Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 20:26, 17 November 2007 (UTC)
[edit]Proteins without matches (10)
[edit]Proteins with a High Potential Match (3)
[edit]Redirected Proteins (12)
[edit]Manual Inspection (Page not found) (13)
[edit]
Protein Status Grid - Date: 20:26, 17 November 2007 (UTC)
[edit]Vebose Log - Date: 20:26, 17 November 2007 (UTC)
[edit]- INFO: Beginning work on ABCC6... {November 17, 2007 12:04:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:04:43 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATP-binding cassette, sub-family C (CFTR/MRP), member 6
| HGNCid = 57
| Symbol = ABCC6
| AltSymbols =; ABC34; ARA; EST349056; MLP1; MOATE; MRP6; PXE; PXE1
| OMIM = 603234
| ECnumber =
| Homologene = 55559
| MGIid = 1351634
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042626 |text = ATPase activity, coupled to transmembrane movement of substances}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0042493 |text = response to drug}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 368
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001125860
| Hs_RefseqmRNA = XM_001125860
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 27421
| Mm_Ensembl = ENSMUSG00000030834
| Mm_RefseqmRNA = NM_018795
| Mm_RefseqProtein = NP_061265
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 45844422
| Mm_GenLoc_end = 45898328
| Mm_Uniprot = Q9R1S7
}}
}}
'''ATP-binding cassette, sub-family C (CFTR/MRP), member 6''', also known as '''ABCC6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ABCC6 ATP-binding cassette, sub-family C (CFTR/MRP), member 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=368| 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 superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). The encoded protein, a member of the MRP subfamily, is involved in multi-drug resistance. Mutations in this gene cause pseudoxanthoma elasticum. Alternatively spliced transcript variants that encode different proteins have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ABCC6 ATP-binding cassette, sub-family C (CFTR/MRP), member 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=368| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Uitto J, Pulkkinen L, Ringpfeil F |title=Molecular genetics of pseudoxanthoma elasticum: a metabolic disorder at the environment-genome interface? |journal=Trends in molecular medicine |volume=7 |issue= 1 |pages= 13-7 |year= 2001 |pmid= 11427982 |doi= }}
*{{cite journal | author=Hu X, Plomp AS, van Soest S, ''et al.'' |title=Pseudoxanthoma elasticum: a clinical, histopathological, and molecular update. |journal=Survey of ophthalmology |volume=48 |issue= 4 |pages= 424-38 |year= 2003 |pmid= 12850230 |doi= }}
*{{cite journal | author=Chassaing N, Martin L, Calvas P, ''et al.'' |title=Pseudoxanthoma elasticum: a clinical, pathophysiological and genetic update including 11 novel ABCC6 mutations. |journal=J. Med. Genet. |volume=42 |issue= 12 |pages= 881-92 |year= 2006 |pmid= 15894595 |doi= 10.1136/jmg.2004.030171 }}
*{{cite journal | author=Uitto J |title=The gene family of ABC transporters--novel mutations, new phenotypes. |journal=Trends in molecular medicine |volume=11 |issue= 8 |pages= 341-3 |year= 2005 |pmid= 15996518 |doi= 10.1016/j.molmed.2005.06.004 }}
*{{cite journal | author=Neldner KH |title=Pseudoxanthoma elasticum. |journal=Clin. Dermatol. |volume=6 |issue= 1 |pages= 1-159 |year= 1988 |pmid= 3359381 |doi= }}
*{{cite journal | author=Pope FM |title=Autosomal dominant pseudoxanthoma elasticum. |journal=J. Med. Genet. |volume=11 |issue= 2 |pages= 152-7 |year= 1974 |pmid= 4841083 |doi= }}
*{{cite journal | author=Allikmets R, Gerrard B, Hutchinson A, Dean M |title=Characterization of the human ABC superfamily: isolation and mapping of 21 new genes using the expressed sequence tags database. |journal=Hum. Mol. Genet. |volume=5 |issue= 10 |pages= 1649-55 |year= 1997 |pmid= 8894702 |doi= }}
*{{cite journal | author=Longhurst TJ, O'Neill GM, Harvie RM, Davey RA |title=The anthracycline resistance-associated (ara) gene, a novel gene associated with multidrug resistance in a human leukaemia cell line. |journal=Br. J. Cancer |volume=74 |issue= 9 |pages= 1331-5 |year= 1996 |pmid= 8912525 |doi= }}
*{{cite journal | author=van Soest S, Swart J, Tijmes N, ''et al.'' |title=A locus for autosomal recessive pseudoxanthoma elasticum, with penetrance of vascular symptoms in carriers, maps to chromosome 16p13.1. |journal=Genome Res. |volume=7 |issue= 8 |pages= 830-4 |year= 1997 |pmid= 9267806 |doi= }}
*{{cite journal | author=Kuss BJ, O'Neill GM, Eyre H, ''et al.'' |title=ARA, a novel ABC transporter, is located at 16p13.1, is deleted in inv(16) leukemias, and is shown to be expressed in primitive hematopoietic precursors. |journal=Genomics |volume=51 |issue= 3 |pages= 455-8 |year= 1998 |pmid= 9721217 |doi= 10.1006/geno.1998.5349 }}
*{{cite journal | author=Kool M, van der Linden M, de Haas M, ''et al.'' |title=Expression of human MRP6, a homologue of the multidrug resistance protein gene MRP1, in tissues and cancer cells. |journal=Cancer Res. |volume=59 |issue= 1 |pages= 175-82 |year= 1999 |pmid= 9892204 |doi= }}
*{{cite journal | author=Belinsky MG, Kruh GD |title=MOAT-E (ARA) is a full-length MRP/cMOAT subfamily transporter expressed in kidney and liver. |journal=Br. J. Cancer |volume=80 |issue= 9 |pages= 1342-9 |year= 1999 |pmid= 10424734 |doi= 10.1038/sj.bjc.6690527 }}
*{{cite journal | author=Loftus BJ, Kim UJ, Sneddon VP, ''et al.'' |title=Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. |journal=Genomics |volume=60 |issue= 3 |pages= 295-308 |year= 1999 |pmid= 10493829 |doi= 10.1006/geno.1999.5927 }}
*{{cite journal | author=Le Saux O, Urban Z, Göring HH, ''et al.'' |title=Pseudoxanthoma elasticum maps to an 820-kb region of the p13.1 region of chromosome 16. |journal=Genomics |volume=62 |issue= 1 |pages= 1-10 |year= 2000 |pmid= 10585762 |doi= 10.1006/geno.1999.5925 }}
*{{cite journal | author=Ringpfeil F, Lebwohl MG, Christiano AM, Uitto J |title=Pseudoxanthoma elasticum: mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 11 |pages= 6001-6 |year= 2000 |pmid= 10811882 |doi= 10.1073/pnas.100041297 }}
*{{cite journal | author=Le Saux O, Urban Z, Tschuch C, ''et al.'' |title=Mutations in a gene encoding an ABC transporter cause pseudoxanthoma elasticum. |journal=Nat. Genet. |volume=25 |issue= 2 |pages= 223-7 |year= 2000 |pmid= 10835642 |doi= 10.1038/76102 }}
*{{cite journal | author=Bergen AA, Plomp AS, Schuurman EJ, ''et al.'' |title=Mutations in ABCC6 cause pseudoxanthoma elasticum. |journal=Nat. Genet. |volume=25 |issue= 2 |pages= 228-31 |year= 2000 |pmid= 10835643 |doi= 10.1038/76109 }}
*{{cite journal | author=Germain DP, Perdu J, Remones V, Jeunemaitre X |title=Homozygosity for the R1268Q mutation in MRP6, the pseudoxanthoma elasticum gene, is not disease-causing. |journal=Biochem. Biophys. Res. Commun. |volume=274 |issue= 2 |pages= 297-301 |year= 2000 |pmid= 10913334 |doi= 10.1006/bbrc.2000.3101 }}
*{{cite journal | author=Struk B, Cai L, Zäch S, ''et al.'' |title=Mutations of the gene encoding the transmembrane transporter protein ABC-C6 cause pseudoxanthoma elasticum. |journal=J. Mol. Med. |volume=78 |issue= 5 |pages= 282-6 |year= 2000 |pmid= 10954200 |doi= }}
*{{cite journal | author=Germain DP, Remones V, Perdu J, Jeunemaitre X |title=Identification of two polymorphisms (c189G>C; c190T>C) in exon 2 of the human MRP6 gene (ABCC6) by screening of Pseudoxanthoma elasticum patients: possible sequence correction? |journal=Hum. Mutat. |volume=16 |issue= 5 |pages= 449 |year= 2000 |pmid= 11058917 |doi= 10.1002/1098-1004(200011)16:5<449::AID-HUMU24>3.0.CO;2-O }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYB5R3... {November 17, 2007 12:04:43 PM PST}
- SEARCH REDIRECT: Control Box Found: CYB5R3 {November 17, 2007 12:05:17 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:05:18 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:05:18 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:05:18 PM PST}
- UPDATED: Updated protein page: CYB5R3 {November 17, 2007 12:05:25 PM PST}
- INFO: Beginning work on DISC1... {November 17, 2007 12:19:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:20:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Disrupted in schizophrenia 1
| HGNCid = 2888
| Symbol = DISC1
| AltSymbols =; SCZD9; KIAA0457
| OMIM = 605210
| ECnumber =
| Homologene = 10257
| MGIid = 2447658
| GeneAtlas_image1 = PBB_GE_DISC1_206090_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DISC1_207759_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005874 |text = microtubule}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 27185
| Hs_Ensembl = ENSG00000162946
| Hs_RefseqProtein = NP_001012975
| Hs_RefseqmRNA = NM_001012957
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 229829184
| Hs_GenLoc_end = 230243641
| Hs_Uniprot = Q9NRI5
| Mm_EntrezGene = 244667
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_170596
| Mm_RefseqProtein = NP_733484
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Disrupted in schizophrenia 1''', also known as '''DISC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DISC1 disrupted in schizophrenia 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27185| 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 with multiple coiled coil motifs which is located in the nucleus, cytoplasm and mitochondria. The protein is involved in neurite outgrowth and cortical development through its interaction with other proteins. This gene is disrupted in a t(1;11)(q42.1;q14.3) translocation which segregates with schizophrenia and related psychiatric disorders in a large Scottish family. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: DISC1 disrupted in schizophrenia 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27185| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Blackwood DH, Muir WJ |title=Clinical phenotypes associated with DISC1, a candidate gene for schizophrenia. |journal=Neurotoxicity research |volume=6 |issue= 1 |pages= 35-41 |year= 2004 |pmid= 15184103 |doi= }}
*{{cite journal | author=Millar JK, James R, Brandon NJ, Thomson PA |title=DISC1 and DISC2: discovering and dissecting molecular mechanisms underlying psychiatric illness. |journal=Ann. Med. |volume=36 |issue= 5 |pages= 367-78 |year= 2005 |pmid= 15478311 |doi= }}
*{{cite journal | author=Porteous DJ, Thomson P, Brandon NJ, Millar JK |title=The genetics and biology of DISC1--an emerging role in psychosis and cognition. |journal=Biol. Psychiatry |volume=60 |issue= 2 |pages= 123-31 |year= 2006 |pmid= 16843095 |doi= 10.1016/j.biopsych.2006.04.008 }}
*{{cite journal | author=Lipska BK, Mitkus SN, Mathew SV, ''et al.'' |title=Functional genomics in postmortem human brain: abnormalities in a DISC1 molecular pathway in schizophrenia. |journal=Dialogues in clinical neuroscience |volume=8 |issue= 3 |pages= 353-7 |year= 2006 |pmid= 17117617 |doi= }}
*{{cite journal | author=Seki N, Ohira M, Nagase T, ''et al.'' |title=Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. |journal=DNA Res. |volume=4 |issue= 5 |pages= 345-9 |year= 1998 |pmid= 9455484 |doi= }}
*{{cite journal | author=Millar JK, Wilson-Annan JC, Anderson S, ''et al.'' |title=Disruption of two novel genes by a translocation co-segregating with schizophrenia. |journal=Hum. Mol. Genet. |volume=9 |issue= 9 |pages= 1415-23 |year= 2000 |pmid= 10814723 |doi= }}
*{{cite journal | author=Millar JK, Christie S, Semple CA, Porteous DJ |title=Chromosomal location and genomic structure of the human translin-associated factor X gene (TRAX; TSNAX) revealed by intergenic splicing to DISC1, a gene disrupted by a translocation segregating with schizophrenia. |journal=Genomics |volume=67 |issue= 1 |pages= 69-77 |year= 2001 |pmid= 10945471 |doi= 10.1006/geno.2000.6239 }}
*{{cite journal | author=Blackwood DH, Fordyce A, Walker MT, ''et al.'' |title=Schizophrenia and affective disorders--cosegregation with a translocation at chromosome 1q42 that directly disrupts brain-expressed genes: clinical and P300 findings in a family. |journal=Am. J. Hum. Genet. |volume=69 |issue= 2 |pages= 428-33 |year= 2001 |pmid= 11443544 |doi= }}
*{{cite journal | author=Ekelund J, Hovatta I, Parker A, ''et al.'' |title=Chromosome 1 loci in Finnish schizophrenia families. |journal=Hum. Mol. Genet. |volume=10 |issue= 15 |pages= 1611-7 |year= 2001 |pmid= 11468279 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Ozeki Y, Tomoda T, Kleiderlein J, ''et al.'' |title=Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 1 |pages= 289-94 |year= 2003 |pmid= 12506198 |doi= 10.1073/pnas.0136913100 }}
*{{cite journal | author=Taylor MS, Devon RS, Millar JK, Porteous DJ |title=Evolutionary constraints on the Disrupted in Schizophrenia locus. |journal=Genomics |volume=81 |issue= 1 |pages= 67-77 |year= 2003 |pmid= 12573262 |doi= }}
*{{cite journal | author=Morris JA, Kandpal G, Ma L, Austin CP |title=DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. |journal=Hum. Mol. Genet. |volume=12 |issue= 13 |pages= 1591-608 |year= 2004 |pmid= 12812986 |doi= }}
*{{cite journal | author=Miyoshi K, Honda A, Baba K, ''et al.'' |title=Disrupted-In-Schizophrenia 1, a candidate gene for schizophrenia, participates in neurite outgrowth. |journal=Mol. Psychiatry |volume=8 |issue= 7 |pages= 685-94 |year= 2004 |pmid= 12874605 |doi= 10.1038/sj.mp.4001352 }}
*{{cite journal | author=Hennah W, Varilo T, Kestilä M, ''et al.'' |title=Haplotype transmission analysis provides evidence of association for DISC1 to schizophrenia and suggests sex-dependent effects. |journal=Hum. Mol. Genet. |volume=12 |issue= 23 |pages= 3151-9 |year= 2004 |pmid= 14532331 |doi= 10.1093/hmg/ddg341 }}
*{{cite journal | author=Millar JK, Christie S, Porteous DJ |title=Yeast two-hybrid screens implicate DISC1 in brain development and function. |journal=Biochem. Biophys. Res. Commun. |volume=311 |issue= 4 |pages= 1019-25 |year= 2004 |pmid= 14623284 |doi= }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Brandon NJ, Handford EJ, Schurov I, ''et al.'' |title=Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated protein complex: implications for schizophrenia and other major neurological disorders. |journal=Mol. Cell. Neurosci. |volume=25 |issue= 1 |pages= 42-55 |year= 2004 |pmid= 14962739 |doi= 10.1016/j.mcn.2003.09.009 }}
*{{cite journal | author=Miyoshi K, Asanuma M, Miyazaki I, ''et al.'' |title=DISC1 localizes to the centrosome by binding to kendrin. |journal=Biochem. Biophys. Res. Commun. |volume=317 |issue= 4 |pages= 1195-9 |year= 2004 |pmid= 15094396 |doi= 10.1016/j.bbrc.2004.03.163 }}
*{{cite journal | author=James R, Adams RR, Christie S, ''et al.'' |title=Disrupted in Schizophrenia 1 (DISC1) is a multicompartmentalized protein that predominantly localizes to mitochondria. |journal=Mol. Cell. Neurosci. |volume=26 |issue= 1 |pages= 112-22 |year= 2004 |pmid= 15121183 |doi= 10.1016/j.mcn.2004.01.013 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DMBT1... {November 17, 2007 12:05:25 PM PST}
- SEARCH REDIRECT: Control Box Found: DMBT1 {November 17, 2007 12:05:49 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:05:52 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:05:52 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:05:52 PM PST}
- UPDATED: Updated protein page: DMBT1 {November 17, 2007 12:05:59 PM PST}
- INFO: Beginning work on DOK1... {November 17, 2007 12:05:59 PM PST}
- SEARCH REDIRECT: Control Box Found: DOK1 {November 17, 2007 12:06:22 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:06:25 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:06:25 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:06:25 PM PST}
- UPDATED: Updated protein page: DOK1 {November 17, 2007 12:06:34 PM PST}
- INFO: Beginning work on EPHB4... {November 17, 2007 12:06:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:07:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_EPHB4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2bba.
| PDB = {{PDB2|2bba}}, {{PDB2|2hle}}
| Name = EPH receptor B4
| HGNCid = 3395
| Symbol = EPHB4
| AltSymbols =; HTK; MYK1; TYRO11
| OMIM = 600011
| ECnumber =
| Homologene = 20939
| MGIid = 104757
| GeneAtlas_image1 = PBB_GE_EPHB4_202894_at_tn.png
| GeneAtlas_image2 = PBB_GE_EPHB4_216680_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005003 |text = ephrin receptor activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008046 |text = axon guidance receptor activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to 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}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0007612 |text = learning}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0045765 |text = regulation of angiogenesis}} {{GNF_GO|id=GO:0048168 |text = regulation of neuronal synaptic plasticity}} {{GNF_GO|id=GO:0048170 |text = positive regulation of long-term neuronal synaptic plasticity}} {{GNF_GO|id=GO:0050770 |text = regulation of axonogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2050
| Hs_Ensembl = ENSG00000196411
| Hs_RefseqProtein = NP_004435
| Hs_RefseqmRNA = NM_004444
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 100238123
| Hs_GenLoc_end = 100263079
| Hs_Uniprot = P54760
| Mm_EntrezGene = 13846
| Mm_Ensembl = ENSMUSG00000029710
| Mm_RefseqmRNA = NM_010144
| Mm_RefseqProtein = NP_034274
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 137579897
| Mm_GenLoc_end = 137604298
| Mm_Uniprot = Q3V1K8
}}
}}
'''EPH receptor B4''', also known as '''EPHB4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPHB4 EPH receptor B4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2050| 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 = Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene binds to ephrin-B2 and plays an essential role in vascular development.<ref name="entrez">{{cite web | title = Entrez Gene: EPHB4 EPH receptor B4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2050| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Flanagan JG, Vanderhaeghen P |title=The ephrins and Eph receptors in neural development. |journal=Annu. Rev. Neurosci. |volume=21 |issue= |pages= 309-45 |year= 1998 |pmid= 9530499 |doi= 10.1146/annurev.neuro.21.1.309 }}
*{{cite journal | author=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151-81 |year= 1998 |pmid= 9576626 |doi= }}
*{{cite journal | author=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis. |journal=Development |volume=126 |issue= 10 |pages= 2033-44 |year= 1999 |pmid= 10207129 |doi= }}
*{{cite journal | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly. |journal=Int. Rev. Cytol. |volume=196 |issue= |pages= 177-244 |year= 2000 |pmid= 10730216 |doi= }}
*{{cite journal | author=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=355 |issue= 1399 |pages= 993-1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635 }}
*{{cite journal | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155-64 |year= 2001 |pmid= 11256076 |doi= }}
*{{cite journal | author=Andres AC, Reid HH, Zürcher G, ''et al.'' |title=Expression of two novel eph-related receptor protein tyrosine kinases in mammary gland development and carcinogenesis. |journal=Oncogene |volume=9 |issue= 5 |pages= 1461-7 |year= 1994 |pmid= 8152808 |doi= }}
*{{cite journal | author=Bennett BD, Wang Z, Kuang WJ, ''et al.'' |title=Cloning and characterization of HTK, a novel transmembrane tyrosine kinase of the EPH subfamily. |journal=J. Biol. Chem. |volume=269 |issue= 19 |pages= 14211-8 |year= 1994 |pmid= 8188704 |doi= }}
*{{cite journal | author=Berclaz G, Andres AC, Albrecht D, ''et al.'' |title=Expression of the receptor protein tyrosine kinase myk-1/htk in normal and malignant mammary epithelium. |journal=Biochem. Biophys. Res. Commun. |volume=226 |issue= 3 |pages= 869-75 |year= 1996 |pmid= 8831703 |doi= 10.1006/bbrc.1996.1442 }}
*{{cite journal | author= |title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. |journal=Cell |volume=90 |issue= 3 |pages= 403-4 |year= 1997 |pmid= 9267020 |doi= }}
*{{cite journal | author=Nikolova Z, Djonov V, Zuercher G, ''et al.'' |title=Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis. |journal=J. Cell. Sci. |volume=111 ( Pt 18) |issue= |pages= 2741-51 |year= 1998 |pmid= 9718367 |doi= }}
*{{cite journal | author=Tang XX, Brodeur GM, Campling BG, Ikegaki N |title=Coexpression of transcripts encoding EPHB receptor protein tyrosine kinases and their ephrin-B ligands in human small cell lung carcinoma. |journal=Clin. Cancer Res. |volume=5 |issue= 2 |pages= 455-60 |year= 1999 |pmid= 10037197 |doi= }}
*{{cite journal | author=Gerety SS, Wang HU, Chen ZF, Anderson DJ |title=Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development. |journal=Mol. Cell |volume=4 |issue= 3 |pages= 403-14 |year= 1999 |pmid= 10518221 |doi= }}
*{{cite journal | author=Dalva MB, Takasu MA, Lin MZ, ''et al.'' |title=EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. |journal=Cell |volume=103 |issue= 6 |pages= 945-56 |year= 2001 |pmid= 11136979 |doi= }}
*{{cite journal | author=Wilson MD, Riemer C, Martindale DW, ''et al.'' |title=Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5. |journal=Nucleic Acids Res. |volume=29 |issue= 6 |pages= 1352-65 |year= 2001 |pmid= 11239002 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GNAO1... {November 17, 2007 12:07:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:08:08 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O
| HGNCid = 4389
| Symbol = GNAO1
| AltSymbols =; DKFZp686O0962; G-ALPHA-o; GNAO
| OMIM = 139311
| ECnumber =
| Homologene = 39203
| MGIid = 95775
| GeneAtlas_image1 = PBB_GE_GNAO1_204762_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GNAO1_204763_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_GNAO1_215912_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007212 |text = dopamine receptor signaling pathway}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0007626 |text = locomotory behavior}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2775
| Hs_Ensembl = ENSG00000087258
| Hs_RefseqProtein = NP_066268
| Hs_RefseqmRNA = NM_020988
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 54783389
| Hs_GenLoc_end = 54948651
| Hs_Uniprot = P09471
| Mm_EntrezGene = 14681
| Mm_Ensembl = ENSMUSG00000031748
| Mm_RefseqmRNA = NM_010308
| Mm_RefseqProtein = NP_034438
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 96699967
| Mm_GenLoc_end = 96858351
| Mm_Uniprot = Q543S2
}}
}}
'''Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O''', also known as '''GNAO1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GNAO1 guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2775| 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=Raymond JR, Mukhin YV, Gelasco A, ''et al.'' |title=Multiplicity of mechanisms of serotonin receptor signal transduction. |journal=Pharmacol. Ther. |volume=92 |issue= 2-3 |pages= 179-212 |year= 2002 |pmid= 11916537 |doi= }}
*{{cite journal | author=Coupry I, Duzic E, Lanier SM |title=Factors determining the specificity of signal transduction by guanine nucleotide-binding protein-coupled receptors. II. Preferential coupling of the alpha 2C-adrenergic receptor to the guanine nucleotide-binding protein, Go. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 9852-7 |year= 1992 |pmid= 1349607 |doi= }}
*{{cite journal | author=Denker BM, Neer EJ, Schmidt CJ |title=Mutagenesis of the amino terminus of the alpha subunit of the G protein Go. In vitro characterization of alpha o beta gamma interactions. |journal=J. Biol. Chem. |volume=267 |issue= 9 |pages= 6272-7 |year= 1992 |pmid= 1556134 |doi= }}
*{{cite journal | author=Murtagh JJ, Eddy R, Shows TB, ''et al.'' |title=Different forms of Go alpha mRNA arise by alternative splicing of transcripts from a single gene on human chromosome 16. |journal=Mol. Cell. Biol. |volume=11 |issue= 2 |pages= 1146-55 |year= 1991 |pmid= 1899283 |doi= }}
*{{cite journal | author=Yi F, Denker BM, Neer EJ |title=Structural and functional studies of cross-linked Go protein subunits. |journal=J. Biol. Chem. |volume=266 |issue= 6 |pages= 3900-6 |year= 1991 |pmid= 1899868 |doi= }}
*{{cite journal | author=Tsukamoto T, Toyama R, Itoh H, ''et al.'' |title=Structure of the human gene and two rat cDNAs encoding the alpha chain of GTP-binding regulatory protein Go: two different mRNAs are generated by alternative splicing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 8 |pages= 2974-8 |year= 1991 |pmid= 1901650 |doi= }}
*{{cite journal | author=Gabrion J, Brabet P, Nguyen Than Dao B, ''et al.'' |title=Ultrastructural localization of the GTP-binding protein Go in neurons. |journal=Cell. Signal. |volume=1 |issue= 1 |pages= 107-23 |year= 1990 |pmid= 2518353 |doi= }}
*{{cite journal | author=Lavu S, Clark J, Swarup R, ''et al.'' |title=Molecular cloning and DNA sequence analysis of the human guanine nucleotide-binding protein Go alpha. |journal=Biochem. Biophys. Res. Commun. |volume=150 |issue= 2 |pages= 811-5 |year= 1988 |pmid= 3124840 |doi= }}
*{{cite journal | author=Zumbihl R, Breuiller-Fouché M, Carrette J, ''et al.'' |title=Up-regulation in late pregnancy of both Go1 alpha and Go2 alpha isoforms in human myometrium. |journal=Eur. J. Pharmacol. |volume=288 |issue= 1 |pages= 9-15 |year= 1995 |pmid= 7705473 |doi= }}
*{{cite journal | author=Grassie MA, Milligan G |title=Analysis of the relative interactions between the alpha 2C10 adrenoceptor and the guanine-nucleotide-binding proteins G(o)1 alpha and Gi 2 alpha following co-expression of these polypeptides in rat 1 fibroblasts. |journal=Biochem. J. |volume=306 ( Pt 2) |issue= |pages= 525-30 |year= 1995 |pmid= 7887906 |doi= }}
*{{cite journal | author=Wu HC, Lin CT |title=Association of heterotrimeric GTP binding regulatory protein (Go) with mitosis. |journal=Lab. Invest. |volume=71 |issue= 2 |pages= 175-81 |year= 1994 |pmid= 8078296 |doi= }}
*{{cite journal | author=Nitta K, Uchida K, Kawashima A, ''et al.'' |title=Identification of GTP-binding proteins in human glomeruli. |journal=Nippon Jinzo Gakkai shi |volume=36 |issue= 1 |pages= 9-12 |year= 1994 |pmid= 8107314 |doi= }}
*{{cite journal | author=Georgoussi Z, Carr C, Milligan G |title=Direct measurements of in situ interactions of rat brain opioid receptors with the guanine nucleotide-binding protein Go. |journal=Mol. Pharmacol. |volume=44 |issue= 1 |pages= 62-9 |year= 1993 |pmid= 8393523 |doi= }}
*{{cite journal | author=Laugwitz KL, Allgeier A, Offermanns S, ''et al.'' |title=The human thyrotropin receptor: a heptahelical receptor capable of stimulating members of all four G protein families. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 116-20 |year= 1996 |pmid= 8552586 |doi= }}
*{{cite journal | author=Kawano N, Ito T, Kitamura H, ''et al.'' |title=Immunoexpression of the alpha subunit of a guanine nucleotide-binding protein (Go) in pulmonary neuroendocrine cells and neoplasms. |journal=Pathol. Int. |volume=46 |issue= 6 |pages= 393-8 |year= 1997 |pmid= 8869990 |doi= }}
*{{cite journal | author=De Vries L, Elenko E, Hubler L, ''et al.'' |title=GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 26 |pages= 15203-8 |year= 1997 |pmid= 8986788 |doi= }}
*{{cite journal | author=Valenzuela D, Han X, Mende U, ''et al.'' |title=G alpha(o) is necessary for muscarinic regulation of Ca2+ channels in mouse heart. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 5 |pages= 1727-32 |year= 1997 |pmid= 9050846 |doi= }}
*{{cite journal | author=Chen C, Zheng B, Han J, Lin SC |title=Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8679-85 |year= 1997 |pmid= 9079700 |doi= }}
*{{cite journal | author=Natochin M, Lipkin VM, Artemyev NO |title=Interaction of human retinal RGS with G-protein alpha-subunits. |journal=FEBS Lett. |volume=411 |issue= 2-3 |pages= 179-82 |year= 1997 |pmid= 9271201 |doi= }}
*{{cite journal | author=Busconi L, Denker BM |title=Analysis of the N-terminal binding domain of Go alpha. |journal=Biochem. J. |volume=328 ( Pt 1) |issue= |pages= 23-31 |year= 1998 |pmid= 9359829 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GRB10... {November 17, 2007 12:08:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:08:48 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GRB10_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nrv.
| PDB = {{PDB2|1nrv}}
| Name = Growth factor receptor-bound protein 10
| HGNCid = 4564
| Symbol = GRB10
| AltSymbols =; GRB-IR; IRBP; KIAA0207; MEG1; RSS
| OMIM = 601523
| ECnumber =
| Homologene = 3882
| MGIid = 103232
| GeneAtlas_image1 = PBB_GE_GRB10_209409_at_tn.png
| GeneAtlas_image2 = PBB_GE_GRB10_209410_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_GRB10_210999_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}} {{GNF_GO|id=GO:0048009 |text = insulin-like growth factor receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2887
| Hs_Ensembl = ENSG00000106070
| Hs_RefseqProtein = NP_001001549
| Hs_RefseqmRNA = NM_001001549
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 50625260
| Hs_GenLoc_end = 50828652
| Hs_Uniprot = Q13322
| Mm_EntrezGene = 14783
| Mm_Ensembl = ENSMUSG00000020176
| Mm_RefseqmRNA = NM_010345
| Mm_RefseqProtein = NP_034475
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 11830511
| Mm_GenLoc_end = 11937390
| Mm_Uniprot = Q3TFU9
}}
}}
'''Growth factor receptor-bound protein 10''', also known as '''GRB10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GRB10 growth factor receptor-bound protein 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2887| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The product of this gene belongs to a small family of adapter proteins that are known to interact with a number of receptor tyrosine kinases and signaling molecules. This gene encodes a growth factor receptor-binding protein that interacts with insulin receptors and insulin-like growth-factor receptors. Overexpression of some isoforms of the encoded protein inhibits tyrosine kinase activity and results in growth suppression. This gene is imprinted in a highly isoform- and tissue-specific manner. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: GRB10 growth factor receptor-bound protein 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2887| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ramírez-Dueñas ML, Medina C, Ocampo-Campos R, Rivera H |title=Severe Silver-Russell syndrome and translocation (17;20) (q25;q13) |journal=Clin. Genet. |volume=41 |issue= 1 |pages= 51-3 |year= 1992 |pmid= 1633648 |doi= }}
*{{cite journal | author=Liu F, Roth RA |title=Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 22 |pages= 10287-91 |year= 1995 |pmid= 7479769 |doi= }}
*{{cite journal | author=Pandey A, Duan H, Di Fiore PP, Dixit VM |title=The Ret receptor protein tyrosine kinase associates with the SH2-containing adapter protein Grb10. |journal=J. Biol. Chem. |volume=270 |issue= 37 |pages= 21461-3 |year= 1995 |pmid= 7665556 |doi= }}
*{{cite journal | author=Midro AT, Debek K, Sawicka A, ''et al.'' |title=Second observation of Silver-Russel syndrome in a carrier of a reciprocal translocation with one breakpoint at site 17q25. |journal=Clin. Genet. |volume=44 |issue= 1 |pages= 53-5 |year= 1993 |pmid= 8403458 |doi= }}
*{{cite journal | author=Hansen H, Svensson U, Zhu J, ''et al.'' |title=Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus. |journal=J. Biol. Chem. |volume=271 |issue= 15 |pages= 8882-6 |year= 1996 |pmid= 8621530 |doi= }}
*{{cite journal | author=Morrione A, Valentinis B, Li S, ''et al.'' |title=Grb10: A new substrate of the insulin-like growth factor I receptor. |journal=Cancer Res. |volume=56 |issue= 14 |pages= 3165-7 |year= 1996 |pmid= 8764099 |doi= }}
*{{cite journal | author=O'Neill TJ, Rose DW, Pillay TS, ''et al.'' |title=Interaction of a GRB-IR splice variant (a human GRB10 homolog) with the insulin and insulin-like growth factor I receptors. Evidence for a role in mitogenic signaling. |journal=J. Biol. Chem. |volume=271 |issue= 37 |pages= 22506-13 |year= 1996 |pmid= 8798417 |doi= }}
*{{cite journal | author=Stein E, Cerretti DP, Daniel TO |title=Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23588-93 |year= 1996 |pmid= 8798570 |doi= }}
*{{cite journal | author=Frantz JD, Giorgetti-Peraldi S, Ottinger EA, Shoelson SE |title=Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2659-67 |year= 1997 |pmid= 9006901 |doi= }}
*{{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=Jerome CA, Scherer SW, Tsui LC, ''et al.'' |title=Assignment of growth factor receptor-bound protein 10 (GRB10) to human chromosome 7p11.2-p12. |journal=Genomics |volume=40 |issue= 1 |pages= 215-6 |year= 1997 |pmid= 9070953 |doi= 10.1006/geno.1996.4535 }}
*{{cite journal | author=Dong LQ, Du H, Porter SG, ''et al.'' |title=Cloning, chromosome localization, expression, and characterization of an Src homology 2 and pleckstrin homology domain-containing insulin receptor binding protein hGrb10gamma. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29104-12 |year= 1997 |pmid= 9360986 |doi= }}
*{{cite journal | author=He W, Rose DW, Olefsky JM, Gustafson TA |title=Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains. |journal=J. Biol. Chem. |volume=273 |issue= 12 |pages= 6860-7 |year= 1998 |pmid= 9506989 |doi= }}
*{{cite journal | author=Nantel A, Mohammad-Ali K, Sherk J, ''et al.'' |title=Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases. |journal=J. Biol. Chem. |volume=273 |issue= 17 |pages= 10475-84 |year= 1998 |pmid= 9553107 |doi= }}
*{{cite journal | author=Moutoussamy S, Renaudie F, Lago F, ''et al.'' |title=Grb10 identified as a potential regulator of growth hormone (GH) signaling by cloning of GH receptor target proteins. |journal=J. Biol. Chem. |volume=273 |issue= 26 |pages= 15906-12 |year= 1998 |pmid= 9632636 |doi= }}
*{{cite journal | author=Bai RY, Jahn T, Schrem S, ''et al.'' |title=The SH2-containing adapter protein GRB10 interacts with BCR-ABL. |journal=Oncogene |volume=17 |issue= 8 |pages= 941-8 |year= 1998 |pmid= 9747873 |doi= 10.1038/sj.onc.1202024 }}
*{{cite journal | author=Mano H, Ohya K, Miyazato A, ''et al.'' |title=Grb10/GrbIR as an in vivo substrate of Tec tyrosine kinase. |journal=Genes Cells |volume=3 |issue= 7 |pages= 431-41 |year= 1998 |pmid= 9753425 |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=Angrist M, Bolk S, Bentley K, ''et al.'' |title=Genomic structure of the gene for the SH2 and pleckstrin homology domain-containing protein GRB10 and evaluation of its role in Hirschsprung disease. |journal=Oncogene |volume=17 |issue= 23 |pages= 3065-70 |year= 1999 |pmid= 9881709 |doi= 10.1038/sj.onc.1202226 }}
*{{cite journal | author=Wang J, Dai H, Yousaf N, ''et al.'' |title=Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis. |journal=Mol. Cell. Biol. |volume=19 |issue= 9 |pages= 6217-28 |year= 1999 |pmid= 10454568 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HCFC1... {November 17, 2007 12:08:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:09:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Host cell factor C1 (VP16-accessory protein)
| HGNCid = 4839
| Symbol = HCFC1
| AltSymbols =; CFF; HCF-1; HCF1; HFC1; MGC70925; VCAF
| OMIM = 300019
| ECnumber =
| Homologene = 3898
| MGIid = 105942
| GeneAtlas_image1 = PBB_GE_HCFC1_202474_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HCFC1_202473_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0019046 |text = reactivation of latent virus}} {{GNF_GO|id=GO:0043254 |text = regulation of protein complex assembly}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}} {{GNF_GO|id=GO:0045787 |text = positive regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3054
| Hs_Ensembl = ENSG00000172534
| Hs_RefseqProtein = NP_005325
| Hs_RefseqmRNA = NM_005334
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 152866198
| Hs_GenLoc_end = 152890452
| Hs_Uniprot = P51610
| Mm_EntrezGene = 15161
| Mm_Ensembl = ENSMUSG00000031386
| Mm_RefseqmRNA = NM_008224
| Mm_RefseqProtein = NP_032250
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 70195515
| Mm_GenLoc_end = 70219035
| Mm_Uniprot = Q3USQ6
}}
}}
'''Host cell factor C1 (VP16-accessory protein)''', also known as '''HCFC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HCFC1 host cell factor C1 (VP16-accessory protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3054| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the host cell factor family and encodes a protein with five Kelch repeats, a fibronectin-like motif, and six HCF repeats, each of which contains a highly specific cleavage signal. This nuclear coactivator is proteolytically cleaved at one of the six possible sites, resulting in the creation of an N-terminal chain and the corresponding C-terminal chain. The final form of this protein consists of noncovalently bound N- and C-terminal chains. The protein is involved in control of the cell cycle and transcriptional regulation during herpes simplex virus infection. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.<ref name="entrez">{{cite web | title = Entrez Gene: HCFC1 host cell factor C1 (VP16-accessory protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3054| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Oehler T, Angel P |title=A common intermediary factor (p52/54) recognizing "acidic blob"-type domains is required for transcriptional activation by the Jun proteins. |journal=Mol. Cell. Biol. |volume=12 |issue= 12 |pages= 5508-15 |year= 1992 |pmid= 1448082 |doi= }}
*{{cite journal | author=Wilson AC, Peterson MG, Herr W |title=The HCF repeat is an unusual proteolytic cleavage signal. |journal=Genes Dev. |volume=9 |issue= 20 |pages= 2445-58 |year= 1995 |pmid= 7590226 |doi= }}
*{{cite journal | author=Klemm RD, Goodrich JA, Zhou S, Tjian R |title=Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 13 |pages= 5788-92 |year= 1995 |pmid= 7597030 |doi= }}
*{{cite journal | author=Frattini A, Faranda S, Redolfi E, ''et al.'' |title=Genomic organization of the human VP16 accessory protein, a housekeeping gene (HCFC1) mapping to Xq28. |journal=Genomics |volume=23 |issue= 1 |pages= 30-5 |year= 1995 |pmid= 7829097 |doi= 10.1006/geno.1994.1455 }}
*{{cite journal | author=Kristie TM, Pomerantz JL, Twomey TC, ''et al.'' |title=The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4387-94 |year= 1995 |pmid= 7876203 |doi= }}
*{{cite journal | author=Wilson AC, LaMarco K, Peterson MG, Herr W |title=The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein. |journal=Cell |volume=74 |issue= 1 |pages= 115-25 |year= 1993 |pmid= 8392914 |doi= }}
*{{cite journal | author=Kristie TM, Sharp PA |title=Purification of the cellular C1 factor required for the stable recognition of the Oct-1 homeodomain by the herpes simplex virus alpha-trans-induction factor (VP16). |journal=J. Biol. Chem. |volume=268 |issue= 9 |pages= 6525-34 |year= 1993 |pmid= 8454622 |doi= }}
*{{cite journal | author=Zoppè M, Frattini A, Faranda S, Vezzoni P |title=The complete sequence of the host cell factor 1 (HCFC1) gene and its promoter: a role for YY1 transcription factor in the regulation of its expression. |journal=Genomics |volume=34 |issue= 1 |pages= 85-91 |year= 1996 |pmid= 8661027 |doi= 10.1006/geno.1996.0244 }}
*{{cite journal | author=Wilson AC, Freiman RN, Goto H, ''et al.'' |title=VP16 targets an amino-terminal domain of HCF involved in cell cycle progression. |journal=Mol. Cell. Biol. |volume=17 |issue= 10 |pages= 6139-46 |year= 1997 |pmid= 9315674 |doi= }}
*{{cite journal | author=Freiman RN, Herr W |title=Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP. |journal=Genes Dev. |volume=11 |issue= 23 |pages= 3122-7 |year= 1998 |pmid= 9389645 |doi= }}
*{{cite journal | author=Lu R, Yang P, Padmakumar S, Misra V |title=The herpesvirus transactivator VP16 mimics a human basic domain leucine zipper protein, luman, in its interaction with HCF. |journal=J. Virol. |volume=72 |issue= 8 |pages= 6291-7 |year= 1998 |pmid= 9658067 |doi= }}
*{{cite journal | author=Ge H, Si Y, Roeder RG |title=Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation. |journal=EMBO J. |volume=17 |issue= 22 |pages= 6723-9 |year= 1999 |pmid= 9822615 |doi= 10.1093/emboj/17.22.6723 }}
*{{cite journal | author=La Boissière S, Hughes T, O'Hare P |title=HCF-dependent nuclear import of VP16. |journal=EMBO J. |volume=18 |issue= 2 |pages= 480-9 |year= 1999 |pmid= 9889203 |doi= 10.1093/emboj/18.2.480 }}
*{{cite journal | author=Lu R, Misra V |title=Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency. |journal=J. Virol. |volume=74 |issue= 2 |pages= 934-43 |year= 2000 |pmid= 10623756 |doi= }}
*{{cite journal | author=Mahajan SS, Wilson AC |title=Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP. |journal=Mol. Cell. Biol. |volume=20 |issue= 3 |pages= 919-28 |year= 2000 |pmid= 10629049 |doi= }}
*{{cite journal | author=Ajuh PM, Browne GJ, Hawkes NA, ''et al.'' |title=Association of a protein phosphatase 1 activity with the human factor C1 (HCF) complex. |journal=Nucleic Acids Res. |volume=28 |issue= 3 |pages= 678-86 |year= 2000 |pmid= 10637318 |doi= }}
*{{cite journal | author=Vogel JL, Kristie TM |title=The novel coactivator C1 (HCF) coordinates multiprotein enhancer formation and mediates transcription activation by GABP. |journal=EMBO J. |volume=19 |issue= 4 |pages= 683-90 |year= 2000 |pmid= 10675337 |doi= 10.1093/emboj/19.4.683 }}
*{{cite journal | author=Scarr RB, Smith MR, Beddall M, Sharp PA |title=A novel 50-kilodalton fragment of host cell factor 1 (C1) in G(0) cells. |journal=Mol. Cell. Biol. |volume=20 |issue= 10 |pages= 3568-75 |year= 2000 |pmid= 10779346 |doi= }}
*{{cite journal | author=Choi Y, Asada S, Uesugi M |title=Divergent hTAFII31-binding motifs hidden in activation domains. |journal=J. Biol. Chem. |volume=275 |issue= 21 |pages= 15912-6 |year= 2000 |pmid= 10821850 |doi= }}
*{{cite journal | author=Lu R, Misra V |title=Zhangfei: a second cellular protein interacts with herpes simplex virus accessory factor HCF in a manner similar to Luman and VP16. |journal=Nucleic Acids Res. |volume=28 |issue= 12 |pages= 2446-54 |year= 2000 |pmid= 10871379 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DMB... {November 17, 2007 12:09:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:09:50 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HLA-DMB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hdm.
