P66B_MOUSE
ID P66B_MOUSE Reviewed; 594 AA.
AC Q8VHR5; Q8C9Q3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
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;
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 [MRNA] (ISOFORM 1).
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123; SER-130 AND
RP SER-136, AND 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123 AND SER-136, 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 THR-121; SER-123; SER-130;
RP SER-135; SER-136; SER-339 AND SER-341, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Transcriptional repressor (By similarity). Enhances MBD2-
CC mediated repression. Efficient repression requires the presence of
CC GATAD2A (By similarity). Targets MBD3 to discrete loci in the nucleus
CC (By similarity). Plays a role in synapse development (By similarity).
CC {ECO:0000250|UniProtKB:Q8WXI9}.
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 Interacts with ERCC6 (By similarity). {ECO:0000250|UniProtKB:Q8WXI9}.
CC -!- INTERACTION:
CC Q8VHR5; P12813: Nr4a1; NbExp=2; IntAct=EBI-3043880, EBI-10896863;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q8WXI9}.
CC Note=Speckled nuclear localization requires both CR1 and CR2 regions.
CC {ECO:0000250|UniProtKB:Q8WXI9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VHR5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHR5-2; Sequence=VSP_010930, VSP_010931;
CC -!- DOMAIN: Both CR1 and CR2 regions are required for speckled nuclear
CC localization. {ECO:0000250|UniProtKB:Q8WXI9}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
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DR EMBL; AF411837; AAL39081.1; -; mRNA.
DR EMBL; AK041594; BAC30997.1; -; mRNA.
DR CCDS; CCDS17526.1; -. [Q8VHR5-1]
DR RefSeq; NP_647465.1; NM_139304.1. [Q8VHR5-1]
DR RefSeq; XP_006501422.2; XM_006501359.3.
DR RefSeq; XP_006501424.1; XM_006501361.2.
DR AlphaFoldDB; Q8VHR5; -.
DR SMR; Q8VHR5; -.
DR BioGRID; 230858; 19.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q8VHR5; -.
DR DIP; DIP-62049N; -.
DR IntAct; Q8VHR5; 8.
DR MINT; Q8VHR5; -.
DR STRING; 10090.ENSMUSP00000041370; -.
DR iPTMnet; Q8VHR5; -.
DR PhosphoSitePlus; Q8VHR5; -.
DR EPD; Q8VHR5; -.
DR jPOST; Q8VHR5; -.
DR MaxQB; Q8VHR5; -.
DR PaxDb; Q8VHR5; -.
DR PeptideAtlas; Q8VHR5; -.
DR PRIDE; Q8VHR5; -.
DR ProteomicsDB; 294313; -. [Q8VHR5-1]
DR ProteomicsDB; 294314; -. [Q8VHR5-2]
DR Antibodypedia; 1795; 285 antibodies from 30 providers.
DR DNASU; 229542; -.
DR Ensembl; ENSMUST00000049382; ENSMUSP00000041370; ENSMUSG00000042390. [Q8VHR5-1]
DR Ensembl; ENSMUST00000199607; ENSMUSP00000142617; ENSMUSG00000042390. [Q8VHR5-1]
DR Ensembl; ENSMUST00000199754; ENSMUSP00000142514; ENSMUSG00000042390. [Q8VHR5-1]
DR GeneID; 229542; -.
DR KEGG; mmu:229542; -.
DR UCSC; uc008qca.1; mouse. [Q8VHR5-1]
DR CTD; 57459; -.
DR MGI; MGI:2443225; Gatad2b.
DR VEuPathDB; HostDB:ENSMUSG00000042390; -.
DR eggNOG; KOG3740; Eukaryota.
DR GeneTree; ENSGT00390000004097; -.
DR InParanoid; Q8VHR5; -.
DR OMA; PEERMHQ; -.
DR OrthoDB; 885815at2759; -.
DR PhylomeDB; Q8VHR5; -.
DR TreeFam; TF321369; -.
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; 229542; 4 hits in 63 CRISPR screens.
DR ChiTaRS; Gatad2b; mouse.
DR PRO; PR:Q8VHR5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VHR5; protein.
DR Bgee; ENSMUSG00000042390; Expressed in secondary oocyte and 226 other tissues.
DR ExpressionAtlas; Q8VHR5; baseline and differential.
DR Genevisible; Q8VHR5; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016581; C:NuRD complex; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:0016575; P:histone deacetylation; ISO: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; 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 Alternative splicing; Coiled coil; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..594
FT /note="Transcriptional repressor p66-beta"
FT /id="PRO_0000083503"
FT ZN_FING 415..468
FT /note="GATA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 62..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..191
FT /note="CR1; interaction with MBD2 and MBD3"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT REGION 214..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..481
FT /note="CR2; histone tail-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT COILED 141..195
FT /evidence="ECO:0000255"
FT COILED 450..483
FT /evidence="ECO:0000255"
FT COMPBIAS 91..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 66
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 468
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT CROSSLNK 499
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WXI9"
FT VAR_SEQ 475..485
FT /note="EIEQRLQQQAA -> VRTLTPTCTVI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010930"
FT VAR_SEQ 486..594
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010931"
SQ SEQUENCE 594 AA; 65411 MW; C57330259EADAAE6 CRC64;
MDRMTEDALR LNLLKRSLDP ADERDDVLAK RLKMEGHEAM ERLKMLALLK RKDLANLEVP
HELPTKQDGS GVKGYEEKLN GNLRPHGDNN RTAGRPGKEN INDEPVDMSA RRSEPDRGRL
TPSPDIIVLS DNEASSPRSS SRMEERLKAA NLEMFKGKGM EERQQLIKQL RDELRLEEAR
LVLLKKLRQS QLQKENVVQK TPVVQNAASI VQPSPAHVGQ QGLSKLPSRP GAQGIEPQNM
RTLQGHSVIR SATNTTLPHM LMSQRVIAPN PAQLQGQRGP PKPGIVRTTT PNMNPAISYQ
PQSSSSVPCQ RTTSSAIYMN LASHIQPGTV NRVSSPLPSP SAMSDAANSQ AAAKLALRKQ
LEKTLLEIPP PKPPAPLLHF LPSAANSEFI YMVGLEEVVQ SVIDSQGKNC ASLLRVEPFV
CAQCRTDFTP HWKQEKNGKI LCEQCMTSNQ KKALKAEHTN RLKNAFVKAL QQEQEIEQRL
QQQAALSPTT APAVSSVSKQ ETIMRHHTLR QAPQPQSSLQ RGIPTSARSM LSNFAQAPQL
SVPGGLLGMP GVNIAYLNTG IGGHKAPSLA DRQREYLLDM IPPRSISQSI SGQK
