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O94776

- MTA2_HUMAN

UniProt

O94776 - MTA2_HUMAN

Protein

Metastasis-associated protein MTA2

Gene

MTA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    May be involved in the regulation of gene expression as repressor and activator. The repression might be related to covalent modification of histone proteins.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri367 – 39428GATA-type; atypicalAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. histone deacetylase activity Source: Ensembl
    3. protein binding Source: IntAct
    4. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    5. RNA polymerase II transcription factor binding Source: BHF-UCL
    6. sequence-specific DNA binding Source: InterPro
    7. sequence-specific DNA binding transcription factor activity Source: InterPro
    8. transcription factor binding transcription factor activity Source: Ensembl
    9. transcription regulatory region DNA binding Source: Ensembl
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. ATP-dependent chromatin remodeling Source: UniProt
    2. chromatin assembly or disassembly Source: ProtInc
    3. DNA methylation Source: Ensembl
    4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl

    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 MTA2
    Alternative name(s):
    Metastasis-associated 1-like 1
    Short name:
    MTA1-L1 protein
    p53 target protein in deacetylase complex
    Gene namesi
    Name:MTA2
    Synonyms:MTA1L1, PID
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7411. MTA2.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. histone deacetylase complex Source: ProtInc
    2. membrane Source: UniProtKB
    3. nuclear chromatin Source: UniProt
    4. nucleus Source: HPA
    5. NuRD complex Source: UniProtKB
    6. protein complex Source: UniProt
    7. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31219.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 668668Metastasis-associated protein MTA2PRO_0000083496Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei152 – 1521N6-acetyllysine1 Publication
    Modified residuei433 – 4331Phosphoserine1 Publication
    Modified residuei435 – 4351Phosphoserine3 Publications
    Modified residuei460 – 4601N6-acetyllysineBy similarity
    Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)Curated
    Modified residuei522 – 5221N6-acetyllysineBy similarity
    Modified residuei531 – 5311N6-acetyllysineBy similarity
    Modified residuei534 – 5341Phosphothreonine1 Publication
    Modified residuei548 – 5481Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO94776.
    PaxDbiO94776.
    PeptideAtlasiO94776.
    PRIDEiO94776.

    PTM databases

    PhosphoSiteiO94776.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiO94776.
    BgeeiO94776.
    CleanExiHS_MTA2.
    GenevestigatoriO94776.

    Organism-specific databases

    HPAiCAB005315.
    CAB017522.
    HPA006214.

    Interactioni

    Subunit structurei

    Component of the nucleosome-remodeling and histone-deacetylase multiprotein complex (NuRD). Interacts with HDAC7, p53/TP53, MINT and MBD3 By similarity. Interacts with FAM64A. Interacts with NACC2.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ESR1P033723EBI-1783035,EBI-78473
    PARK7Q994973EBI-1783035,EBI-1164361

    Protein-protein interaction databases

    BioGridi114652. 93 interactions.
    DIPiDIP-46519N.
    IntActiO94776. 28 interactions.
    STRINGi9606.ENSP00000278823.

    Structurei

    3D structure databases

    ProteinModelPortaliO94776.
    SMRiO94776. Positions 145-321, 366-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 144144BAHPROSITE-ProRule annotationAdd
    BLAST
    Domaini145 – 256112ELM2PROSITE-ProRule annotationAdd
    BLAST
    Domaini263 – 31553SANTPROSITE-ProRule annotationAdd
    BLAST

    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 fingeri367 – 39428GATA-type; atypicalAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG252834.
    HOGENOMiHOG000045387.
    HOVERGENiHBG002598.
    InParanoidiO94776.
    KOiK11660.
    OMAiNAVKAEC.
    OrthoDBiEOG780RM1.
    PhylomeDBiO94776.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O94776-1) [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 PYLVRRIEEL NKTANGNVEA KVVCLFRRRD    50
    ISSSLNSLAD SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT 100
    HIRGKCSVTL LNETDILSQY LEKEDCFFYS LVFDPVQKTL LADQGEIRVG 150
    CKYQAEIPDR LVEGESDNRN QQKMEMKVWD PDNPLTDRQI DQFLVVARAV 200
    GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR NGYDLAKAMS 250
    TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL 300
    ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV 350
    GSKPGMNGAG FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK 400
    YGGLKTPTQL EGATRGTTEP HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN 450
    RQTFLLQTTK LTRLARRMCR DLLQPRRAAR RPYAPINANA IKAECSIRLP 500
    KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT PINRNQLSQN 550
    RGLGGIMVKR AYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD 600
    APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLIAVRPPVP 650
    LPAPSHPAST NEPIVLED 668
    Length:668
    Mass (Da):75,023
    Last modified:May 1, 1999 - v1
    Checksum:i65087AF798BA64EC
    GO
    Isoform 2 (identifier: O94776-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-173: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:495
    Mass (Da):55,037
    Checksum:iF6072C422C0F80C6
    GO

    Sequence cautioni

    The sequence AAH23656.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751V → M in BAA36707. (PubMed:9929979)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 173173Missing in isoform 2. 2 PublicationsVSP_055083Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012922 Genomic DNA. Translation: BAA36562.1.
    AB016591 mRNA. Translation: BAA36707.1.
    AF295807 mRNA. Translation: AAG02241.1.
    AK301569 mRNA. Translation: BAG63063.1.
    CR749481 mRNA. Translation: CAH18309.1.
    AP001458 Genomic DNA. No translation available.
    BC023656 mRNA. Translation: AAH23656.1. Sequence problems.
    BC053650 mRNA. Translation: AAH53650.1.
    CCDSiCCDS8022.1. [O94776-1]
    RefSeqiNP_004730.2. NM_004739.3.
    UniGeneiHs.173043.

    Genome annotation databases

    EnsembliENST00000278823; ENSP00000278823; ENSG00000149480. [O94776-1]
    ENST00000524902; ENSP00000431346; ENSG00000149480. [O94776-2]
    ENST00000527204; ENSP00000431797; ENSG00000149480. [O94776-2]
    GeneIDi9219.
    KEGGihsa:9219.
    UCSCiuc001ntq.2. human. [O94776-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB012922 Genomic DNA. Translation: BAA36562.1 .
    AB016591 mRNA. Translation: BAA36707.1 .
    AF295807 mRNA. Translation: AAG02241.1 .
    AK301569 mRNA. Translation: BAG63063.1 .
    CR749481 mRNA. Translation: CAH18309.1 .
    AP001458 Genomic DNA. No translation available.
    BC023656 mRNA. Translation: AAH23656.1 . Sequence problems.
    BC053650 mRNA. Translation: AAH53650.1 .
    CCDSi CCDS8022.1. [O94776-1 ]
    RefSeqi NP_004730.2. NM_004739.3.
    UniGenei Hs.173043.

    3D structure databases

    ProteinModelPortali O94776.
    SMRi O94776. Positions 145-321, 366-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114652. 93 interactions.
    DIPi DIP-46519N.
    IntActi O94776. 28 interactions.
    STRINGi 9606.ENSP00000278823.

    PTM databases

    PhosphoSitei O94776.

    Proteomic databases

    MaxQBi O94776.
    PaxDbi O94776.
    PeptideAtlasi O94776.
    PRIDEi O94776.

    Protocols and materials databases

    DNASUi 9219.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278823 ; ENSP00000278823 ; ENSG00000149480 . [O94776-1 ]
    ENST00000524902 ; ENSP00000431346 ; ENSG00000149480 . [O94776-2 ]
    ENST00000527204 ; ENSP00000431797 ; ENSG00000149480 . [O94776-2 ]
    GeneIDi 9219.
    KEGGi hsa:9219.
    UCSCi uc001ntq.2. human. [O94776-1 ]

    Organism-specific databases

    CTDi 9219.
    GeneCardsi GC11M062360.
    HGNCi HGNC:7411. MTA2.
    HPAi CAB005315.
    CAB017522.
    HPA006214.
    MIMi 603947. gene.
    neXtProti NX_O94776.
    PharmGKBi PA31219.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252834.
    HOGENOMi HOG000045387.
    HOVERGENi HBG002598.
    InParanoidi O94776.
    KOi K11660.
    OMAi NAVKAEC.
    OrthoDBi EOG780RM1.
    PhylomeDBi O94776.
    TreeFami TF106444.

    Enzyme and pathway databases

    Reactomei REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    ChiTaRSi MTA2. human.
    GeneWikii MTA2.
    GenomeRNAii 9219.
    NextBioi 34563.
    PROi O94776.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94776.
    Bgeei O94776.
    CleanExi HS_MTA2.
    Genevestigatori O94776.

    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. "Molecular cloning, mapping and characterization of a novel human gene, MTA1-L1. showing homology to a metastasis-associated gene, MTA1."
      Futamura M., Nishimori H., Shiratsuchi T., Saji S., Nakamura Y., Tokino T.
      J. Hum. Genet. 44:52-56(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Deacetylation of p53 modulates its effect on cell growth and apoptosis."
      Luo J., Su F., Chen D., Shiloh A., Gu W.
      Nature 408:377-381(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Mammary gland.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Retina.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1).
      Tissue: Brain and Uterus.
    7. "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
      Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
      Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MINT.
    8. "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.
    9. "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.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "RCS1, a substrate of APC/C, controls the metaphase to anaphase transition."
      Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III, Fang G.
      Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAM64A.
    13. "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-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-435 AND THR-534, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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: SUMOYLATION.
    18. "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-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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.

    Entry informationi

    Entry nameiMTA2_HUMAN
    AccessioniPrimary (citable) accession number: O94776
    Secondary accession number(s): Q68DB1, Q9UQB5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3