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Q08775 (RUNX2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Runx2
Synonyms:Aml3, Cbfa1, Osf2, Pebp2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.8 Ref.14

Subunit structure

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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Nucleus.

Tissue specificity

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 stage

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.

Domain

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

Post-translational modification

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. Ref.9 Ref.14

Sequence similarities

Contains 1 Runt domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from mutant phenotype PubMed 20843790. Source: BHF-UCL

T cell differentiation

Inferred from direct assay PubMed 7862157. Source: MGI

cell maturation

Inferred from mutant phenotype PubMed 15389629. Source: MGI

cellular response to BMP stimulus

Inferred from mutant phenotype PubMed 20843790. Source: BHF-UCL

chondrocyte development

Inferred from mutant phenotype PubMed 10213384. Source: MGI

chondrocyte differentiation

Inferred from mutant phenotype PubMed 22916278. Source: MGI

embryonic cranial skeleton morphogenesis

Inferred from genetic interaction PubMed 15030764. Source: MGI

embryonic forelimb morphogenesis

Inferred from mutant phenotype PubMed 22916278. Source: MGI

endochondral ossification

Inferred from mutant phenotype PubMed 10072783. Source: MGI

negative regulation of smoothened signaling pathway

Inferred from mutant phenotype PubMed 15668330. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18804520. Source: UniProtKB

odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 15136142PubMed 15668330. Source: MGI

osteoblast development

Inferred from genetic interaction PubMed 18986983. Source: MGI

osteoblast differentiation

Inferred from mutant phenotype PubMed 15389629. Source: MGI

osteoblast fate commitment

Inferred from genetic interaction PubMed 15150273. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15668330. Source: MGI

positive regulation of chondrocyte differentiation

Inferred from mutant phenotype PubMed 10072783. Source: MGI

positive regulation of osteoblast differentiation

Inferred from direct assay PubMed 15175325. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12434156PubMed 15030764PubMed 15107406PubMed 15150273PubMed 15990875PubMed 18487609PubMed 19144722. Source: MGI

positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus

Inferred from mutant phenotype PubMed 20843790. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12551949. Source: MGI

regulation of fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 15136142. Source: MGI

regulation of odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 14688224. Source: MGI

regulation of ossification

Inferred from mutant phenotype PubMed 10213384. Source: MGI

regulation of osteoblast differentiation

Inferred from direct assay PubMed 21628588. Source: MGI

skeletal system development

Inferred from mutant phenotype PubMed 14688224PubMed 15050892. Source: MGI

skeletal system morphogenesis

Inferred from mutant phenotype PubMed 15030764. Source: MGI

stem cell differentiation

Inferred from direct assay PubMed 17693062. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15225881PubMed 17182356. Source: MGI

nuclear chromatin

Inferred from direct assay PubMed 17352693. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12434156PubMed 12551949PubMed 15150273PubMed 15565649PubMed 17182356PubMed 19144722. Source: MGI

transcription factor complex

Inferred from direct assay Ref.11. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from direct assay PubMed 12807883PubMed 15107406. Source: MGI

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay Ref.2. Source: NTNU_SB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay Ref.2. Source: NTNU_SB

bHLH transcription factor binding

Inferred from physical interaction PubMed 19144722. Source: MGI

chromatin binding

Inferred from direct assay PubMed 15537544PubMed 18487609. Source: MGI

protein domain specific binding

Inferred from physical interaction PubMed 15030764. Source: MGI

repressing transcription factor binding

Inferred from physical interaction PubMed 12551949. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12551949PubMed 15030764. Source: MGI

transcription regulatory region DNA binding

Inferred from direct assay PubMed 12551949. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q08775-1)

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.
Isoform 2 (identifier: Q08775-2)

The sequence of this isoform differs from the canonical sequence as follows:
     47-57: Missing.
Isoform 3 (identifier: Q08775-3)

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.
Isoform 4 (identifier: Q08775-4)

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.
Isoform 5 (identifier: Q08775-5)

Also known as: G1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
Isoform 6 (identifier: Q08775-6)

Also known as: G2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     316-373: Missing.
Isoform 7 (identifier: Q08775-7)

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.
Isoform 8 (identifier: Q08775-8)

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
Isoform 9 (identifier: Q08775-9)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 607607Runt-related transcription factor 2
PRO_0000174660

Regions

Domain187 – 315129Runt
Region1 – 8888Interaction with IFI204
Region242 – 25817Required for interaction with FOXO1
Region422 – 525104Interaction with KAT6A By similarity
Region460 – 55495Interaction with KAT6B By similarity
Compositional bias128 – 15629Poly-Gln
Compositional bias158 – 17518Poly-Ala
Compositional bias323 – 607285Pro/Ser/Thr-rich

Amino acid modifications

Modified residue5371Phosphoserine; by CDK1 By similarity

Natural variations

Alternative sequence1 – 9898MLHSP…QSFFW → MRIPV in isoform 3 and isoform 4.
VSP_005940
Alternative sequence1 – 7979Missing in isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9.
VSP_005939
Alternative sequence47 – 5711Missing in isoform 2.
VSP_005941
Alternative sequence1561Missing in isoform 3 and isoform 4.
VSP_005942
Alternative sequence316 – 37358Missing in isoform 6 and isoform 9.
VSP_005943
Alternative sequence399 – 4002PS → LS in isoform 4.
VSP_005944
Alternative sequence401 – 607207Missing in isoform 4.
VSP_005945
Alternative sequence427 – 43913DDDTA…FCLWP → GFCGTTTTTTTKL in isoform 7.
VSP_005946
Alternative sequence428 – 607180DDTAT…VWRPY → SEPSTLDSQSSTTLFLSSEE PGPSTAALPSPSSSCEPQPF SPSPMLPPLLQPLSTASTVP APCVPRRTGLYTIVTSSPEA APHLVDWMPSCPTATSPGVR GKDHERPQTMMAPAPALASE RGHSQHAGPARDDHAEHPGT SPKPCAPPAAAATLEASVGD ILVELRTMNGHLDIIAKALT KLASSLVPQSQPVPEAPDAN in isoform 8 and isoform 9.
VSP_005947
Alternative sequence440 – 607168Missing in isoform 7.
VSP_005948

Experimental info

Sequence conflict2661A → S in AAC78626. Ref.4
Sequence conflict2801G → S in AAC78626. Ref.4
Sequence conflict3731D → N in AAC78626. Ref.4
Sequence conflict3751R → T in AAC78626. Ref.4
Sequence conflict3961M → L in AAC78626. Ref.4
Sequence conflict4591P → L in AAC78626. Ref.4
Sequence conflict4721R → P in AAC78626. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: E87A4497ED19EE0E

FASTA60766,205
        10         20         30         40         50         60 
MLHSPHKQPQ NHKCGANFLQ EDCKKALAFK WLISAGHYQP PRPTESVSAL TTVHAGIFKA 

        70         80         90        100        110        120 
ASSIYNRGHK FYLEKKGGTM ASNSLFSAVT PCQQSFFWDP STSRRFSPPS SSLQPGKMSD 

       130        140        150        160        170        180 
VSPVVAAQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQEAAA AAAAAAAAAA AAAAAVPRLR 

       190        200        210        220        230        240 
PPHDNRTMVE IIADHPAELV RTDSPNFLCS VLPSHWRCNK TLPVAFKVVA LGEVPDGTVV 

       250        260        270        280        290        300 
TVMAGNDENY SAELRNASAV MKNQVARFND LRFVGRSGRG KSFTLTITVF TNPPQVATYH 

       310        320        330        340        350        360 
RAIKVTVDGP REPRRHRQKL DDSKPSLFSD RLSDLGRIPH PSMRVGVPPQ NPRPSLNSAP 

       370        380        390        400        410        420 
SPFNPQGQSQ ITDPRQAQSS PPWSYDQSYP SYLSQMTSPS IHSTTPLSST RGTGLPAITD 

       430        440        450        460        470        480 
VPRRISDDDT ATSDFCLWPS SLSKKSQAGA SELGPFSDPR QFPSISSLTE SRFSNPRMHY 

       490        500        510        520        530        540 
PATFTYTPPV TSGMSLGMSA TTHYHTYLPP PYPGSSQSQS GPFQTSSTPY LYYGTSSASY 

       550        560        570        580        590        600 
QFPMVPGGDR SPSRMVPPCT TTSNGSTLLN PNLPNQNDGV DADGSHSSSP TVLNSSGRMD 


ESVWRPY 

« Hide

Isoform 2 [UniParc].

