| IED ID |
IndEnz0001000177 |
| Enzyme Type ID |
amylase000177 |
| Protein Name |
Metastasis-associated protein MTA1
|
| Gene Name |
Mta1 Zg29 |
| Organism |
Rattus norvegicus (Rat) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Euarchontoglires
Glires (Rodents and rabbits)
Rodentia
Myomorpha (mice and others)
Muroidea
Muridae
Murinae
Rattus
Rattus norvegicus (Rat)
|
| Enzyme Sequence |
MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSSLIALADKHATLSVCYRAGPGADTGEEGEVEEEVENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKDGEEDGRDQSKLETKVWEAHNPLVDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNSVKASVVNGTGTPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRNNMSPHGIPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYMPINSAAIKAECTARLPEASQSPLVLKQVVRKPLEAVLRYLETHPRPPKPDPVKSSSSVLSSLTPAKSAPVINNGSPTILGKRSYEQHNGVDGLANHGQTRHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPLRPPPPAPVNDEPIVIED |
| Enzyme Length |
703 |
| Uniprot Accession Number |
Q62599 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
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| catalytic Activity |
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| DNA Binding |
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| EC Number |
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| Enzyme Function |
FUNCTION: Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression (By similarity). Isoform 2 may be involved in the sorting of amylase during zymogen granule formation in the pancreas. With Tfcp2l1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity). {ECO:0000250|UniProtKB:Q13330, ECO:0000250|UniProtKB:Q8K4B0, ECO:0000269|PubMed:10933808}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
|
| Features |
Alternative sequence (2); Chain (1); Compositional bias (1); Cross-link (4); Domain (3); Modified residue (8); Motif (3); Region (3); Zinc finger (1) |
| Keywords |
Acetylation;Activator;Alternative initiation;Alternative splicing;Biological rhythms;Cytoplasm;Cytoplasmic vesicle;Cytoskeleton;DNA-binding;Endoplasmic reticulum;Golgi apparatus;Isopeptide bond;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Repressor;Transcription;Transcription regulation;Ubl conjugation;Zinc;Zinc-finger |
| Interact With |
Q9ET75 |
| Induction |
INDUCTION: [Isoform 1]: Induced by dexamethasone and, in pancreas, by treatment with the proteinase inhibitor FOY-305 which binds to activated trypsin and induces release of cholecystokinin. {ECO:0000269|PubMed:10393810}. |
| Subcellular Location |
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:10393810}. Nucleus envelope {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with microtubules. Localization at the nuclear envelope is TPR-dependent (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Rough endoplasmic reticulum {ECO:0000269|PubMed:10393810}. Golgi apparatus {ECO:0000269|PubMed:10393810}. Zymogen granule {ECO:0000269|PubMed:10393810}. |
| Modified Residue |
MOD_RES 386; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q13330; MOD_RES 449; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q13330; MOD_RES 522; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 564; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q13330; MOD_RES 576; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 578; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q13330; MOD_RES 614; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q13330; MOD_RES 627; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q13330 |
| Post Translational Modification |
PTM: Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances corepression of estrogen receptor (ER). {ECO:0000250}.; PTM: Acetylation is essential for its transcriptional coactivator activity. {ECO:0000250}.; PTM: Sumoylation positively regulates its transcriptional corepressor activity but does not affect the protein stability. Sumoylated preferentially by SUMO2 or SUMO3 than SUMO1. Sumoylation is enhanced by PIAS1/3/4 and preferentially sumoylated by SUMO2 in the presence of PIAS1/3/4. Desumoylated by SENP1 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by COP1, which leads to proteasomal degradation. {ECO:0000250}. |
| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
14760703;
15942958;
17666527;
18067919;
20010697;
25217305;
|
| Motif |
MOTIF 545..552; /note=SH3-binding; /evidence=ECO:0000255; MOTIF 684..693; /note=SH3-binding; /evidence=ECO:0000255; MOTIF 699..703; /note=SUMO interaction motif 1 (SIM); crucial for efficient sumoylation; /evidence=ECO:0000250 |
| Gene Encoded By |
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| Mass |
79,412 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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