MTA1_MOUSE
ID MTA1_MOUSE Reviewed; 715 AA.
AC Q8K4B0; Q80UI1; Q8K4D4; Q924K9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Metastasis-associated protein MTA1;
GN Name=Mta1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=12370427; DOI=10.1073/pnas.212392399;
RA Zhou J., Ashouian N., Delepine M., Matsuda F., Chevillard C., Riblet R.,
RA Schildkraut C.L., Birshtein B.K.;
RT "The origin of a developmentally regulated Igh replicon is located near the
RT border of regulatory domains for Igh replication and expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13693-13698(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=129/Sv;
RX PubMed=11483358; DOI=10.1016/s0378-1119(01)00563-7;
RA Simpson A., Uitto J., Rodeck U., Mahoney M.G.;
RT "Differential expression and subcellular distribution of the mouse
RT metastasis-associated proteins Mta1 and Mta3.";
RL Gene 273:29-39(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RA Takiguchi S.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION BY CSNK1G2/CK1, MUTAGENESIS OF SER-322, INTERACTION WITH
RP CSNK1G2, AND SUBCELLULAR LOCATION.
RX PubMed=15077195; DOI=10.1038/sj.onc.1207569;
RA Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.;
RT "Metastatic tumor antigen 1 short form (MTA1s) associates with casein
RT kinase I-gamma2, an estrogen-responsive kinase.";
RL Oncogene 23:4422-4429(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16617102; DOI=10.1073/pnas.0601989103;
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RT "MTA1, a transcriptional activator of breast cancer amplified sequence 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6670-6675(2006).
RN [6]
RP ERRATUM OF PUBMED:16617102.
RA Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H.,
RA Balasenthil S., Talukder A.H., Landberg G., Kumar R.;
RL Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013).
RN [7]
RP FUNCTION.
RX PubMed=17671180; DOI=10.1158/0008-5472.can-07-0750;
RA Balasenthil S., Gururaj A.E., Talukder A.H., Bagheri-Yarmand R.,
RA Arrington T., Haas B.J., Braisted J.C., Kim I., Lee N.H., Kumar R.;
RT "Identification of Pax5 as a target of MTA1 in B-cell lymphomas.";
RL Cancer Res. 67:7132-7138(2007).
RN [8]
RP INTERACTION WITH SIX3.
RX PubMed=17666527; DOI=10.1073/pnas.0705878104;
RA Manavathi B., Peng S., Rayala S.K., Talukder A.H., Wang M.H., Wang R.A.,
RA Balasenthil S., Agarwal N., Frishman L.J., Kumar R.;
RT "Repression of Six3 by a corepressor regulates rhodopsin expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13128-13133(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, AND IDENTIFICATION BY
RP 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 [10]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=19837670; DOI=10.1074/jbc.m109.056499;
RA Li D.Q., Divijendra Natha Reddy S., Pakala S.B., Wu X., Zhang Y.,
RA Rayala S.K., Kumar R.;
RT "MTA1 coregulator regulates p53 stability and function.";
RL J. Biol. Chem. 284:34545-34552(2009).
RN [11]
RP FUNCTION.
RX PubMed=19805145; DOI=10.1073/pnas.0908027106;
RA Li D.Q., Ohshiro K., Reddy S.D., Pakala S.B., Lee M.H., Zhang Y.,
RA Rayala S.K., Kumar R.;
RT "E3 ubiquitin ligase COP1 regulates the stability and functions of MTA1.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:17493-17498(2009).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20682799; DOI=10.1158/0008-5472.can-10-0909;
RA Kumar R., Balasenthil S., Manavathi B., Rayala S.K., Pakala S.B.;
RT "Metastasis-associated protein 1 and its short form variant stimulates Wnt1
RT transcription through promoting its derepression from Six3 corepressor.";
RL Cancer Res. 70:6649-6658(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-449; THR-564 AND
RP SER-576, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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 [14]
RP FUNCTION.
RX PubMed=20071335; DOI=10.1074/jbc.m109.079095;
RA Li D.Q., Pakala S.B., Reddy S.D., Ohshiro K., Peng S.H., Lian Y., Fu S.W.,
RA Kumar R.;
RT "Revelation of p53-independent function of MTA1 in DNA damage response via
RT modulation of the p21 WAF1-proliferating cell nuclear antigen pathway.";
RL J. Biol. Chem. 285:10044-10052(2010).
RN [15]
RP CAUTION.
RX PubMed=20519513; DOI=10.1074/jbc.m110.139469;
RA Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S., Rayala S.K.,
RA Behringer R.R., Kumar R.;
RT "Regulation of NF-kappaB circuitry by a component of the nucleosome
RT remodeling and deacetylase complex controls inflammatory response
RT homeostasis.";
RL J. Biol. Chem. 285:23590-23597(2010).
RN [16]
RP CAUTION, AND RETRACTION NOTICE OF PUBMED:20519513.
RX PubMed=28314777; DOI=10.1074/jbc.a117.139469;
RA Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S., Rayala S.K.,
RA Behringer R.R., Kumar R.;
RL J. Biol. Chem. 292:4764-4764(2017).
RN [17]
RP FUNCTION.
RX PubMed=21965678; DOI=10.1074/jbc.m111.267237;
RA Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1
RT (MTA1) synergistically regulate its transcriptional repressor function.";
RL J. Biol. Chem. 286:43793-43808(2011).
RN [18]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CLOCK AND ARNTL.
RX PubMed=24089055; DOI=10.1038/ncomms3545;
RA Li D.Q., Pakala S.B., Reddy S.D., Peng S., Balasenthil S., Deng C.X.,
RA Lee C.C., Rea M.A., Kumar R.;
RT "Metastasis-associated protein 1 is an integral component of the circadian
RT molecular machinery.";
RL Nat. Commun. 4:2545-2545(2013).
RN [19]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24970816; DOI=10.18632/oncotarget.2095;
RA Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C.,
RA Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.;
RT "The subcellular distribution and function of MTA1 in cancer
RT differentiation.";
RL Oncotarget 5:5153-5164(2014).
RN [20]
RP FUNCTION, AND INTERACTION WITH TFCP2L1.
RX PubMed=28982712; DOI=10.1242/jcs.206532;
RA Liu K., Zhang Y., Liu D., Ying Q.L., Ye S.;
RT "Tfcp2l1 represses multiple lineage commitment of mouse embryonic stem
RT cells through MTA1 and LEF1.";
RL J. Cell Sci. 130:3809-3817(2017).
RN [21]
RP INTERACTION WITH PWWP2A AND PWWP2B.
RX PubMed=30228260; DOI=10.1038/s41467-018-06235-9;
RA Zhang T., Wei G., Millard C.J., Fischer R., Konietzny R., Kessler B.M.,
RA Schwabe J.W.R., Brockdorff N.;
RT "A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to regulate
RT transcription at active genes.";
RL Nat. Commun. 9:3798-3798(2018).
RN [22]
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: Transcriptional coregulator which can act as both a
CC transcriptional corepressor and coactivator. As a part of the histone-
CC deacetylase multiprotein complex (NuRD), regulates transcription of its
CC targets by modifying the acetylation status of the target chromatin and
CC cofactor accessibility to the target DNA. In conjunction with other
CC components of NuRD, acts as a transcriptional corepressor of BRCA1,
CC ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3,
CC PAX5 and SUMO2, independent of the NuRD complex. Stimulates the
CC expression of WNT1 by inhibiting the expression of its transcriptional
CC corepressor SIX3. Regulates p53-dependent and -independent DNA repair
CC processes following genotoxic stress. Regulates the stability and
CC function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2
CC thereby regulating the p53-dependent DNA repair. Plays an important
CC role in tumorigenesis, tumor invasion, and metastasis. Plays a role in
CC the regulation of the circadian clock and is essential for the
CC generation and maintenance of circadian rhythms under constant light
CC and for normal entrainment of behavior to light-dark (LD) cycles.
CC Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated
CC transcriptional activation of its own transcription and the
CC transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by
CC regulating SIRT1 expression, resulting in derepressing CRY1-mediated
CC transcription repression. With Tfcp2l1, promotes establishment and
CC maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits
CC endoderm differentiation (PubMed:28982712).
CC {ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:19805145,
CC ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:20071335,
CC ECO:0000269|PubMed:20682799, ECO:0000269|PubMed:21965678,
CC ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:28982712}.
CC -!- SUBUNIT: Component of the nucleosome-remodeling and histone-deacetylase
CC multiprotein complex (NuRD). Interacts with HDAC1 and ITGB3BP/CENPR (By
CC similarity). Binds to CSNK1G2 in the cytoplasm (PubMed:15077195).
CC Interacts with NACC2. Interacts with EP300, TFAP2C, IFI16, TPR,
CC UBE2I/UBC9, PIAS1, PIAS3, PIAS4, MDM2, COP1, SUMO1, SUMO2, SENP1 and
CC SENP2 (By similarity). Interacts with ARNTL/BMAL1 and CLOCK
CC (PubMed:24089055). Interacts with p53/TP53 (PubMed:19837670). Interacts
CC with HDAC2 (By similarity). Interacts with SIX3; facilitates the
CC binding of SIX3 to the core DNA motif of SIX3 promoter
CC (PubMed:17666527). Interacts with TFCP2L1; which is indispensable for
CC TFCP2L1-mediated self-renewal-promoting effect and endoderm-inhibiting
CC action (PubMed:28982712). Interacts with PWWP2A and PWWP2B
CC (PubMed:30228260, PubMed:34180153). {ECO:0000250|UniProtKB:Q13330,
CC ECO:0000269|PubMed:15077195, ECO:0000269|PubMed:17666527,
CC ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:20682799,
CC ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:28982712,
CC ECO:0000269|PubMed:30228260, ECO:0000269|PubMed:34180153}.
CC -!- INTERACTION:
CC Q8K4B0; Q64364: Cdkn2a; NbExp=2; IntAct=EBI-1216353, EBI-1202287;
CC Q8K4B0; Q62233: Six3; NbExp=2; IntAct=EBI-1216353, EBI-2297327;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus envelope {ECO:0000255|PROSITE-
CC ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. Cytoplasm.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with
CC microtubules. Primarily localized in the cytoplasm in embryonic
CC tissues. Localization at the nuclear envelope is TPR-dependent.
CC -!- TISSUE SPECIFICITY: Widely expressed but not in skeletal muscle. Highly
CC expressed in the brain, liver, kidney and cardiac muscle and in mammary
CC tumors. {ECO:0000269|PubMed:16617102, ECO:0000269|PubMed:24970816}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in embryonic nerve
CC tissues, such as the brain, eyes, and spinal cord.
CC -!- PTM: Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances
CC corepression of estrogen receptor (ER). {ECO:0000269|PubMed:15077195}.
CC -!- PTM: Acetylation is essential for its transcriptional coactivator
CC activity. {ECO:0000250}.
CC -!- PTM: Sumoylation positively regulates its transcriptional corepressor
CC activity but does not affect the protein stability. Sumoylated
CC preferentially by SUMO2 or SUMO3 than SUMO1. Sumoylation is enhanced by
CC PIAS1/3/4 and preferentially sumoylated by SUMO2 in the presence of
CC PIAS1/3/4. Desumoylated by SENP1 (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by COP1, which leads to proteasomal degradation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit a disruption of the free-running
CC period of circadian rhythms under constant light and normal entrainment
CC of behavior to light-dark (LD) cycles. {ECO:0000269|PubMed:24089055}.
CC -!- CAUTION: Was originally thought to play a role in inflammatory
CC responses both as a target and as a component of the NF-kappa-B
CC signaling, to interact with the HDAC2, and be induced by
CC lipopolysaccharide (LPS) (PubMed:20519513). However, this work was
CC later retracted (PubMed:28314777). Nevertheless, the interaction with
CC HDAC2 has been demonstrated by several publications in the human
CC ortholog. {ECO:0000269|PubMed:20519513, ECO:0000305|PubMed:28314777}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC57413.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF463504; AAM97588.1; -; mRNA.
DR EMBL; AF450245; AAM97587.1; -; Genomic_DNA.
DR EMBL; AF288137; AAK83044.1; -; mRNA.
DR EMBL; AB039744; BAC57413.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_006515485.1; XM_006515422.1.
DR AlphaFoldDB; Q8K4B0; -.
DR SMR; Q8K4B0; -.
DR BioGRID; 228045; 61.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-954; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q8K4B0; -.
DR DIP; DIP-38226N; -.
DR IntAct; Q8K4B0; 46.
DR MINT; Q8K4B0; -.
DR STRING; 10090.ENSMUSP00000009099; -.
DR iPTMnet; Q8K4B0; -.
DR PhosphoSitePlus; Q8K4B0; -.
DR EPD; Q8K4B0; -.
DR jPOST; Q8K4B0; -.
DR MaxQB; Q8K4B0; -.
DR PaxDb; Q8K4B0; -.
DR PRIDE; Q8K4B0; -.
DR ProteomicsDB; 290066; -.
DR Antibodypedia; 90; 437 antibodies from 37 providers.
DR Ensembl; ENSMUST00000009099; ENSMUSP00000009099; ENSMUSG00000021144.
DR UCSC; uc007pfw.1; mouse.
DR MGI; MGI:2150037; Mta1.
DR VEuPathDB; HostDB:ENSMUSG00000021144; -.
DR eggNOG; KOG3554; Eukaryota.
DR GeneTree; ENSGT01030000234573; -.
DR InParanoid; Q8K4B0; -.
DR OMA; HEWLILT; -.
DR OrthoDB; 802091at2759; -.
DR PhylomeDB; Q8K4B0; -.
DR TreeFam; TF106444; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-3232118; SUMOylation of transcription factors.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
DR BioGRID-ORCS; 116870; 8 hits in 97 CRISPR screens.
DR ChiTaRS; Mta1; mouse.
DR PRO; PR:Q8K4B0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8K4B0; protein.
DR Bgee; ENSMUSG00000021144; Expressed in somite and 254 other tissues.
DR ExpressionAtlas; Q8K4B0; baseline and differential.
DR Genevisible; Q8K4B0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016581; C:NuRD complex; IPI:MGI.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0045475; P:locomotor rhythm; IMP:UniProtKB.
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:1902499; P:positive regulation of protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
DR GO; GO:0033363; P:secretory granule organization; ISO:MGI.
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; 2.
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 Acetylation; Activator; Biological rhythms; Cytoplasm; Cytoskeleton;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..715
FT /note="Metastasis-associated protein MTA1"
FT /id="PRO_0000083494"
FT DOMAIN 1..164
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 165..276
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 283..335
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 393..420
FT /note="GATA-type; atypical"
FT REGION 437..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 545..552
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 696..705
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 711..715
FT /note="SUMO interaction motif 1 (SIM); crucial for
FT efficient sumoylation"
FT /evidence="ECO:0000250"
FT COMPBIAS 554..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13330"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13330"
FT MOD_RES 626
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13330"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13330"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13330"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2 and SUMO3)"
FT /evidence="ECO:0000250"
FT CROSSLNK 549
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13330"
FT CROSSLNK 626
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13330"
FT MUTAGEN 322
FT /note="S->A: Reduction in the ability of MTA1S to repress
FT ER transactivation."
FT /evidence="ECO:0000269|PubMed:15077195"
FT CONFLICT 64
FT /note="T -> R (in Ref. 2; AAK83044)"
FT /evidence="ECO:0000305"
FT CONFLICT 65..81
FT /note="Missing (in Ref. 2; AAK83044)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="C -> W (in Ref. 2; AAK83044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 80798 MW; 135152CD3554278D CRC64;
MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTANGNVEA KVVCFYRRRD ISSSLIALAD
KHATLSVCYR AGPGADTGEE GEVEEEVENP EMVDLPEKLK HQLRHRELFL SRQLESLPAT
HIRGKCSVTL LNETESLKSY LEREDFFFYS LVYDPQQKTL LADKGEIRVG NRYQADITDL
LKEGEEDGRD QSKLETKVWE AHNPLVDKQI DQFLVVARSV GTFARALDCS SSVRQPSLHM
SAAAASRDIT LFHAMDTLHK NIYDISKAIS ALVPQGGPVL CRDEMEEWSA SEANLFEEAL
EKYGKDFTDI QQDFLPWKSL TSIIEYYYMW KTTDRYVQQK RLKAAEAESK LKQVYIPNYN
KPNPNQISAS SVKATVVNGT GTPGQSPGAG RACESCYTTQ SYQWYSWGPP NMQCRLCASC
WTYWKKYGGL KMPTRLDGER PGPNRNNMSP HGIPARSSGS PKFAMKTRQA FYLHTTKLTR
IARRLCREIL RPWHAARHPY MPINSAAIKA ECTARLPEAS QSPLVLKQVV RKPLEAVLRY
LETHPRPPKP DPVKSSSSVL SSLTPAKSAP VINNGSPTIL GKRSYEQHNG VDGNMKKRLL
MPSRGLANHG QTRHMGPSRN LLLNGKSYPT KVRLIRGGSL PPVKRRRMNW IDAPDDVFYM
ATEETRKIRK LLSSSETKRA ARRPYKPIAL RQSQALPLRP PPPAPVNDEP IVIED