| PDB = {{PDB2|1hdm}}, {{PDB2|2bc4}}
| Name = Major histocompatibility complex, class II, DM beta
| HGNCid = 4935
| Symbol = HLA-DMB
| AltSymbols =; D6S221E; RING7
| OMIM = 142856
| ECnumber =
| Homologene = 68231
| MGIid = 95922
| GeneAtlas_image1 = PBB_GE_HLA-DMB_203932_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3109
| Hs_Ensembl = ENSG00000206294
| Hs_RefseqProtein = NP_002109
| Hs_RefseqmRNA = NM_002118
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_QBL
| Hs_GenLoc_start = 32973998
| Hs_GenLoc_end = 32980399
| Hs_Uniprot = P28068
| Mm_EntrezGene = 14999
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_010387
| Mm_RefseqProtein = NP_034517
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Major histocompatibility complex, class II, DM beta''', also known as '''HLA-DMB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HLA-DMB major histocompatibility complex, class II, DM beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3109| 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 = HLA-DMB belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DMA) and a beta (DMB) chain, both anchored in the membrane. It is located in intracellular vesicles. DM plays a central role in the peptide loading of MHC class II molecules by helping to release the CLIP (class II-associated invariant chain peptide) molecule from the peptide binding site. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail.<ref name="entrez">{{cite web | title = Entrez Gene: HLA-DMB major histocompatibility complex, class II, DM beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3109| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vogt AB, Kropshofer H |title=HLA-DM - an endosomal and lysosomal chaperone for the immune system. |journal=Trends Biochem. Sci. |volume=24 |issue= 4 |pages= 150-4 |year= 1999 |pmid= 10322421 |doi= }}
*{{cite journal | author=Kropshofer H, Hämmerling GJ, Vogt AB |title=The impact of the non-classical MHC proteins HLA-DM and HLA-DO on loading of MHC class II molecules. |journal=Immunol. Rev. |volume=172 |issue= |pages= 267-78 |year= 2000 |pmid= 10631952 |doi= }}
*{{cite journal | author=Piatier-Tonneau D, Gastinel LN, Amblard F, ''et al.'' |title=Interaction of CD4 with HLA class II antigens and HIV gp120. |journal=Immunogenetics |volume=34 |issue= 2 |pages= 121-8 |year= 1991 |pmid= 1869305 |doi= }}
*{{cite journal | author=Kelly AP, Monaco JJ, Cho SG, Trowsdale J |title=A new human HLA class II-related locus, DM. |journal=Nature |volume=353 |issue= 6344 |pages= 571-3 |year= 1991 |pmid= 1922365 |doi= 10.1038/353571a0 }}
*{{cite journal | author=Rosenstein Y, Burakoff SJ, Herrmann SH |title=HIV-gp120 can block CD4-class II MHC-mediated adhesion. |journal=J. Immunol. |volume=144 |issue= 2 |pages= 526-31 |year= 1990 |pmid= 1967269 |doi= }}
*{{cite journal | author=Bowman MR, MacFerrin KD, Schreiber SL, Burakoff SJ |title=Identification and structural analysis of residues in the V1 region of CD4 involved in interaction with human immunodeficiency virus envelope glycoprotein gp120 and class II major histocompatibility complex molecules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 9052-6 |year= 1991 |pmid= 1978941 |doi= }}
*{{cite journal | author=Clayton LK, Sieh M, Pious DA, Reinherz EL |title=Identification of human CD4 residues affecting class II MHC versus HIV-1 gp120 binding. |journal=Nature |volume=339 |issue= 6225 |pages= 548-51 |year= 1989 |pmid= 2543930 |doi= 10.1038/339548a0 }}
*{{cite journal | author=Diamond DC, Sleckman BP, Gregory T, ''et al.'' |title=Inhibition of CD4+ T cell function by the HIV envelope protein, gp120. |journal=J. Immunol. |volume=141 |issue= 11 |pages= 3715-7 |year= 1988 |pmid= 2846691 |doi= }}
*{{cite journal | author=Andrieu JM, Even P, Venet A |title=AIDS and related syndromes as a viral-induced autoimmune disease of the immune system: an anti-MHC II disorder. Therapeutic implications. |journal=AIDS research |volume=2 |issue= 3 |pages= 163-74 |year= 1986 |pmid= 3489470 |doi= }}
*{{cite journal | author=Houlgatte R, Scarmato P, el Marhomy S, ''et al.'' |title=HLA class II antigens and the HIV envelope glycoprotein gp120 bind to the same face of CD4. |journal=J. Immunol. |volume=152 |issue= 9 |pages= 4475-88 |year= 1994 |pmid= 7512597 |doi= }}
*{{cite journal | author=Shaman J, von Scheven E, Morris P, ''et al.'' |title=Analysis of HLA-DMB mutants and -DMB genomic structure. |journal=Immunogenetics |volume=41 |issue= 2-3 |pages= 117-24 |year= 1995 |pmid= 7528727 |doi= }}
*{{cite journal | author=Chirmule N, McCloskey TW, Hu R, ''et al.'' |title=HIV gp120 inhibits T cell activation by interfering with expression of costimulatory molecules CD40 ligand and CD80 (B71). |journal=J. Immunol. |volume=155 |issue= 2 |pages= 917-24 |year= 1995 |pmid= 7541827 |doi= }}
*{{cite journal | author=Rowell JF, Stanhope PE, Siliciano RF |title=Endocytosis of endogenously synthesized HIV-1 envelope protein. Mechanism and role in processing for association with class II MHC. |journal=J. Immunol. |volume=155 |issue= 1 |pages= 473-88 |year= 1995 |pmid= 7602119 |doi= }}
*{{cite journal | author=Sherman MA, Weber DA, Jensen PE |title=DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide. |journal=Immunity |volume=3 |issue= 2 |pages= 197-205 |year= 1995 |pmid= 7648393 |doi= }}
*{{cite journal | author=Radley E, Alderton RP, Kelly A, ''et al.'' |title=Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene organization of all six class II families in the human major histocompatibility complex. |journal=J. Biol. Chem. |volume=269 |issue= 29 |pages= 18834-8 |year= 1994 |pmid= 8034636 |doi= }}
*{{cite journal | author=Chen YH, Böck G, Vornhagen R, ''et al.'' |title=HIV-1 gp41 binding proteins and antibodies to gp41 could inhibit enhancement of human Raji cell MHC class I and II expression by gp41. |journal=Mol. Immunol. |volume=31 |issue= 13 |pages= 977-82 |year= 1994 |pmid= 8084338 |doi= }}
*{{cite journal | author=Fling SP, Arp B, Pious D |title=HLA-DMA and -DMB genes are both required for MHC class II/peptide complex formation in antigen-presenting cells. |journal=Nature |volume=368 |issue= 6471 |pages= 554-8 |year= 1994 |pmid= 8139690 |doi= 10.1038/368554a0 }}
*{{cite journal | author=Chirmule N, Wang XP, Hu R, ''et al.'' |title=Envelope glycoproteins of HIV-1 interfere with T-cell-dependent B cell differentiation: role of CD4-MHC class II interaction in the effector phase of T cell help. |journal=Cell. Immunol. |volume=155 |issue= 1 |pages= 169-82 |year= 1994 |pmid= 8168144 |doi= 10.1006/cimm.1994.1110 }}
*{{cite journal | author=Sanderson F, Powis SH, Kelly AP, Trowsdale J |title=Limited polymorphism in HLA-DM does not involve the peptide binding groove. |journal=Immunogenetics |volume=39 |issue= 1 |pages= 56-8 |year= 1993 |pmid= 8225438 |doi= }}
*{{cite journal | author=Callahan KM, Rowell JF, Soloski MJ, ''et al.'' |title=HIV-1 envelope protein is expressed on the surface of infected cells before its processing and presentation to class II-restricted T lymphocytes. |journal=J. Immunol. |volume=151 |issue= 6 |pages= 2928-42 |year= 1993 |pmid= 8376762 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HOXA9... {November 17, 2007 12:09:50 PM PST}
- SEARCH REDIRECT: Control Box Found: HOXA9 {November 17, 2007 12:11:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:11:07 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:11:07 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:11:07 PM PST}
- UPDATED: Updated protein page: HOXA9 {November 17, 2007 12:11:13 PM PST}
- INFO: Beginning work on ICAM3... {November 17, 2007 12:11:13 PM PST}
- SEARCH REDIRECT: Control Box Found: ICAM3 {November 17, 2007 12:11:37 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:11:41 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:11:41 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:11:41 PM PST}
- UPDATED: Updated protein page: ICAM3 {November 17, 2007 12:11:47 PM PST}
- INFO: Beginning work on ITGB5... {November 17, 2007 12:12:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:13:02 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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 = Integrin, beta 5
| HGNCid = 6160
| Symbol = ITGB5
| AltSymbols =; FLJ26658
| OMIM = 147561
| ECnumber =
| Homologene = 20511
| MGIid = 96614
| GeneAtlas_image1 = PBB_GE_ITGB5_201124_at_tn.png
| GeneAtlas_image2 = PBB_GE_ITGB5_201125_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3693
| Hs_Ensembl = ENSG00000082781
| Hs_RefseqProtein = XP_001129224
| Hs_RefseqmRNA = XM_001129224
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 125964488
| Hs_GenLoc_end = 126088842
| Hs_Uniprot = P18084
| Mm_EntrezGene = 16419
| Mm_Ensembl = ENSMUSG00000022817
| Mm_RefseqmRNA = NM_010580
| Mm_RefseqProtein = NP_034710
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 33749412
| Mm_GenLoc_end = 33868892
| Mm_Uniprot = Q6PE70
}}
}}
'''Integrin, beta 5''', also known as '''ITGB5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ITGB5 integrin, beta 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3693| 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=Evans JP |title=Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. |journal=Bioessays |volume=23 |issue= 7 |pages= 628-39 |year= 2001 |pmid= 11462216 |doi= 10.1002/bies.1088 }}
*{{cite journal | author=Smith JW, Vestal DJ, Irwin SV, ''et al.'' |title=Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin. |journal=J. Biol. Chem. |volume=265 |issue= 19 |pages= 11008-13 |year= 1990 |pmid= 1694173 |doi= }}
*{{cite journal | author=Adams JC, Watt FM |title=Expression of beta 1, beta 3, beta 4, and beta 5 integrins by human epidermal keratinocytes and non-differentiating keratinocytes. |journal=J. Cell Biol. |volume=115 |issue= 3 |pages= 829-41 |year= 1991 |pmid= 1918165 |doi= }}
*{{cite journal | author=McLean JW, Vestal DJ, Cheresh DA, Bodary SC |title=cDNA sequence of the human integrin beta 5 subunit. |journal=J. Biol. Chem. |volume=265 |issue= 28 |pages= 17126-31 |year= 1990 |pmid= 2211615 |doi= }}
*{{cite journal | author=Ramaswamy H, Hemler ME |title=Cloning, primary structure and properties of a novel human integrin beta subunit. |journal=EMBO J. |volume=9 |issue= 5 |pages= 1561-8 |year= 1990 |pmid= 2328726 |doi= }}
*{{cite journal | author=Suzuki S, Huang ZS, Tanihara H |title=Cloning of an integrin beta subunit exhibiting high homology with integrin beta 3 subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 14 |pages= 5354-8 |year= 1990 |pmid= 2371275 |doi= }}
*{{cite journal | author=Hu DD, Lin EC, Kovach NL, ''et al.'' |title=A biochemical characterization of the binding of osteopontin to integrins alpha v beta 1 and alpha v beta 5. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26232-8 |year= 1995 |pmid= 7592829 |doi= }}
*{{cite journal | author=Vogel BE, Lee SJ, Hildebrand A, ''et al.'' |title=A novel integrin specificity exemplified by binding of the alpha v beta 5 integrin to the basic domain of the HIV Tat protein and vitronectin. |journal=J. Cell Biol. |volume=121 |issue= 2 |pages= 461-8 |year= 1993 |pmid= 7682219 |doi= }}
*{{cite journal | author=Pasqualini R, Bodorova J, Ye S, Hemler ME |title=A study of the structure, function and distribution of beta 5 integrins using novel anti-beta 5 monoclonal antibodies. |journal=J. Cell. Sci. |volume=105 ( Pt 1) |issue= |pages= 101-11 |year= 1993 |pmid= 7689573 |doi= }}
*{{cite journal | author=Lafrenie RM, Wahl LM, Epstein JS, ''et al.'' |title=HIV-1-Tat protein promotes chemotaxis and invasive behavior by monocytes. |journal=J. Immunol. |volume=157 |issue= 3 |pages= 974-7 |year= 1996 |pmid= 8757599 |doi= }}
*{{cite journal | author=Rabb H, Barroso-Vicens E, Adams R, ''et al.'' |title=Alpha-V/beta-3 and alpha-V/beta-5 integrin distribution in neoplastic kidney. |journal=Am. J. Nephrol. |volume=16 |issue= 5 |pages= 402-8 |year= 1997 |pmid= 8886177 |doi= }}
*{{cite journal | author=Liliental J, Chang DD |title=Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2379-83 |year= 1998 |pmid= 9442085 |doi= }}
*{{cite journal | author=Memmo LM, McKeown-Longo P |title=The alphavbeta5 integrin functions as an endocytic receptor for vitronectin. |journal=J. Cell. Sci. |volume=111 ( Pt 4) |issue= |pages= 425-33 |year= 1998 |pmid= 9443892 |doi= }}
*{{cite journal | author=Zhang H, Tan SM, Lu J |title=cDNA cloning reveals two mouse beta5 integrin transcripts distinct in cytoplasmic domains as a result of alternative splicing. |journal=Biochem. J. |volume=331 ( Pt 2) |issue= |pages= 631-7 |year= 1998 |pmid= 9531507 |doi= }}
*{{cite journal | author=Barillari G, Sgadari C, Palladino C, ''et al.'' |title=Inflammatory cytokines synergize with the HIV-1 Tat protein to promote angiogenesis and Kaposi's sarcoma via induction of basic fibroblast growth factor and the alpha v beta 3 integrin. |journal=J. Immunol. |volume=163 |issue= 4 |pages= 1929-35 |year= 1999 |pmid= 10438928 |doi= }}
*{{cite journal | author=Carriero MV, Del Vecchio S, Capozzoli M, ''et al.'' |title=Urokinase receptor interacts with alpha(v)beta5 vitronectin receptor, promoting urokinase-dependent cell migration in breast cancer. |journal=Cancer Res. |volume=59 |issue= 20 |pages= 5307-14 |year= 1999 |pmid= 10537314 |doi= }}
*{{cite journal | author=Tang S, Gao Y, Ware JA |title=Enhancement of endothelial cell migration and in vitro tube formation by TAP20, a novel beta 5 integrin-modulating, PKC theta-dependent protein. |journal=J. Cell Biol. |volume=147 |issue= 5 |pages= 1073-84 |year= 1999 |pmid= 10579726 |doi= }}
*{{cite journal | author=Cirulli V, Beattie GM, Klier G, ''et al.'' |title=Expression and function of alpha(v)beta(3) and alpha(v)beta(5) integrins in the developing pancreas: roles in the adhesion and migration of putative endocrine progenitor cells. |journal=J. Cell Biol. |volume=150 |issue= 6 |pages= 1445-60 |year= 2000 |pmid= 10995448 |doi= }}
*{{cite journal | author=Albert ML, Kim JI, Birge RB |title=alphavbeta5 integrin recruits the CrkII-Dock180-rac1 complex for phagocytosis of apoptotic cells. |journal=Nat. Cell Biol. |volume=2 |issue= 12 |pages= 899-905 |year= 2001 |pmid= 11146654 |doi= 10.1038/35046549 }}
*{{cite journal | author=Zhou M, Graham R, Russell G, Croucher PI |title=MDC-9 (ADAM-9/Meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 2 |pages= 574-80 |year= 2001 |pmid= 11162558 |doi= 10.1006/bbrc.2000.4155 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on JUNB... {November 17, 2007 12:13:03 PM PST}
- SEARCH REDIRECT: Control Box Found: JUNB {November 17, 2007 12:13:23 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:13:26 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:13:26 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:13:26 PM PST}
- UPDATED: Updated protein page: JUNB {November 17, 2007 12:13:32 PM PST}
- INFO: Beginning work on LCN2... {November 17, 2007 12:13:32 PM PST}
- SEARCH REDIRECT: Control Box Found: LCN2 {November 17, 2007 12:13:54 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:13:56 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:13:56 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:13:56 PM PST}
- UPDATED: Updated protein page: LCN2 {November 17, 2007 12:14:02 PM PST}
- INFO: Beginning work on MCM3... {November 17, 2007 12:14:02 PM PST}
- SEARCH REDIRECT: Control Box Found: MCM3 {November 17, 2007 12:14:29 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:14:31 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:14:31 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:14:31 PM PST}
- UPDATED: Updated protein page: MCM3 {November 17, 2007 12:14:38 PM PST}
- INFO: Beginning work on MDM4... {November 17, 2007 12:14:38 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:15:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MDM4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2cr8.
| PDB = {{PDB2|2cr8}}
| Name = Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)
| HGNCid = 6974
| Symbol = MDM4
| AltSymbols =; DKFZp781B1423; MDMX; MGC132766; MRP1
| OMIM = 602704
| ECnumber =
| Homologene = 1794
| MGIid = 107934
| GeneAtlas_image1 = PBB_GE_MDM4_205655_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein 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}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0042177 |text = negative regulation of protein catabolic process}} {{GNF_GO|id=GO:0045023 |text = G0 to G1 transition}} {{GNF_GO|id=GO:0050821 |text = protein stabilization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4194
| Hs_Ensembl = ENSG00000198625
| Hs_RefseqProtein = NP_002384
| Hs_RefseqmRNA = NM_002393
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 202752134
| Hs_GenLoc_end = 202793871
| Hs_Uniprot = O15151
| Mm_EntrezGene = 17248
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_008575
| Mm_RefseqProtein = NP_032601
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)''', also known as '''MDM4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4194| 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 human MDM4 gene, which plays a role in apoptosis, encodes a 490-amino acid protein containing a RING finger domain and a putative nuclear localization signal. The MDM4 putative nuclear localization signal, which all Mdm proteins contain, is located in the C-terminal region of the protein. The mRNA is expressed at a high level in thymus and at lower levels in all other tissues tested. MDM4 protein produced by in vitro translation interacts with p53 via a binding domain located in the N-terminal region of the MDM4 protein. MDM4 shows significant structural similarity to p53-binding protein MDM2<ref name="entrez">{{cite web | title = Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4194| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Meulmeester E, Pereg Y, Shiloh Y, Jochemsen AG |title=ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. |journal=Cell Cycle |volume=4 |issue= 9 |pages= 1166-70 |year= 2006 |pmid= 16082221 |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=Shvarts A, Steegenga WT, Riteco N, ''et al.'' |title=MDMX: a novel p53-binding protein with some functional properties of MDM2. |journal=EMBO J. |volume=15 |issue= 19 |pages= 5349-57 |year= 1996 |pmid= 8895579 |doi= }}
*{{cite journal | author=Shvarts A, Bazuine M, Dekker P, ''et al.'' |title=Isolation and identification of the human homolog of a new p53-binding protein, Mdmx. |journal=Genomics |volume=43 |issue= 1 |pages= 34-42 |year= 1997 |pmid= 9226370 |doi= 10.1006/geno.1997.4775 }}
*{{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=Tanimura S, Ohtsuka S, Mitsui K, ''et al.'' |title=MDM2 interacts with MDMX through their RING finger domains. |journal=FEBS Lett. |volume=447 |issue= 1 |pages= 5-9 |year= 1999 |pmid= 10218570 |doi= }}
*{{cite journal | author=Ongkeko WM, Wang XQ, Siu WY, ''et al.'' |title=MDM2 and MDMX bind and stabilize the p53-related protein p73. |journal=Curr. Biol. |volume=9 |issue= 15 |pages= 829-32 |year= 1999 |pmid= 10469568 |doi= }}
*{{cite journal | author=Sharp DA, Kratowicz SA, Sank MJ, George DL |title=Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. |journal=J. Biol. Chem. |volume=274 |issue= 53 |pages= 38189-96 |year= 2000 |pmid= 10608892 |doi= }}
*{{cite journal | author=Jackson MW, Lindstrom MS, Berberich SJ |title=MdmX binding to ARF affects Mdm2 protein stability and p53 transactivation. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 25336-41 |year= 2001 |pmid= 11297540 |doi= 10.1074/jbc.M010685200 }}
*{{cite journal | author=Parant J, Chavez-Reyes A, Little NA, ''et al.'' |title=Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. |journal=Nat. Genet. |volume=29 |issue= 1 |pages= 92-5 |year= 2001 |pmid= 11528400 |doi= 10.1038/ng714 }}
*{{cite journal | author=Gentiletti F, Mancini F, D'Angelo M, ''et al.'' |title=MDMX stability is regulated by p53-induced caspase cleavage in NIH3T3 mouse fibroblasts. |journal=Oncogene |volume=21 |issue= 6 |pages= 867-77 |year= 2002 |pmid= 11840332 |doi= 10.1038/sj.onc.1205137 }}
*{{cite journal | author=Harris RA, Yang A, Stein RC, ''et al.'' |title=Cluster analysis of an extensive human breast cancer cell line protein expression map database. |journal=Proteomics |volume=2 |issue= 2 |pages= 212-23 |year= 2002 |pmid= 11840567 |doi= }}
*{{cite journal | author=Gu J, Kawai H, Nie L, ''et al.'' |title=Mutual dependence of MDM2 and MDMX in their functional inactivation of p53. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19251-4 |year= 2002 |pmid= 11953423 |doi= 10.1074/jbc.C200150200 }}
*{{cite journal | author=Migliorini D, Lazzerini Denchi E, Danovi D, ''et al.'' |title=Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development. |journal=Mol. Cell. Biol. |volume=22 |issue= 15 |pages= 5527-38 |year= 2002 |pmid= 12101245 |doi= }}
*{{cite journal | author=Wistow G, Bernstein SL, Wyatt MK, ''et al.'' |title=Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants. |journal=Mol. Vis. |volume=8 |issue= |pages= 205-20 |year= 2002 |pmid= 12107410 |doi= }}
*{{cite journal | author=Sabbatini P, McCormick F |title=MDMX inhibits the p300/CBP-mediated acetylation of p53. |journal=DNA Cell Biol. |volume=21 |issue= 7 |pages= 519-25 |year= 2002 |pmid= 12162806 |doi= 10.1089/104454902320219077 }}
*{{cite journal | author=Li C, Chen L, Chen J |title=DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms. |journal=Mol. Cell. Biol. |volume=22 |issue= 21 |pages= 7562-71 |year= 2002 |pmid= 12370303 |doi= }}
*{{cite journal | author=Badciong JC, Haas AL |title=MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49668-75 |year= 2003 |pmid= 12393902 |doi= 10.1074/jbc.M208593200 }}
*{{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=Kadakia M, Brown TL, McGorry MM, Berberich SJ |title=MdmX inhibits Smad transactivation. |journal=Oncogene |volume=21 |issue= 57 |pages= 8776-85 |year= 2003 |pmid= 12483531 |doi= 10.1038/sj.onc.1205993 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MNAT1... {November 17, 2007 12:15:07 PM PST}
- SEARCH REDIRECT: Control Box Found: MNAT1 {November 17, 2007 12:15:32 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:15:34 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:15:34 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:15:34 PM PST}
- UPDATED: Updated protein page: MNAT1 {November 17, 2007 12:15:40 PM PST}
- INFO: Beginning work on MYBPC3... {November 17, 2007 12:15:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:16:13 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MYBPC3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gxe.
| PDB = {{PDB2|1gxe}}, {{PDB2|1pd6}}, {{PDB2|2avg}}
| Name = Myosin binding protein C, cardiac
| HGNCid = 7551
| Symbol = MYBPC3
| AltSymbols =; FHC; CMH4; MYBP-C
| OMIM = 600958
| ECnumber =
| Homologene = 215
| MGIid = 102844
| GeneAtlas_image1 = PBB_GE_MYBPC3_208040_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008307 |text = structural constituent of muscle}}
| Component = {{GNF_GO|id=GO:0005863 |text = striated muscle thick filament}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006942 |text = regulation of striated muscle contraction}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0055010 |text = ventricular cardiac muscle morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4607
| Hs_Ensembl = ENSG00000134571
| Hs_RefseqProtein = NP_000247
| Hs_RefseqmRNA = NM_000256
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 47309527
| Hs_GenLoc_end = 47330806
| Hs_Uniprot = Q14896
| Mm_EntrezGene = 17868
| Mm_Ensembl = ENSMUSG00000002100
| Mm_RefseqmRNA = NM_008653
| Mm_RefseqProtein = NP_032679
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 90918983
| Mm_GenLoc_end = 90937350
| Mm_Uniprot = Q3TF37
}}
}}
'''Myosin binding protein C, cardiac''', also known as '''MYBPC3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MYBPC3 myosin binding protein C, cardiac| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4607| 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 = MYBPC3 encodes the cardiac isoform of myosin-binding protein C. Myosin-binding protein C is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. MYBPC3, the cardiac isoform, is expressed exclussively in heart muscle. Regulatory phosphorylation of the cardiac isoform in vivo by cAMP-dependent protein kinase (PKA) upon adrenergic stimulation may be linked to modulation of cardiac contraction. Mutations in MYBPC3 are one cause of familial hypertrophic cardiomyopathy.<ref name="entrez">{{cite web | title = Entrez Gene: MYBPC3 myosin binding protein C, cardiac| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4607| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vikstrom KL, Leinwand LA |title=Contractile protein mutations and heart disease. |journal=Curr. Opin. Cell Biol. |volume=8 |issue= 1 |pages= 97-105 |year= 1996 |pmid= 8791411 |doi= }}
*{{cite journal | author=Schaub MC, Hefti MA, Zuellig RA, Morano I |title=Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms. |journal=Cardiovasc. Res. |volume=37 |issue= 2 |pages= 381-404 |year= 1998 |pmid= 9614495 |doi= }}
*{{cite journal | author=Bonne G, Carrier L, Richard P, ''et al.'' |title=Familial hypertrophic cardiomyopathy: from mutations to functional defects. |journal=Circ. Res. |volume=83 |issue= 6 |pages= 580-93 |year= 1998 |pmid= 9742053 |doi= }}
*{{cite journal | author=Jääskeläinen P, Miettinen R, Kärkkäinen P, ''et al.'' |title=Genetics of hypertrophic cardiomyopathy in eastern Finland: few founder mutations with benign or intermediary phenotypes. |journal=Ann. Med. |volume=36 |issue= 1 |pages= 23-32 |year= 2004 |pmid= 15000344 |doi= }}
*{{cite journal | author=Starr R, Offer G |title=The interaction of C-protein with heavy meromyosin and subfragment-2. |journal=Biochem. J. |volume=171 |issue= 3 |pages= 813-6 |year= 1978 |pmid= 352343 |doi= }}
*{{cite journal | author=Moos C, Feng IN |title=Effect of C-protein on actomyosin ATPase. |journal=Biochim. Biophys. Acta |volume=632 |issue= 2 |pages= 141-9 |year= 1980 |pmid= 6448079 |doi= }}
*{{cite journal | author=Watkins H, Conner D, Thierfelder L, ''et al.'' |title=Mutations in the cardiac myosin binding protein-C gene on chromosome 11 cause familial hypertrophic cardiomyopathy. |journal=Nat. Genet. |volume=11 |issue= 4 |pages= 434-7 |year= 1996 |pmid= 7493025 |doi= 10.1038/ng1295-434 }}
*{{cite journal | author=Bonne G, Carrier L, Bercovici J, ''et al.'' |title=Cardiac myosin binding protein-C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathy. |journal=Nat. Genet. |volume=11 |issue= 4 |pages= 438-40 |year= 1996 |pmid= 7493026 |doi= 10.1038/ng1295-438 }}
*{{cite journal | author=Gautel M, Zuffardi O, Freiburg A, Labeit S |title=Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction? |journal=EMBO J. |volume=14 |issue= 9 |pages= 1952-60 |year= 1995 |pmid= 7744002 |doi= }}
*{{cite journal | author=Carrier L, Hengstenberg C, Beckmann JS, ''et al.'' |title=Mapping of a novel gene for familial hypertrophic cardiomyopathy to chromosome 11. |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 311-3 |year= 1993 |pmid= 8358441 |doi= 10.1038/ng0793-311 }}
*{{cite journal | author=Freiburg A, Gautel M |title=A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. |journal=Eur. J. Biochem. |volume=235 |issue= 1-2 |pages= 317-23 |year= 1996 |pmid= 8631348 |doi= }}
*{{cite journal | author=Carrier L, Bonne G, Bährend E, ''et al.'' |title=Organization and sequence of human cardiac myosin binding protein C gene (MYBPC3) and identification of mutations predicted to produce truncated proteins in familial hypertrophic cardiomyopathy. |journal=Circ. Res. |volume=80 |issue= 3 |pages= 427-34 |year= 1997 |pmid= 9048664 |doi= }}
*{{cite journal | author=Rottbauer W, Gautel M, Zehelein J, ''et al.'' |title=Novel splice donor site mutation in the cardiac myosin-binding protein-C gene in familial hypertrophic cardiomyopathy. Characterization Of cardiac transcript and protein. |journal=J. Clin. Invest. |volume=100 |issue= 2 |pages= 475-82 |year= 1997 |pmid= 9218526 |doi= }}
*{{cite journal | author=Yu B, French JA, Carrier L, ''et al.'' |title=Molecular pathology of familial hypertrophic cardiomyopathy caused by mutations in the cardiac myosin binding protein C gene. |journal=J. Med. Genet. |volume=35 |issue= 3 |pages= 205-10 |year= 1998 |pmid= 9541104 |doi= }}
*{{cite journal | author=Moolman-Smook JC, Mayosi B, Brink P, Corfield VA |title=Identification of a new missense mutation in MyBP-C associated with hypertrophic cardiomyopathy. |journal=J. Med. Genet. |volume=35 |issue= 3 |pages= 253-4 |year= 1998 |pmid= 9541115 |doi= }}
*{{cite journal | author=Niimura H, Bachinski LL, Sangwatanaroj S, ''et al.'' |title=Mutations in the gene for cardiac myosin-binding protein C and late-onset familial hypertrophic cardiomyopathy. |journal=N. Engl. J. Med. |volume=338 |issue= 18 |pages= 1248-57 |year= 1998 |pmid= 9562578 |doi= }}
*{{cite journal | author=Richard P, Isnard R, Carrier L, ''et al.'' |title=Double heterozygosity for mutations in the beta-myosin heavy chain and in the cardiac myosin binding protein C genes in a family with hypertrophic cardiomyopathy. |journal=J. Med. Genet. |volume=36 |issue= 7 |pages= 542-5 |year= 1999 |pmid= 10424815 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NEDD8... {November 17, 2007 12:16:13 PM PST}
- SEARCH REDIRECT: Control Box Found: NEDD8 {November 17, 2007 12:16:39 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:16:40 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:16:40 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:16:40 PM PST}
- UPDATED: Updated protein page: NEDD8 {November 17, 2007 12:16:46 PM PST}
- INFO: Beginning work on NOTCH4... {November 17, 2007 12:16:47 PM PST}
- SEARCH REDIRECT: Control Box Found: NOTCH4 {November 17, 2007 12:17:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:17:18 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:17:18 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:17:18 PM PST}
- UPDATED: Updated protein page: NOTCH4 {November 17, 2007 12:17:24 PM PST}
- INFO: Beginning work on PIK3R2... {November 17, 2007 12:17:24 PM PST}
- SEARCH REDIRECT: Control Box Found: PIK3R2 {November 17, 2007 12:17:56 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:17:59 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:17:59 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:17:59 PM PST}
- UPDATED: Updated protein page: PIK3R2 {November 17, 2007 12:18:05 PM PST}
- INFO: Beginning work on PRKAA1... {November 17, 2007 12:18:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:19:01 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| update_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_PRKAA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2h6d.
| PDB = {{PDB2|2h6d}}
| Name = Protein kinase, AMP-activated, alpha 1 catalytic subunit
| HGNCid = 9376
| Symbol = PRKAA1
| AltSymbols =; AMPK; AMPKa1; MGC33776; MGC57364
| OMIM = 602739
| ECnumber =
| Homologene = 49590
| MGIid = 2145955
| GeneAtlas_image1 = PBB_GE_PRKAA1_209799_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004691 |text = cAMP-dependent protein kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042557 |text = eukaryotic elongation factor-2 kinase activator activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0001666 |text = response to hypoxia}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0006695 |text = cholesterol biosynthetic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0017148 |text = negative regulation of protein biosynthetic process}} {{GNF_GO|id=GO:0045542 |text = positive regulation of cholesterol biosynthetic process}} {{GNF_GO|id=GO:0045722 |text = positive regulation of gluconeogenesis}} {{GNF_GO|id=GO:0045768 |text = positive regulation of anti-apoptosis}} {{GNF_GO|id=GO:0046318 |text = negative regulation of glucosylceramide biosynthetic process}} {{GNF_GO|id=GO:0046321 |text = positive regulation of fatty acid oxidation}} {{GNF_GO|id=GO:0046326 |text = positive regulation of glucose import}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5562
| Hs_Ensembl = ENSG00000132356
| Hs_RefseqProtein = NP_006242
| Hs_RefseqmRNA = NM_006251
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 40795239
| Hs_GenLoc_end = 40834046
| Hs_Uniprot = Q13131
| Mm_EntrezGene = 105787
| Mm_Ensembl = ENSMUSG00000050697
| Mm_RefseqmRNA = XM_973840
| Mm_RefseqProtein = XP_978934
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 5091090
| Mm_GenLoc_end = 5129114
| Mm_Uniprot = Q3TUQ7
}}
}}
'''Protein kinase, AMP-activated, alpha 1 catalytic subunit''', also known as '''PRKAA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKAA1 protein kinase, AMP-activated, alpha 1 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5562| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed.<ref name="entrez">{{cite web | title = Entrez Gene: PRKAA1 protein kinase, AMP-activated, alpha 1 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5562| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Munday MR, Campbell DG, Carling D, Hardie DG |title=Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase. |journal=Eur. J. Biochem. |volume=175 |issue= 2 |pages= 331-8 |year= 1988 |pmid= 2900138 |doi= }}
*{{cite journal | author=Stapleton D, Mitchelhill KI, Gao G, ''et al.'' |title=Mammalian AMP-activated protein kinase subfamily. |journal=J. Biol. Chem. |volume=271 |issue= 2 |pages= 611-4 |year= 1996 |pmid= 8557660 |doi= }}
*{{cite journal | author=Woods A, Cheung PC, Smith FC, ''et al.'' |title=Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro. |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10282-90 |year= 1996 |pmid= 8626596 |doi= }}
*{{cite journal | author=Hawley SA, Davison M, Woods A, ''et al.'' |title=Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27879-87 |year= 1996 |pmid= 8910387 |doi= }}
*{{cite journal | author=Stapleton D, Woollatt E, Mitchelhill KI, ''et al.'' |title=AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location. |journal=FEBS Lett. |volume=409 |issue= 3 |pages= 452-6 |year= 1997 |pmid= 9224708 |doi= }}
*{{cite journal | author=Velasco G, Gómez del Pulgar T, Carling D, Guzmán M |title=Evidence that the AMP-activated protein kinase stimulates rat liver carnitine palmitoyltransferase I by phosphorylating cytoskeletal components. |journal=FEBS Lett. |volume=439 |issue= 3 |pages= 317-20 |year= 1998 |pmid= 9845345 |doi= }}
*{{cite journal | author=Crute BE, Seefeld K, Gamble J, ''et al.'' |title=Functional domains of the alpha1 catalytic subunit of the AMP-activated protein kinase. |journal=J. Biol. Chem. |volume=273 |issue= 52 |pages= 35347-54 |year= 1999 |pmid= 9857077 |doi= }}
*{{cite journal | author=da Silva Xavier G, Leclerc I, Salt IP, ''et al.'' |title=Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4023-8 |year= 2000 |pmid= 10760274 |doi= }}
*{{cite journal | author=Hallows KR, Raghuram V, Kemp BE, ''et al.'' |title=Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase. |journal=J. Clin. Invest. |volume=105 |issue= 12 |pages= 1711-21 |year= 2000 |pmid= 10862786 |doi= }}
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi= }}
*{{cite journal | author=Chen ZP, McConell GK, Michell BJ, ''et al.'' |title=AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation. |journal=Am. J. Physiol. Endocrinol. Metab. |volume=279 |issue= 5 |pages= E1202-6 |year= 2000 |pmid= 11052978 |doi= }}
*{{cite journal | author=Blázquez C, Geelen MJ, Velasco G, Guzmán M |title=The AMP-activated protein kinase prevents ceramide synthesis de novo and apoptosis in astrocytes. |journal=FEBS Lett. |volume=489 |issue= 2-3 |pages= 149-53 |year= 2001 |pmid= 11165240 |doi= }}
*{{cite journal | author=Diggle TA, Subkhankulova T, Lilley KS, ''et al.'' |title=Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity. |journal=Biochem. J. |volume=353 |issue= Pt 3 |pages= 621-6 |year= 2001 |pmid= 11171059 |doi= }}
*{{cite journal | author=Wang X, Li W, Williams M, ''et al.'' |title=Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. |journal=EMBO J. |volume=20 |issue= 16 |pages= 4370-9 |year= 2001 |pmid= 11500364 |doi= 10.1093/emboj/20.16.4370 }}
*{{cite journal | author=Xi X, Han J, Zhang JZ |title=Stimulation of glucose transport by AMP-activated protein kinase via activation of p38 mitogen-activated protein kinase. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 41029-34 |year= 2001 |pmid= 11546797 |doi= 10.1074/jbc.M102824200 }}
*{{cite journal | author=Fryer LG, Foufelle F, Barnes K, ''et al.'' |title=Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells. |journal=Biochem. J. |volume=363 |issue= Pt 1 |pages= 167-74 |year= 2002 |pmid= 11903059 |doi= }}
*{{cite journal | author=Yang CS, Weiner H |title=Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol. |journal=Arch. Biochem. Biophys. |volume=400 |issue= 1 |pages= 105-10 |year= 2002 |pmid= 11913976 |doi= 10.1006/abbi.2002.2778 }}
*{{cite journal | author=Bolster DR, Crozier SJ, Kimball SR, Jefferson LS |title=AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. |journal=J. Biol. Chem. |volume=277 |issue= 27 |pages= 23977-80 |year= 2002 |pmid= 11997383 |doi= 10.1074/jbc.C200171200 }}
*{{cite journal | author=Esumi H, Izuishi K, Kato K, ''et al.'' |title=Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32791-8 |year= 2002 |pmid= 12091379 |doi= 10.1074/jbc.M112270200 }}
*{{cite journal | author=Horman S, Browne G, Krause U, ''et al.'' |title=Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis. |journal=Curr. Biol. |volume=12 |issue= 16 |pages= 1419-23 |year= 2003 |pmid= 12194824 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMA6... {November 17, 2007 12:19:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:19:35 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSMA6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iru.
| PDB = {{PDB2|1iru}}
| Name = Proteasome (prosome, macropain) subunit, alpha type, 6
| HGNCid = 9535
| Symbol = PSMA6
| AltSymbols =; IOTA; MGC22756; MGC2333; MGC23846; PROS27; p27K
| OMIM = 602855
| ECnumber =
| Homologene = 2085
| MGIid = 1347006
| GeneAtlas_image1 = PBB_GE_PSMA6_208805_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5687
| Hs_Ensembl = ENSG00000100902
| Hs_RefseqProtein = NP_002782
| Hs_RefseqmRNA = NM_002791
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 34831314
| Hs_GenLoc_end = 34856431
| Hs_Uniprot = P60900
| Mm_EntrezGene = 26443
| Mm_Ensembl = ENSMUSG00000021024
| Mm_RefseqmRNA = NM_011968
| Mm_RefseqProtein = NP_036098
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 56317018
| Mm_GenLoc_end = 56336579
| Mm_Uniprot = Q0VGS3
}}
}}
'''Proteasome (prosome, macropain) subunit, alpha type, 6''', also known as '''PSMA6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMA6 proteasome (prosome, macropain) subunit, alpha type, 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5687| 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 proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure 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. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. A pseudogene has been identified on the Y chromosome.<ref name="entrez">{{cite web | title = Entrez Gene: PSMA6 proteasome (prosome, macropain) subunit, alpha type, 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5687| 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=DeMartino GN, Orth K, McCullough ML, ''et al.'' |title=The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous. |journal=Biochim. Biophys. Acta |volume=1079 |issue= 1 |pages= 29-38 |year= 1991 |pmid= 1888762 |doi= }}
*{{cite journal | author=Bey F, Silva Pereira I, Coux O, ''et al.'' |title=The prosomal RNA-binding protein p27K is a member of the alpha-type human prosomal gene family. |journal=Mol. Gen. Genet. |volume=237 |issue= 1-2 |pages= 193-205 |year= 1993 |pmid= 7681138 |doi= }}
*{{cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |doi= }}
*{{cite journal | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi= }}
*{{cite journal | author=Nederlof PM, Wang HR, Baumeister W |title=Nuclear localization signals of human and Thermoplasma proteasomal alpha subunits are functional in vitro. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 26 |pages= 12060-4 |year= 1996 |pmid= 8618844 |doi= }}
*{{cite journal | author=Bureau JP, Olink-Coux M, Brouard N, ''et al.'' |title=Characterization of prosomes in human lymphocyte subpopulations and their presence as surface antigens. |journal=Exp. Cell Res. |volume=231 |issue= 1 |pages= 50-60 |year= 1997 |pmid= 9056411 |doi= 10.1006/excr.1996.3453 }}
*{{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=Gerards WL, de Jong WW, Bloemendal H, Boelens W |title=The human proteasomal subunit HsC8 induces ring formation of other alpha-type subunits. |journal=J. Mol. Biol. |volume=275 |issue= 1 |pages= 113-21 |year= 1998 |pmid= 9451443 |doi= 10.1006/jmbi.1997.1429 }}
*{{cite journal | author=Henry L, Baz A, Château MT, ''et al.'' |title=Proteasome (prosome) subunit variations during the differentiation of myeloid U937 cells. |journal=Analytical cellular pathology : the journal of the European Society for Analytical Cellular Pathology |volume=15 |issue= 3 |pages= 131-44 |year= 1998 |pmid= 9497851 |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=Elenich LA, Nandi D, Kent AE, ''et al.'' |title=The complete primary structure of mouse 20S proteasomes. |journal=Immunogenetics |volume=49 |issue= 10 |pages= 835-42 |year= 1999 |pmid= 10436176 |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=Kleijnen MF, Shih AH, Zhou P, ''et al.'' |title=The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. |journal=Mol. Cell |volume=6 |issue= 2 |pages= 409-19 |year= 2000 |pmid= 10983987 |doi= }}
*{{cite journal | author=Feng Y, Longo DL, Ferris DK |title=Polo-like kinase interacts with proteasomes and regulates their activity. |journal=Cell Growth Differ. |volume=12 |issue= 1 |pages= 29-37 |year= 2001 |pmid= 11205743 |doi= }}
*{{cite journal | author=Engidawork E, Juranville JF, Fountoulakis M, ''et al.'' |title=Selective upregulation of the ubiquitin-proteasome proteolytic pathway proteins, proteasome zeta chain and isopeptidase T in fetal Down syndrome. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 117-30 |year= 2002 |pmid= 11771738 |doi= }}
*{{cite journal | author=Sjakste T, Sjakste N, Scherrer K |title=Exon/intron organisation of human proteasome PROS-27 K gene. |journal=DNA Seq. |volume=12 |issue= 4 |pages= 261-5 |year= 2002 |pmid= 11924531 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RBPJ... {November 17, 2007 12:11:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:12:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RBPJ_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2f8x.
| PDB = {{PDB2|2f8x}}
| Name = Recombination signal binding protein for immunoglobulin kappa J region
| HGNCid = 5724
| Symbol = RBPJ
| AltSymbols =; CBF1; IGKJRB; IGKJRB1; KBF2; MGC61669; RBP-J; RBPJK; RBPSUH; SUH; csl
| OMIM = 147183
| ECnumber =
| Homologene = 7511
| MGIid = 96522
| GeneAtlas_image1 = PBB_GE_RBPJ_211974_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000150 |text = recombinase activity}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005730 |text = nucleolus}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001837 |text = epithelial to mesenchymal transition}} {{GNF_GO|id=GO:0006310 |text = DNA recombination}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007219 |text = Notch signaling pathway}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030183 |text = B cell differentiation}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0045892 |text = negative regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3516
| Hs_Ensembl = ENSG00000168214
| Hs_RefseqProtein = NP_005340
| Hs_RefseqmRNA = NM_005349
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 25930430
| Hs_GenLoc_end = 26045851
| Hs_Uniprot = Q06330
| Mm_EntrezGene = 19664
| Mm_Ensembl = ENSMUSG00000039191
| Mm_RefseqmRNA = NM_001080927
| Mm_RefseqProtein = NP_001074396
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 53878598
| Mm_GenLoc_end = 53944383
| Mm_Uniprot = A0N920
}}
}}
'''Recombination signal binding protein for immunoglobulin kappa J region''', also known as '''RBPJ''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RBPJ recombination signal binding protein for immunoglobulin kappa J region| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3516| 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=Oka C, Kawaichi M |title=V(D)J recombination of immunoglobulin genes. |journal=Adv. Biophys. |volume=31 |issue= |pages= 163-80 |year= 1995 |pmid= 7625272 |doi= }}
*{{cite journal | author=Matsunami N, Hamaguchi Y, Yamamoto Y, ''et al.'' |title=A protein binding to the J kappa recombination sequence of immunoglobulin genes contains a sequence related to the integrase motif. |journal=Nature |volume=342 |issue= 6252 |pages= 934-7 |year= 1990 |pmid= 2556644 |doi= 10.1038/342934a0 }}
*{{cite journal | author=Tong X, Drapkin R, Yalamanchili R, ''et al.'' |title=The Epstein-Barr virus nuclear protein 2 acidic domain forms a complex with a novel cellular coactivator that can interact with TFIIE. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 4735-44 |year= 1995 |pmid= 7651391 |doi= }}
*{{cite journal | author=Amakawa R, Jing W, Ozawa K, ''et al.'' |title=Human Jk recombination signal binding protein gene (IGKJRB): comparison with its mouse homologue. |journal=Genomics |volume=17 |issue= 2 |pages= 306-15 |year= 1993 |pmid= 8406481 |doi= 10.1006/geno.1993.1326 }}
*{{cite journal | author=Zhao B, Marshall DR, Sample CE |title=A conserved domain of the Epstein-Barr virus nuclear antigens 3A and 3C binds to a discrete domain of Jkappa. |journal=J. Virol. |volume=70 |issue= 7 |pages= 4228-36 |year= 1996 |pmid= 8676443 |doi= }}
*{{cite journal | author=Tamura K, Taniguchi Y, Minoguchi S, ''et al.'' |title=Physical interaction between a novel domain of the receptor Notch and the transcription factor RBP-J kappa/Su(H). |journal=Curr. Biol. |volume=5 |issue= 12 |pages= 1416-23 |year= 1997 |pmid= 8749394 |doi= }}
*{{cite journal | author=Gress TM, Müller-Pillasch F, Geng M, ''et al.'' |title=A pancreatic cancer-specific expression profile. |journal=Oncogene |volume=13 |issue= 8 |pages= 1819-30 |year= 1996 |pmid= 8895530 |doi= }}
*{{cite journal | author=Hsieh JJ, Nofziger DE, Weinmaster G, Hayward SD |title=Epstein-Barr virus immortalization: Notch2 interacts with CBF1 and blocks differentiation. |journal=J. Virol. |volume=71 |issue= 3 |pages= 1938-45 |year= 1997 |pmid= 9032325 |doi= }}
*{{cite journal | author=Aster JC, Robertson ES, Hasserjian RP, ''et al.'' |title=Oncogenic forms of NOTCH1 lacking either the primary binding site for RBP-Jkappa or nuclear localization sequences retain the ability to associate with RBP-Jkappa and activate transcription. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11336-43 |year= 1997 |pmid= 9111040 |doi= }}
*{{cite journal | author=Tang X, Saito-Ohara F, Song J, ''et al.'' |title=Assignment of the human gene for KBF2/RBP-Jk to chromosome 9p12-13 and 9q13 by fluorescence in situ hybridization. |journal=Jpn. J. Hum. Genet. |volume=42 |issue= 2 |pages= 337-41 |year= 1997 |pmid= 9290259 |doi= }}
*{{cite journal | author=Kao HY, Ordentlich P, Koyano-Nakagawa N, ''et al.'' |title=A histone deacetylase corepressor complex regulates the Notch signal transduction pathway. |journal=Genes Dev. |volume=12 |issue= 15 |pages= 2269-77 |year= 1998 |pmid= 9694793 |doi= }}
*{{cite journal | author=Hsieh JJ, Zhou S, Chen L, ''et al.'' |title=CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 1 |pages= 23-8 |year= 1999 |pmid= 9874765 |doi= }}
*{{cite journal | author=Scanlan MJ, Gordan JD, Williamson B, ''et al.'' |title=Antigens recognized by autologous antibody in patients with renal-cell carcinoma. |journal=Int. J. Cancer |volume=83 |issue= 4 |pages= 456-64 |year= 1999 |pmid= 10508479 |doi= }}
*{{cite journal | author=Callahan J, Aster J, Sklar J, ''et al.'' |title=Intracellular forms of human NOTCH1 interact at distinctly different levels with RBP-jkappa in human B and T cells. |journal=Leukemia |volume=14 |issue= 1 |pages= 84-92 |year= 2000 |pmid= 10637481 |doi= }}
*{{cite journal | author=Smith PR, de Jesus O, Turner D, ''et al.'' |title=Structure and coding content of CST (BART) family RNAs of Epstein-Barr virus. |journal=J. Virol. |volume=74 |issue= 7 |pages= 3082-92 |year= 2000 |pmid= 10708423 |doi= }}
*{{cite journal | author=Zhou S, Fujimuro M, Hsieh JJ, ''et al.'' |title=SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function. |journal=Mol. Cell. Biol. |volume=20 |issue= 7 |pages= 2400-10 |year= 2000 |pmid= 10713164 |doi= }}
*{{cite journal | author=Kurooka H, Honjo T |title=Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 17211-20 |year= 2000 |pmid= 10747963 |doi= 10.1074/jbc.M000909200 }}
*{{cite journal | author=Beatus P, Lundkvist J, Oberg C, ''et al.'' |title=The origin of the ankyrin repeat region in Notch intracellular domains is critical for regulation of HES promoter activity. |journal=Mech. Dev. |volume=104 |issue= 1-2 |pages= 3-20 |year= 2001 |pmid= 11404076 |doi= }}
*{{cite journal | author=Zhou S, Hayward SD |title=Nuclear localization of CBF1 is regulated by interactions with the SMRT corepressor complex. |journal=Mol. Cell. Biol. |volume=21 |issue= 18 |pages= 6222-32 |year= 2001 |pmid= 11509665 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
