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O94776 (MTA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metastasis-associated protein MTA2
Alternative name(s):
Metastasis-associated 1-like 1
Short name=MTA1-L1 protein
p53 target protein in deacetylase complex
Gene names
Name:MTA2
Synonyms:MTA1L1, PID
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length668 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins.

Subunit structure

Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC7, p53/TP53, MINT and MBD3 By similarity. Interacts with FAM64A. Ref.4 Ref.9

Subcellular location

Nucleus By similarity.

Tissue specificity

Widely expressed.

Sequence similarities

Contains 1 BAH domain.

Contains 1 ELM2 domain.

Contains 1 GATA-type zinc finger.

Contains 1 SANT domain.

Sequence caution

The sequence AAH23656.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from electronic annotation. Source: Ensembl

chromatin assembly or disassembly

Traceable author statement PubMed 10444591. Source: ProtInc

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentNuRD complex

Inferred from direct assay PubMed 19644445. Source: UniProtKB

histone deacetylase complex

Traceable author statement PubMed 10444591. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

transcription factor complex

Inferred from direct assay PubMed 15920471. Source: BHF-UCL

   Molecular_functionRNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 22926524. Source: BHF-UCL

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 15920471. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: InterPro

histone deacetylase activity

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 668668Metastasis-associated protein MTA2
PRO_0000083496

Regions

Domain1 – 144144BAH
Domain145 – 256112ELM2
Domain263 – 31553SANT
Zinc finger367 – 39428GATA-type; atypical

Amino acid modifications

Modified residue1521N6-acetyllysine Ref.11
Modified residue4331Phosphoserine Ref.8
Modified residue4351Phosphoserine Ref.8 Ref.10 Ref.12
Modified residue4601N6-acetyllysine By similarity
Modified residue5221N6-acetyllysine By similarity
Modified residue5311N6-acetyllysine By similarity
Modified residue5341Phosphothreonine Ref.12
Modified residue5481Phosphoserine Ref.14

Experimental info

Sequence conflict751V → M in BAA36707. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O94776 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 65087AF798BA64EC

FASTA66875,023
        10         20         30         40         50         60 
MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD ISSSLNSLAD 

        70         80         90        100        110        120 
SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT HIRGKCSVTL LNETDILSQY 

       130        140        150        160        170        180 
LEKEDCFFYS LVFDPVQKTL LADQGEIRVG CKYQAEIPDR LVEGESDNRN QQKMEMKVWD 

       190        200        210        220        230        240 
PDNPLTDRQI DQFLVVARAV GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR 

       250        260        270        280        290        300 
NGYDLAKAMS TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL 

       310        320        330        340        350        360 
ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV GSKPGMNGAG 

       370        380        390        400        410        420 
FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK YGGLKTPTQL EGATRGTTEP 

       430        440        450        460        470        480 
HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN RQTFLLQTTK LTRLARRMCR DLLQPRRAAR 

       490        500        510        520        530        540 
RPYAPINANA IKAECSIRLP KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT 

       550        560        570        580        590        600 
PINRNQLSQN RGLGGIMVKR AYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD 

       610        620        630        640        650        660 
APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLIAVRPPVP LPAPSHPAST 


NEPIVLED 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, mapping and characterization of a novel human gene, MTA1-L1. showing homology to a metastasis-associated gene, MTA1."
Futamura M., Nishimori H., Shiratsuchi T., Saji S., Nakamura Y., Tokino T.
J. Hum. Genet. 44:52-56(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Deacetylation of p53 modulates its effect on cell growth and apoptosis."
Luo J., Su F., Chen D., Shiloh A., Gu W.
Nature 408:377-381(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
Tissue: Brain and Uterus.
[4]"Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MINT.
[5]"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.
[6]"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.
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-433 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"RCS1, a substrate of APC/C, controls the metaphase to anaphase transition."
Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III, Fang G.
Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FAM64A.
[10]"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-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-435 AND THR-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012922 Genomic DNA. Translation: BAA36562.1.
AB016591 mRNA. Translation: BAA36707.1.
AF295807 mRNA. Translation: AAG02241.1.
BC023656 mRNA. Translation: AAH23656.1. Sequence problems.
BC053650 mRNA. Translation: AAH53650.1.
RefSeqNP_004730.2. NM_004739.3.
UniGeneHs.173043.

3D structure databases

ProteinModelPortalO94776.
SMRO94776. Positions 5-141, 145-321, 366-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114652. 89 interactions.
DIPDIP-46519N.
IntActO94776. 28 interactions.
STRING9606.ENSP00000278823.

PTM databases

PhosphoSiteO94776.

Proteomic databases

PaxDbO94776.
PeptideAtlasO94776.
PRIDEO94776.

Protocols and materials databases

DNASU9219.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278823; ENSP00000278823; ENSG00000149480.
GeneID9219.
KEGGhsa:9219.
UCSCuc001ntq.2. human.

Organism-specific databases

CTD9219.
GeneCardsGC11M062360.
HGNCHGNC:7411. MTA2.
HPACAB005315.
CAB017522.
HPA006214.
MIM603947. gene.
neXtProtNX_O94776.
PharmGKBPA31219.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG252834.
HOGENOMHOG000045387.
HOVERGENHBG002598.
InParanoidO94776.
KOK11660.
OMANAVKAEC.
OrthoDBEOG780RM1.
PhylomeDBO94776.
TreeFamTF106444.

Gene expression databases

ArrayExpressO94776.
BgeeO94776.
CleanExHS_MTA2.
GenevestigatorO94776.

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

ChiTaRSMTA2. human.
GeneWikiMTA2.
GenomeRNAi9219.
NextBio34563.
PROO94776.
SOURCESearch...

Entry information

Entry nameMTA2_HUMAN
AccessionPrimary (citable) accession number: O94776
Secondary accession number(s): Q9UQB5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 126 of the entry and version 1 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

MIM cross-references

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

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM