_001041732
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 99942895
| Mm_GenLoc_end = 100026541
| Mm_Uniprot = Q3TKD0
}}
}}
'''Transportin 1''', also known as '''TNPO1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNPO1 transportin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3842| 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 beta subunit of the karyopherin receptor complex which interacts with nuclear localization signals to target nuclear proteins to the nucleus. The karyopherin receptor complex is a heterodimer of an alpha subunit which recognizes the nuclear localization signal and a beta subunit which docks the complex at nucleoporins. Alternate splicing of this gene results in two transcript variants encoding different proteins.<ref name="entrez">{{cite web | title = Entrez Gene: TNPO1 transportin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3842| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bukrinsky MI, Haffar OK |title=HIV-1 nuclear import: in search of a leader. |journal=Front. Biosci. |volume=2 |issue= |pages= d578-87 |year= 2004 |pmid= 9366553 |doi= }}
*{{cite journal | author=Bukrinsky MI, Haffar OK |title=HIV-1 nuclear import: matrix protein is back on center stage, this time together with Vpr. |journal=Mol. Med. |volume=4 |issue= 3 |pages= 138-43 |year= 1998 |pmid= 9562972 |doi= }}
*{{cite journal | author=Bukrinsky MI, Sharova N, Dempsey MP, ''et al.'' |title=Active nuclear import of human immunodeficiency virus type 1 preintegration complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 14 |pages= 6580-4 |year= 1992 |pmid= 1631159 |doi= }}
*{{cite journal | author=Moroianu J, Hijikata M, Blobel G, Radu A |title=Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 14 |pages= 6532-6 |year= 1995 |pmid= 7604027 |doi= }}
*{{cite journal | author=Bukrinsky MI, Haggerty S, Dempsey MP, ''et al.'' |title=A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells. |journal=Nature |volume=365 |issue= 6447 |pages= 666-9 |year= 1993 |pmid= 8105392 |doi= 10.1038/365666a0 }}
*{{cite journal | author=Michael WM, Choi M, Dreyfuss G |title=A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway. |journal=Cell |volume=83 |issue= 3 |pages= 415-22 |year= 1996 |pmid= 8521471 |doi= }}
*{{cite journal | author=Pollard VW, Michael WM, Nakielny S, ''et al.'' |title=A novel receptor-mediated nuclear protein import pathway. |journal=Cell |volume=86 |issue= 6 |pages= 985-94 |year= 1996 |pmid= 8808633 |doi= }}
*{{cite journal | author=Nakielny S, Siomi MC, Siomi H, ''et al.'' |title=Transportin: nuclear transport receptor of a novel nuclear protein import pathway. |journal=Exp. Cell Res. |volume=229 |issue= 2 |pages= 261-6 |year= 1997 |pmid= 8986607 |doi= 10.1006/excr.1996.0369 }}
*{{cite journal | author=Bonifaci N, Moroianu J, Radu A, Blobel G |title=Karyopherin beta2 mediates nuclear import of a mRNA binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 10 |pages= 5055-60 |year= 1997 |pmid= 9144189 |doi= }}
*{{cite journal | author=Fridell RA, Truant R, Thorne L, ''et al.'' |title=Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta. |journal=J. Cell. Sci. |volume=110 ( Pt 11) |issue= |pages= 1325-31 |year= 1997 |pmid= 9202393 |doi= }}
*{{cite journal | author=Gallay P, Hope T, Chin D, Trono D |title=HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 18 |pages= 9825-30 |year= 1997 |pmid= 9275210 |doi= }}
*{{cite journal | author=Siomi MC, Eder PS, Kataoka N, ''et al.'' |title=Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins. |journal=J. Cell Biol. |volume=138 |issue= 6 |pages= 1181-92 |year= 1997 |pmid= 9298975 |doi= }}
*{{cite journal | author=Henderson BR, Percipalle P |title=Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. |journal=J. Mol. Biol. |volume=274 |issue= 5 |pages= 693-707 |year= 1998 |pmid= 9405152 |doi= 10.1006/jmbi.1997.1420 }}
*{{cite journal | author=Efthymiadis A, Briggs LJ, Jans DA |title=The HIV-1 Tat nuclear localization sequence confers novel nuclear import properties. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1623-8 |year= 1998 |pmid= 9430704 |doi= }}
*{{cite journal | author=Vodicka MA, Koepp DM, Silver PA, Emerman M |title=HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection. |journal=Genes Dev. |volume=12 |issue= 2 |pages= 175-85 |year= 1998 |pmid= 9436978 |doi= }}
*{{cite journal | author=Popov S, Rexach M, Zybarth G, ''et al.'' |title=Viral protein R regulates nuclear import of the HIV-1 pre-integration complex. |journal=EMBO J. |volume=17 |issue= 4 |pages= 909-17 |year= 1998 |pmid= 9463369 |doi= 10.1093/emboj/17.4.909 }}
*{{cite journal | author=Popov S, Rexach M, Ratner L, ''et al.'' |title=Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex. |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 13347-52 |year= 1998 |pmid= 9582382 |doi= }}
*{{cite journal | author=Fouchier RA, Meyer BE, Simon JH, ''et al.'' |title=Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex. |journal=J. Virol. |volume=72 |issue= 7 |pages= 6004-13 |year= 1998 |pmid= 9621063 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TOP2B... {November 17, 2007 10:06:44 AM PST}
- SEARCH REDIRECT: Control Box Found: TOP2B {November 17, 2007 10:07:08 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:07:11 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:07:11 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:07:11 AM PST}
- UPDATED: Updated protein page: TOP2B {November 17, 2007 10:07:17 AM PST}
- INFO: Beginning work on TPH1... {November 17, 2007 10:07:17 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:07:45 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
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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_TPH1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mlw.
| PDB = {{PDB2|1mlw}}
| Name = Tryptophan hydroxylase 1 (tryptophan 5-monooxygenase)
| HGNCid = 12008
| Symbol = TPH1
| AltSymbols =; MGC119994; TPH; TPRH
| OMIM = 191060
| ECnumber =
| Homologene = 3080
| MGIid = 98796
| GeneAtlas_image1 = PBB_GE_TPH1_214601_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004510 |text = tryptophan 5-monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016597 |text = amino acid binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006587 |text = serotonin biosynthetic process from tryptophan}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0009072 |text = aromatic amino acid family metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7166
| Hs_Ensembl = ENSG00000129167
| Hs_RefseqProtein = NP_004170
| Hs_RefseqmRNA = NM_004179
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 17997772
| Hs_GenLoc_end = 18018885
| Hs_Uniprot = P17752
| Mm_EntrezGene = 21990
| Mm_Ensembl = ENSMUSG00000040046
| Mm_RefseqmRNA = NM_009414
| Mm_RefseqProtein = NP_033440
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 46515203
| Mm_GenLoc_end = 46540579
| Mm_Uniprot = Q3UK52
}}
}}
'''Tryptophan hydroxylase 1 (tryptophan 5-monooxygenase)''', also known as '''TPH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TPH1 tryptophan hydroxylase 1 (tryptophan 5-monooxygenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7166| 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 = Tryptophan hydroxylase (TPH; EC 1.14.16.4) catalyzes the biopterin-dependent monooxygenation of tryptophan to 5-hydroxytryptophan (5HT), which is subsequently decarboxylated to form the neurotransmitter serotonin. It is thus the rate-limiting enzyme in the biosynthesis of serotonin. TPH expression is limited to a few specialized tissues: raphe neurons, pinealocytes, mast cells, mononuclear leukocytes, beta-cells of the islets of Langerhans, and intestinal and pancreatic enterochromaffin cells.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: TPH1 tryptophan hydroxylase 1 (tryptophan 5-monooxygenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7166| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Li D, He L |title=Further clarification of the contribution of the tryptophan hydroxylase (TPH) gene to suicidal behavior using systematic allelic and genotypic meta-analyses. |journal=Hum. Genet. |volume=119 |issue= 3 |pages= 233-40 |year= 2007 |pmid= 16450114 |doi= 10.1007/s00439-005-0113-x }}
*{{cite journal | author=Nielsen DA, Dean M, Goldman D |title=Genetic mapping of the human tryptophan hydroxylase gene on chromosome 11, using an intronic conformational polymorphism. |journal=Am. J. Hum. Genet. |volume=51 |issue= 6 |pages= 1366-71 |year= 1993 |pmid= 1463016 |doi= }}
*{{cite journal | author=Craig SP, Boularand S, Darmon MC, ''et al.'' |title=Localization of human tryptophan hydroxylase (TPH) to chromosome 11p15.3----p14 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=56 |issue= 3-4 |pages= 157-9 |year= 1991 |pmid= 2055111 |doi= }}
*{{cite journal | author=Boularand S, Darmon MC, Ganem Y, ''et al.'' |title=Complete coding sequence of human tryptophan hydroxylase. |journal=Nucleic Acids Res. |volume=18 |issue= 14 |pages= 4257 |year= 1990 |pmid= 2377472 |doi= }}
*{{cite journal | author=Ledley FD, Grenett HE, Bartos DP, ''et al.'' |title=Assignment of human tryptophan hydroxylase locus to chromosome 11: gene duplication and translocation in evolution of aromatic amino acid hydroxylases. |journal=Somat. Cell Mol. Genet. |volume=13 |issue= 5 |pages= 575-80 |year= 1987 |pmid= 2889273 |doi= }}
*{{cite journal | author=Ichimura T, Uchiyama J, Kunihiro O, ''et al.'' |title=Identification of the site of interaction of the 14-3-3 protein with phosphorylated tryptophan hydroxylase. |journal=J. Biol. Chem. |volume=270 |issue= 48 |pages= 28515-8 |year= 1996 |pmid= 7499362 |doi= }}
*{{cite journal | author=Tipper JP, Citron BA, Ribeiro P, Kaufman S |title=Cloning and expression of rabbit and human brain tryptophan hydroxylase cDNA in Escherichia coli. |journal=Arch. Biochem. Biophys. |volume=315 |issue= 2 |pages= 445-53 |year= 1995 |pmid= 7986090 |doi= 10.1006/abbi.1994.1523 }}
*{{cite journal | author=Furukawa Y, Ikuta N, Omata S, ''et al.'' |title=Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein. |journal=Biochem. Biophys. Res. Commun. |volume=194 |issue= 1 |pages= 144-9 |year= 1993 |pmid= 8101440 |doi= 10.1006/bbrc.1993.1796 }}
*{{cite journal | author=Kuhn DM, Arthur R, States JC |title=Phosphorylation and activation of brain tryptophan hydroxylase: identification of serine-58 as a substrate site for protein kinase A. |journal=J. Neurochem. |volume=68 |issue= 5 |pages= 2220-3 |year= 1997 |pmid= 9109552 |doi= }}
*{{cite journal | author=Wang GA, Coon SL, Kaufman S |title=Alternative splicing at the 3'-cDNA of human tryptophan hydroxylase. |journal=J. Neurochem. |volume=71 |issue= 4 |pages= 1769-72 |year= 1998 |pmid= 9751214 |doi= }}
*{{cite journal | author=Austin MC, O'Donnell SM |title=Regional distribution and cellular expression of tryptophan hydroxylase messenger RNA in postmortem human brainstem and pineal gland. |journal=J. Neurochem. |volume=72 |issue= 5 |pages= 2065-73 |year= 1999 |pmid= 10217286 |doi= }}
*{{cite journal | author=Yu PL, Fujimura M, Okumiya K, ''et al.'' |title=Immunohistochemical localization of tryptophan hydroxylase in the human and rat gastrointestinal tracts. |journal=J. Comp. Neurol. |volume=411 |issue= 4 |pages= 654-65 |year= 1999 |pmid= 10421874 |doi= }}
*{{cite journal | author=Kowlessur D, Kaufman S |title=Cloning and expression of recombinant human pineal tryptophan hydroxylase in Escherichia coli: purification and characterization of the cloned enzyme. |journal=Biochim. Biophys. Acta |volume=1434 |issue= 2 |pages= 317-30 |year= 1999 |pmid= 10525150 |doi= }}
*{{cite journal | author=McKinney J, Teigen K, Frøystein NA, ''et al.'' |title=Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity. |journal=Biochemistry |volume=40 |issue= 51 |pages= 15591-601 |year= 2002 |pmid= 11747434 |doi= }}
*{{cite journal | author=Serretti A, Cristina S, Lilli R, ''et al.'' |title=Family-based association study of 5-HTTLPR, TPH, MAO-A, and DRD4 polymorphisms in mood disorders. |journal=Am. J. Med. Genet. |volume=114 |issue= 4 |pages= 361-9 |year= 2002 |pmid= 11992558 |doi= 10.1002/ajmg.10356 }}
*{{cite journal | author=Slominski A, Pisarchik A, Semak I, ''et al.'' |title=Serotoninergic and melatoninergic systems are fully expressed in human skin. |journal=FASEB J. |volume=16 |issue= 8 |pages= 896-8 |year= 2002 |pmid= 12039872 |doi= 10.1096/fj.01-0952fje }}
*{{cite journal | author=Yohrling IV GJ, Jiang GC, DeJohn MM, ''et al.'' |title=Inhibition of tryptophan hydroxylase activity and decreased 5-HT1A receptor binding in a mouse model of Huntington's disease. |journal=J. Neurochem. |volume=82 |issue= 6 |pages= 1416-23 |year= 2002 |pmid= 12354289 |doi= }}
*{{cite journal | author=Wang L, Erlandsen H, Haavik J, ''et al.'' |title=Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin. |journal=Biochemistry |volume=41 |issue= 42 |pages= 12569-74 |year= 2002 |pmid= 12379098 |doi= }}
*{{cite journal | author=Slominski A, Pisarchik A, Semak I, ''et al.'' |title=Serotoninergic system in hamster skin. |journal=J. Invest. Dermatol. |volume=119 |issue= 4 |pages= 934-42 |year= 2002 |pmid= 12406341 |doi= 10.1046/j.1523-1747.2002.00156.x }}
*{{cite journal | author=Ono H, Shirakawa O, Kitamura N, ''et al.'' |title=Tryptophan hydroxylase immunoreactivity is altered by the genetic variation in postmortem brain samples of both suicide victims and controls. |journal=Mol. Psychiatry |volume=7 |issue= 10 |pages= 1127-32 |year= 2003 |pmid= 12476329 |doi= 10.1038/sj.mp.4001150 }}
}}
{{refend}}
{{protein-stub}}
end log.
