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Q08775

- RUNX2_MOUSE

UniProt

Q08775 - RUNX2_MOUSE

Protein

Runt-related transcription factor 2

Gene

Runx2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (02 Nov 2001)
      Previous versions | rss
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    Functioni

    Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. 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, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. Inhibits KAT6B-dependent transcriptional activation By similarity. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE).By similarity2 Publications

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. bHLH transcription factor binding Source: MGI
    3. chromatin binding Source: MGI
    4. DNA binding Source: MGI
    5. protein binding Source: IntAct
    6. protein domain specific binding Source: MGI
    7. repressing transcription factor binding Source: MGI
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    10. sequence-specific DNA binding transcription factor activity Source: MGI
    11. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. BMP signaling pathway Source: BHF-UCL
    2. cell maturation Source: MGI
    3. cellular response to BMP stimulus Source: BHF-UCL
    4. chondrocyte development Source: MGI
    5. chondrocyte differentiation Source: MGI
    6. embryonic cranial skeleton morphogenesis Source: MGI
    7. embryonic forelimb morphogenesis Source: MGI
    8. endochondral ossification Source: MGI
    9. negative regulation of smoothened signaling pathway Source: MGI
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. odontogenesis of dentin-containing tooth Source: MGI
    12. osteoblast development Source: MGI
    13. osteoblast differentiation Source: MGI
    14. osteoblast fate commitment Source: MGI
    15. positive regulation of cell proliferation Source: MGI
    16. positive regulation of chondrocyte differentiation Source: MGI
    17. positive regulation of osteoblast differentiation Source: MGI
    18. positive regulation of transcription, DNA-templated Source: MGI
    19. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    20. positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: BHF-UCL
    21. regulation of fibroblast growth factor receptor signaling pathway Source: MGI
    22. regulation of odontogenesis of dentin-containing tooth Source: MGI
    23. regulation of ossification Source: MGI
    24. regulation of osteoblast differentiation Source: MGI
    25. skeletal system development Source: MGI
    26. skeletal system morphogenesis Source: MGI
    27. stem cell differentiation Source: MGI
    28. T cell differentiation Source: MGI

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Runt-related transcription factor 2
    Alternative name(s):
    Acute myeloid leukemia 3 protein
    Core-binding factor subunit alpha-1
    Short name:
    CBF-alpha-1
    Oncogene AML-3
    Osteoblast-specific transcription factor 2
    Short name:
    OSF-2
    Polyomavirus enhancer-binding protein 2 alpha A subunit
    Short name:
    PEA2-alpha A
    Short name:
    PEBP2-alpha A
    SL3-3 enhancer factor 1 alpha A subunit
    SL3/AKV core-binding factor alpha A subunit
    Gene namesi
    Name:Runx2
    Synonyms:Aml3, Cbfa1, Osf2, Pebp2a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:99829. Runx2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nuclear chromatin Source: BHF-UCL
    3. nucleoplasm Source: Reactome
    4. nucleus Source: MGI
    5. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 607607Runt-related transcription factor 2PRO_0000174660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei537 – 5371Phosphoserine; by CDK1By similarity

    Post-translational modificationi

    Phosphorylated; probably by MAP kinases (MAPK). Phosphorylation by HIPK3 is required for the SPEN/MINT and FGF2 transactivation during osteoblastic differentiation. Phosphorylation at Ser-537 by CDK1 promotes endothelial cell proliferation required for tumor angiogenesis probably by facilitating cell cycle progression By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ08775.
    PRIDEiQ08775.

    PTM databases

    PhosphoSiteiQ08775.

    Expressioni

    Tissue specificityi

    Found in thymus and testis, T-cell lines but not in B-cell lines. Isoform 2 is exclusively found in bone, particularly in osteoblasts; isoforms 3 and 4 are expressed in T-cell lines; isoforms 5, 6, 7, 8 and 9 can be found in osteoblasts and osteosarcoma cell lines.

    Developmental stagei

    Expression occurs early during skeletal development and is restricted to cells of the mesenchymal condensations and of the osteoblast lineage. Expression of isoform 2 in the embryo reaches a peak at 12.5 dpc.

    Gene expression databases

    ArrayExpressiQ08775.
    BgeeiQ08775.
    CleanExiMM_RUNX2.
    GenevestigatoriQ08775.

    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 XRCC6 (Ku70) and XRCC5 (Ku80). Interacts with CCNB1, KAT6A and KAT6B By similarity. Interacts with HIVEP3. Interacts with IFI204. Interaction with SATB2; the interaction results in enhanced DNA binding and transactivation by these transcription factors. Binds to HIPK3. Interacts (isoform 3) with DDX5. Interacts with FOXO1 (via a C-terminal region); the interaction inhibits RUNX2 transcriptional activity towards BGLAP.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX5P178442EBI-6119991,EBI-351962From a different organism.
    Ddx5Q6AYI12EBI-903354,EBI-931635From a different organism.
    Hdac4Q6NZM93EBI-903354,EBI-646397
    Twist2Q9D0302EBI-903354,EBI-2903190

    Protein-protein interaction databases

    BioGridi198518. 21 interactions.
    DIPiDIP-36316N.
    IntActiQ08775. 11 interactions.
    MINTiMINT-4133380.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08775.
    SMRiQ08775. Positions 189-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini187 – 315129RuntPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8888Interaction with IFI204Add
    BLAST
    Regioni242 – 25817Required for interaction with FOXO1Add
    BLAST
    Regioni422 – 525104Interaction with KAT6ABy similarityAdd
    BLAST
    Regioni460 – 55495Interaction with KAT6BBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi128 – 15629Poly-GlnAdd
    BLAST
    Compositional biasi158 – 17518Poly-AlaAdd
    BLAST
    Compositional biasi323 – 607285Pro/Ser/Thr-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 Runt domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG123889.
    GeneTreeiENSGT00390000016964.
    HOVERGENiHBG060268.
    InParanoidiQ08775.
    KOiK09278.
    OMAiXVVALGE.
    OrthoDBiEOG7WQ7TV.
    PhylomeDBiQ08775.

    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.
    [Graphical view]
    PANTHERiPTHR11950. PTHR11950. 1 hit.
    PfamiPF00853. Runt. 1 hit.
    PF08504. RunxI. 1 hit.
    [Graphical view]
    PRINTSiPR00967. ONCOGENEAML1.
    SUPFAMiSSF49417. SSF49417. 1 hit.
    PROSITEiPS51062. RUNT. 1 hit.
    [Graphical view]

    Sequences (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q08775-1) [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

    MLHSPHKQPQ NHKCGANFLQ EDCKKALAFK WLISAGHYQP PRPTESVSAL    50
    TTVHAGIFKA ASSIYNRGHK FYLEKKGGTM ASNSLFSAVT PCQQSFFWDP 100
    STSRRFSPPS SSLQPGKMSD VSPVVAAQQQ QQQQQQQQQQ QQQQQQQQQQ 150
    QQQQQQEAAA AAAAAAAAAA AAAAAVPRLR PPHDNRTMVE IIADHPAELV 200
    RTDSPNFLCS VLPSHWRCNK TLPVAFKVVA LGEVPDGTVV TVMAGNDENY 250
    SAELRNASAV MKNQVARFND LRFVGRSGRG KSFTLTITVF TNPPQVATYH 300
    RAIKVTVDGP REPRRHRQKL DDSKPSLFSD RLSDLGRIPH PSMRVGVPPQ 350
    NPRPSLNSAP SPFNPQGQSQ ITDPRQAQSS PPWSYDQSYP SYLSQMTSPS 400
    IHSTTPLSST RGTGLPAITD VPRRISDDDT ATSDFCLWPS SLSKKSQAGA 450
    SELGPFSDPR QFPSISSLTE SRFSNPRMHY PATFTYTPPV TSGMSLGMSA 500
    TTHYHTYLPP PYPGSSQSQS GPFQTSSTPY LYYGTSSASY QFPMVPGGDR 550
    SPSRMVPPCT TTSNGSTLLN PNLPNQNDGV DADGSHSSSP TVLNSSGRMD 600
    ESVWRPY 607
    Length:607
    Mass (Da):66,205
    Last modified:November 2, 2001 - v2
    Checksum:iE87A4497ED19EE0E
    GO
    Isoform 2 (identifier: Q08775-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         47-57: Missing.

    Show »
    Length:596
    Mass (Da):65,154
    Checksum:i3365DB4F7F199BA0
    GO
    Isoform 3 (identifier: Q08775-3) [UniParc]FASTAAdd to Basket

    Also known as: PEBP2-alpha A1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-98: MLHSPHKQPQ...VTPCQQSFFW → MRIPV
         156-156: Missing.

    Show »
    Length:513
    Mass (Da):55,752
    Checksum:iEAF92506819B2D28
    GO
    Isoform 4 (identifier: Q08775-4) [UniParc]FASTAAdd to Basket

    Also known as: PEBP2-alpha A2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-98: MLHSPHKQPQ...VTPCQQSFFW → MRIPV
         156-156: Missing.
         399-400: PS → LS
         401-607: Missing.

    Show »
    Length:306
    Mass (Da):33,599
    Checksum:i0CF6BFF4B8CD4DBB
    GO
    Isoform 5 (identifier: Q08775-5) [UniParc]FASTAAdd to Basket

    Also known as: G1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.

    Show »
    Length:528
    Mass (Da):57,417
    Checksum:i1675D3EA1CB5D4EE
    GO
    Isoform 6 (identifier: Q08775-6) [UniParc]FASTAAdd to Basket

    Also known as: G2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.
         316-373: Missing.

    Show »
    Length:470
    Mass (Da):51,032
    Checksum:iE77D395B48886713
    GO
    Isoform 7 (identifier: Q08775-7) [UniParc]FASTAAdd to Basket

    Also known as: U1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.
         427-439: DDDTATSDFCLWP → GFCGTTTTTTTKL
         440-607: Missing.

    Show »
    Length:360
    Mass (Da):39,277
    Checksum:i38F2DE7E6AC8747C
    GO
    Isoform 8 (identifier: Q08775-8) [UniParc]FASTAAdd to Basket

    Also known as: Y1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.
         428-607: DDTATSDFCL...RMDESVWRPY → SEPSTLDSQS...QPVPEAPDAN

    Show »
    Length:548
    Mass (Da):58,669
    Checksum:iC05C800013B5A912
    GO
    Isoform 9 (identifier: Q08775-9) [UniParc]FASTAAdd to Basket

    Also known as: Y2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.
         316-373: Missing.
         428-607: DDTATSDFCL...RMDESVWRPY → SEPSTLDSQS...QPVPEAPDAN

    Show »
    Length:490
    Mass (Da):52,285
    Checksum:i86043D899DFA524F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti266 – 2661A → S in AAC78626. (PubMed:9651525)Curated
    Sequence conflicti280 – 2801G → S in AAC78626. (PubMed:9651525)Curated
    Sequence conflicti373 – 3731D → N in AAC78626. (PubMed:9651525)Curated
    Sequence conflicti375 – 3751R → T in AAC78626. (PubMed:9651525)Curated
    Sequence conflicti396 – 3961M → L in AAC78626. (PubMed:9651525)Curated
    Sequence conflicti459 – 4591P → L in AAC78626. (PubMed:9651525)Curated
    Sequence conflicti472 – 4721R → P in AAC78626. (PubMed:9651525)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9898MLHSP…QSFFW → MRIPV in isoform 3 and isoform 4. 2 PublicationsVSP_005940Add
    BLAST
    Alternative sequencei1 – 7979Missing in isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9. 1 PublicationVSP_005939Add
    BLAST
    Alternative sequencei47 – 5711Missing in isoform 2. 2 PublicationsVSP_005941Add
    BLAST
    Alternative sequencei156 – 1561Missing in isoform 3 and isoform 4. 2 PublicationsVSP_005942
    Alternative sequencei316 – 37358Missing in isoform 6 and isoform 9. 1 PublicationVSP_005943Add
    BLAST
    Alternative sequencei399 – 4002PS → LS in isoform 4. 2 PublicationsVSP_005944
    Alternative sequencei401 – 607207Missing in isoform 4. 2 PublicationsVSP_005945Add
    BLAST
    Alternative sequencei427 – 43913DDDTA…FCLWP → GFCGTTTTTTTKL in isoform 7. 1 PublicationVSP_005946Add
    BLAST
    Alternative sequencei428 – 607180DDTAT…VWRPY → SEPSTLDSQSSTTLFLSSEE PGPSTAALPSPSSSCEPQPF SPSPMLPPLLQPLSTASTVP APCVPRRTGLYTIVTSSPEA APHLVDWMPSCPTATSPGVR GKDHERPQTMMAPAPALASE RGHSQHAGPARDDHAEHPGT SPKPCAPPAAAATLEASVGD ILVELRTMNGHLDIIAKALT KLASSLVPQSQPVPEAPDAN in isoform 8 and isoform 9. 1 PublicationVSP_005947Add
    BLAST
    Alternative sequencei440 – 607168Missing in isoform 7. 1 PublicationVSP_005948Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14636 mRNA. Translation: BAA03485.1.
    D14637 mRNA. Translation: BAA03486.1.
    AF010284 mRNA. Translation: AAB65409.1.
    AF005936 mRNA. Translation: AAB82419.1.
    AF053948 Genomic DNA. Translation: AAC77440.1.
    AF053951 mRNA. Translation: AAC78623.1.
    AF053956 mRNA. Translation: AAC78626.1.
    AF134836 Genomic DNA. Translation: AAF22568.1.
    AF134836 Genomic DNA. Translation: AAF22569.1.
    AB013129 Genomic DNA. Translation: BAA85345.1.
    AB013129 Genomic DNA. Translation: BAA85346.1.
    AH009404 Genomic DNA. Translation: AAF73290.1.
    CCDSiCCDS37624.2. [Q08775-5]
    PIRiA48233.
    RefSeqiNP_001139510.1. NM_001146038.2. [Q08775-5]
    NP_001258556.1. NM_001271627.1. [Q08775-5]
    NP_033950.2. NM_009820.5. [Q08775-5]
    XP_006523607.1. XM_006523544.1. [Q08775-1]
    XP_006523608.1. XM_006523545.1. [Q08775-2]
    UniGeneiMm.391013.
    Mm.391017.
    Mm.491666.

    Genome annotation databases

    EnsembliENSMUST00000113571; ENSMUSP00000109201; ENSMUSG00000039153. [Q08775-5]
    ENSMUST00000159943; ENSMUSP00000124918; ENSMUSG00000039153. [Q08775-5]
    ENSMUST00000160673; ENSMUSP00000123743; ENSMUSG00000039153. [Q08775-2]
    GeneIDi12393.
    KEGGimmu:12393.
    UCSCiuc008cqa.2. mouse. [Q08775-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14636 mRNA. Translation: BAA03485.1 .
    D14637 mRNA. Translation: BAA03486.1 .
    AF010284 mRNA. Translation: AAB65409.1 .
    AF005936 mRNA. Translation: AAB82419.1 .
    AF053948 Genomic DNA. Translation: AAC77440.1 .
    AF053951 mRNA. Translation: AAC78623.1 .
    AF053956 mRNA. Translation: AAC78626.1 .
    AF134836 Genomic DNA. Translation: AAF22568.1 .
    AF134836 Genomic DNA. Translation: AAF22569.1 .
    AB013129 Genomic DNA. Translation: BAA85345.1 .
    AB013129 Genomic DNA. Translation: BAA85346.1 .
    AH009404 Genomic DNA. Translation: AAF73290.1 .
    CCDSi CCDS37624.2. [Q08775-5 ]
    PIRi A48233.
    RefSeqi NP_001139510.1. NM_001146038.2. [Q08775-5 ]
    NP_001258556.1. NM_001271627.1. [Q08775-5 ]
    NP_033950.2. NM_009820.5. [Q08775-5 ]
    XP_006523607.1. XM_006523544.1. [Q08775-1 ]
    XP_006523608.1. XM_006523545.1. [Q08775-2 ]
    UniGenei Mm.391013.
    Mm.391017.
    Mm.491666.

    3D structure databases

    ProteinModelPortali Q08775.
    SMRi Q08775. Positions 189-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198518. 21 interactions.
    DIPi DIP-36316N.
    IntActi Q08775. 11 interactions.
    MINTi MINT-4133380.

    Chemistry

    ChEMBLi CHEMBL1681609.

    PTM databases

    PhosphoSitei Q08775.

    Proteomic databases

    PaxDbi Q08775.
    PRIDEi Q08775.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000113571 ; ENSMUSP00000109201 ; ENSMUSG00000039153 . [Q08775-5 ]
    ENSMUST00000159943 ; ENSMUSP00000124918 ; ENSMUSG00000039153 . [Q08775-5 ]
    ENSMUST00000160673 ; ENSMUSP00000123743 ; ENSMUSG00000039153 . [Q08775-2 ]
    GeneIDi 12393.
    KEGGi mmu:12393.
    UCSCi uc008cqa.2. mouse. [Q08775-1 ]

    Organism-specific databases

    CTDi 860.
    MGIi MGI:99829. Runx2.

    Phylogenomic databases

    eggNOGi NOG123889.
    GeneTreei ENSGT00390000016964.
    HOVERGENi HBG060268.
    InParanoidi Q08775.
    KOi K09278.
    OMAi XVVALGE.
    OrthoDBi EOG7WQ7TV.
    PhylomeDBi Q08775.

    Enzyme and pathway databases

    Reactomei REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.

    Miscellaneous databases

    ChiTaRSi RUNX2. mouse.
    NextBioi 281136.
    PROi Q08775.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08775.
    Bgeei Q08775.
    CleanExi MM_RUNX2.
    Genevestigatori Q08775.

    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.
    [Graphical view ]
    PANTHERi PTHR11950. PTHR11950. 1 hit.
    Pfami PF00853. Runt. 1 hit.
    PF08504. RunxI. 1 hit.
    [Graphical view ]
    PRINTSi PR00967. ONCOGENEAML1.
    SUPFAMi SSF49417. SSF49417. 1 hit.
    PROSITEi PS51062. RUNT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PEBP2/PEA2 represents a family of transcription factors homologous to the products of the Drosophila runt gene and the human AML1 gene."
      Ogawa E., Maruyama M., Kagoshima H., Inuzuka M., Lu J., Satake M., Shigesada K., Ito Y.
      Proc. Natl. Acad. Sci. U.S.A. 90:6859-6863(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    2. "Osf2/Cbfa1: a transcriptional activator of osteoblast differentiation."
      Ducy P., Zhang R., Geoffroy V., Ridall A.L., Karsenty G.
      Cell 89:747-754(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Osteoblast.
    3. "Proviral insertions induce the expression of bone-specific isoforms of PEBP2alphaA (CBFA1): evidence for a new myc collaborating oncogene."
      Stewart M., Terry A., Hu M., O'Hara M., Blyth K., Baxter E., Cameron E., Onions D.E., Neil J.C.
      Proc. Natl. Acad. Sci. U.S.A. 94:8646-8651(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8 AND 9).
      Strain: CD2-MYC.
    4. "Genomic structure and isoform expression of the mouse, rat and human Cbfa1/Osf2 transcription factor."
      Xiao Z.S., Thomas R., Hinson T.K., Quarles L.D.
      Gene 214:187-197(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 6), ALTERNATIVE SPLICING.
    5. "Isolation and characterization of the distal promoter region of mouse Cbfa1."
      Fujiwara M., Tagashira S., Harada H., Ogawa S., Katsumata T., Nakatsuka M., Komori T., Takada H.
      Biochim. Biophys. Acta 1446:265-272(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98 (ISOFORMS 1 AND 2).
    6. "Molecular cloning and characterization of PEBP2 beta, the heterodimeric partner of a novel Drosophila runt-related DNA binding protein PEBP2 alpha."
      Ogawa E., Inuzuka M., Maruyama M., Satake M., Naito-Fujimoto M., Ito Y., Shigesada K.
      Virology 194:314-331(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 263-277 AND 305-319.
    7. "Analysis of the two PEBP2aA/cbfa1 promoter regions."
      Chi X.-Z., Bae S.-C.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
      Strain: 129.
    8. "Targeted disruption of Cbfa1 results in a complete lack of bone formation owing to maturational arrest of osteoblasts."
      Komori T., Yagi H., Nomura S., Yamaguchi A., Sasaki K., Deguchi K., Shimizu Y., Bronson R.T., Gao Y.-H., Inada M., Sato M., Okamoto R., Kitamura Y., Yoshiki S., Kishimoto T.
      Cell 89:755-764(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "MAPK pathways activate and phosphorylate the osteoblast-specific transcription factor, Cbfa1."
      Xiao G., Jiang D., Thomas P., Benson M.D., Guan K., Karsenty G., Franceschi R.T.
      J. Biol. Chem. 275:4453-4459(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    10. "The interferon-inducible p204 protein acts as a transcriptional coactivator of Cbfa1 and enhances osteoblast differentiation."
      Liu C.-J., Chang E., Yu J., Carlson C.S., Prazak L., Yu X.-P., Ding B., Lengyel P., Di Cesare P.E.
      J. Biol. Chem. 280:2788-2796(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFI204.
    11. "SATB2 is a multifunctional determinant of craniofacial patterning and osteoblast differentiation."
      Dobreva G., Chahrour M., Dautzenberg M., Chirivella L., Kanzler B., Farinas I., Karsenty G., Grosschedl R.
      Cell 125:971-986(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SATB2.
    12. "Regulation of adult bone mass by the zinc finger adapter protein Schnurri-3."
      Jones D.C., Wein M.N., Oukka M., Hofstaetter J.G., Glimcher M.J., Glimcher L.H.
      Science 312:1223-1227(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIVEP3.
    13. Cited for: INTERACTION WITH DDX5.
    14. "Runx2 trans-activation mediated by the MSX2-interacting nuclear target requires homeodomain interacting protein kinase-3."
      Sierra O.L., Towler D.A.
      Mol. Endocrinol. 24:1478-1497(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY HIPK3, INTERACTION WITH HIPK3.
    15. "Foxo1 mediates insulin-like growth factor 1 (IGF1)/insulin regulation of osteocalcin expression by antagonizing Runx2 in osteoblasts."
      Yang S., Xu H., Yu S., Cao H., Fan J., Ge C., Fransceschi R.T., Dong H.H., Xiao G.
      J. Biol. Chem. 286:19149-19158(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXO1.

    Entry informationi

    Entry nameiRUNX2_MOUSE
    AccessioniPrimary (citable) accession number: Q08775
    Secondary accession number(s): O35183
    , Q08776, Q9JLN0, Q9QUQ6, Q9QY29, Q9R0U4, Q9Z2J7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: November 2, 2001
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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