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Q8K4B0

- MTA1_MOUSE

UniProt

Q8K4B0 - MTA1_MOUSE

Protein

Metastasis-associated protein MTA1

Gene

Mta1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    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. Plays a role in the inflammatory responses, both as a target and as a component of the NF-kappa-B signaling and regulates a subset of proinflammatory cytokines such as IL1B, MIP2, and TNF. 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.8 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri393 – 42028GATA-type; atypicalAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. protein binding Source: MGI
    3. sequence-specific DNA binding Source: InterPro
    4. sequence-specific DNA binding transcription factor activity Source: InterPro
    5. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metastasis-associated protein MTA1
    Gene namesi
    Name:Mta1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:2150037. Mta1.

    Subcellular locationi

    Nucleus. Nucleus envelope PROSITE-ProRule annotation. Cytoplasm. Cytoplasmcytoskeleton By similarity
    Note: Associated with microtubules. Primarily localized in the cytoplasm in embryonic tissues. Localization at the nuclear envelope is TPR-dependent.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: MGI
    3. NuRD complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice exhibit a disruption of the free-running period of circadian rhythms under constant light and normal entrainment of behavior to light-dark (LD) cycles.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi322 – 3221S → A: Reduction in the ability of MTA1S to repress ER transactivation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 715715Metastasis-associated protein MTA1PRO_0000083494Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki182 – 182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei386 – 3861PhosphoserineBy similarity
    Modified residuei449 – 4491PhosphoserineBy similarity
    Cross-linki509 – 509Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)By similarity
    Modified residuei522 – 5221PhosphoserineBy similarity
    Modified residuei564 – 5641Phosphothreonine2 Publications
    Modified residuei576 – 5761PhosphoserineBy similarity
    Modified residuei578 – 5781PhosphothreonineBy similarity
    Modified residuei626 – 6261N6-acetyllysineBy similarity
    Cross-linki626 – 626Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei639 – 6391PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances corepression of estrogen receptor (ER).2 Publications
    Acetylation is essential for its transcriptional coactivator activity.By similarity
    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.By similarity
    Ubiquitinated by RFWD2, which leads to proteasomal degradation.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8K4B0.
    PaxDbiQ8K4B0.
    PRIDEiQ8K4B0.

    PTM databases

    PhosphoSiteiQ8K4B0.

    Expressioni

    Tissue specificityi

    Widely expressed but not in skeletal muscle. Highly expressed in the brain, liver, kidney and cardiac muscle and in mammary tumors.2 Publications

    Developmental stagei

    Expressed at high levels in embryonic nerve tissues, such as the brain, eyes, and spinal cord.

    Inductioni

    By lipopolyssacharide (LPS).1 Publication

    Gene expression databases

    ArrayExpressiQ8K4B0.
    BgeeiQ8K4B0.
    CleanExiMM_MTA1.
    GenevestigatoriQ8K4B0.

    Interactioni

    Subunit structurei

    Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC1 and ITGB3BP/CENPR By similarity. Binds to CSNK1G2 in the cytoplasm. Interacts with NACC2. Interacts with EP300, TFAP2C, IFI16, TPR, UBE2I/UBC9, PIAS1, PIAS3, PIAS4, MDM2, RFWD2, SUMO1, SUMO2, SENP1 and SENP2 By similarity. Interacts with ARNTL/BMAL1 and CLOCK. Interacts with p53/TP53, SIX3 and HDAC2.By similarity5 Publications

    Protein-protein interaction databases

    DIPiDIP-38226N.
    IntActiQ8K4B0. 9 interactions.
    MINTiMINT-1350646.
    STRINGi10090.ENSMUSP00000105349.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K4B0.
    SMRiQ8K4B0. Positions 165-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 164164BAHPROSITE-ProRule annotationAdd
    BLAST
    Domaini165 – 276112ELM2PROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 33553SANTPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi545 – 5528SH3-bindingSequence Analysis
    Motifi696 – 70510SH3-bindingSequence Analysis
    Motifi711 – 7155SUMO interaction motif 1 (SIM); crucial for efficient sumoylationBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi700 – 7056Poly-Pro

    Sequence similaritiesi

    Contains 1 BAH domain.PROSITE-ProRule annotation
    Contains 1 ELM2 domain.PROSITE-ProRule annotation
    Contains 1 GATA-type zinc finger.Curated
    Contains 1 SANT domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri393 – 42028GATA-type; atypicalAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG252834.
    GeneTreeiENSGT00580000081398.
    HOGENOMiHOG000045387.
    HOVERGENiHBG002598.
    InParanoidiQ8K4B0.
    KOiK11660.
    OMAiDKHATLS.
    OrthoDBiEOG780RM1.
    PhylomeDBiQ8K4B0.
    TreeFamiTF106444.

    Family and domain databases

    InterProiIPR001025. BAH_dom.
    IPR000949. ELM2_dom.
    IPR009057. Homeodomain-like.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    IPR000679. Znf_GATA.
    [Graphical view]
    PfamiPF01426. BAH. 1 hit.
    PF01448. ELM2. 1 hit.
    PF00320. GATA. 1 hit.
    [Graphical view]
    SMARTiSM00439. BAH. 1 hit.
    SM00717. SANT. 1 hit.
    SM00401. ZnF_GATA. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    PROSITEiPS51038. BAH. 1 hit.
    PS51156. ELM2. 1 hit.
    PS51293. SANT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8K4B0-1 [UniParc]FASTAAdd to Basket

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    MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTANGNVEA KVVCFYRRRD    50
    ISSSLIALAD KHATLSVCYR AGPGADTGEE GEVEEEVENP EMVDLPEKLK 100
    HQLRHRELFL SRQLESLPAT HIRGKCSVTL LNETESLKSY LEREDFFFYS 150
    LVYDPQQKTL LADKGEIRVG NRYQADITDL LKEGEEDGRD QSKLETKVWE 200
    AHNPLVDKQI DQFLVVARSV GTFARALDCS SSVRQPSLHM SAAAASRDIT 250
    LFHAMDTLHK NIYDISKAIS ALVPQGGPVL CRDEMEEWSA SEANLFEEAL 300
    EKYGKDFTDI QQDFLPWKSL TSIIEYYYMW KTTDRYVQQK RLKAAEAESK 350
    LKQVYIPNYN KPNPNQISAS SVKATVVNGT GTPGQSPGAG RACESCYTTQ 400
    SYQWYSWGPP NMQCRLCASC WTYWKKYGGL KMPTRLDGER PGPNRNNMSP 450
    HGIPARSSGS PKFAMKTRQA FYLHTTKLTR IARRLCREIL RPWHAARHPY 500
    MPINSAAIKA ECTARLPEAS QSPLVLKQVV RKPLEAVLRY LETHPRPPKP 550
    DPVKSSSSVL SSLTPAKSAP VINNGSPTIL GKRSYEQHNG VDGNMKKRLL 600
    MPSRGLANHG QTRHMGPSRN LLLNGKSYPT KVRLIRGGSL PPVKRRRMNW 650
    IDAPDDVFYM ATEETRKIRK LLSSSETKRA ARRPYKPIAL RQSQALPLRP 700
    PPPAPVNDEP IVIED 715
    Length:715
    Mass (Da):80,798
    Last modified:October 1, 2002 - v1
    Checksum:i135152CD3554278D
    GO

    Sequence cautioni

    The sequence BAC57413.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641T → R in AAK83044. (PubMed:11483358)Curated
    Sequence conflicti65 – 8117Missing in AAK83044. (PubMed:11483358)CuratedAdd
    BLAST
    Sequence conflicti420 – 4201C → W in AAK83044. (PubMed:11483358)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF463504 mRNA. Translation: AAM97588.1.
    AF450245 Genomic DNA. Translation: AAM97587.1.
    AF288137 mRNA. Translation: AAK83044.1.
    AB039744 Genomic DNA. Translation: BAC57413.1. Different initiation.
    RefSeqiXP_006515485.1. XM_006515422.1.
    XP_006536382.1. XM_006536319.1.
    UniGeneiMm.212577.

    Genome annotation databases

    EnsembliENSMUST00000009099; ENSMUSP00000009099; ENSMUSG00000021144.
    GeneIDi116870.
    KEGGimmu:116870.
    UCSCiuc007pfw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF463504 mRNA. Translation: AAM97588.1 .
    AF450245 Genomic DNA. Translation: AAM97587.1 .
    AF288137 mRNA. Translation: AAK83044.1 .
    AB039744 Genomic DNA. Translation: BAC57413.1 . Different initiation.
    RefSeqi XP_006515485.1. XM_006515422.1.
    XP_006536382.1. XM_006536319.1.
    UniGenei Mm.212577.

    3D structure databases

    ProteinModelPortali Q8K4B0.
    SMRi Q8K4B0. Positions 165-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-38226N.
    IntActi Q8K4B0. 9 interactions.
    MINTi MINT-1350646.
    STRINGi 10090.ENSMUSP00000105349.

    PTM databases

    PhosphoSitei Q8K4B0.

    Proteomic databases

    MaxQBi Q8K4B0.
    PaxDbi Q8K4B0.
    PRIDEi Q8K4B0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000009099 ; ENSMUSP00000009099 ; ENSMUSG00000021144 .
    GeneIDi 116870.
    KEGGi mmu:116870.
    UCSCi uc007pfw.1. mouse.

    Organism-specific databases

    CTDi 9112.
    MGIi MGI:2150037. Mta1.

    Phylogenomic databases

    eggNOGi NOG252834.
    GeneTreei ENSGT00580000081398.
    HOGENOMi HOG000045387.
    HOVERGENi HBG002598.
    InParanoidi Q8K4B0.
    KOi K11660.
    OMAi DKHATLS.
    OrthoDBi EOG780RM1.
    PhylomeDBi Q8K4B0.
    TreeFami TF106444.

    Miscellaneous databases

    ChiTaRSi MTA1. mouse.
    PROi Q8K4B0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8K4B0.
    Bgeei Q8K4B0.
    CleanExi MM_MTA1.
    Genevestigatori Q8K4B0.

    Family and domain databases

    InterProi IPR001025. BAH_dom.
    IPR000949. ELM2_dom.
    IPR009057. Homeodomain-like.
    IPR001005. SANT/Myb.
    IPR017884. SANT_dom.
    IPR000679. Znf_GATA.
    [Graphical view ]
    Pfami PF01426. BAH. 1 hit.
    PF01448. ELM2. 1 hit.
    PF00320. GATA. 1 hit.
    [Graphical view ]
    SMARTi SM00439. BAH. 1 hit.
    SM00717. SANT. 1 hit.
    SM00401. ZnF_GATA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    PROSITEi PS51038. BAH. 1 hit.
    PS51156. ELM2. 1 hit.
    PS51293. SANT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The origin of a developmentally regulated Igh replicon is located near the border of regulatory domains for Igh replication and expression."
      Zhou J., Ashouian N., Delepine M., Matsuda F., Chevillard C., Riblet R., Schildkraut C.L., Birshtein B.K.
      Proc. Natl. Acad. Sci. U.S.A. 99:13693-13698(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: BALB/c.
    2. "Differential expression and subcellular distribution of the mouse metastasis-associated proteins Mta1 and Mta3."
      Simpson A., Uitto J., Rodeck U., Mahoney M.G.
      Gene 273:29-39(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Strain: 129/Sv.
    3. Takiguchi S.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
      Tissue: Liver.
    4. "Metastatic tumor antigen 1 short form (MTA1s) associates with casein kinase I-gamma2, an estrogen-responsive kinase."
      Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.
      Oncogene 23:4422-4429(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CSNK1G2/CK1, MUTAGENESIS OF SER-322, INTERACTION WITH CSNK1G2, SUBCELLULAR LOCATION.
    5. Cited for: TISSUE SPECIFICITY.
    6. Erratum
      Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.
      Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013)
    7. Cited for: FUNCTION.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. Cited for: FUNCTION, INTERACTION WITH TP53.
    10. Cited for: FUNCTION.
    11. "Metastasis-associated protein 1 and its short form variant stimulates Wnt1 transcription through promoting its derepression from Six3 corepressor."
      Kumar R., Balasenthil S., Manavathi B., Rayala S.K., Pakala S.B.
      Cancer Res. 70:6649-6658(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SIX3, SUBCELLULAR LOCATION.
    12. "Revelation of p53-independent function of MTA1 in DNA damage response via modulation of the p21 WAF1-proliferating cell nuclear antigen pathway."
      Li D.Q., Pakala S.B., Reddy S.D., Ohshiro K., Peng S.H., Lian Y., Fu S.W., Kumar R.
      J. Biol. Chem. 285:10044-10052(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Regulation of NF-kappaB circuitry by a component of the nucleosome remodeling and deacetylase complex controls inflammatory response homeostasis."
      Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S., Rayala S.K., Behringer R.R., Kumar R.
      J. Biol. Chem. 285:23590-23597(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HDAC2, INDUCTION.
    14. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
      Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
      J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Metastasis-associated protein 1 is an integral component of the circadian molecular machinery."
      Li D.Q., Pakala S.B., Reddy S.D., Peng S., Balasenthil S., Deng C.X., Lee C.C., Rea M.A., Kumar R.
      Nat. Commun. 4:2545-2545(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CLOCK AND ARNTL.
    16. "The subcellular distribution and function of MTA1 in cancer differentiation."
      Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C., Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.
      Oncotarget 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiMTA1_MOUSE
    AccessioniPrimary (citable) accession number: Q8K4B0
    Secondary accession number(s): Q80UI1, Q8K4D4, Q924K9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3