P66A_HUMAN
ID P66A_HUMAN Reviewed; 633 AA.
AC Q86YP4; B5MC40; Q7L3J2; Q96F28; Q9NPU2; Q9NXS1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Transcriptional repressor p66-alpha;
DE Short=Hp66alpha;
DE AltName: Full=GATA zinc finger domain-containing protein 2A;
GN Name=GATAD2A;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH MBD2 AND
RP MBD3, SUBCELLULAR LOCATION, TISSUE 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Ovary, and Skin;
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 417-633 (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-633 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-107 AND SER-114, AND
RP IDENTIFICATION BY 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 [9]
RP FUNCTION, INTERACTION WITH MBD2 AND HISTONE TAILS, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF LYS-149, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100 AND SER-107, AND
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107;
RP SER-114; SER-546; SER-548 AND SER-598, 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107;
RP SER-114; THR-189 AND SER-340, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107; SER-546
RP AND SER-548, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107 AND
RP SER-343, AND 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; THR-49; SER-100; SER-107;
RP SER-114; SER-137; THR-189; SER-275; SER-340; SER-512; SER-546; SER-548;
RP SER-556 AND SER-598, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107 AND
RP THR-189, AND 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 [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-249; ARG-258; ARG-273; ARG-285
RP AND ARG-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-487 AND LYS-550, AND
RP IDENTIFICATION BY MASS 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-487 AND LYS-550, AND
RP IDENTIFICATION BY MASS 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-487, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [24]
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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-178; LYS-204; LYS-233;
RP LYS-464; LYS-487; LYS-550; LYS-585 AND LYS-605, AND IDENTIFICATION BY MASS
RP 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).
RN [26]
RP STRUCTURE BY NMR OF 137-178 IN COMPLEX WITH MBD2, SUBUNIT, AND INTERACTION
RP WITH MBD2.
RX PubMed=21490301; DOI=10.1073/pnas.1015341108;
RA Gnanapragasam M.N., Scarsdale J.N., Amaya M.L., Webb H.D., Desai M.A.,
RA Walavalkar N.M., Wang S.Z., Zu Zhu S., Ginder G.D., Williams D.C. Jr.;
RT "p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical
RT for globin gene silencing by the MBD2-NuRD complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7487-7492(2011).
CC -!- FUNCTION: Transcriptional repressor. Enhances MBD2-mediated repression.
CC Efficient repression requires the presence of GATAD2B.
CC {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}.
CC -!- SUBUNIT: Interacts with MBD2 and MBD3 (PubMed:12183469,
CC PubMed:16415179, PubMed:21490301). Interaction with MBD2 is required
CC for the enhancement of MBD2-mediated repression and for targeting to
CC the chromatin (PubMed:12183469, PubMed:16415179, PubMed:21490301).
CC Component of the MeCP1 histone deacetylase complex (PubMed:21490301).
CC Interacts with histone tails, including that of histones H2A, H2B, H3
CC and H4 (PubMed:16415179). This interaction is reduced by histone
CC acetylation (PubMed:16415179). Interacts with ERCC6 (PubMed:26030138).
CC {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179,
CC ECO:0000269|PubMed:21490301, ECO:0000269|PubMed:26030138}.
CC -!- INTERACTION:
CC Q86YP4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-726224, EBI-618309;
CC Q86YP4; Q14532: KRT32; NbExp=3; IntAct=EBI-726224, EBI-1044146;
CC Q86YP4; O76011: KRT34; NbExp=3; IntAct=EBI-726224, EBI-1047093;
CC Q86YP4; Q9UBB5: MBD2; NbExp=8; IntAct=EBI-726224, EBI-923391;
CC Q86YP4; O95983-2: MBD3; NbExp=3; IntAct=EBI-726224, EBI-11978579;
CC Q86YP4; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-726224, EBI-12516603;
CC Q86YP4-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-10261080, EBI-10171697;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12183469,
CC ECO:0000269|PubMed:16415179}. Note=Speckled nuclear localization
CC requires both CR1 and CR2 regions. {ECO:0000269|PubMed:16415179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86YP4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86YP4-2; Sequence=VSP_010929;
CC Name=3;
CC IsoId=Q86YP4-3; Sequence=VSP_053410;
CC -!- TISSUE SPECIFICITY: Ubiquitous, both in fetal and adult tissues.
CC {ECO:0000269|PubMed:12183469}.
CC -!- DOMAIN: Both CR1 and CR2 regions are required for speckled nuclear
CC localization. {ECO:0000269|PubMed:16415179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11684.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90939.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY186731; AAO31797.1; -; mRNA.
DR EMBL; AC003030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84819.1; -; Genomic_DNA.
DR EMBL; BC011684; AAH11684.1; ALT_INIT; mRNA.
DR EMBL; BC012902; AAH12902.2; -; mRNA.
DR EMBL; AK000092; BAA90939.1; ALT_INIT; mRNA.
DR EMBL; AL390164; CAB99095.1; -; mRNA.
DR CCDS; CCDS12402.2; -. [Q86YP4-1]
DR CCDS; CCDS77270.1; -. [Q86YP4-3]
DR PIR; T51878; T51878.
DR RefSeq; NP_001287875.1; NM_001300946.1. [Q86YP4-3]
DR RefSeq; NP_060130.3; NM_017660.3. [Q86YP4-1]
DR RefSeq; XP_011526407.1; XM_011528105.1.
DR PDB; 2L2L; NMR; -; A=137-178.
DR PDBsum; 2L2L; -.
DR AlphaFoldDB; Q86YP4; -.
DR BMRB; Q86YP4; -.
DR SMR; Q86YP4; -.
DR BioGRID; 120172; 173.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q86YP4; -.
DR DIP; DIP-36053N; -.
DR IntAct; Q86YP4; 66.
DR MINT; Q86YP4; -.
DR STRING; 9606.ENSP00000353463; -.
DR GlyGen; Q86YP4; 17 sites, 2 O-linked glycans (17 sites).
DR iPTMnet; Q86YP4; -.
DR MetOSite; Q86YP4; -.
DR PhosphoSitePlus; Q86YP4; -.
DR BioMuta; GATAD2A; -.
DR DMDM; 50401012; -.
DR EPD; Q86YP4; -.
DR jPOST; Q86YP4; -.
DR MassIVE; Q86YP4; -.
DR MaxQB; Q86YP4; -.
DR PaxDb; Q86YP4; -.
DR PeptideAtlas; Q86YP4; -.
DR PRIDE; Q86YP4; -.
DR ProteomicsDB; 5986; -.
DR ProteomicsDB; 70446; -. [Q86YP4-1]
DR ProteomicsDB; 70447; -. [Q86YP4-2]
DR Antibodypedia; 1819; 245 antibodies from 28 providers.
DR DNASU; 54815; -.
DR Ensembl; ENST00000358713.7; ENSP00000351552.3; ENSG00000167491.18. [Q86YP4-1]
DR Ensembl; ENST00000360315.7; ENSP00000353463.3; ENSG00000167491.18. [Q86YP4-1]
DR Ensembl; ENST00000404158.5; ENSP00000384899.2; ENSG00000167491.18. [Q86YP4-3]
DR Ensembl; ENST00000683918.1; ENSP00000508398.1; ENSG00000167491.18. [Q86YP4-3]
DR GeneID; 54815; -.
DR KEGG; hsa:54815; -.
DR MANE-Select; ENST00000683918.1; ENSP00000508398.1; NM_001384528.1; NP_001371457.1. [Q86YP4-3]
DR UCSC; uc010xqt.3; human. [Q86YP4-1]
DR CTD; 54815; -.
DR DisGeNET; 54815; -.
DR GeneCards; GATAD2A; -.
DR HGNC; HGNC:29989; GATAD2A.
DR HPA; ENSG00000167491; Low tissue specificity.
DR MIM; 614997; gene.
DR neXtProt; NX_Q86YP4; -.
DR OpenTargets; ENSG00000167491; -.
DR PharmGKB; PA142671746; -.
DR VEuPathDB; HostDB:ENSG00000167491; -.
DR eggNOG; KOG3740; Eukaryota.
DR GeneTree; ENSGT00390000004097; -.
DR HOGENOM; CLU_014315_1_0_1; -.
DR InParanoid; Q86YP4; -.
DR OMA; MGRCEGQ; -.
DR PhylomeDB; Q86YP4; -.
DR TreeFam; TF321369; -.
DR PathwayCommons; Q86YP4; -.
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; Q86YP4; -.
DR SIGNOR; Q86YP4; -.
DR BioGRID-ORCS; 54815; 132 hits in 1087 CRISPR screens.
DR ChiTaRS; GATAD2A; human.
DR GenomeRNAi; 54815; -.
DR Pharos; Q86YP4; Tbio.
DR PRO; PR:Q86YP4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86YP4; protein.
DR Bgee; ENSG00000167491; Expressed in buccal mucosa cell and 192 other tissues.
DR ExpressionAtlas; Q86YP4; baseline and differential.
DR Genevisible; Q86YP4; HS.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006306; P:DNA methylation; TAS:UniProtKB.
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; IDA:UniProtKB.
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 InterPro; IPR040386; P66.
DR InterPro; IPR032346; P66_CC.
DR InterPro; IPR000679; Znf_GATA.
DR PANTHER; PTHR13455; PTHR13455; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF16563; P66_CC; 1.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..633
FT /note="Transcriptional repressor p66-alpha"
FT /id="PRO_0000083500"
FT ZN_FING 411..464
FT /note="GATA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..178
FT /note="CR1; interaction with MBD2"
FT /evidence="ECO:0000269|PubMed:12183469"
FT REGION 172..238
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 REGION 561..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..174
FT /evidence="ECO:0000255"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHY6"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 225
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHY6"
FT MOD_RES 249
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 258
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 273
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 285
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 539
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 539
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 93
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 464
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 550
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 CROSSLNK 585
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 401
FT /note="Q -> QA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053410"
FT VAR_SEQ 500..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_010929"
FT VARIANT 17
FT /note="R -> Q (in dbSNP:rs10426883)"
FT /id="VAR_059308"
FT VARIANT 296
FT /note="N -> S (in dbSNP:rs2288851)"
FT /id="VAR_059309"
FT MUTAGEN 149
FT /note="K->R: Disruption of MBD2-binding, loss of
FT enhancement of MBD2-mediated repression and loss of
FT speckled nuclear localization."
FT /evidence="ECO:0000269|PubMed:16415179"
FT CONFLICT 432
FT /note="K -> E (in Ref. 5; BAA90939)"
FT /evidence="ECO:0000305"
FT HELIX 138..168
FT /evidence="ECO:0007829|PDB:2L2L"
SQ SEQUENCE 633 AA; 68063 MW; 64F0066B4BEFCB39 CRC64;
MTEEACRTRS QKRALERDPT EDDVESKKIK MERGLLASDL NTDGDMRVTP EPGAGPTQGL
LRATEATAMA MGRGEGLVGD GPVDMRTSHS DMKSERRPPS PDVIVLSDNE QPSSPRVNGL
TTVALKETST EALMKSSPEE RERMIKQLKE ELRLEEAKLV LLKKLRQSQI QKEATAQKPT
GSVGSTVTTP PPLVRGTQNI PAGKPSLQTS SARMPGSVIP PPLVRGGQQA SSKLGPQASS
QVVMPPLVRG AQQIHSIRQH SSTGPPPLLL APRASVPSVQ IQGQRIIQQG LIRVANVPNT
SLLVNIPQPT PASLKGTTAT SAQANSTPTS VASVVTSAES PASRQAAAKL ALRKQLEKTL
LEIPPPKPPA PEMNFLPSAA NNEFIYLVGL EEVVQNLLET QGRMSAATVL SREPYMCAQC
KTDFTCRWRE EKSGAIMCEN CMTTNQKKAL KVEHTSRLKA AFVKALQQEQ EIEQRLLQQG
TAPAQAKAEP TAAPHPVLKQ VIKPRRKLAF RSGEARDWSN GAVLQASSQL SRGSATTPRG
VLHTFSPSPK LQNSASATAL VSRTGRHSER TVSAGKGSAT SNWKKTPLST GGTLAFVSPS
LAVHKSSSAV DRQREYLLDM IPPRSIPQSA TWK
