Q9R190 · MTA2_MOUSE

  • Protein
    Metastasis-associated protein MTA2
  • Gene
    Mta2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May function as a transcriptional coregulator (By similarity).
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity).

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 Componentchromosome, telomeric region
Cellular Componenthistone deacetylase complex
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentNuRD complex
Molecular Functionchromatin binding
Molecular Functionhistone deacetylase activity
Molecular Functionhistone deacetylase binding
Molecular Functionmetal ion binding
Molecular FunctionRNA polymerase II-specific DNA-binding transcription factor binding
Molecular Functionsequence-specific DNA binding
Molecular Functiontranscription coactivator activity
Molecular Functiontranscription coregulator activity
Molecular Functiontranscription corepressor activity
Biological Processchromatin remodeling
Biological Processchromosome organization
Biological Processgenomic imprinting
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 transcription by RNA polymerase II
Biological Processregulation of cell fate specification
Biological Processregulation of fibroblast migration
Biological Processregulation of stem cell differentiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Metastasis-associated protein MTA2
  • Alternative names
    • Metastasis-associated 1-like 1

Gene names

    • Name
      Mta2
    • Synonyms
      Mta1l1

Organism names

  • Taxonomic identifier
  • Strains
    • 129/SvJ
    • C57BL/6J
    • NOD
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9R190
  • Secondary accessions
    • Q3TVT8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00000834971-668Metastasis-associated protein MTA2
Modified residue52Phosphoserine
Modified residue54Phosphoserine
Modified residue152N6-acetyllysine
Modified residue433Phosphoserine
Modified residue435Phosphoserine
Modified residue460N6-acetyllysine
Cross-link492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3); alternate
Cross-link492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link508Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue522N6-acetyllysine
Modified residue531N6-acetyllysine
Modified residue534Phosphothreonine
Cross-link559Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Gene expression 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:10444591, PubMed:27806305).
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:27806305).
Interacts with CHD3 (By similarity).
Interacts with CHD4 (By similarity).
Interacts with GATAD2A (By similarity).
Interacts with HDAC7 (PubMed:10984530).
Interacts with MBD3 (PubMed:12124384).
Interacts with p53/TP53 (By similarity).
Interacts with MINT (By similarity).
Interacts with PIMREG (By similarity).
Interacts with NACC2 (By similarity).
Interacts with ERCC6 (By similarity).
Interacts with PWWP2B (PubMed:34180153).

Binary interactions

View interactors in UniProtKB
View CPX-953 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, zinc finger, region.

TypeIDPosition(s)Description
Domain1-144BAH
Domain145-256ELM2
Domain263-315SANT
Zinc finger367-394GATA-type; atypical
Region412-437Disordered
Region580-599Disordered
Region647-668Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    668
  • Mass (Da)
    75,030
  • Last updated
    2000-05-01 v1
  • Checksum
    88996F779BA6F4D1
MAANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEESKQPGVSEQQRHQLKHRELFLSRQFESLPATHIRGKCSVTLLNETDILNQYLDKEDCFFYSLVFDPVQKTLLADQGEIRVGCKFQAEIPDRLAEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQRNGYDLAKAMSTLVPQGGPVLCRDEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKTTDRYIQQKRLKAAEADSKLKQVYIPTYTKPNPNQIISVGSKPGMNGAGFQKGLTCESCHTTQSAQWYAWGPPNMQCRLCASCWIYWKKYGGLKTPTQLEGAARGTTEPHSRGHLSRPEAQSLSPYTTSANRAKLLAKNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLVRLPLATIVKDLVAQAPLKPKTPRGTKTPINRNQLTQNRGLGGIMVKRSYETMAGAGVPFSANGRPLASGIRSSSQPAAKRQKLNPADAPNPVVFVATKDTRALRKALTHLEMRRAARRPNLPLKVKPTLMTVRPPVPLPASSHPASTNEPIVLED

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict489in Ref. 4; BAC40180

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF159259
EMBL· GenBank· DDBJ
AAD51281.1
EMBL· GenBank· DDBJ
mRNA
AF348083
EMBL· GenBank· DDBJ
AAL30174.1
EMBL· GenBank· DDBJ
Genomic DNA
AB047977
EMBL· GenBank· DDBJ
BAB79231.1
EMBL· GenBank· DDBJ
Genomic DNA
AK088158
EMBL· GenBank· DDBJ
BAC40180.1
EMBL· GenBank· DDBJ
mRNA
AK147099
EMBL· GenBank· DDBJ
BAE27675.1
EMBL· GenBank· DDBJ
mRNA
AK159979
EMBL· GenBank· DDBJ
BAE35530.1
EMBL· GenBank· DDBJ
mRNA
BC079847
EMBL· GenBank· DDBJ
AAH79847.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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