INFO: Beginning work on CDK9... {November 1, 2007 11:06:28 AM PDT}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 11:07:13 AM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cyclin-dependent kinase 9 (CDC2-related kinase)
| HGNCid = 1780
| Symbol = CDK9
| AltSymbols =; C-2k; CDC2L4; PITALRE; TAK
| OMIM = 603251
| ECnumber =
| Homologene = 55566
| MGIid = 1328368
| GeneAtlas_image1 = PBB_GE_CDK9_203198_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004693 |text = cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0017069 |text = snRNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0008023 |text = transcription elongation factor complex}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006367 |text = transcription initiation from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006368 |text = RNA elongation from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1025
| Hs_Ensembl = ENSG00000136807
| Hs_RefseqProtein = NP_001252
| Hs_RefseqmRNA = NM_001261
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 129587898
| Hs_GenLoc_end = 129592887
| Hs_Uniprot = P50750
| Mm_EntrezGene = 107951
| Mm_Ensembl = ENSMUSG00000009555
| Mm_RefseqmRNA = NM_130860
| Mm_RefseqProtein = NP_570930
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 32529447
| Mm_GenLoc_end = 32534794
| Mm_Uniprot = Q99J95
}}
}}
'''Cyclin-dependent kinase 9 (CDC2-related kinase)''', also known as '''CDK9''', is a human [[gene]].
<!-- 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 cyclin-dependent protein kinase (CDK) family. CDK family members are highly similar to the gene products of S. cerevisiae cdc28, and S. pombe cdc2, and known as important cell cycle regulators. This kinase was found to be a component of the multiprotein complex TAK/P-TEFb, which is an elongation factor for RNA polymerase II-directed transcription and functions by phosphorylating the C-terminal domain of the largest subunit of RNA polymerase II. This protein forms a complex with and is regulated by its regulatory subunit cyclin T or cyclin K. HIV-1 Tat protein was found to interact with this protein and cyclin T, which suggested a possible involvement of this protein in AIDS.<ref>{{cite web | title = Entrez Gene: CDK9 cyclin-dependent kinase 9 (CDC2-related kinase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1025| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24-7 |year= 1998 |pmid= 9570510 |doi= }}
*{{cite journal | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447-9 |year= 1998 |pmid= 9651670 |doi= }}
*{{cite journal | author=Romano G, Kasten M, De Falco G, ''et al.'' |title=Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression. |journal=J. Cell. Biochem. |volume=75 |issue= 3 |pages= 357-68 |year= 2000 |pmid= 10536359 |doi= }}
*{{cite journal | author=Marcello A, Zoppé M, Giacca M |title=Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. |journal=IUBMB Life |volume=51 |issue= 3 |pages= 175-81 |year= 2002 |pmid= 11547919 |doi= }}
*{{cite journal | author=Huigen MC, Kamp W, Nottet HS |title=Multiple effects of HIV-1 trans-activator protein on the pathogenesis of HIV-1 infection. |journal=Eur. J. Clin. Invest. |volume=34 |issue= 1 |pages= 57-66 |year= 2004 |pmid= 14984439 |doi= }}
*{{cite journal | author=Rice AP, Herrmann CH |title=Regulation of TAK/P-TEFb in CD4+ T lymphocytes and macrophages. |journal=Curr. HIV Res. |volume=1 |issue= 4 |pages= 395-404 |year= 2004 |pmid= 15049426 |doi= }}
*{{cite journal | author=Minghetti L, Visentin S, Patrizio M, ''et al.'' |title=Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions. |journal=Neurochem. Res. |volume=29 |issue= 5 |pages= 965-78 |year= 2004 |pmid= 15139295 |doi= }}
*{{cite journal | author=Liou LY, Herrmann CH, Rice AP |title=HIV-1 infection and regulation of Tat function in macrophages. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 9 |pages= 1767-75 |year= 2005 |pmid= 15183343 |doi= 10.1016/j.biocel.2004.02.018 }}
*{{cite journal | author=Pugliese A, Vidotto V, Beltramo T, ''et al.'' |title=A review of HIV-1 Tat protein biological effects. |journal=Cell Biochem. Funct. |volume=23 |issue= 4 |pages= 223-7 |year= 2005 |pmid= 15473004 |doi= 10.1002/cbf.1147 }}
*{{cite journal | author=Bannwarth S, Gatignol A |title=HIV-1 TAR RNA: the target of molecular interactions between the virus and its host. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 61-71 |year= 2005 |pmid= 15638724 |doi= }}
*{{cite journal | author=Gibellini D, Vitone F, Schiavone P, Re MC |title=HIV-1 tat protein and cell proliferation and survival: a brief review. |journal=New Microbiol. |volume=28 |issue= 2 |pages= 95-109 |year= 2005 |pmid= 16035254 |doi= }}
*{{cite journal | author=Peruzzi F |title=The multiple functions of HIV-1 Tat: proliferation versus apoptosis. |journal=Front. Biosci. |volume=11 |issue= |pages= 708-17 |year= 2006 |pmid= 16146763 |doi= }}
}}
{{refend}}
{{protein-stub}}
INFO: Beginning work on HD... {November 1, 2007 11:17:34 AM PDT}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 11:18:07 AM PDT} HD (gene) is the current page for the gene , but I have requested it moved to Huntingtin which is where the bot was linked to originally.Leevanjackson (talk) 15:38, 14 January 2008 (UTC)
<!-- 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 = Huntingtin (Huntington disease)
| HGNCid = 4851
| Symbol = HD
| AltSymbols =; HTT; IT15
| OMIM = 143100
| ECnumber =
| Homologene = 1593
| MGIid = 96067
| GeneAtlas_image1 = PBB_GE_HD_202389_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008017 |text = microtubule binding}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007610 |text = behavior}} {{GNF_GO|id=GO:0009405 |text = pathogenesis}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3064
| Hs_Ensembl = ENSG00000197386
| Hs_RefseqProtein = NP_002102
| Hs_RefseqmRNA = NM_002111
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 3046206
| Hs_GenLoc_end = 3215484
| Hs_Uniprot = P42858
| Mm_EntrezGene = 15194
| Mm_Ensembl = ENSMUSG00000029104
| Mm_RefseqmRNA = NM_010414
| Mm_RefseqProtein = NP_034544
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 35078597
| Mm_GenLoc_end = 35226253
| Mm_Uniprot = P42859
}}
}}
'''Huntingtin (Huntington disease)''', also known as '''HD''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Huntingtin is a disease gene linked to Huntington's disease, a neurodegenerative disorder characterized by loss of striatal neurons. This is thought to be caused by an expanded, unstable trinucleotide repeat in the huntingtin gene, which translates as a polyglutamine repeat in the protein product. A fairly broad range in the number of trinucleotide repeats has been identified in normal controls, and repeat numbers in excess of 40 have been described as pathological. The huntingtin locus is large, spanning 180 kb and consisting of 67 exons. The huntingtin gene is widely expressed and is required for normal development. It is expressed as 2 alternatively polyadenylated forms displaying different relative abundance in various fetal and adult tissues. The larger transcript is approximately 13.7 kb and is expressed predominantly in adult and fetal brain whereas the smaller transcript of approximately 10.3 kb is more widely expressed. The genetic defect leading to Huntington's disease may not necessarily eliminate transcription, but may confer a new property on the mRNA or alter the function of the protein. One candidate is the huntingtin-associated protein-1, highly expressed in brain, which has increased affinity for huntingtin protein with expanded polyglutamine repeats. This gene contains an upstream open reading frame in the 5' UTR that inhibits expression of the huntingtin gene product through translational repression.<ref>{{cite web | title = Entrez Gene: HD huntingtin (Huntington disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3064| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=MacDonald ME, Novelletto A, Lin C, ''et al.'' |title=The Huntington's disease candidate region exhibits many different haplotypes. |journal=Nat. Genet. |volume=1 |issue= 2 |pages= 99-103 |year= 1993 |pmid= 1302016 |doi= 10.1038/ng0592-99 }}
*{{cite journal | author=Jones AL |title=The localization and interactions of huntingtin. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=354 |issue= 1386 |pages= 1021-7 |year= 1999 |pmid= 10434301 |doi= 10.1098/rstb.1999.0454 }}
*{{cite journal | author=Young AB |title=Huntingtin in health and disease. |journal=J. Clin. Invest. |volume=111 |issue= 3 |pages= 299-302 |year= 2003 |pmid= 12569151 |doi= }}
*{{cite journal | author=Rangone H, Humbert S, Saudou F |title=Huntington's disease: how does huntingtin, an anti-apoptotic protein, become toxic? |journal=Pathol. Biol. |volume=52 |issue= 6 |pages= 338-42 |year= 2004 |pmid= 15261377 |doi= 10.1016/j.patbio.2003.06.004 }}
*{{cite journal | author=Li SH, Li XJ |title=Huntingtin and its role in neuronal degeneration. |journal=The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry |volume=10 |issue= 5 |pages= 467-75 |year= 2005 |pmid= 15359012 |doi= 10.1177/1073858404266777 }}
*{{cite journal | author=Myers RH |title=Huntington's disease genetics. |journal=NeuroRx : the journal of the American Society for Experimental NeuroTherapeutics |volume=1 |issue= 2 |pages= 255-62 |year= 2005 |pmid= 15717026 |doi= }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 11:24:29 AM PDT}
<!-- 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_MECP2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qk9.
| PDB = {{PDB2|1qk9}}, {{PDB2|1ub1}}
| Name = Methyl CpG binding protein 2 (Rett syndrome)
| HGNCid = 6990
| Symbol = MECP2
| AltSymbols =; RTS; AUTSX3; DKFZp686A24160; MRX16; MRX79; PPMX; RTT
| OMIM = 300005
| ECnumber =
| Homologene = 3657
| MGIid = 99918
| GeneAtlas_image1 = PBB_GE_MECP2_202616_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MECP2_202617_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_MECP2_202618_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}}
| Component = {{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:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4204
| Hs_Ensembl = ENSG00000169057
| Hs_RefseqProtein = NP_004983
| Hs_RefseqmRNA = NM_004992
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 152940218
| Hs_GenLoc_end = 153016406
| Hs_Uniprot = P51608
| Mm_EntrezGene = 17257
| Mm_Ensembl = ENSMUSG00000031393
| Mm_RefseqmRNA = NM_001081979
| Mm_RefseqProtein = NP_001075448
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 70288072
| Mm_GenLoc_end = 70338332
| Mm_Uniprot = Q3TYG1
}}
}}
'''Methyl CpG binding protein 2 (Rett syndrome)''', also known as '''MECP2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1 and MBD2 can also repress transcription from methylated gene promoters. In contrast to other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is dispensible in stem cells, but is essential for embryonic development. MECP2 gene mutations are the cause of some cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common causes of mental retardation in females.<ref>{{cite web | title = Entrez Gene: MECP2 methyl CpG binding protein 2 (Rett syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4204| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Shahbazian MD, Zoghbi HY |title=Rett syndrome and MeCP2: linking epigenetics and neuronal function. |journal=Am. J. Hum. Genet. |volume=71 |issue= 6 |pages= 1259-72 |year= 2003 |pmid= 12442230 |doi= }}
*{{cite journal | author=Moog U, Smeets EE, van Roozendaal KE, ''et al.'' |title=Neurodevelopmental disorders in males related to the gene causing Rett syndrome in females (MECP2). |journal=Eur. J. Paediatr. Neurol. |volume=7 |issue= 1 |pages= 5-12 |year= 2003 |pmid= 12615169 |doi= }}
*{{cite journal | author=Miltenberger-Miltenyi G, Laccone F |title=Mutations and polymorphisms in the human methyl CpG-binding protein MECP2. |journal=Hum. Mutat. |volume=22 |issue= 2 |pages= 107-15 |year= 2004 |pmid= 12872250 |doi= 10.1002/humu.10243 }}
*{{cite journal | author=Weaving LS, Ellaway CJ, Gécz J, Christodoulou J |title=Rett syndrome: clinical review and genetic update. |journal=J. Med. Genet. |volume=42 |issue= 1 |pages= 1-7 |year= 2006 |pmid= 15635068 |doi= 10.1136/jmg.2004.027730 }}
*{{cite journal | author=Caballero IM, Hendrich B |title=MeCP2 in neurons: closing in on the causes of Rett syndrome. |journal=Hum. Mol. Genet. |volume=14 Spec No 1 |issue= |pages= R19-26 |year= 2005 |pmid= 15809268 |doi= 10.1093/hmg/ddi102 }}
*{{cite journal | author=Bapat S, Galande S |title=Association by guilt: identification of DLX5 as a target for MeCP2 provides a molecular link between genomic imprinting and Rett syndrome. |journal=Bioessays |volume=27 |issue= 7 |pages= 676-80 |year= 2005 |pmid= 15954098 |doi= 10.1002/bies.20266 }}
*{{cite journal | author=Zlatanova J |title=MeCP2: the chromatin connection and beyond. |journal=Biochem. Cell Biol. |volume=83 |issue= 3 |pages= 251-62 |year= 2005 |pmid= 15959553 |doi= 10.1139/o05-048 }}
*{{cite journal | author=Kaufmann WE, Johnston MV, Blue ME |title=MeCP2 expression and function during brain development: implications for Rett syndrome's pathogenesis and clinical evolution. |journal=Brain Dev. |volume=27 Suppl 1 |issue= |pages= S77-S87 |year= 2006 |pmid= 16182491 |doi= 10.1016/j.braindev.2004.10.008 }}
*{{cite journal | author=Armstrong DD |title=Can we relate MeCP2 deficiency to the structural and chemical abnormalities in the Rett brain? |journal=Brain Dev. |volume=27 Suppl 1 |issue= |pages= S72-S76 |year= 2006 |pmid= 16182497 |doi= 10.1016/j.braindev.2004.10.009 }}
*{{cite journal | author=Santos M, Coelho PA, Maciel P |title=Chromatin remodeling and neuronal function: exciting links. |journal=Genes Brain Behav. |volume=5 Suppl 2 |issue= |pages= 80-91 |year= 2006 |pmid= 16681803 |doi= 10.1111/j.1601-183X.2006.00227.x }}
*{{cite journal | author=Bienvenu T, Chelly J |title=Molecular genetics of Rett syndrome: when DNA methylation goes unrecognized. |journal=Nat. Rev. Genet. |volume=7 |issue= 6 |pages= 415-26 |year= 2006 |pmid= 16708070 |doi= 10.1038/nrg1878 }}
*{{cite journal | author=Francke U |title=Mechanisms of disease: neurogenetics of MeCP2 deficiency. |journal=Nature clinical practice. Neurology |volume=2 |issue= 4 |pages= 212-21 |year= 2007 |pmid= 16932552 |doi= 10.1038/ncpneuro0148 }}
}}
{{refend}}
{{protein-stub}}
INFO: Beginning work on PML... {November 1, 2007 11:32:05 AM PDT}
UPLOAD: Added new Image to wiki: {November 1, 2007 11:32:20 AM PDT}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 11:32:37 AM PDT}
<!-- 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_PML_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bor.
| PDB = {{PDB2|1bor}}
| Name = Promyelocytic leukemia
| HGNCid = 9113
| Symbol = PML
| AltSymbols =; MYL; PP8675; RNF71; TRIM19
| OMIM = 102578
| ECnumber =
| Homologene = 13245
| MGIid = 104662
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005626 |text = insoluble fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0016363 |text = nuclear matrix}} {{GNF_GO|id=GO:0016605 |text = PML body}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006977 |text = DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007569 |text = cell aging}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0030578 |text = PML body organization and biogenesis}} {{GNF_GO|id=GO:0031065 |text = positive regulation of histone deacetylation}} {{GNF_GO|id=GO:0042771 |text = DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5371
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001132060
| Hs_RefseqmRNA = XM_001132060
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 18854
| Mm_Ensembl = ENSMUSG00000036986
| Mm_RefseqmRNA = NM_008884
| Mm_RefseqProtein = NP_032910
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 58016222
| Mm_GenLoc_end = 58047923
| Mm_Uniprot = O89066
}}
}}
'''Promyelocytic leukemia''', also known as '''PML''', is a human [[gene]].
<!-- 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 tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This phosphoprotein localizes to nuclear bodies where it functions as a transcription factor and tumor suppressor. Its expression is cell-cycle related and it regulates the p53 response to oncogenic signals. The gene is often involved in the translocation with the retinoic acid receptor alpha gene associated with acute promyelocytic leukemia (APL). Extensive alternative splicing of this gene results in several variations of the protein's central and C-terminal regions; all variants encode the same N-terminus. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref>{{cite web | title = Entrez Gene: PML promyelocytic leukemia| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5371| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zhong S, Salomoni P, Pandolfi PP |title=The transcriptional role of PML and the nuclear body. |journal=Nat. Cell Biol. |volume=2 |issue= 5 |pages= E85-90 |year= 2000 |pmid= 10806494 |doi= 10.1038/35010583 }}
*{{cite journal | author=Jensen K, Shiels C, Freemont PS |title=PML protein isoforms and the RBCC/TRIM motif. |journal=Oncogene |volume=20 |issue= 49 |pages= 7223-33 |year= 2001 |pmid= 11704850 |doi= 10.1038/sj.onc.1204765 }}
*{{cite journal | author=Pearson M, Pelicci PG |title=PML interaction with p53 and its role in apoptosis and replicative senescence. |journal=Oncogene |volume=20 |issue= 49 |pages= 7250-6 |year= 2001 |pmid= 11704853 |doi= 10.1038/sj.onc.1204856 }}
*{{cite journal | author=Salomoni P, Pandolfi PP |title=The role of PML in tumor suppression. |journal=Cell |volume=108 |issue= 2 |pages= 165-70 |year= 2002 |pmid= 11832207 |doi= }}
*{{cite journal | author=Combes R, Balls M, Bansil L, ''et al.'' |title=An assessment of progress in the use of alternatives in toxicity testing since the publication of the report of the second FRAME Toxicity Committee (1991). |journal=Alternatives to laboratory animals : ATLA |volume=30 |issue= 4 |pages= 365-406 |year= 2002 |pmid= 12234245 |doi= }}
*{{cite journal | author=Bernardi R, Pandolfi PP |title=Role of PML and the PML-nuclear body in the control of programmed cell death. |journal=Oncogene |volume=22 |issue= 56 |pages= 9048-57 |year= 2004 |pmid= 14663483 |doi= 10.1038/sj.onc.1207106 }}
}}
{{refend}}
{{protein-stub}}
INFO: Beginning work on PRKCZ... {November 1, 2007 11:33:52 AM PDT}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 11:34:28 AM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Protein kinase C, zeta
| HGNCid = 9412
| Symbol = PRKCZ
| AltSymbols =; PKC2
| OMIM = 176982
| ECnumber =
| Homologene = 55681
| MGIid = 97602
| GeneAtlas_image1 = PBB_GE_PRKCZ_202178_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004700 |text = atypical protein kinase C activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005923 |text = tight junction}} {{GNF_GO|id=GO:0005938 |text = cell cortex}} {{GNF_GO|id=GO:0045179 |text = apical cortex}}
| Process = {{GNF_GO|id=GO:0000226 |text = microtubule cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5590
| Hs_Ensembl = ENSG00000067606
| Hs_RefseqProtein = NP_001028753
| Hs_RefseqmRNA = NM_001033581
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 1971769
| Hs_GenLoc_end = 2106694
| Hs_Uniprot = Q05513
| Mm_EntrezGene = 18762
| Mm_Ensembl = ENSMUSG00000029053
| Mm_RefseqmRNA = NM_001039079
| Mm_RefseqProtein = NP_001034168
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 154103920
| Mm_GenLoc_end = 154205191
| Mm_Uniprot = Q3UHM5
}}
}}
'''Protein kinase C, zeta''', also known as '''PRKCZ''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Protein kinase C (PKC) zeta is a member of the PKC family of serine/threonine kinases which are involved in a variety of cellular processes such as proliferation, differentiation and secretion. Unlike the classical PKC isoenzymes which are calcium-dependent, PKC zeta exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors and cannot be activated by phorbol ester. Unlike the classical PKC isoenzymes, it has only a single zinc finger module. These structural and biochemical properties indicate that the zeta subspecies is related to, but distinct from other isoenzymes of PKC. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref>{{cite web | title = Entrez Gene: PRKCZ protein kinase C, zeta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5590| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Slater SJ, Ho C, Stubbs CD |title=The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions. |journal=Chem. Phys. Lipids |volume=116 |issue= 1-2 |pages= 75-91 |year= 2003 |pmid= 12093536 |doi= }}
*{{cite journal | author=Carter CA, Kane CJ |title=Therapeutic potential of natural compounds that regulate the activity of protein kinase C. |journal=Curr. Med. Chem. |volume=11 |issue= 21 |pages= 2883-902 |year= 2005 |pmid= 15544481 |doi= }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 11:22:41 AM PDT}
<!-- 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
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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_SMAD2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dev.
| PDB = {{PDB2|1dev}}, {{PDB2|1khx}}, {{PDB2|1mjs}}, {{PDB2|1mk2}}, {{PDB2|1u7f}}, {{PDB2|1u7v}}
| Name = SMAD family member 2
| HGNCid = 6768
| Symbol = SMAD2
| AltSymbols =; JV18; JV18-1; MADH2; MADR2; MGC22139; MGC34440; hMAD-2; hSMAD2
| OMIM = 601366
| ECnumber =
| Homologene = 21197
| MGIid = 108051
| GeneAtlas_image1 = PBB_GE_SMAD2_203075_at_tn.png
| GeneAtlas_image2 = PBB_GE_SMAD2_203076_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SMAD2_203077_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003690 |text = double-stranded DNA binding}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0001707 |text = mesoderm formation}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0007179 |text = transforming growth factor beta receptor signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0009952 |text = anterior/posterior pattern formation}} {{GNF_GO|id=GO:0045165 |text = cell fate commitment}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0048340 |text = paraxial mesoderm morphogenesis}} {{GNF_GO|id=GO:0051098 |text = regulation of binding}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4087
| Hs_Ensembl = ENSG00000175387
| Hs_RefseqProtein = NP_001003652
| Hs_RefseqmRNA = NM_001003652
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 43618435
| Hs_GenLoc_end = 43711221
| Hs_Uniprot = Q15796
| Mm_EntrezGene = 17126
| Mm_Ensembl = ENSMUSG00000024563
| Mm_RefseqmRNA = NM_010754
| Mm_RefseqProtein = NP_034884
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 76367274
| Mm_GenLoc_end = 76431096
| Mm_Uniprot = Q8C2P1
}}
}}
'''SMAD family member 2''', also known as '''SMAD2''', is a human [[gene]].
<!-- 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 SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signal of the transforming growth factor (TGF)-beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants encoding the same protein have been observed.<ref>{{cite web | title = Entrez Gene: SMAD2 SMAD family member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4087| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wrana JL |title=TGF-beta receptors and signalling mechanisms. |journal=Mineral and electrolyte metabolism |volume=24 |issue= 2-3 |pages= 120-30 |year= 1998 |pmid= 9525694 |doi= }}
*{{cite journal | author=Massagué J |title=TGF-beta signal transduction. |journal=Annu. Rev. Biochem. |volume=67 |issue= |pages= 753-91 |year= 1998 |pmid= 9759503 |doi= 10.1146/annurev.biochem.67.1.753 }}
*{{cite journal | author=Verschueren K, Huylebroeck D |title=Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells. |journal=Cytokine Growth Factor Rev. |volume=10 |issue= 3-4 |pages= 187-99 |year= 2000 |pmid= 10647776 |doi= }}
*{{cite journal | author=Wrana JL, Attisano L |title=The Smad pathway. |journal=Cytokine Growth Factor Rev. |volume=11 |issue= 1-2 |pages= 5-13 |year= 2000 |pmid= 10708948 |doi= }}
*{{cite journal | author=Miyazono K |title=TGF-beta signaling by Smad proteins. |journal=Cytokine Growth Factor Rev. |volume=11 |issue= 1-2 |pages= 15-22 |year= 2000 |pmid= 10708949 |doi= }}
*{{cite journal | author=Zannis VI, Kan HY, Kritis A, ''et al.'' |title=Transcriptional regulation of the human apolipoprotein genes. |journal=Front. Biosci. |volume=6 |issue= |pages= D456-504 |year= 2001 |pmid= 11229886 |doi= }}
}}
{{refend}}
{{protein-stub}}
AMBIGUITY: Did not locate an acceptable page to update. {November 1, 2007 11:36:23 AM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TBP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c9b.
| PDB = {{PDB2|1c9b}}, {{PDB2|1cdw}}, {{PDB2|1jfi}}, {{PDB2|1nvp}}, {{PDB2|1tgh}}
| Name = TATA box binding protein
| HGNCid = 11588
| Symbol = TBP
| AltSymbols =; GTF2D; GTF2D1; MGC117320; MGC126054; MGC126055; SCA17; TFIID
| OMIM = 600075
| ECnumber =
| Homologene = 2404
| MGIid = 101838
| GeneAtlas_image1 = PBB_GE_TBP_203135_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005669 |text = transcription factor TFIID complex}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006367 |text = transcription initiation from RNA polymerase II promoter}} {{GNF_GO|id=GO:0008219 |text = cell death}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6908
| Hs_Ensembl = ENSG00000112592
| Hs_RefseqProtein = NP_003185
| Hs_RefseqmRNA = NM_003194
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 170705390
| Hs_GenLoc_end = 170723871
| Hs_Uniprot = P20226
| Mm_EntrezGene = 21374
| Mm_Ensembl = ENSMUSG00000014767
| Mm_RefseqmRNA = NM_013684
| Mm_RefseqProtein = NP_038712
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 15204851
| Mm_GenLoc_end = 15222390
| Mm_Uniprot = Q6LEM2
}}
}}
'''TATA box binding protein''', also known as '''TBP''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes TBP, the TATA-binding protein. A distinctive feature of TBP is a long string of glutamines in the N-terminal. This region of the protein modulates the DNA binding activity of the C terminus, and modulation of DNA binding affects the rate of transcription complex formation and initiation of transcription. Mutations that expand the number of CAG repeats encoding this polyglutamine tract, and thus increase the length of the polyglutamine string, are associated with spinocerebellar ataxia 17, a neurodegenerative disorder classified as a polyglutamine disease.<ref>{{cite web | title = Entrez Gene: TBP TATA box binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6908| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}