MTA2_MOUSE
ID MTA2_MOUSE Reviewed; 668 AA.
AC Q9R190; Q3TVT8;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Metastasis-associated protein MTA2;
DE AltName: Full=Metastasis-associated 1-like 1;
GN Name=Mta2; Synonyms=Mta1l1;
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], AND SUBUNIT.
RX PubMed=10444591; DOI=10.1101/gad.13.15.1924;
RA Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A., Reinberg D.;
RT "Analysis of the NuRD subunits reveals a histone deacetylase core complex
RT and a connection with DNA methylation.";
RL Genes Dev. 13:1924-1935(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11368903; DOI=10.1016/s0378-1119(01)00429-2;
RA Xia L., Zhang Y.;
RT "Sp1 and ETS family transcription factors regulate the mouse Mta2 gene
RT expression.";
RL Gene 268:77-85(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=11749719; DOI=10.1089/104454901753340596;
RA Matsusue K., Takiguchi S., Toh Y., Kono A.;
RT "Characterization of mouse metastasis-associated gene 2: genomic structure,
RT nuclear localization signal, and alternative potentials as transcriptional
RT activator and repressor.";
RL DNA Cell Biol. 20:603-611(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP INTERACTION WITH HDAC7.
RX PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT "Identification of a nuclear domain with deacetylase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN [7]
RP INTERACTION WITH MBD3.
RX PubMed=12124384; DOI=10.1074/jbc.m203455200;
RA Saito M., Ishikawa F.;
RT "The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts
RT with NuRD/Mi2 components HDAC1 and MTA2.";
RL J. Biol. Chem. 277:35434-35439(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-435, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-460; LYS-522 AND LYS-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP INTERACTION WITH PWWP2B.
RX PubMed=34180153; DOI=10.1002/advs.202102060;
RA Yan L., Jin W., Zhao Q., Cui X., Shi T., Xu Y., Li F., Jin W., Zhang Z.,
RA Zhang Z., Tang Q.Q., Pan D.;
RT "PWWP2B Fine-Tunes Adipose Thermogenesis by Stabilizing HDACs in a NuRD
RT Subcomplex.";
RL Adv. Sci. 8:e2102060-e2102060(2021).
CC -!- FUNCTION: May be involved in the regulation of gene expression as
CC repressor and activator. The repression might be related to covalent
CC modification of histone proteins.
CC -!- SUBUNIT: Component of the nucleosome-remodeling and histone-deacetylase
CC multiprotein complex (NuRD) (PubMed:10444591). Interacts with HDAC7
CC (PubMed:10984530). Interacts with MBD3 (PubMed:12124384). Interacts
CC with p53/TP53, MINT, PIMREG, NACC2 and ERCC6 (By similarity). Interacts
CC with PWWP2B (PubMed:34180153). {ECO:0000250|UniProtKB:O94776,
CC ECO:0000269|PubMed:10444591, ECO:0000269|PubMed:10984530,
CC ECO:0000269|PubMed:12124384, ECO:0000269|PubMed:34180153}.
CC -!- INTERACTION:
CC Q9R190; Q61539: Esrrb; NbExp=2; IntAct=EBI-904134, EBI-2312731;
CC Q9R190; O09106: Hdac1; NbExp=7; IntAct=EBI-904134, EBI-301912;
CC Q9R190; P70288: Hdac2; NbExp=7; IntAct=EBI-904134, EBI-302251;
CC Q9R190; P12813: Nr4a1; NbExp=2; IntAct=EBI-904134, EBI-10896863;
CC Q9R190; P20263: Pou5f1; NbExp=6; IntAct=EBI-904134, EBI-1606219;
CC Q9R190; Q8BX22: Sall4; NbExp=3; IntAct=EBI-904134, EBI-2312582;
CC Q9R190; Q8VI24: Satb2; NbExp=2; IntAct=EBI-904134, EBI-5737999;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:11749719}.
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DR EMBL; AF159259; AAD51281.1; -; mRNA.
DR EMBL; AF348083; AAL30174.1; -; Genomic_DNA.
DR EMBL; AB047977; BAB79231.1; -; Genomic_DNA.
DR EMBL; AK088158; BAC40180.1; -; mRNA.
DR EMBL; AK147099; BAE27675.1; -; mRNA.
DR EMBL; AK159979; BAE35530.1; -; mRNA.
DR EMBL; BC079847; AAH79847.1; -; mRNA.
DR CCDS; CCDS29561.1; -.
DR RefSeq; NP_035972.3; NM_011842.3.
DR AlphaFoldDB; Q9R190; -.
DR SMR; Q9R190; -.
DR BioGRID; 204807; 56.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q9R190; -.
DR DIP; DIP-36630N; -.
DR IntAct; Q9R190; 47.
DR MINT; Q9R190; -.
DR STRING; 10090.ENSMUSP00000093959; -.
DR iPTMnet; Q9R190; -.
DR PhosphoSitePlus; Q9R190; -.
DR SwissPalm; Q9R190; -.
DR REPRODUCTION-2DPAGE; IPI00128230; -.
DR EPD; Q9R190; -.
DR jPOST; Q9R190; -.
DR MaxQB; Q9R190; -.
DR PaxDb; Q9R190; -.
DR PeptideAtlas; Q9R190; -.
DR PRIDE; Q9R190; -.
DR ProteomicsDB; 290211; -.
DR Antibodypedia; 1799; 426 antibodies from 41 providers.
DR DNASU; 23942; -.
DR Ensembl; ENSMUST00000096240; ENSMUSP00000093959; ENSMUSG00000071646.
DR GeneID; 23942; -.
DR KEGG; mmu:23942; -.
DR UCSC; uc008gof.1; mouse.
DR CTD; 9219; -.
DR MGI; MGI:1346340; Mta2.
DR VEuPathDB; HostDB:ENSMUSG00000071646; -.
DR eggNOG; KOG3554; Eukaryota.
DR GeneTree; ENSGT01030000234573; -.
DR HOGENOM; CLU_006585_2_0_1; -.
DR InParanoid; Q9R190; -.
DR OMA; IRVGCKF; -.
DR OrthoDB; 802091at2759; -.
DR PhylomeDB; Q9R190; -.
DR TreeFam; TF106444; -.
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; 23942; 12 hits in 79 CRISPR screens.
DR ChiTaRS; Mta2; mouse.
DR PRO; PR:Q9R190; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9R190; protein.
DR Bgee; ENSMUSG00000071646; Expressed in retinal neural layer and 224 other tissues.
DR Genevisible; Q9R190; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016581; C:NuRD complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0051276; P:chromosome organization; TAS:MGI.
DR GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
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:0010762; P:regulation of fibroblast migration; ISO:MGI.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR040138; MIER/MTA.
DR InterPro; IPR035170; MTA1_R1.
DR InterPro; IPR037964; MTA2.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR000679; Znf_GATA.
DR PANTHER; PTHR10865; PTHR10865; 1.
DR PANTHER; PTHR10865:SF4; PTHR10865:SF4; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF17226; MTA_R1; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..668
FT /note="Metastasis-associated protein MTA2"
FT /id="PRO_0000083497"
FT DOMAIN 1..144
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 145..256
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 263..315
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 367..394
FT /note="GATA-type; atypical"
FT REGION 412..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94776"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O94776"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94776"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 522
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 531
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94776"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2 and SUMO3); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O94776"
FT CROSSLNK 508
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94776"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94776"
FT CROSSLNK 595
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94776"
FT CONFLICT 489
FT /note="N -> I (in Ref. 4; BAC40180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 75030 MW; 88996F779BA6F4D1 CRC64;
MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD ISSSLNSLAD
SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT HIRGKCSVTL LNETDILNQY
LDKEDCFFYS LVFDPVQKTL LADQGEIRVG CKFQAEIPDR LAEGESDNRN QQKMEMKVWD
PDNPLTDRQI DQFLVVARAV GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR
NGYDLAKAMS TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL
ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV GSKPGMNGAG
FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK YGGLKTPTQL EGAARGTTEP
HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN RQTFLLQTTK LTRLARRMCR DLLQPRRAAR
RPYAPINANA IKAECSIRLP KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT
PINRNQLTQN RGLGGIMVKR SYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD
APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLMTVRPPVP LPASSHPAST
NEPIVLED
