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Showing Protein Zinc finger and BTB domain-containing protein 7A (HMDBP14488)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14488
Secondary Accession Numbers None
Name Zinc finger and BTB domain-containing protein 7A
Synonyms
  1. Factor binding IST protein 1
  2. Factor that binds to inducer of short transcripts protein 1
  3. HIV-1 1st-binding protein 1
  4. Leukemia/lymphoma-related factor
  5. POZ and Krueppel erythroid myeloid ontogenic factor
  6. TTF-I-interacting peptide 21
  7. Zinc finger protein 857A
  8. FBI-1
  9. POK erythroid myeloid ontogenic factor
  10. Pokemon
  11. Pokemon 1
  12. TIP21
Gene Name ZBTB7A
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Transcription factor that represses the transcription of a wide range of genes involved in cell proliferation and differentiation (PubMed:14701838, PubMed:17595526, PubMed:20812024, PubMed:25514493, PubMed:26455326, PubMed:26816381). Directly and specifically binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses transcription both by regulating the organization of chromatin and through the direct recruitment of transcription factors to gene regulatory regions (PubMed:12004059, PubMed:17595526, PubMed:20812024, PubMed:25514493, PubMed:26816381). Negatively regulates SMAD4 transcriptional activity in the TGF-beta signaling pathway through these two mechanisms (PubMed:25514493). That is, recruits the chromatin regulator HDAC1 to the SMAD4-DNA complex and in parallel prevents the recruitment of the transcriptional activators CREBBP and EP300 (PubMed:25514493). Collaborates with transcription factors like RELA to modify the accessibility of gene transcription regulatory regions to secondary transcription factors (By similarity). Also directly interacts with transcription factors like SP1 to prevent their binding to DNA (PubMed:12004059). Functions as an androgen receptor/AR transcriptional corepressor by recruiting NCOR1 and NCOR2 to the androgen response elements/ARE on target genes (PubMed:20812024). Thereby, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Involved in the switch between fetal and adult globin expression during erythroid cells maturation (PubMed:26816381). Through its interaction with the NuRD complex regulates chromatin at the fetal globin genes to repress their transcription (PubMed:26816381). Specifically represses the transcription of the tumor suppressor ARF isoform from the CDKN2A gene (By similarity). Efficiently abrogates E2F1-dependent CDKN2A transactivation (By similarity). Regulates chondrogenesis through the transcriptional repression of specific genes via a mechanism that also requires histone deacetylation (By similarity). Regulates cell proliferation through the transcriptional regulation of genes involved in glycolysis (PubMed:26455326). Involved in adipogenesis through the regulation of genes involved in adipocyte differentiation (PubMed:14701838). Plays a key role in the differentiation of lymphoid progenitors into B and T lineages (By similarity). Promotes differentiation towards the B lineage by inhibiting the T-cell instructive Notch signaling pathway through the specific transcriptional repression of Notch downstream target genes (By similarity). Also regulates osteoclast differentiation (By similarity). May also play a role, independently of its transcriptional activity, in double-strand break repair via classical non-homologous end joining/cNHEJ (By similarity). Recruited to double-strand break sites on damage DNA, interacts with the DNA-dependent protein kinase complex and directly regulates its stability and activity in DNA repair (By similarity). May also modulate the splicing activity of KHDRBS1 toward BCL2L1 in a mechanism which is histone deacetylase-dependent and thereby negatively regulates the pro-apoptotic effect of KHDRBS1 (PubMed:24514149).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
fat cell differentiation
chromatin organization
regulation of glycolysis
double-strand break repair via classical nonhomologous end joining
regulation of transcription regulatory region DNA binding
B cell differentiation
erythrocyte maturation
chromatin remodeling
regulation of transcription from RNA polymerase II promoter
negative regulation of transcription, DNA-dependent
regulation of alternative mRNA splicing, via spliceosome
negative regulation of transcription from RNA polymerase II promoter
regulation of apoptotic process
negative regulation of Notch signaling pathway
negative regulation of transforming growth factor beta receptor signaling pathway
positive regulation of NF-kappaB transcription factor activity
transcription, DNA-dependent
regulation of sequence-specific DNA binding transcription factor activity
negative regulation of androgen receptor signaling pathway
protein localization to nucleus
Cellular Component
site of double-strand break
cytoplasm
nucleus
DNA-dependent protein kinase complex
Molecular Function
metal ion binding
DNA-binding transcription repressor activity, RNA polymerase II-specific
transcription corepressor binding
sequence-specific DNA binding transcription factor activity
histone acetyltransferase binding
androgen receptor binding
activating transcription factor binding
DNA-binding transcription factor activity, RNA polymerase II-specific
RNA polymerase II core promoter proximal region sequence-specific DNA binding
sequence-specific double-stranded DNA binding
DNA binding
SMAD binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 584
Molecular Weight 61438.505
Theoretical pI 5.183
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID O95365
UniProtKB/Swiss-Prot Entry Name ZBT7A_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  5. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26. [PubMed:18220336 ]
  7. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [PubMed:20068231 ]
  8. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [PubMed:23186163 ]
  9. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569 ]
  10. Hendriks IA, Lyon D, Young C, Jensen LJ, Vertegaal AC, Nielsen ML: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. Nat Struct Mol Biol. 2017 Mar;24(3):325-336. doi: 10.1038/nsmb.3366. Epub 2017 Jan 23. [PubMed:28112733 ]
  11. Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC: Uncovering global SUMOylation signaling networks in a site-specific manner. Nat Struct Mol Biol. 2014 Oct;21(10):927-36. doi: 10.1038/nsmb.2890. Epub 2014 Sep 14. [PubMed:25218447 ]
  12. Impens F, Radoshevich L, Cossart P, Ribet D: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. Proc Natl Acad Sci U S A. 2014 Aug 26;111(34):12432-7. doi: 10.1073/pnas.1413825111. Epub 2014 Aug 11. [PubMed:25114211 ]
  13. Yang Y, Cui J, Xue F, Zhang C, Mei Z, Wang Y, Bi M, Shan D, Meredith A, Li H, Xu ZQ: Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced transcriptional responses. Biochim Biophys Acta. 2015 Mar;1849(3):270-81. doi: 10.1016/j.bbagrm.2014.12.008. Epub 2014 Dec 13. [PubMed:25514493 ]
  14. Morrison DJ, Pendergrast PS, Stavropoulos P, Colmenares SU, Kobayashi R, Hernandez N: FBI-1, a factor that binds to the HIV-1 inducer of short transcripts (IST), is a POZ domain protein. Nucleic Acids Res. 1999 Mar 1;27(5):1251-62. doi: 10.1093/nar/27.5.1251. [PubMed:9973611 ]
  15. Davies JM, Hawe N, Kabarowski J, Huang QH, Zhu J, Brand NJ, Leprince D, Dhordain P, Cook M, Morriss-Kay G, Zelent A: Novel BTB/POZ domain zinc-finger protein, LRF, is a potential target of the LAZ-3/BCL-6 oncogene. Oncogene. 1999 Jan 14;18(2):365-75. doi: 10.1038/sj.onc.1202332. [PubMed:9927193 ]
  16. Lee DK, Suh D, Edenberg HJ, Hur MW: POZ domain transcription factor, FBI-1, represses transcription of ADH5/FDH by interacting with the zinc finger and interfering with DNA binding activity of Sp1. J Biol Chem. 2002 Jul 26;277(30):26761-8. doi: 10.1074/jbc.M202078200. Epub 2002 May 9. [PubMed:12004059 ]
  17. Laudes M, Christodoulides C, Sewter C, Rochford JJ, Considine RV, Sethi JK, Vidal-Puig A, O'Rahilly S: Role of the POZ zinc finger transcription factor FBI-1 in human and murine adipogenesis. J Biol Chem. 2004 Mar 19;279(12):11711-8. doi: 10.1074/jbc.M310240200. Epub 2003 Dec 30. [PubMed:14701838 ]
  18. Maeda T, Hobbs RM, Merghoub T, Guernah I, Zelent A, Cordon-Cardo C, Teruya-Feldstein J, Pandolfi PP: Role of the proto-oncogene Pokemon in cellular transformation and ARF repression. Nature. 2005 Jan 20;433(7023):278-85. doi: 10.1038/nature03203. [PubMed:15662416 ]
  19. Roh HE, Lee MN, Jeon BN, Choi WI, Kim YJ, Yu MY, Hur MW: Regulation of pokemon 1 activity by sumoylation. Cell Physiol Biochem. 2007;20(1-4):167-80. doi: 10.1159/000104164. [PubMed:17595526 ]
  20. Cui J, Yang Y, Zhang C, Hu P, Kan W, Bai X, Liu X, Song H: FBI-1 functions as a novel AR co-repressor in prostate cancer cells. Cell Mol Life Sci. 2011 Mar;68(6):1091-103. doi: 10.1007/s00018-010-0511-7. Epub 2010 Sep 2. [PubMed:20812024 ]
  21. Bielli P, Busa R, Di Stasi SM, Munoz MJ, Botti F, Kornblihtt AR, Sette C: The transcription factor FBI-1 inhibits SAM68-mediated BCL-X alternative splicing and apoptosis. EMBO Rep. 2014 Apr;15(4):419-27. doi: 10.1002/embr.201338241. Epub 2014 Feb 10. [PubMed:24514149 ]
  22. Liu XS, Chandramouly G, Rass E, Guan Y, Wang G, Hobbs RM, Rajendran A, Xie A, Shah JV, Davis AJ, Scully R, Lunardi A, Pandolfi PP: LRF maintains genome integrity by regulating the non-homologous end joining pathway of DNA repair. Nat Commun. 2015 Oct 8;6:8325. doi: 10.1038/ncomms9325. [PubMed:26446488 ]
  23. Liu XS, Liu Z, Gerarduzzi C, Choi DE, Ganapathy S, Pandolfi PP, Yuan ZM: Somatic human ZBTB7A zinc finger mutations promote cancer progression. Oncogene. 2016 Jun 9;35(23):3071-8. doi: 10.1038/onc.2015.371. Epub 2015 Oct 12. [PubMed:26455326 ]
  24. Masuda T, Wang X, Maeda M, Canver MC, Sher F, Funnell AP, Fisher C, Suciu M, Martyn GE, Norton LJ, Zhu C, Kurita R, Nakamura Y, Xu J, Higgs DR, Crossley M, Bauer DE, Orkin SH, Kharchenko PV, Maeda T: Transcription factors LRF and BCL11A independently repress expression of fetal hemoglobin. Science. 2016 Jan 15;351(6270):285-9. doi: 10.1126/science.aad3312. [PubMed:26816381 ]
  25. Ramos Pittol JM, Oruba A, Mittler G, Saccani S, van Essen D: Zbtb7a is a transducer for the control of promoter accessibility by NF-kappa B and multiple other transcription factors. PLoS Biol. 2018 May 29;16(5):e2004526. doi: 10.1371/journal.pbio.2004526. eCollection 2018 May. [PubMed:29813070 ]
  26. Schubot FD, Tropea JE, Waugh DS: Structure of the POZ domain of human LRF, a master regulator of oncogenesis. Biochem Biophys Res Commun. 2006 Dec 8;351(1):1-6. doi: 10.1016/j.bbrc.2006.09.167. Epub 2006 Oct 9. [PubMed:17052694 ]
  27. Stogios PJ, Chen L, Prive GG: Crystal structure of the BTB domain from the LRF/ZBTB7 transcriptional regulator. Protein Sci. 2007 Feb;16(2):336-42. doi: 10.1110/ps.062660907. Epub 2006 Dec 22. [PubMed:17189472 ]