Checksum: 3365DB4F7F199BA0
Show »

FASTA59665,154
Isoform 3 (PEBP2-alpha A1) [UniParc].

Checksum: EAF92506819B2D28
Show »

FASTA51355,752
Isoform 4 (PEBP2-alpha A2) [UniParc].

Checksum: 0CF6BFF4B8CD4DBB
Show »

FASTA30633,599
Isoform 5 (G1) [UniParc].

Checksum: 1675D3EA1CB5D4EE
Show »

FASTA52857,417
Isoform 6 (G2) [UniParc].

Checksum: E77D395B48886713
Show »

FASTA47051,032
Isoform 7 (U1) [UniParc].

Checksum: 38F2DE7E6AC8747C
Show »

FASTA36039,277
Isoform 8 (Y1) [UniParc].

Checksum: C05C800013B5A912
Show »

FASTA54858,669
Isoform 9 (Y2) [UniParc].

Checksum: 86043D899DFA524F
Show »

FASTA49052,285

References

[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]"p68 (Ddx5) interacts with Runx2 and regulates osteoblast differentiation."
Jensen E.D., Niu L., Caretti G., Nicol S.M., Teplyuk N., Stein G.S., Sartorelli V., van Wijnen A.J., Fuller-Pace F.V., Westendorf J.J.
J. Cell. Biochem. 103:1438-1451(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA48233.
RefSeqNP_001139510.1. NM_001146038.2.
NP_001258556.1. NM_001271627.1.
NP_033950.2. NM_009820.5.
XP_006523607.1. XM_006523544.1.
XP_006523608.1. XM_006523545.1.
UniGeneMm.391013.
Mm.391017.
Mm.491666.

3D structure databases

ProteinModelPortalQ08775.
SMRQ08775. Positions 198-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198518. 21 interactions.
DIPDIP-36316N.
IntActQ08775. 11 interactions.
MINTMINT-4133380.

Chemistry

ChEMBLCHEMBL1681609.

PTM databases

PhosphoSiteQ08775.

Proteomic databases

PaxDbQ08775.
PRIDEQ08775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113571; ENSMUSP00000109201; ENSMUSG00000039153. [Q08775-5]
ENSMUST00000159943; ENSMUSP00000124918; ENSMUSG00000039153. [Q08775-5]
ENSMUST00000160673; ENSMUSP00000123743; ENSMUSG00000039153. [Q08775-2]
GeneID12393.
KEGGmmu:12393.
UCSCuc008cqa.2. mouse. [Q08775-1]

Organism-specific databases

CTD860.
MGIMGI:99829. Runx2.

Phylogenomic databases

eggNOGNOG123889.
GeneTreeENSGT00390000016964.
HOVERGENHBG060268.
InParanoidQ08775.
KOK09278.
OMAXVVALGE.
OrthoDBEOG7WQ7TV.
PhylomeDBQ08775.

Enzyme and pathway databases

ReactomeREACT_78136. Gene Expression.

Gene expression databases

ArrayExpressQ08775.
BgeeQ08775.
CleanExMM_RUNX2.
GenevestigatorQ08775.

Family and domain databases

Gene3D2.60.40.720. 1 hit.
4.10.770.10. 1 hit.
InterProIPR000040. 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]
PANTHERPTHR11950. PTHR11950. 1 hit.
PfamPF00853. Runt. 1 hit.
PF08504. RunxI. 1 hit.
[Graphical view]
PRINTSPR00967. ONCOGENEAML1.
SUPFAMSSF49417. SSF49417. 1 hit.
PROSITEPS51062. RUNT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRUNX2. mouse.
NextBio281136.
PROQ08775.
SOURCESearch...

Entry information

Entry nameRUNX2_MOUSE
AccessionPrimary (citable) accession number: Q08775
Secondary accession number(s): O35183 expand/collapse secondary AC list , Q08776, Q9JLN0, Q9QUQ6, Q9QY29, Q9R0U4, Q9Z2J7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 2, 2001
Last modified: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot