P66A_MOUSE
ID P66A_MOUSE Reviewed; 629 AA.
AC Q8CHY6; Q8BTQ2; Q8VEC9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Transcriptional repressor p66 alpha;
DE AltName: Full=GATA zinc finger domain-containing protein 2A;
GN Name=Gatad2a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-103 AND SER-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-103 AND SER-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-103; SER-109 AND
RP SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-221; ARG-245 AND ARG-536, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
CC -!- FUNCTION: Transcriptional repressor (By similarity). Enhances MBD2-
CC mediated repression. Efficient repression requires the presence of
CC GATAD2B (By similarity). {ECO:0000250|UniProtKB:Q86YP4}.
CC -!- SUBUNIT: Interacts with MBD2 and MBD3 (By similarity). Interaction with
CC MBD2 is required for the enhancement of MBD2-mediated repression and
CC for targeting to the chromatin (By similarity). Component of the MeCP1
CC histone deacetylase complex (By similarity). Interacts with histone
CC tails, including that of histones H2A, H2B, H3 and H4 (By similarity).
CC This interaction is reduced by histone acetylation (By similarity).
CC Interacts with ERCC6 (By similarity). {ECO:0000250|UniProtKB:Q86YP4}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q86YP4}.
CC Note=Speckled nuclear localization requires both CR1 and CR2 regions.
CC {ECO:0000250|UniProtKB:Q86YP4}.
CC -!- DOMAIN: Both CR1 and CR2 regions are required for speckled nuclear
CC localization. {ECO:0000250|UniProtKB:Q86YP4}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19178.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH31407.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC40736.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK089074; BAC40736.1; ALT_INIT; mRNA.
DR EMBL; BC019178; AAH19178.1; ALT_INIT; mRNA.
DR EMBL; BC031407; AAH31407.1; ALT_INIT; mRNA.
DR EMBL; BC038221; AAH38221.2; -; mRNA.
DR CCDS; CCDS52567.1; -.
DR RefSeq; NP_001106817.1; NM_001113346.1.
DR RefSeq; XP_011240597.1; XM_011242295.2.
DR AlphaFoldDB; Q8CHY6; -.
DR BMRB; Q8CHY6; -.
DR BioGRID; 231518; 13.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR IntAct; Q8CHY6; 7.
DR MINT; Q8CHY6; -.
DR STRING; 10090.ENSMUSP00000070229; -.
DR iPTMnet; Q8CHY6; -.
DR PhosphoSitePlus; Q8CHY6; -.
DR EPD; Q8CHY6; -.
DR jPOST; Q8CHY6; -.
DR MaxQB; Q8CHY6; -.
DR PaxDb; Q8CHY6; -.
DR PeptideAtlas; Q8CHY6; -.
DR PRIDE; Q8CHY6; -.
DR ProteomicsDB; 294097; -.
DR ABCD; Q8CHY6; 40 sequenced antibodies.
DR Antibodypedia; 1819; 245 antibodies from 28 providers.
DR DNASU; 234366; -.
DR Ensembl; ENSMUST00000116463; ENSMUSP00000112164; ENSMUSG00000036180.
DR Ensembl; ENSMUST00000212478; ENSMUSP00000148474; ENSMUSG00000036180.
DR GeneID; 234366; -.
DR KEGG; mmu:234366; -.
DR UCSC; uc009lyf.2; mouse.
DR CTD; 54815; -.
DR MGI; MGI:2384585; Gatad2a.
DR VEuPathDB; HostDB:ENSMUSG00000036180; -.
DR eggNOG; KOG3740; Eukaryota.
DR GeneTree; ENSGT00390000004097; -.
DR InParanoid; Q8CHY6; -.
DR OrthoDB; 885815at2759; -.
DR PhylomeDB; Q8CHY6; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR BioGRID-ORCS; 234366; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Gatad2a; mouse.
DR PRO; PR:Q8CHY6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8CHY6; protein.
DR Bgee; ENSMUSG00000036180; Expressed in animal zygote and 250 other tissues.
DR ExpressionAtlas; Q8CHY6; baseline and differential.
DR Genevisible; Q8CHY6; MM.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:UniProtKB.
DR GO; GO:0021506; P:anterior neuropore closure; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
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; ISS:UniProtKB.
DR GO; GO:0001842; P:neural fold formation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0012501; P:programmed cell death; IMP:MGI.
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 PANTHER; PTHR13455; PTHR13455; 1.
DR Pfam; PF16563; P66_CC; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..629
FT /note="Transcriptional repressor p66 alpha"
FT /id="PRO_0000083501"
FT ZN_FING 410..462
FT /note="GATA-type"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..174
FT /note="CR1; interaction with MBD2"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT REGION 169..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..478
FT /note="CR2; histone tail-binding"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT REGION 560..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..170
FT /evidence="ECO:0000255"
FT COMPBIAS 1..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 221
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 245
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 253
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 268
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 280
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 536
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 536
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 581
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CROSSLNK 601
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86YP4"
FT CONFLICT 248
FT /note="Q -> QQ (in Ref. 1; BAC40736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 629 AA; 67334 MW; 5EA79CC71C9E29A4 CRC64;
MSEEACRTRS QKRTLEPDLT EDDVENKKMK MEKGSSELTV DGDSRVMPEP SAGSAQGLLR
TTEAMGTGSG EGLLGDGPVD MRTSHSDMKS EKRPPSPDVI VLSDSEQPSS PRVNGLTTVA
LKDTSTEALL KSSPEERERM IKQLKEELRL EEAKLVLLKK LRQSQIQKEA TAQKPTASSG
STVTTPPPLV RGTQNIPAGK TSLQTSSTRI PGSIIPPPLV RGGQQVSAKL GPQASSQVVM
PPLVRGAQIH NIRQHSSTGP PPLLLAPRAS VPSMQIQGQR IIQQGLIRVA NVPNTSLLVN
IPQPTAASMK GTAVASAQAN STPTSVASVV ASAESPASRQ AAAKLALRKQ LEKTLLEIPP
PKPPAPEMNF LPSAANNEFI YLVGLEEVVQ NLLETQAGRI SATAAAAVLS REPYMCVQCK
TDFTCRWREK GGAVMCENCM TSNQKKALKV EHTSRLKAAF VKALQQEQEM EQRLLQQGVG
TASIKAEPAA PHPTLKQVIK PRRKLAFRSG EARVWNNGSS LQASSQLSRG SATAPRGVLH
TFSQSPKLQN AASATALVSR TGRHSERVVG TGKGTASNWK KTPLSTGGTL AFVSPSLAVH
KTSSAVDRQR EYLLDMIPPR SIPQSATWK
