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Q13330

- MTA1_HUMAN

UniProt

Q13330 - MTA1_HUMAN

Protein

Metastasis-associated protein MTA1

Gene

MTA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (22 Sep 2009)
      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. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. 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. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses.6 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: IntAct
    3. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    4. sequence-specific DNA binding Source: InterPro
    5. sequence-specific DNA binding transcription factor activity Source: InterPro
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. secretory granule organization Source: Ensembl
    2. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_953. RNA Polymerase I Transcription Initiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metastasis-associated protein MTA1
    Gene namesi
    Name:MTA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:7410. MTA1.

    Subcellular locationi

    Isoform Long : Nucleus. Nucleus envelope. Cytoplasm. Cytoplasmcytoskeleton
    Note: Associated with microtubules. Localization at the nuclear envelope is TPR-dependent.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. endoplasmic reticulum Source: Ensembl
    3. intracellular membrane-bounded organelle Source: HPA
    4. nucleus Source: HPA
    5. NuRD complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi182 – 1821K → A: Reduced ubiquitination. Significant reduction in ubiquitination; when associated with A-626. 1 Publication
    Mutagenesisi509 – 5091K → R: Reduced sumoylation and transcriptional corepressor activity. 1 Publication
    Mutagenesisi626 – 6261K → A: Loss of acetylation and transcriptional coactivator activity. Reduced ubiquitination. Significant reduction in ubiquitination; when associated with A-182. 3 Publications
    Mutagenesisi711 – 7133IVI → AAA: Significant loss of interaction with SUMO1 and SUMO2 and reduced transcriptional corepressor activity.

    Organism-specific databases

    PharmGKBiPA31218.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 715715Metastasis-associated protein MTA1PRO_0000083493Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki182 – 182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei386 – 3861Phosphoserine7 Publications
    Modified residuei446 – 4461Phosphoserine3 Publications
    Modified residuei449 – 4491Phosphoserine4 Publications
    Cross-linki509 – 509Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)
    Modified residuei522 – 5221Phosphoserine5 Publications
    Modified residuei564 – 5641Phosphothreonine4 Publications
    Modified residuei576 – 5761Phosphoserine5 Publications
    Modified residuei578 – 5781Phosphothreonine4 Publications
    Modified residuei626 – 6261N6-acetyllysine3 Publications
    Cross-linki626 – 626Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei639 – 6391Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylation by CSNK1G2/CK1 triggered by estrogen enhances corepression of estrogen receptor (ER).7 Publications
    Acetylation is essential for its transcriptional coactivator activity.3 Publications
    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 SENP1.1 Publication
    Ubiquitinated by RFWD2, which leads to proteasomal degradation.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13330.
    PaxDbiQ13330.
    PRIDEiQ13330.

    PTM databases

    PhosphoSiteiQ13330.

    Expressioni

    Tissue specificityi

    Widely expressed. High expression in brain, liver, kidney, and cardiac muscle, ovaries, adrenal glands and virgin mammary glands. Higher in tumors than in adjacent normal tissue from the same individual. Up-regulated in a wide variety of cancers including breast, liver, ovarian, and colorectal cancer and its expression levels are closely correlated with tumor aggressiveness and metastasis.2 Publications

    Developmental stagei

    Highly expressed in metastatic cells.

    Gene expression databases

    ArrayExpressiQ13330.
    BgeeiQ13330.
    CleanExiHS_MTA1.
    GenevestigatoriQ13330.

    Organism-specific databases

    HPAiCAB004508.
    HPA005544.

    Interactioni

    Subunit structurei

    Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC1 and ITGB3BP/CENPR. Binds to CSNK1G2 in the cytoplasm. Interacts with NACC2. Interacts with ARNTL/BMAL1 and CLOCK. Interacts with EP300, TFAP2C, IFI16, TPR, SIX3, HDAC2, UBE2I/UBC9, PIAS1, PIAS3, PIAS4, p53/TP53, MDM2, RFWD2, SUMO1, SUMO2, SENP1 and SENP2.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ESR1P033724EBI-714236,EBI-78473
    HDAC1Q135474EBI-714236,EBI-301834
    HDAC2Q927694EBI-714236,EBI-301821
    HIF1AQ166656EBI-714236,EBI-447269

    Protein-protein interaction databases

    BioGridi114562. 59 interactions.
    DIPiDIP-41751N.
    IntActiQ13330. 13 interactions.
    MINTiMINT-255103.
    STRINGi9606.ENSP00000333633.

    Structurei

    Secondary structure

    1
    715
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni171 – 1733
    Turni192 – 1943
    Beta strandi195 – 1995
    Helixi207 – 22418
    Helixi238 – 2469
    Helixi248 – 26013
    Turni261 – 2633
    Helixi265 – 2728
    Helixi284 – 2874
    Helixi290 – 30314
    Helixi307 – 3137
    Helixi320 – 33011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BKXX-ray3.00A162-335[»]
    4PBYX-ray2.50C/D656-686[»]
    4PBZX-ray2.15B670-695[»]
    4PC0X-ray2.50C/D670-711[»]
    ProteinModelPortaliQ13330.
    SMRiQ13330. Positions 165-333.
    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 sumoylation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi697 – 7059Poly-Pro

    Domaini

    Isoform Short contains a Leu-Arg-Ile-Leu-Leu motif (ER binding motif).

    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.
    HOGENOMiHOG000045387.
    HOVERGENiHBG002598.
    InParanoidiQ13330.
    KOiK11660.
    OMAiDKHATLS.
    OrthoDBiEOG780RM1.
    PhylomeDBiQ13330.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q13330-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTANGNVEA KVVCFYRRRD    50
    ISSTLIALAD KHATLSVCYK AGPGADNGEE GEIEEEMENP EMVDLPEKLK 100
    HQLRHRELFL SRQLESLPAT HIRGKCSVTL LNETESLKSY LEREDFFFYS 150
    LVYDPQQKTL LADKGEIRVG NRYQADITDL LKEGEEDGRD QSRLETQVWE 200
    AHNPLTDKQI DQFLVVARSV GTFARALDCS SSVRQPSLHM SAAAASRDIT 250
    LFHAMDTLHK NIYDISKAIS ALVPQGGPVL CRDEMEEWSA SEANLFEEAL 300
    EKYGKDFTDI QQDFLPWKSL TSIIEYYYMW KTTDRYVQQK RLKAAEAESK 350
    LKQVYIPNYN KPNPNQISVN NVKAGVVNGT GAPGQSPGAG RACESCYTTQ 400
    SYQWYSWGPP NMQCRLCASC WTYWKKYGGL KMPTRLDGER PGPNRSNMSP 450
    HGLPARSSGS PKFAMKTRQA FYLHTTKLTR IARRLCREIL RPWHAARHPY 500
    LPINSAAIKA ECTARLPEAS QSPLVLKQAV RKPLEAVLRY LETHPRPPKP 550
    DPVKSVSSVL SSLTPAKVAP VINNGSPTIL GKRSYEQHNG VDGNMKKRLL 600
    MPSRGLANHG QARHMGPSRN LLLNGKSYPT KVRLIRGGSL PPVKRRRMNW 650
    IDAPDDVFYM ATEETRKIRK LLSSSETKRA ARRPYKPIAL RQSQALPPRP 700
    PPPAPVNDEP IVIED 715
    Length:715
    Mass (Da):80,786
    Last modified:September 22, 2009 - v2
    Checksum:i2D5330F0489AE62E
    GO
    Isoform Short (identifier: Q13330-2) [UniParc]FASTAAdd to Basket

    Also known as: MTA1S

    The sequence of this isoform differs from the canonical sequence as follows:
         398-430: TTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGL → MSSLRILLDILEEIWWLENANPVRWREARTKPQ
         431-715: Missing.

    Show »
    Length:430
    Mass (Da):49,017
    Checksum:iDE4B752E9476C6CE
    GO
    Isoform 3 (identifier: Q13330-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         64-81: TLSVCYKAGPGADNGEEG → R

    Show »
    Length:698
    Mass (Da):79,192
    Checksum:iBCF775330376172E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti498 – 4981H → N in AAA78935. (PubMed:8083195)Curated
    Sequence conflicti545 – 5451P → R in AAI42942. (PubMed:15489334)Curated
    Sequence conflicti655 – 6551D → G in AAA78935. (PubMed:8083195)Curated
    Sequence conflicti661 – 6622AT → PK in AAA78935. (PubMed:8083195)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti372 – 3721V → I.
    Corresponds to variant rs4983413 [ dbSNP | Ensembl ].
    VAR_055847
    Natural varianti612 – 6121A → T.3 Publications
    Corresponds to variant rs13707 [ dbSNP | Ensembl ].
    VAR_058965

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei64 – 8118TLSVC…NGEEG → R in isoform 3. 1 PublicationVSP_042207Add
    BLAST
    Alternative sequencei398 – 43033TTQSY…KYGGL → MSSLRILLDILEEIWWLENA NPVRWREARTKPQ in isoform Short. 1 PublicationVSP_001601Add
    BLAST
    Alternative sequencei431 – 715285Missing in isoform Short. 1 PublicationVSP_001602Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35113 mRNA. Translation: AAA78935.1.
    AF508978 mRNA. Translation: AAN01613.1.
    AL928654 Genomic DNA. No translation available.
    BC009443 mRNA. Translation: AAH09443.2.
    BC142941 mRNA. Translation: AAI42942.1.
    BX248776 mRNA. Translation: CAD66583.1.
    CCDSiCCDS32169.1. [Q13330-1]
    CCDS55954.1. [Q13330-2]
    RefSeqiNP_001190187.1. NM_001203258.1. [Q13330-2]
    NP_004680.2. NM_004689.3. [Q13330-1]
    UniGeneiHs.525629.

    Genome annotation databases

    EnsembliENST00000331320; ENSP00000333633; ENSG00000182979. [Q13330-1]
    ENST00000405646; ENSP00000384180; ENSG00000182979. [Q13330-3]
    ENST00000438610; ENSP00000393438; ENSG00000182979. [Q13330-2]
    GeneIDi9112.
    KEGGihsa:9112.
    UCSCiuc001yqx.3. human. [Q13330-1]
    uc001yqy.3. human. [Q13330-2]

    Polymorphism databases

    DMDMi259016275.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35113 mRNA. Translation: AAA78935.1 .
    AF508978 mRNA. Translation: AAN01613.1 .
    AL928654 Genomic DNA. No translation available.
    BC009443 mRNA. Translation: AAH09443.2 .
    BC142941 mRNA. Translation: AAI42942.1 .
    BX248776 mRNA. Translation: CAD66583.1 .
    CCDSi CCDS32169.1. [Q13330-1 ]
    CCDS55954.1. [Q13330-2 ]
    RefSeqi NP_001190187.1. NM_001203258.1. [Q13330-2 ]
    NP_004680.2. NM_004689.3. [Q13330-1 ]
    UniGenei Hs.525629.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BKX X-ray 3.00 A 162-335 [» ]
    4PBY X-ray 2.50 C/D 656-686 [» ]
    4PBZ X-ray 2.15 B 670-695 [» ]
    4PC0 X-ray 2.50 C/D 670-711 [» ]
    ProteinModelPortali Q13330.
    SMRi Q13330. Positions 165-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114562. 59 interactions.
    DIPi DIP-41751N.
    IntActi Q13330. 13 interactions.
    MINTi MINT-255103.
    STRINGi 9606.ENSP00000333633.

    PTM databases

    PhosphoSitei Q13330.

    Polymorphism databases

    DMDMi 259016275.

    Proteomic databases

    MaxQBi Q13330.
    PaxDbi Q13330.
    PRIDEi Q13330.

    Protocols and materials databases

    DNASUi 9112.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331320 ; ENSP00000333633 ; ENSG00000182979 . [Q13330-1 ]
    ENST00000405646 ; ENSP00000384180 ; ENSG00000182979 . [Q13330-3 ]
    ENST00000438610 ; ENSP00000393438 ; ENSG00000182979 . [Q13330-2 ]
    GeneIDi 9112.
    KEGGi hsa:9112.
    UCSCi uc001yqx.3. human. [Q13330-1 ]
    uc001yqy.3. human. [Q13330-2 ]

    Organism-specific databases

    CTDi 9112.
    GeneCardsi GC14P105886.
    HGNCi HGNC:7410. MTA1.
    HPAi CAB004508.
    HPA005544.
    MIMi 603526. gene.
    neXtProti NX_Q13330.
    PharmGKBi PA31218.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252834.
    HOGENOMi HOG000045387.
    HOVERGENi HBG002598.
    InParanoidi Q13330.
    KOi K11660.
    OMAi DKHATLS.
    OrthoDBi EOG780RM1.
    PhylomeDBi Q13330.
    TreeFami TF106444.

    Enzyme and pathway databases

    Reactomei REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    ChiTaRSi MTA1. human.
    GeneWikii MTA1.
    GenomeRNAii 9112.
    NextBioi 34153.
    PROi Q13330.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13330.
    Bgeei Q13330.
    CleanExi HS_MTA1.
    Genevestigatori Q13330.

    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. "A novel candidate metastasis-associated gene, mta1, differentially expressed in highly metastatic mammary adenocarcinoma cell lines. cDNA cloning, expression, and protein analyses."
      Toh Y., Pencil S.D., Nicolson G.L.
      J. Biol. Chem. 269:22958-22963(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT THR-612.
    2. "Analysis of the complete sequence of the novel metastasis-associated candidate gene, mta1, differentially expressed in mammary adenocarcinoma and breast cancer cell lines."
      Toh Y., Pencil S.D., Nicolson G.L.
      Gene 159:97-104(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT THR-612.
    3. "A naturally occurring MTA1 variant sequesters oestrogen receptor-alpha in the cytoplasm."
      Kumar R., Wang R.-A., Mazumdar A., Talukder A.H., Mandal M., Yang Z., Bagheri-Yarmand R., Sahin A., Hortobagyi G., Adam L., Barnes C.J., Vadlamudi R.K.
      Nature 418:654-657(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), SUBCELLULAR LOCATION.
      Tissue: Mammary gland.
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT THR-612.
      Tissue: Brain.
    6. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-299 (ISOFORM 3).
      Tissue: Cervix carcinoma.
    7. "NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities."
      Xue Y., Wong J., Moreno G.T., Young M.K., Cote J., Wang W.
      Mol. Cell 2:851-861(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN NURD COMPLEX.
    8. "Metastasis-associated protein 1 interacts with NRIF3, an estrogen-inducible nuclear receptor coregulator."
      Talukder A.H., Gururaj A., Mishra S.K., Vadlamudi R.K., Kumar R.
      Mol. Cell. Biol. 24:6581-6591(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB3BP.
    9. "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, INTERACTION WITH CSNK1G2, SUBCELLULAR LOCATION.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND THR-564, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACETYLATION AT LYS-626, MUTAGENESIS OF LYS-626, INTERACTION WITH EP300.
    13. 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)
    14. Cited for: FUNCTION, INTERACTION WITH HDAC2, ACETYLATION AT LYS-626, MUTAGENESIS OF LYS-626.
    15. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "MTA1-mediated transcriptional repression of BRCA1 tumor suppressor gene."
      Molli P.R., Singh R.R., Lee S.W., Kumar R.
      Oncogene 27:1971-1980(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-449; SER-522; THR-564 AND SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53.
    21. Cited for: UBIQUITINATION AT LYS-182 AND LYS-626, ACETYLATION AT LYS-626, MUTAGENESIS OF LYS-182 AND LYS-626, INTERACTION WITH RFWD2 AND HDAC2.
    22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-522; THR-564; SER-576 AND THR-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "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: INTERACTION WITH SIX3.
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-446; SER-449; SER-522; SER-576 AND THR-578, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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, SUMOYLATION AT LYS-509, SUBCELLULAR LOCATION, INTERACTION WITH HDAC2; UBE2I; PIAS1; PIAS3; PIAS4; SUMO1; SUMO2; SENP1 AND SENP2, SUMO INTERACTION MOTIF, MUTAGENESIS OF LYS-509 AND 711-ILE--ILE-713.
    27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-446; SER-449; SER-522; SER-576; THR-578 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Metastasis-associated protein 1/nucleosome remodeling and histone deacetylase complex in cancer."
      Li D.Q., Pakala S.B., Nair S.S., Eswaran J., Kumar R.
      Cancer Res. 72:387-394(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    29. "RBB, a novel transcription repressor, represses the transcription of HDM2 oncogene."
      Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L., Yao Z., Shang Y.
      Oncogene 32:3711-3721(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NACC2.
    30. "Differential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1."
      Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y., Kim Y.N., Seong J.K., Lee M.O.
      Cancer Res. 74:1484-1494(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TFAP2C AND IFI16, SUBCELLULAR LOCATION.
    31. "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, INTERACTION WITH TPR AND HDAC2.

    Entry informationi

    Entry nameiMTA1_HUMAN
    AccessioniPrimary (citable) accession number: Q13330
    Secondary accession number(s): A5PLK4
    , Q86SW2, Q8NFI8, Q96GI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3