MTA3_HUMAN
ID MTA3_HUMAN Reviewed; 594 AA.
AC Q9BTC8; Q9NSP2; Q9ULF4;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Metastasis-associated protein MTA3;
GN Name=MTA3; Synonyms=KIAA1266;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-594.
RC TISSUE=Testis;
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 [5]
RP IDENTIFICATION IN NURD COMPLEX, INDUCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND FUNCTION.
RX PubMed=12705869; DOI=10.1016/s0092-8674(03)00234-4;
RA Fujita N., Jaye D.L., Kajita M., Geigerman C., Moreno C.S., Wade P.A.;
RT "MTA3, a Mi-2/NuRD complex subunit, regulates an invasive growth pathway in
RT breast cancer.";
RL Cell 113:207-219(2003).
RN [6]
RP FUNCTION, INTERACTION WITH BCL6, AND IDENTIFICATION IN THE NURD COMPLEX.
RX PubMed=15454082; DOI=10.1016/j.cell.2004.09.014;
RA Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M.,
RA Wade P.A.;
RT "MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte
RT differentiation.";
RL Cell 119:75-86(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-519, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-519, AND
RP IDENTIFICATION BY MASS 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 [9]
RP INTERACTION WITH NACC2.
RX PubMed=22926524; DOI=10.1038/onc.2012.386;
RA Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L., Yao Z.,
RA Shang Y.;
RT "RBB, a novel transcription repressor, represses the transcription of HDM2
RT oncogene.";
RL Oncogene 32:3711-3721(2013).
CC -!- FUNCTION: Plays a role in maintenance of the normal epithelial
CC architecture through the repression of SNAI1 transcription in a histone
CC deacetylase-dependent manner, and thus the regulation of E-cadherin
CC levels. Contributes to transcriptional repression by BCL6.
CC {ECO:0000269|PubMed:12705869, ECO:0000269|PubMed:15454082}.
CC -!- SUBUNIT: Component of the nucleosome-remodeling and histone-deacetylase
CC multiprotein complex (NuRD) (PubMed:12705869, PubMed:15454082).
CC Interacts with BCL6 (PubMed:15454082). Interacts with NACC2
CC (PubMed:22926524). Interacts with PWWP2B (By similarity).
CC {ECO:0000250|UniProtKB:Q924K8, ECO:0000269|PubMed:12705869,
CC ECO:0000269|PubMed:15454082, ECO:0000269|PubMed:22926524}.
CC -!- INTERACTION:
CC Q9BTC8; Q96KQ7: EHMT2; NbExp=18; IntAct=EBI-2461787, EBI-744366;
CC Q9BTC8; P23771: GATA3; NbExp=18; IntAct=EBI-2461787, EBI-6664760;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:12705869}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BTC8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTC8-2; Sequence=VSP_001603, VSP_001604;
CC -!- TISSUE SPECIFICITY: Expressed in germinal centers of lymphoid tissues.
CC No expression in nonepithelial cells. {ECO:0000269|PubMed:12705869}.
CC -!- INDUCTION: By estrogen. {ECO:0000269|PubMed:12705869}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86580.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MTA3ID41445ch2p21.html";
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DR EMBL; AB033092; BAA86580.1; ALT_INIT; mRNA.
DR EMBL; AK027304; BAB55028.1; -; mRNA.
DR EMBL; BC004227; AAH04227.1; -; mRNA.
DR EMBL; BC053631; AAH53631.1; -; mRNA.
DR EMBL; AL161954; CAB82305.1; -; mRNA.
DR CCDS; CCDS46267.1; -. [Q9BTC8-2]
DR CCDS; CCDS82441.1; -. [Q9BTC8-1]
DR PIR; T47180; T47180.
DR RefSeq; NP_001269684.1; NM_001282755.1.
DR RefSeq; NP_001269685.1; NM_001282756.1.
DR RefSeq; NP_001317371.1; NM_001330442.1. [Q9BTC8-1]
DR RefSeq; NP_065795.1; NM_020744.3. [Q9BTC8-2]
DR AlphaFoldDB; Q9BTC8; -.
DR SMR; Q9BTC8; -.
DR BioGRID; 121568; 156.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q9BTC8; -.
DR DIP; DIP-47460N; -.
DR IntAct; Q9BTC8; 60.
DR MINT; Q9BTC8; -.
DR STRING; 9606.ENSP00000383973; -.
DR iPTMnet; Q9BTC8; -.
DR MetOSite; Q9BTC8; -.
DR PhosphoSitePlus; Q9BTC8; -.
DR BioMuta; MTA3; -.
DR DMDM; 29840798; -.
DR EPD; Q9BTC8; -.
DR jPOST; Q9BTC8; -.
DR MassIVE; Q9BTC8; -.
DR MaxQB; Q9BTC8; -.
DR PaxDb; Q9BTC8; -.
DR PeptideAtlas; Q9BTC8; -.
DR PRIDE; Q9BTC8; -.
DR ProteomicsDB; 78971; -. [Q9BTC8-1]
DR ProteomicsDB; 78972; -. [Q9BTC8-2]
DR Antibodypedia; 29760; 274 antibodies from 28 providers.
DR DNASU; 57504; -.
DR Ensembl; ENST00000405094.2; ENSP00000385823.1; ENSG00000057935.14. [Q9BTC8-1]
DR Ensembl; ENST00000407270.7; ENSP00000385045.3; ENSG00000057935.14. [Q9BTC8-2]
DR GeneID; 57504; -.
DR KEGG; hsa:57504; -.
DR MANE-Select; ENST00000405094.2; ENSP00000385823.1; NM_001330442.2; NP_001317371.1.
DR UCSC; uc002rsq.5; human. [Q9BTC8-1]
DR CTD; 57504; -.
DR DisGeNET; 57504; -.
DR GeneCards; MTA3; -.
DR HGNC; HGNC:23784; MTA3.
DR HPA; ENSG00000057935; Tissue enhanced (lymphoid).
DR MalaCards; MTA3; -.
DR MIM; 609050; gene.
DR neXtProt; NX_Q9BTC8; -.
DR OpenTargets; ENSG00000057935; -.
DR PharmGKB; PA134953540; -.
DR VEuPathDB; HostDB:ENSG00000057935; -.
DR eggNOG; KOG3554; Eukaryota.
DR GeneTree; ENSGT01030000234573; -.
DR InParanoid; Q9BTC8; -.
DR OMA; GPAHMQC; -.
DR OrthoDB; 802091at2759; -.
DR PhylomeDB; Q9BTC8; -.
DR TreeFam; TF106444; -.
DR PathwayCommons; Q9BTC8; -.
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-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; Q9BTC8; -.
DR SIGNOR; Q9BTC8; -.
DR BioGRID-ORCS; 57504; 23 hits in 1104 CRISPR screens.
DR ChiTaRS; MTA3; human.
DR GeneWiki; MTA3; -.
DR GenomeRNAi; 57504; -.
DR Pharos; Q9BTC8; Tbio.
DR PRO; PR:Q9BTC8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BTC8; protein.
DR Bgee; ENSG00000057935; Expressed in right adrenal gland cortex and 159 other tissues.
DR ExpressionAtlas; Q9BTC8; baseline and differential.
DR Genevisible; Q9BTC8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0120325; F:NuRD complex binding; IEA:Ensembl.
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:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1990739; P:granulosa cell proliferation; IEA:Ensembl.
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; IMP:CACAO.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1904197; P:positive regulation of granulosa cell proliferation; IEA:Ensembl.
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 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; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR000679; Znf_GATA.
DR PANTHER; PTHR10865; PTHR10865; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF17226; MTA_R1; 1.
DR Pfam; PF00249; Myb_DNA-binding; 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 Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..594
FT /note="Metastasis-associated protein MTA3"
FT /id="PRO_0000083498"
FT DOMAIN 1..147
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 148..259
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 266..318
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 379..406
FT /note="GATA-type; atypical"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924K8"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 509..515
FT /note="YADRHAE -> CKMLLNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_001603"
FT VAR_SEQ 516..594
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_001604"
FT CONFLICT 1..9
FT /note="MAANMYRVG -> ATGGFPRDR (in Ref. 1; BAA86580)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="Missing (in Ref. 1; BAA86580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 67504 MW; E773603F65A16DF1 CRC64;
MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTASGNVEA KVVCFYRRRD ISNTLIMLAD
KHAKEIEEES ETTVEADLTD KQKHQLKHRE LFLSRQYESL PATHIRGKCS VALLNETESV
LSYLDKEDTF FYSLVYDPSL KTLLADKGEI RVGPRYQADI PEMLLEGESD EREQSKLEVK
VWDPNSPLTD RQIDQFLVVA RAVGTFARAL DCSSSVRQPS LHMSAAAASR DITLFHAMDT
LYRHSYDLSS AISVLVPLGG PVLCRDEMEE WSASEASLFE EALEKYGKDF NDIRQDFLPW
KSLTSIIEYY YMWKTTDRYV QQKRLKAAEA ESKLKQVYIP TYSKPNPNQI STSNGKPGAV
NGAVGTTFQP QNPLLGRACE SCYATQSHQW YSWGPPNMQC RLCAICWLYW KKYGGLKMPT
QSEEEKLSPS PTTEDPRVRS HVSRQAMQGM PVRNTGSPKS AVKTRQAFFL HTTYFTKFAR
QVCKNTLRLR QAARRPFVAI NYAAIRAEYA DRHAELSGSP LKSKSTRKPL ACIIGYLEIH
PAKKPNVIRS TPSLQTPTTK RMLTTPNHTS LSILGKRNYS HHNGLDELTC CVSD
