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Q13330 (MTA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metastasis-associated protein MTA1
Gene names
Name:MTA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length715 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the regulation of gene expression by covalent modification of histone proteins. Isoform Long is a corepressor of estrogen receptor (ER). Isoform Short binds to ER and sequesters it in the cytoplasm and enhances non-genomic responses of ER.

Subunit structure

Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC1 and ITGB3BP/CENPR. Binds to CSNK1G2 in the cytoplasm. Ref.7 Ref.8 Ref.9

Subcellular location

Isoform Short: Cytoplasm Ref.3 Ref.9.

Isoform Long: Nucleus Ref.3 Ref.9.

Tissue specificity

Widely expressed. High expression in brain, ovaries, adrenal glands and virgin mammary glands. Higher in tumors than in adjacent normal tissue from the same individual.

Developmental stage

Highly expressed in metastatic cells.

Domain

Isoform Short contains a Leu-Arg-Ile-Leu-Leu motif (ER binding motif).

Post-translational modification

Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances corepression of estrogen receptor (ER).

Sequence similarities

Contains 1 BAH domain.

Contains 1 ELM2 domain.

Contains 1 GATA-type zinc finger.

Contains 1 SANT domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q13330-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q13330-2)

Also known as: MTA1S;

The sequence of this isoform differs from the canonical sequence as follows:
     398-430: TTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGL → MSSLRILLDILEEIWWLENANPVRWREARTKPQ
     431-715: Missing.
Isoform 3 (identifier: Q13330-3)

The sequence of this isoform differs from the canonical sequence as follows:
     64-81: TLSVCYKAGPGADNGEEG → R

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 715715Metastasis-associated protein MTA1
PRO_0000083493

Regions

Domain1 – 164164BAH
Domain165 – 276112ELM2
Domain283 – 33553SANT
Zinc finger393 – 42028GATA-type; atypical
Motif545 – 5528SH3-binding Potential
Motif696 – 70510SH3-binding Potential
Compositional bias697 – 7059Poly-Pro

Amino acid modifications

Modified residue3861Phosphoserine Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19
Modified residue4461Phosphoserine Ref.17 Ref.19
Modified residue4491Phosphoserine Ref.14 Ref.17 Ref.19
Modified residue5221Phosphoserine Ref.14 Ref.16 Ref.17 Ref.19
Modified residue5641Phosphothreonine Ref.11 Ref.14 Ref.16
Modified residue5761Phosphoserine Ref.14 Ref.16 Ref.17 Ref.19
Modified residue5781Phosphothreonine Ref.16 Ref.17 Ref.19
Modified residue6391Phosphoserine Ref.19

Natural variations

Alternative sequence64 – 8118TLSVC…NGEEG → R in isoform 3.
VSP_042207
Alternative sequence398 – 43033TTQSY…KYGGL → MSSLRILLDILEEIWWLENA NPVRWREARTKPQ in isoform Short.
VSP_001601
Alternative sequence431 – 715285Missing in isoform Short.
VSP_001602
Natural variant3721V → I.
Corresponds to variant rs4983413 [ dbSNP | Ensembl ].
VAR_055847
Natural variant6121A → T. Ref.1 Ref.2 Ref.5
Corresponds to variant rs13707 [ dbSNP | Ensembl ].
VAR_058965

Experimental info

Sequence conflict4981H → N in AAA78935. Ref.1
Sequence conflict5451P → R in AAI42942. Ref.5
Sequence conflict6551D → G in AAA78935. Ref.1
Sequence conflict661 – 6622AT → PK in AAA78935. Ref.1

Secondary structure

....................... 715
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 2D5330F0489AE62E

FASTA71580,786
        10         20         30         40         50         60 
MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTANGNVEA KVVCFYRRRD ISSTLIALAD 

        70         80         90        100        110        120 
KHATLSVCYK AGPGADNGEE GEIEEEMENP EMVDLPEKLK HQLRHRELFL SRQLESLPAT 

       130        140        150        160        170        180 
HIRGKCSVTL LNETESLKSY LEREDFFFYS LVYDPQQKTL LADKGEIRVG NRYQADITDL 

       190        200        210        220        230        240 
LKEGEEDGRD QSRLETQVWE AHNPLTDKQI DQFLVVARSV GTFARALDCS SSVRQPSLHM 

       250        260        270        280        290        300 
SAAAASRDIT LFHAMDTLHK NIYDISKAIS ALVPQGGPVL CRDEMEEWSA SEANLFEEAL 

       310        320        330        340        350        360 
EKYGKDFTDI QQDFLPWKSL TSIIEYYYMW KTTDRYVQQK RLKAAEAESK LKQVYIPNYN 

       370        380        390        400        410        420 
KPNPNQISVN NVKAGVVNGT GAPGQSPGAG RACESCYTTQ SYQWYSWGPP NMQCRLCASC 

       430        440        450        460        470        480 
WTYWKKYGGL KMPTRLDGER PGPNRSNMSP HGLPARSSGS PKFAMKTRQA FYLHTTKLTR 

       490        500        510        520        530        540 
IARRLCREIL RPWHAARHPY LPINSAAIKA ECTARLPEAS QSPLVLKQAV RKPLEAVLRY 

       550        560        570        580        590        600 
LETHPRPPKP DPVKSVSSVL SSLTPAKVAP VINNGSPTIL GKRSYEQHNG VDGNMKKRLL 

       610        620        630        640        650        660 
MPSRGLANHG QARHMGPSRN LLLNGKSYPT KVRLIRGGSL PPVKRRRMNW IDAPDDVFYM 

       670        680        690        700        710 
ATEETRKIRK LLSSSETKRA ARRPYKPIAL RQSQALPPRP PPPAPVNDEP IVIED 

« Hide

Isoform Short (MTA1S) [UniParc].

