Q9R190 · MTA2_MOUSE
- ProteinMetastasis-associated protein MTA2
- GeneMta2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids668 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMetastasis-associated protein MTA2
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9R190
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000083497 | 1-668 | Metastasis-associated protein MTA2 | |||
Sequence: MAANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEESKQPGVSEQQRHQLKHRELFLSRQFESLPATHIRGKCSVTLLNETDILNQYLDKEDCFFYSLVFDPVQKTLLADQGEIRVGCKFQAEIPDRLAEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQRNGYDLAKAMSTLVPQGGPVLCRDEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKTTDRYIQQKRLKAAEADSKLKQVYIPTYTKPNPNQIISVGSKPGMNGAGFQKGLTCESCHTTQSAQWYAWGPPNMQCRLCASCWIYWKKYGGLKTPTQLEGAARGTTEPHSRGHLSRPEAQSLSPYTTSANRAKLLAKNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLVRLPLATIVKDLVAQAPLKPKTPRGTKTPINRNQLTQNRGLGGIMVKRSYETMAGAGVPFSANGRPLASGIRSSSQPAAKRQKLNPADAPNPVVFVATKDTRALRKALTHLEMRRAARRPNLPLKVKPTLMTVRPPVPLPASSHPASTNEPIVLED | ||||||
Modified residue | 52 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 54 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 152 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 433 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 435 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 460 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 492 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3); alternate | ||||
Sequence: K | ||||||
Cross-link | 492 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Cross-link | 508 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 522 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 531 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 534 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 559 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 595 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9R190 | Esrrb Q61539 | 3 | EBI-904134, EBI-2312731 | |
BINARY | Q9R190 | Hdac1 O09106 | 7 | EBI-904134, EBI-301912 | |
BINARY | Q9R190 | Hdac2 P70288 | 7 | EBI-904134, EBI-302251 | |
BINARY | Q9R190 | Nr4a1 P12813 | 2 | EBI-904134, EBI-10896863 | |
BINARY | Q9R190 | Pou5f1 P20263 | 6 | EBI-904134, EBI-1606219 | |
BINARY | Q9R190 | Sall4 Q8BX22 | 3 | EBI-904134, EBI-2312582 | |
BINARY | Q9R190 | Satb2 Q8VI24 | 2 | EBI-904134, EBI-5737999 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, zinc finger, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-144 | BAH | ||||
Sequence: MAANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEESKQPGVSEQQRHQLKHRELFLSRQFESLPATHIRGKCSVTLLNETDILNQYLDKEDCFFYSLVFDPVQKTLLADQ | ||||||
Domain | 145-256 | ELM2 | ||||
Sequence: GEIRVGCKFQAEIPDRLAEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQRNGYDLAKAMSTLVPQG | ||||||
Domain | 263-315 | SANT | ||||
Sequence: DEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKTTDR | ||||||
Zinc finger | 367-394 | GATA-type; atypical | ||||
Sequence: CESCHTTQSAQWYAWGPPNMQCRLCASC | ||||||
Region | 412-437 | Disordered | ||||
Sequence: GAARGTTEPHSRGHLSRPEAQSLSPY | ||||||
Region | 580-599 | Disordered | ||||
Sequence: ASGIRSSSQPAAKRQKLNPA | ||||||
Region | 647-668 | Disordered | ||||
Sequence: PPVPLPASSHPASTNEPIVLED |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length668
- Mass (Da)75,030
- Last updated2000-05-01 v1
- Checksum88996F779BA6F4D1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 489 | in Ref. 4; BAC40180 | ||||
Sequence: N → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |