P66B_HUMAN
ID P66B_HUMAN Reviewed; 593 AA.
AC Q8WXI9; D3DUZ2; Q5VUR2; Q7LG68; Q9ULS0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Transcriptional repressor p66-beta;
DE AltName: Full=GATA zinc finger domain-containing protein 2B;
DE AltName: Full=p66/p68;
GN Name=GATAD2B; Synonyms=KIAA1150;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP INTERACTION WITH MBD2; MBD3 AND THE MECP1 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11756549; DOI=10.1128/mcb.22.2.536-546.2002;
RA Feng Q., Cao R., Xia L., Erdjument-Bromage H., Tempst P., Zhang Y.;
RT "Identification and functional characterization of the p66/p68 components
RT of the MeCP1 complex.";
RL Mol. Cell. Biol. 22:536-546(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-593.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP FUNCTION, INTERACTION WITH MBD2 AND MBD3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DOMAIN CR1.
RX PubMed=12183469; DOI=10.1074/jbc.m207467200;
RA Brackertz M., Boeke J., Zhang R., Renkawitz R.;
RT "Two highly related p66 proteins comprise a new family of potent
RT transcriptional repressors interacting with MBD2 and MBD3.";
RL J. Biol. Chem. 277:40958-40966(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP FUNCTION, INTERACTION WITH MBD2 AND HISTONE TAILS, SUBCELLULAR LOCATION,
RP AND DOMAINS CR1 AND CR2.
RX PubMed=16415179; DOI=10.1093/nar/gkj437;
RA Brackertz M., Gong Z., Leers J., Renkawitz R.;
RT "p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone
RT interaction.";
RL Nucleic Acids Res. 34:397-406(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120; SER-122; SER-129;
RP SER-134; SER-135; SER-333 AND SER-486, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120; SER-122; SER-129;
RP SER-134 AND SER-135, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120; SER-122; SER-129;
RP SER-135; SER-338 AND SER-486, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120; SER-122 AND SER-129, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP INVOLVEMENT IN GAND.
RX PubMed=23644463; DOI=10.1136/jmedgenet-2012-101490;
RA Willemsen M.H., Nijhof B., Fenckova M., Nillesen W.M., Bongers E.M.,
RA Castells-Nobau A., Asztalos L., Viragh E., van Bon B.W., Tezel E.,
RA Veltman J.A., Brunner H.G., de Vries B.B., de Ligt J., Yntema H.G.,
RA van Bokhoven H., Isidor B., Le Caignec C., Lorino E., Asztalos Z.,
RA Koolen D.A., Vissers L.E., Schenck A., Kleefstra T.;
RT "GATAD2B loss-of-function mutations cause a recognisable syndrome with
RT intellectual disability and are associated with learning deficits and
RT synaptic undergrowth in Drosophila.";
RL J. Med. Genet. 50:507-514(2013).
RN [18]
RP INVOLVEMENT IN GAND, AND VARIANTS VAL-316 AND LEU-586.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-120; SER-122;
RP SER-129; SER-135; SER-208; SER-338 AND SER-486, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [23]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-66; LYS-97; LYS-147;
RP LYS-199; LYS-281; LYS-353; LYS-454; LYS-467 AND LYS-498, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcriptional repressor. Enhances MBD2-mediated repression.
CC Efficient repression requires the presence of GATAD2A. Targets MBD3 to
CC discrete loci in the nucleus. May play a role in synapse development.
CC {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}.
CC -!- SUBUNIT: Interacts with MBD2 and MBD3 (PubMed:11756549,
CC PubMed:12183469, PubMed:16415179). Interaction with MBD2 is required
CC for the enhancement of MBD2-mediated repression and for targeting to
CC the chromatin (PubMed:11756549, PubMed:12183469, PubMed:16415179).
CC Component of the MeCP1 histone deacetylase complex (PubMed:11756549).
CC Interacts with histone tails, including that of histones H2A, H2B, H3
CC and H4 (PubMed:16415179). Interacts with ERCC6 (PubMed:26030138).
CC {ECO:0000269|PubMed:11756549, ECO:0000269|PubMed:12183469,
CC ECO:0000269|PubMed:16415179, ECO:0000269|PubMed:26030138}.
CC -!- INTERACTION:
CC Q8WXI9; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-923440, EBI-739580;
CC Q8WXI9; P55273: CDKN2D; NbExp=3; IntAct=EBI-923440, EBI-745859;
CC Q8WXI9; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-923440, EBI-739624;
CC Q8WXI9; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-923440, EBI-529989;
CC Q8WXI9; Q14192: FHL2; NbExp=3; IntAct=EBI-923440, EBI-701903;
CC Q8WXI9; Q08379: GOLGA2; NbExp=3; IntAct=EBI-923440, EBI-618309;
CC Q8WXI9; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-923440, EBI-347538;
CC Q8WXI9; O95983: MBD3; NbExp=4; IntAct=EBI-923440, EBI-1783068;
CC Q8WXI9; Q9NPG2: NGB; NbExp=3; IntAct=EBI-923440, EBI-10311409;
CC Q8WXI9; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-923440, EBI-744782;
CC Q8WXI9; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-923440, EBI-12025760;
CC Q8WXI9; O43741: PRKAB2; NbExp=4; IntAct=EBI-923440, EBI-1053424;
CC Q8WXI9; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-923440, EBI-1050213;
CC Q8WXI9; P0C264: SBK3; NbExp=3; IntAct=EBI-923440, EBI-17181801;
CC Q8WXI9; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-923440, EBI-742397;
CC Q8WXI9; Q13077: TRAF1; NbExp=4; IntAct=EBI-923440, EBI-359224;
CC Q8WXI9; P14373: TRIM27; NbExp=3; IntAct=EBI-923440, EBI-719493;
CC Q8WXI9; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-923440, EBI-739895;
CC Q8WXI9; O95365: ZBTB7A; NbExp=4; IntAct=EBI-923440, EBI-2795384;
CC Q8WXI9; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-923440, EBI-10183064;
CC Q8WXI9; Q17R98: ZNF827; NbExp=2; IntAct=EBI-923440, EBI-5564776;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11756549,
CC ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}.
CC Note=Speckled nuclear localization requires both CR1 and CR2 regions.
CC {ECO:0000269|PubMed:16415179}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12183469}.
CC -!- DOMAIN: Both CR1 and CR2 regions are required for speckled nuclear
CC localization. {ECO:0000269|PubMed:16415179}.
CC -!- DISEASE: Gand syndrome (GAND) [MIM:615074]: An autosomal dominant
CC syndrome characterized by global developmental delay with motor delay,
CC moderate to severely impaired intellectual development, and poor speech
CC acquisition in most patients. Additional features include hypotonia,
CC feeding difficulties in infancy, and dysmorphic features. More variable
CC features may include seizures, cardiac abnormalities, and non-specific
CC findings on brain imaging. {ECO:0000269|PubMed:23033978,
CC ECO:0000269|PubMed:23644463}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF411836; AAL39080.1; -; mRNA.
DR EMBL; AL513523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53270.1; -; Genomic_DNA.
DR EMBL; BC069419; AAH69419.1; -; mRNA.
DR EMBL; BC112052; AAI12053.1; -; mRNA.
DR EMBL; BC112080; AAI12081.1; -; mRNA.
DR EMBL; AB032976; BAA86464.1; -; mRNA.
DR CCDS; CCDS1054.1; -.
DR RefSeq; NP_065750.1; NM_020699.3.
DR RefSeq; XP_005245421.1; XM_005245364.4.
DR AlphaFoldDB; Q8WXI9; -.
DR SMR; Q8WXI9; -.
DR BioGRID; 121529; 215.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q8WXI9; -.
DR DIP; DIP-36054N; -.
DR IntAct; Q8WXI9; 105.
DR MINT; Q8WXI9; -.
DR STRING; 9606.ENSP00000357644; -.
DR GlyConnect; 2882; 1 O-Linked glycan (1 site).
DR GlyGen; Q8WXI9; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; Q8WXI9; -.
DR MetOSite; Q8WXI9; -.
DR PhosphoSitePlus; Q8WXI9; -.
DR BioMuta; GATAD2B; -.
DR DMDM; 50401096; -.
DR EPD; Q8WXI9; -.
DR jPOST; Q8WXI9; -.
DR MassIVE; Q8WXI9; -.
DR MaxQB; Q8WXI9; -.
DR PaxDb; Q8WXI9; -.
DR PeptideAtlas; Q8WXI9; -.
DR PRIDE; Q8WXI9; -.
DR ProteomicsDB; 75070; -.
DR Antibodypedia; 1795; 285 antibodies from 30 providers.
DR DNASU; 57459; -.
DR Ensembl; ENST00000368655.5; ENSP00000357644.4; ENSG00000143614.10.
DR Ensembl; ENST00000576342.2; ENSP00000458280.1; ENSG00000261992.2.
DR Ensembl; ENST00000634544.1; ENSP00000489184.1; ENSG00000143614.10.
DR GeneID; 57459; -.
DR KEGG; hsa:57459; -.
DR MANE-Select; ENST00000368655.5; ENSP00000357644.4; NM_020699.4; NP_065750.1.
DR UCSC; uc001fdb.5; human.
DR CTD; 57459; -.
DR DisGeNET; 57459; -.
DR GeneCards; GATAD2B; -.
DR HGNC; HGNC:30778; GATAD2B.
DR HPA; ENSG00000143614; Low tissue specificity.
DR MalaCards; GATAD2B; -.
DR MIM; 614998; gene.
DR MIM; 615074; phenotype.
DR neXtProt; NX_Q8WXI9; -.
DR OpenTargets; ENSG00000143614; -.
DR Orphanet; 363686; Severe intellectual disability-poor language-strabismus-grimacing face-long fingers syndrome.
DR PharmGKB; PA142671747; -.
DR VEuPathDB; HostDB:ENSG00000143614; -.
DR eggNOG; KOG3740; Eukaryota.
DR GeneTree; ENSGT00390000004097; -.
DR HOGENOM; CLU_014315_2_0_1; -.
DR InParanoid; Q8WXI9; -.
DR OMA; PEERMHQ; -.
DR OrthoDB; 885815at2759; -.
DR PhylomeDB; Q8WXI9; -.
DR TreeFam; TF321369; -.
DR PathwayCommons; Q8WXI9; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; Q8WXI9; -.
DR SIGNOR; Q8WXI9; -.
DR BioGRID-ORCS; 57459; 29 hits in 1098 CRISPR screens.
DR ChiTaRS; GATAD2B; human.
DR GeneWiki; GATAD2B; -.
DR GenomeRNAi; 57459; -.
DR Pharos; Q8WXI9; Tbio.
DR PRO; PR:Q8WXI9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8WXI9; protein.
DR Bgee; ENSG00000143614; Expressed in colonic epithelium and 104 other tissues.
DR ExpressionAtlas; Q8WXI9; baseline and differential.
DR Genevisible; Q8WXI9; HS.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016581; C:NuRD complex; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR040386; P66.
DR InterPro; IPR032346; P66_CC.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR13455; PTHR13455; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF16563; P66_CC; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Intellectual disability; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..593
FT /note="Transcriptional repressor p66-beta"
FT /id="PRO_0000083502"
FT ZN_FING 414..467
FT /note="GATA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 62..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..195
FT /note="CR1; interaction with MBD2 and MBD3"
FT /evidence="ECO:0000269|PubMed:12183469"
FT REGION 213..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..480
FT /note="CR2; histone tail-binding"
FT /evidence="ECO:0000269|PubMed:16415179"
FT COILED 140..194
FT /evidence="ECO:0000255"
FT COILED 449..482
FT /evidence="ECO:0000255"
FT COMPBIAS 79..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHR5"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 66
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VARIANT 316
FT /note="I -> V"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069363"
FT VARIANT 586
FT /note="S -> L"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069364"
SQ SEQUENCE 593 AA; 65261 MW; 5EB375C7EB24210B CRC64;
MDRMTEDALR LNLLKRSLDP ADERDDVLAK RLKMEGHEAM ERLKMLALLK RKDLANLEVP
HELPTKQDGS GVKGYEEKLN GNLRPHGDNR TAGRPGKENI NDEPVDMSAR RSEPERGRLT
PSPDIIVLSD NEASSPRSSS RMEERLKAAN LEMFKGKGIE ERQQLIKQLR DELRLEEARL
VLLKKLRQSQ LQKENVVQKT PVVQNAASIV QPSPAHVGQQ GLSKLPSRPG AQGVEPQNLR
TLQGHSVIRS ATNTTLPHML MSQRVIAPNP AQLQGQRGPP KPGLVRTTTP NMNPAINYQP
QSSSSVPCQR TTSSAIYMNL ASHIQPGTVN RVSSPLPSPS AMTDAANSQA AAKLALRKQL
EKTLLEIPPP KPPAPLLHFL PSAANSEFIY MVGLEEVVQS VIDSQGKSCA SLLRVEPFVC
AQCRTDFTPH WKQEKNGKIL CEQCMTSNQK KALKAEHTNR LKNAFVKALQ QEQEIEQRLQ
QQAALSPTTA PAVSSVSKQE TIMRHHTLRQ APQPQSSLQR GIPTSARSML SNFAQAPQLS
VPGGLLGMPG VNIAYLNTGI GGHKGPSLAD RQREYLLDMI PPRSISQSIS GQK