Checksum: DE4B752E9476C6CE
Show »

FASTA43049,017
Isoform 3 [UniParc].

Checksum: BCF775330376172E
Show »

FASTA69879,192

References

« Hide 'large scale' references
[1]"A novel candidate metastasis-associated gene, mta1, differentially expressed in highly metastatic mammary adenocarcinoma cell lines. cDNA cloning, expression, and protein analyses."
Toh Y., Pencil S.D., Nicolson G.L.
J. Biol. Chem. 269:22958-22963(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT THR-612.
[2]"Analysis of the complete sequence of the novel metastasis-associated candidate gene, mta1, differentially expressed in mammary adenocarcinoma and breast cancer cell lines."
Toh Y., Pencil S.D., Nicolson G.L.
Gene 159:97-104(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT THR-612.
[3]"A naturally occurring MTA1 variant sequesters oestrogen receptor-alpha in the cytoplasm."
Kumar R., Wang R.-A., Mazumdar A., Talukder A.H., Mandal M., Yang Z., Bagheri-Yarmand R., Sahin A., Hortobagyi G., Adam L., Barnes C.J., Vadlamudi R.K.
Nature 418:654-657(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), SUBCELLULAR LOCATION.
Tissue: Mammary gland.
[4]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT THR-612.
Tissue: Brain.
[6]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-299 (ISOFORM 3).
Tissue: Cervix carcinoma.
[7]"NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities."
Xue Y., Wong J., Moreno G.T., Young M.K., Cote J., Wang W.
Mol. Cell 2:851-861(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN NURD COMPLEX.
[8]"Metastasis-associated protein 1 interacts with NRIF3, an estrogen-inducible nuclear receptor coregulator."
Talukder A.H., Gururaj A., Mishra S.K., Vadlamudi R.K., Kumar R.
Mol. Cell. Biol. 24:6581-6591(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB3BP.
[9]"Metastatic tumor antigen 1 short form (MTA1s) associates with casein kinase I-gamma2, an estrogen-responsive kinase."
Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.
Oncogene 23:4422-4429(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CSNK1G2/CK1, INTERACTION WITH CSNK1G2, SUBCELLULAR LOCATION.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND THR-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-449; SER-522; THR-564 AND SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-522; THR-564; SER-576 AND THR-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-446; SER-449; SER-522; SER-576 AND THR-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-446; SER-449; SER-522; SER-576; THR-578 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U35113 mRNA. Translation: AAA78935.1.
AF508978 mRNA. Translation: AAN01613.1.
AL928654 Genomic DNA. No translation available.
BC009443 mRNA. Translation: AAH09443.2.
BC142941 mRNA. Translation: AAI42942.1.
BX248776 mRNA. Translation: CAD66583.1.
CCDSCCDS32169.1. [Q13330-1]
CCDS55954.1. [Q13330-2]
RefSeqNP_001190187.1. NM_001203258.1. [Q13330-2]
NP_004680.2. NM_004689.3. [Q13330-1]
UniGeneHs.525629.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BKXX-ray3.00A162-335[»]
ProteinModelPortalQ13330.
SMRQ13330. Positions 165-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114562. 59 interactions.
DIPDIP-41751N.
IntActQ13330. 12 interactions.
MINTMINT-255103.
STRING9606.ENSP00000333633.

PTM databases

PhosphoSiteQ13330.

Polymorphism databases

DMDM259016275.

Proteomic databases

MaxQBQ13330.
PaxDbQ13330.
PRIDEQ13330.

Protocols and materials databases

DNASU9112.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331320; ENSP00000333633; ENSG00000182979. [Q13330-1]
ENST00000405646; ENSP00000384180; ENSG00000182979. [Q13330-3]
ENST00000438610; ENSP00000393438; ENSG00000182979. [Q13330-2]
ENST00000603608; ENSP00000473898; ENSG00000270410. [Q13330-1]
ENST00000603666; ENSP00000474399; ENSG00000270410. [Q13330-3]
ENST00000604408; ENSP00000474289; ENSG00000270410. [Q13330-2]
GeneID9112.
KEGGhsa:9112.
UCSCuc001yqx.3. human. [Q13330-1]
uc001yqy.3. human. [Q13330-2]

Organism-specific databases

CTD9112.
GeneCardsGC14P105886.
HGNCHGNC:7410. MTA1.
HPACAB004508.
HPA005544.
MIM603526. gene.
neXtProtNX_Q13330.
PharmGKBPA31218.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG252834.
HOGENOMHOG000045387.
HOVERGENHBG002598.
InParanoidQ13330.
KOK11660.
OMADKHATLS.
OrthoDBEOG780RM1.
PhylomeDBQ13330.
TreeFamTF106444.

Gene expression databases

ArrayExpressQ13330.
BgeeQ13330.
CleanExHS_MTA1.
GenevestigatorQ13330.

Family and domain databases

InterProIPR001025. BAH_dom.
IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR000679. Znf_GATA.
[Graphical view]
PfamPF01426. BAH. 1 hit.
PF01448. ELM2. 1 hit.
PF00320. GATA. 1 hit.
[Graphical view]
SMARTSM00439. BAH. 1 hit.
SM00717. SANT. 1 hit.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS51038. BAH. 1 hit.
PS51156. ELM2. 1 hit.
PS51293. SANT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMTA1. human.
GeneWikiMTA1.
GenomeRNAi9112.
NextBio34153.
PROQ13330.
SOURCESearch...

Entry information

Entry nameMTA1_HUMAN
AccessionPrimary (citable) accession number: Q13330
Secondary accession number(s): A5PLK4 expand/collapse secondary AC list , Q86SW2, Q8NFI8, Q96GI8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM