Q9BTC8 · MTA3_HUMAN

  • Protein
    Metastasis-associated protein MTA3
  • Gene
    MTA3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:12705869, PubMed:16428440, PubMed:28977666).
Plays a role in maintenance of the normal epithelial architecture through the repression of SNAI1 transcription in a histone deacetylase-dependent manner, and thus the regulation of E-cadherin levels (PubMed:12705869).
Contributes to transcriptional repression by BCL6 (PubMed:15454082).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentintracellular membrane-bounded organelle
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentNuRD complex
Molecular Functionchromatin binding
Molecular Functionhistone deacetylase binding
Molecular Functionmetal ion binding
Molecular Functionsequence-specific DNA binding
Molecular Functiontranscription coactivator activity
Molecular Functiontranscription corepressor activity
Biological Processchromatin remodeling
Biological ProcessG2/M transition of mitotic cell cycle
Biological Processgranulosa cell proliferation
Biological Processnegative regulation of DNA-templated transcription
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of G2/M transition of mitotic cell cycle
Biological Processpositive regulation of granulosa cell proliferation
Biological Processregulation of cell fate specification
Biological Processregulation of stem cell differentiation

Keywords

Enzyme and pathway databases

Community curation (1)

The subsequence GAVNGAVGTTFQPQNPLLGRACESCYATQSHQWYSWGPPNMQCRLCAICWLYWKKYGGLKMPTQSEEEKLSPSPTTEDPR, which contains the GATA domain, shows transcriptional activator activity in a high-throughput recruitment assay.

Names & Taxonomy

Protein names

  • Recommended name
    Metastasis-associated protein MTA3

Gene names

    • Name
      MTA3
    • Synonyms
      KIAA1266
Community curation (1)

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9BTC8
  • Secondary accessions
    • Q9NSP2
    • Q9ULF4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 628 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00000834981-594UniProtMetastasis-associated protein MTA3
Modified residue (large scale data)422PRIDEPhosphoserine
Modified residue428UniProtPhosphoserine
Modified residue (large scale data)428PRIDEPhosphoserine
Modified residue430UniProtPhosphoserine
Modified residue (large scale data)430PRIDEPhosphoserine
Modified residue (large scale data)432PRIDEPhosphothreonine
Modified residue455UniProtPhosphothreonine
Modified residue (large scale data)455PRIDEPhosphothreonine
Modified residue (large scale data)457PRIDEPhosphoserine
Modified residue (large scale data)517PRIDEPhosphoserine
Modified residue519UniProtPhosphoserine
Modified residue (large scale data)519PRIDEPhosphoserine
Modified residue (large scale data)593PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in germinal centers of lymphoid tissues. No expression in nonepithelial cells.

Induction

By estrogen.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the nucleosome remodeling and deacetylase (NuRD) repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4, RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5 (PubMed:12705869, PubMed:15454082, PubMed:16428440, PubMed:28977666, PubMed:33283408).
The exact stoichiometry of the NuRD complex is unknown, and some subunits such as MBD2 and MBD3, GATAD2A and GATAD2B, and CHD3, CHD4 and CHD5 define mutually exclusive NuRD complexes (PubMed:16428440, PubMed:28977666).
Interacts with BCL6 (PubMed:15454082).
Interacts with NACC2 (PubMed:22926524).
Interacts with PWWP2B (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9BTC8EHMT2 Q96KQ718EBI-2461787, EBI-744366
BINARY Q9BTC8GATA3 P2377118EBI-2461787, EBI-6664760
View interactors in UniProtKB
View CPX-880 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, zinc finger.

TypeIDPosition(s)Description
Domain1-147BAH
Domain148-259ELM2
Domain266-318SANT
Zinc finger379-406GATA-type; atypical

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9BTC8-1

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.

  • Length
    594
  • Mass (Da)
    67,504
  • Last updated
    2003-02-28 v2
  • Checksum
    E773603F65A16DF1
MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTASGNVEAKVVCFYRRRDISNTLIMLADKHAKEIEEESETTVEADLTDKQKHQLKHRELFLSRQYESLPATHIRGKCSVALLNETESVLSYLDKEDTFFYSLVYDPSLKTLLADKGEIRVGPRYQADIPEMLLEGESDEREQSKLEVKVWDPNSPLTDRQIDQFLVVARAVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLYRHSYDLSSAISVLVPLGGPVLCRDEMEEWSASEASLFEEALEKYGKDFNDIRQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPTYSKPNPNQISTSNGKPGAVNGAVGTTFQPQNPLLGRACESCYATQSHQWYSWGPPNMQCRLCAICWLYWKKYGGLKMPTQSEEEKLSPSPTTEDPRVRSHVSRQAMQGMPVRNTGSPKSAVKTRQAFFLHTTYFTKFARQVCKNTLRLRQAARRPFVAINYAAIRAEYADRHAELSGSPLKSKSTRKPLACIIGYLEIHPAKKPNVIRSTPSLQTPTTKRMLTTPNHTSLSILGKRNYSHHNGLDELTCCVSD

Q9BTC8-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E7EV10E7EV10_HUMANMTA3590
E7EQY4E7EQY4_HUMANMTA3514
C9JR73C9JR73_HUMANMTA317
F6RRE2F6RRE2_HUMANMTA3537
E9PF88E9PF88_HUMANMTA391
E9PCS8E9PCS8_HUMANMTA3392

Sequence caution

The sequence BAA86580.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict1-9in Ref. 1; BAA86580
Sequence conflict343in Ref. 1; BAA86580
Alternative sequenceVSP_001603509-515in isoform 2
Alternative sequenceVSP_001604516-594in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB033092
EMBL· GenBank· DDBJ
BAA86580.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK027304
EMBL· GenBank· DDBJ
BAB55028.1
EMBL· GenBank· DDBJ
mRNA
BC004227
EMBL· GenBank· DDBJ
AAH04227.1
EMBL· GenBank· DDBJ
mRNA
BC053631
EMBL· GenBank· DDBJ
AAH53631.1
EMBL· GenBank· DDBJ
mRNA
AL161954
EMBL· GenBank· DDBJ
CAB82305.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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