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Q13761

- RUNX3_HUMAN

UniProt

Q13761 - RUNX3_HUMAN

Protein

Runt-related transcription factor 3

Gene

RUNX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, lck, IL-3 and GM-CSF promoters.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA polymerase II regulatory region sequence-specific DNA binding Source: BHF-UCL
    4. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
    5. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. axon guidance Source: Ensembl
    2. cell maturation Source: Ensembl
    3. chondrocyte differentiation Source: Ensembl
    4. hair follicle morphogenesis Source: Ensembl
    5. interferon-gamma production Source: Ensembl
    6. negative regulation of cell cycle Source: UniProtKB
    7. negative regulation of epithelial cell proliferation Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    9. peripheral nervous system neuron development Source: BHF-UCL
    10. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    11. protein phosphorylation Source: UniProtKB
    12. regulation of transcription, DNA-templated Source: UniProtKB
    13. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Runt-related transcription factor 3
    Alternative name(s):
    Acute myeloid leukemia 2 protein
    Core-binding factor subunit alpha-3
    Short name:
    CBF-alpha-3
    Oncogene AML-2
    Polyomavirus enhancer-binding protein 2 alpha C subunit
    Short name:
    PEA2-alpha C
    Short name:
    PEBP2-alpha C
    SL3-3 enhancer factor 1 alpha C subunit
    SL3/AKV core-binding factor alpha C subunit
    Gene namesi
    Name:RUNX3
    Synonyms:AML2, CBFA3, PEBP2A3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10473. RUNX3.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation. Cytoplasm 1 Publication
    Note: The tyrosine phosphorylated form localizes to the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nuclear chromatin Source: BHF-UCL
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34886.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 415415Runt-related transcription factor 3PRO_0000174662Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei243 – 2431Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated on tyrosine residues by SRC. Phosphorylated by LCK and FYN.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13761.
    PaxDbiQ13761.
    PRIDEiQ13761.

    PTM databases

    PhosphoSiteiQ13761.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13761.
    BgeeiQ13761.
    CleanExiHS_RUNX3.
    GenevestigatoriQ13761.

    Organism-specific databases

    HPAiCAB025416.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. The alpha subunit binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Interacts with TLE1 and SUV39H1. The tyrosine phosphorylated form (via runt domain) interacts with SRC (via protein kinase domain). Interacts with FYN and LCK.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRD2P254408EBI-925990,EBI-2874802
    CTNNB1P3522212EBI-925990,EBI-491549
    EP300Q094727EBI-925990,EBI-447295
    HDAC4P565249EBI-925990,EBI-308629
    HDAC5Q9UQL65EBI-925990,EBI-715576
    TCF7L2Q9NQB014EBI-925990,EBI-924724
    TLE1Q047243EBI-925990,EBI-711424

    Protein-protein interaction databases

    BioGridi107312. 27 interactions.
    IntActiQ13761. 15 interactions.
    MINTiMINT-6774046.
    STRINGi9606.ENSP00000343477.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13761.
    SMRiQ13761. Positions 56-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 182129RuntPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi23 – 275Poly-Gly
    Compositional biasi191 – 415225Pro/Ser/Thr-richAdd
    BLAST

    Domaini

    A proline/serine/threonine rich region at the C-terminus is necessary for transcriptional activation of target genes.

    Sequence similaritiesi

    Contains 1 Runt domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG123889.
    HOGENOMiHOG000045616.
    HOVERGENiHBG060268.
    KOiK09279.
    OMAiFPYSATP.
    OrthoDBiEOG7WQ7TV.
    PhylomeDBiQ13761.
    TreeFamiTF321496.

    Family and domain databases

    Gene3Di2.60.40.720. 1 hit.
    4.10.770.10. 1 hit.
    InterProiIPR000040. AML1_Runt.
    IPR008967. p53-like_TF_DNA-bd.
    IPR012346. p53/RUNT-type_TF_DNA-bd.
    IPR013524. Runt_dom.
    IPR027384. Runx_central_dom.
    IPR013711. RunxI_C_dom.
    IPR016554. TF_Runt-rel_RUNX.
    [Graphical view]
    PANTHERiPTHR11950. PTHR11950. 1 hit.
    PfamiPF00853. Runt. 1 hit.
    PF08504. RunxI. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009374. TF_Runt-rel_RUNX. 1 hit.
    PRINTSiPR00967. ONCOGENEAML1.
    SUPFAMiSSF49417. SSF49417. 1 hit.
    PROSITEiPS51062. RUNT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13761-1) [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

    MRIPVDPSTS RRFTPPSPAF PCGGGGGKMG ENSGALSAQA AVGPGGRARP    50
    EVRSMVDVLA DHAGELVRTD SPNFLCSVLP SHWRCNKTLP VAFKVVALGD 100
    VPDGTVVTVM AGNDENYSAE LRNASAVMKN QVARFNDLRF VGRSGRGKSF 150
    TLTITVFTNP TQVATYHRAI KVTVDGPREP RRHRQKLEDQ TKPFPDRFGD 200
    LERLRMRVTP STPSPRGSLS TTSHFSSQPQ TPIQGTSELN PFSDPRQFDR 250
    SFPTLPTLTE SRFPDPRMHY PGAMSAAFPY SATPSGTSIS SLSVAGMPAT 300
    SRFHHTYLPP PYPGAPQNQS GPFQANPSPY HLYYGTSSGS YQFSMVAGSS 350
    SGGDRSPTRM LASCTSSAAS VAAGNLMNPS LGGQSDGVEA DGSHSNSPTA 400
    LSTPGRMDEA VWRPY 415
    Length:415
    Mass (Da):44,356
    Last modified:November 1, 1999 - v2
    Checksum:i593FBFB3C4639BBD
    GO
    Isoform 2 (identifier: Q13761-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: MRIPV → MASNSIFDSFPTYSPTFIR

    Show »
    Length:429
    Mass (Da):45,922
    Checksum:iE9A43E96EDF82389
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti249 – 2491D → V in CAA56093. (PubMed:7835892)Curated
    Sequence conflicti253 – 2531P → S in CAA56093. (PubMed:7835892)Curated
    Sequence conflicti256 – 2561P → S in CAA56093. (PubMed:7835892)Curated
    Sequence conflicti259 – 2591T → S in CAA56093. (PubMed:7835892)Curated
    Sequence conflicti268 – 2692MH → IY in CAA56093. (PubMed:7835892)Curated
    Sequence conflicti271 – 2711P → T in CAA56093. (PubMed:7835892)Curated
    Sequence conflicti297 – 2982MP → IS in CAA56093. (PubMed:7835892)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 55MRIPV → MASNSIFDSFPTYSPTFIR in isoform 2. 1 PublicationVSP_005949

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35278 mRNA. Translation: CAA84541.1.
    X79550 mRNA. Translation: CAA56093.2.
    AL023096 Genomic DNA. Translation: CAA18856.1.
    AL445471, AL023096 Genomic DNA. Translation: CAC42093.2.
    AL023096, AL445471 Genomic DNA. Translation: CAI20422.1.
    CH471134 Genomic DNA. Translation: EAW95148.1.
    BC013362 mRNA. Translation: AAH13362.1.
    U14520 Genomic DNA. Translation: AAA86465.1.
    CCDSiCCDS257.1. [Q13761-1]
    CCDS30633.1. [Q13761-2]
    PIRiB55563.
    S60078.
    RefSeqiNP_001026850.1. NM_001031680.2. [Q13761-2]
    NP_004341.1. NM_004350.2. [Q13761-1]
    XP_005246081.1. XM_005246024.2. [Q13761-2]
    UniGeneiHs.170019.

    Genome annotation databases

    EnsembliENST00000308873; ENSP00000308051; ENSG00000020633. [Q13761-1]
    ENST00000338888; ENSP00000343477; ENSG00000020633. [Q13761-2]
    ENST00000399916; ENSP00000382800; ENSG00000020633. [Q13761-2]
    GeneIDi864.
    KEGGihsa:864.
    UCSCiuc001bjq.3. human. [Q13761-1]
    uc001bjr.3. human. [Q13761-2]

    Polymorphism databases

    DMDMi17368453.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35278 mRNA. Translation: CAA84541.1 .
    X79550 mRNA. Translation: CAA56093.2 .
    AL023096 Genomic DNA. Translation: CAA18856.1 .
    AL445471 , AL023096 Genomic DNA. Translation: CAC42093.2 .
    AL023096 , AL445471 Genomic DNA. Translation: CAI20422.1 .
    CH471134 Genomic DNA. Translation: EAW95148.1 .
    BC013362 mRNA. Translation: AAH13362.1 .
    U14520 Genomic DNA. Translation: AAA86465.1 .
    CCDSi CCDS257.1. [Q13761-1 ]
    CCDS30633.1. [Q13761-2 ]
    PIRi B55563.
    S60078.
    RefSeqi NP_001026850.1. NM_001031680.2. [Q13761-2 ]
    NP_004341.1. NM_004350.2. [Q13761-1 ]
    XP_005246081.1. XM_005246024.2. [Q13761-2 ]
    UniGenei Hs.170019.

    3D structure databases

    ProteinModelPortali Q13761.
    SMRi Q13761. Positions 56-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107312. 27 interactions.
    IntActi Q13761. 15 interactions.
    MINTi MINT-6774046.
    STRINGi 9606.ENSP00000343477.

    PTM databases

    PhosphoSitei Q13761.

    Polymorphism databases

    DMDMi 17368453.

    Proteomic databases

    MaxQBi Q13761.
    PaxDbi Q13761.
    PRIDEi Q13761.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308873 ; ENSP00000308051 ; ENSG00000020633 . [Q13761-1 ]
    ENST00000338888 ; ENSP00000343477 ; ENSG00000020633 . [Q13761-2 ]
    ENST00000399916 ; ENSP00000382800 ; ENSG00000020633 . [Q13761-2 ]
    GeneIDi 864.
    KEGGi hsa:864.
    UCSCi uc001bjq.3. human. [Q13761-1 ]
    uc001bjr.3. human. [Q13761-2 ]

    Organism-specific databases

    CTDi 864.
    GeneCardsi GC01M025226.
    HGNCi HGNC:10473. RUNX3.
    HPAi CAB025416.
    MIMi 600210. gene.
    neXtProti NX_Q13761.
    PharmGKBi PA34886.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG123889.
    HOGENOMi HOG000045616.
    HOVERGENi HBG060268.
    KOi K09279.
    OMAi FPYSATP.
    OrthoDBi EOG7WQ7TV.
    PhylomeDBi Q13761.
    TreeFami TF321496.

    Miscellaneous databases

    GeneWikii RUNX3.
    GenomeRNAii 864.
    NextBioi 3602.
    PROi Q13761.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13761.
    Bgeei Q13761.
    CleanExi HS_RUNX3.
    Genevestigatori Q13761.

    Family and domain databases

    Gene3Di 2.60.40.720. 1 hit.
    4.10.770.10. 1 hit.
    InterProi IPR000040. AML1_Runt.
    IPR008967. p53-like_TF_DNA-bd.
    IPR012346. p53/RUNT-type_TF_DNA-bd.
    IPR013524. Runt_dom.
    IPR027384. Runx_central_dom.
    IPR013711. RunxI_C_dom.
    IPR016554. TF_Runt-rel_RUNX.
    [Graphical view ]
    PANTHERi PTHR11950. PTHR11950. 1 hit.
    Pfami PF00853. Runt. 1 hit.
    PF08504. RunxI. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009374. TF_Runt-rel_RUNX. 1 hit.
    PRINTSi PR00967. ONCOGENEAML1.
    SUPFAMi SSF49417. SSF49417. 1 hit.
    PROSITEi PS51062. RUNT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, mapping and expression of PEBP2 alpha C, a third gene encoding the mammalian Runt domain."
      Bae S.-C., Takahashi E., Zhang Y.-W., Ogawa E., Shigesada K., Namba Y., Satake M., Ito Y.
      Gene 159:245-248(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "AML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localization."
      Levanon D., Negreanu V., Bernstein Y., Bar-Am I., Avivi L., Groner Y.
      Genomics 23:425-432(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Groner Y.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 2).
      Tissue: Skin.
    7. "Identification of a new murine runt domain-containing gene, Cbfa3, and localization of the human homolog, CBFA3, to chromosome 1p35-pter."
      Wijmenga C., Speck N.A., Dracopoli N.C., Hofker M.H., Liu P., Collins F.S.
      Genomics 26:611-614(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-148.
    8. "Transcriptional repression by AML1 and LEF-1 is mediated by the TLE/Groucho corepressors."
      Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D., Stifani S., Paroush Z., Groner Y.
      Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TLE1.
    9. Cited for: INTERACTION WITH SUV39H1.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm."
      Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.
      J. Biol. Chem. 285:10122-10129(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH SRC; FYN AND LCK.

    Entry informationi

    Entry nameiRUNX3_HUMAN
    AccessioniPrimary (citable) accession number: Q13761
    Secondary accession number(s): B1AJV5, Q12969, Q13760
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 150 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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