Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13950 (RUNX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length521 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. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) By similarity. Inhibits KAT6B-dependent transcriptional activation. Ref.7

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 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. This interaction is prevented on insulin or IGF1 stimulation as FOXO1 is exported from the nucleus By similarity. Interacts with CCNB1, KAT6A and KAT6B. Ref.6 Ref.7 Ref.8

Subcellular location

Nucleus.

Tissue specificity

Specifically expressed in osteoblasts.

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 By similarity. Phosphorylation at Ser-451 by CDK1 promotes endothelial cell proliferation required for tumor angiogenesis probably by facilitating cell cycle progression. Isoform 3 is phosphorylated on Ser-340. Ref.8

Involvement in disease

Cleidocranial dysplasia (CLCD) [MIM:119600]: Autosomal dominant skeletal disorder with high penetrance and variable expressivity. It is due to defective endochondral and intramembranous bone formation. Typical features include hypoplasia/aplasia of clavicles, patent fontanelles, wormian bones (additional cranial plates caused by abnormal ossification of the calvaria), supernumerary teeth, short stature, and other skeletal changes. In some cases defects in RUNX2 are exclusively associated with dental anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Metaphyseal dysplasia with maxillary hypoplasia with or without brachydactyly (MDMHB) [MIM:156510]: An autosomal dominant bone dysplasia characterized by metaphyseal flaring of long bones, enlargement of the medial halves of the clavicles, maxillary hypoplasia, variable brachydactyly, and dystrophic teeth.
Note: The disease is caused by mutations affecting the gene represented in this entry. Analysis for copy-number variations revealed that a 105 kb duplication within RUNX2 segregated with the MDMHB phenotype in a region with maximum linkage. Real-time PCR for copy-number variation in genomic DNA in eight samples, as well as sequence analysis of fibroblast cDNA from one subject with MDMHB confirmed that affected family members were heterozygous for the presence of an intragenic duplication encompassing exons 3 to 5 of RUNX2. These three exons code for the Q/A domain and the functionally essential DNA-binding Runt domain of RUNX2. The RUNX2 duplication found in individuals with MDMHB leads to a gain of function (Ref.10). Ref.10

Sequence similarities

Contains 1 Runt domain.

Ontologies

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

Inferred from sequence or structural similarity. Source: BHF-UCL

T cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from electronic annotation. Source: Ensembl

cellular response to BMP stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

chondrocyte development

Inferred from electronic annotation. Source: Ensembl

embryonic cranial skeleton morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic forelimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

negative regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.7. Source: UniProtKB

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

ossification

Traceable author statement PubMed 12217689. Source: UniProtKB

osteoblast development

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from expression pattern PubMed 20128911. Source: UniProtKB

osteoblast fate commitment

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

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

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of fibroblast growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

stem cell differentiation

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from direct assay. Source: HPA

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

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

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PIN1Q135267EBI-976402,EBI-714158
SMAD6O435413EBI-976402,EBI-976374

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13950-1)

Also known as: Cbfa1a;

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: Q13950-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MASNSLFSTVTPCQQNFFW → MRIPV
Isoform 3 (identifier: Q13950-3)

Also known as: Cbfa1b;

The sequence of this isoform differs from the canonical sequence as follows:
     341-362: Missing.
Note: Contains a phosphoserine at position 340.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Runt-related transcription factor 2
PRO_0000174659

Regions

Domain101 – 229129Runt
Region242 – 25817Required for interaction with FOXO1 By similarity
Region336 – 439104Interaction with KAT6A By similarity
Region374 – 46895Interaction with KAT6B
Compositional bias49 – 7123Poly-Gln
Compositional bias73 – 8917Poly-Ala
Compositional bias237 – 521285Pro/Ser/Thr-rich

Amino acid modifications

Modified residue4511Phosphoserine; by CDK1 Ref.8

Natural variations

Alternative sequence1 – 1919MASNS…QNFFW → MRIPV in isoform 2.
VSP_005937
Alternative sequence341 – 36222Missing in isoform 3.
VSP_005938
Natural variant531Q → L in CLCD. Ref.17
VAR_064081
Natural variant78 – 836Missing.
VAR_012131
Natural variant841A → AAAAAAAAAAA in CLCD associated with brachydactyly of hands and feet. Ref.1
VAR_012130
Natural variant1131L → R in CLCD. Ref.12
VAR_012132
Natural variant1181S → N in CLCD. Ref.22
VAR_064082
Natural variant1181S → R in CLCD. Ref.12
VAR_012133
Natural variant1211F → C in CLCD. Ref.12
VAR_012134
Natural variant1231C → R in CLCD. Ref.12
VAR_012135
Natural variant1311R → C in CLCD. Ref.22
VAR_064083
Natural variant1311R → G in CLCD. Ref.20
VAR_064084
Natural variant1311R → S in CLCD. Ref.22
VAR_064085
Natural variant1331Missing in CLCD. Ref.13
VAR_012136
Natural variant1361L → P in CLCD. Ref.22
VAR_064086
Natural variant1561V → D in CLCD. Ref.22
VAR_064087
Natural variant1561V → G in CLCD. Ref.19
VAR_064088
Natural variant1691R → P in CLCD. Ref.18 Ref.19
VAR_064089
Natural variant1691R → Q in CLCD. Ref.13
VAR_012137
Natural variant1751M → K in CLCD. Ref.22
VAR_064090
Natural variant1751M → R in CLCD; abolishes DNA binding. Ref.11 Ref.13
VAR_012138
Natural variant1751M → V in CLCD. Ref.22
VAR_064091
Natural variant1871F → S in CLCD. Ref.22
VAR_064092
Natural variant1901R → Q in CLCD; abolishes DNA binding. Ref.13
VAR_012139
Natural variant1901R → W in CLCD; has severely impaired DNA binding and transactivation. Ref.15 Ref.16 Ref.19
VAR_012140
Natural variant1911S → N in CLCD; abolishes DNA binding. Ref.11 Ref.13
VAR_012141
Natural variant1931R → C in CLCD. Ref.13
VAR_012142
Natural variant1931R → Q in CLCD. Ref.22
VAR_064093
Natural variant1971F → S in CLCD; retains heterodimerization activity together with a trace potential for DNA binding; retains a low but still substantial transactivation activity. Ref.14 Ref.16
VAR_012143
Natural variant1991L → F in CLCD; abolishes DNA binding. Ref.13
VAR_012144
Natural variant2001T → A in CLCD; mild; associated also with isolated dental anomalies; normal DNA binding. Ref.13
VAR_012145
Natural variant2001T → I in CLCD. Ref.22
VAR_064094
Natural variant2011I → K in CLCD. Ref.19
VAR_064095
Natural variant2051T → R in CLCD. Ref.12
VAR_012146
Natural variant2091Q → H in CLCD. Ref.22
VAR_064096
Natural variant2091Q → R in CLCD. Ref.13
VAR_012147
Natural variant2111A → P in CLCD. Ref.22
VAR_064097
Natural variant2181K → E in CLCD. Ref.22
VAR_064098
Natural variant2181K → N in CLCD; has severely impaired DNA binding and transactivation. Ref.16
VAR_064099
Natural variant2181K → Q in CLCD. Ref.22
VAR_064100
Natural variant2201T → I in CLCD; has severely impaired DNA binding and transactivation. Ref.16
VAR_064101
Natural variant2251R → L in CLCD. Ref.22
VAR_064102
Natural variant2251R → Q in CLCD; interferes with nuclear localization; abolishes DNA binding. Ref.12 Ref.13 Ref.16 Ref.19 Ref.20
VAR_012148
Natural variant2251R → W in CLCD; interferes with nuclear localization; has severely impaired DNA binding and transactivation. Ref.12 Ref.16 Ref.19 Ref.23
VAR_012149
Natural variant2281R → G in CLCD. Ref.22
VAR_064103
Natural variant2331K → R in CLCD. Ref.22
VAR_064104
Natural variant2871D → N in CLCD. Ref.22
VAR_064105
Natural variant3621A → V in CLCD. Ref.19
VAR_064106
Natural variant4201T → I in CLCD. Ref.21
VAR_064107
Natural variant4201T → N in CLCD. Ref.22
VAR_064108
Natural variant5111G → S in CLCD; unknown pathological significance. Ref.12
Corresponds to variant rs11498198 [ dbSNP | Ensembl ].
VAR_012150

Experimental info

Mutagenesis4511S → A: Reduced DNA-binding and impaired phosphorylation. Ref.8
Sequence conflict161N → S in AAC77441. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Cbfa1a) [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: 44C4F3867D6F3EB1

FASTA52156,648
        10         20         30         40         50         60 
MASNSLFSTV TPCQQNFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ QQQQQQQQQQ 

        70         80         90        100        110        120 
QQQQQQQQQQ QEAAAAAAAA AAAAAAAAAV PRLRPPHDNR TMVEIIADHP AELVRTDSPN 

       130        140        150        160        170        180 
FLCSVLPSHW RCNKTLPVAF KVVALGEVPD GTVVTVMAGN DENYSAELRN ASAVMKNQVA 

       190        200        210        220        230        240 
RFNDLRFVGR SGRGKSFTLT ITVFTNPPQV ATYHRAIKVT VDGPREPRRH RQKLDDSKPS 

       250        260        270        280        290        300 
LFSDRLSDLG RIPHPSMRVG VPPQNPRPSL NSAPSPFNPQ GQSQITDPRQ AQSSPPWSYD 

       310        320        330        340        350        360 
QSYPSYLSQM TSPSIHSTTP LSSTRGTGLP AITDVPRRIS DDDTATSDFC LWPSTLSKKS 

       370        380        390        400        410        420 
QAGASELGPF SDPRQFPSIS SLTESRFSNP RMHYPATFTY TPPVTSGMSL GMSATTHYHT 

       430        440        450        460        470        480 
YLPPPYPGSS QSQSGPFQTS STPYLYYGTS SGSYQFPMVP GGDRSPSRML PPCTTTSNGS 

       490        500        510        520 
TLLNPNLPNQ NDGVDADGSH SSSPTVLNSS GRMDESVWRP Y 

« Hide

Isoform 2 [UniParc].

Checksum: 7228C267328DE1DC
Show »

FASTA50755,054
Isoform 3 (Cbfa1b) [UniParc].

Checksum: 4BA956230C96EB2E
Show »

FASTA49954,249

References

« Hide 'large scale' references
[1]"Mutations involving the transcription factor CBFA1 cause cleidocranial dysplasia."
Mundlos S., Otto F., Mundlos C., Mulliken J.B., Aylsworth A.S., Albright S., Lindhout D., Cole W.G., Henn W., Knoll J.H.M., Owen M.J., Mertelsmann R., Zabel B.U., Olsen B.R.
Cell 89:773-779(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), VARIANT CLCD ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-84 INS, VARIANT 78-ALA--ALA-83 DEL.
[2]"Genomic organization, expression of the human CBFA1 gene, and evidence for an alternative splicing event affecting protein function."
Geoffroy V., Corral D.A., Zhou L., Lee B., Karsenty G.
Mamm. Genome 9:54-57(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 3).
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-19 (ISOFORM 1).
[5]"The cDNA cloning of the transcripts of human PEBP2alphaA/CBFA1 mapped to 6p12.3-p21.1, the locus for cleidocranial dysplasia."
Zhang Y.-W., Bae S.-C., Takahashi E., Ito Y.
Oncogene 15:367-371(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-521 (ISOFORM 3).
[6]"Regulation of osteocalcin gene expression by a novel Ku antigen transcription factor complex."
Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S., Ornitz D.M., Towler D.A.
J. Biol. Chem. 277:37280-37291(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XRCC5 AND XRCC6.
Tissue: Osteoblast.
[7]"MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2."
Pelletier N., Champagne N., Stifani S., Yang X.-J.
Oncogene 21:2729-2740(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAT6A AND KAT6B, FUNCTION.
[8]"Cell cycle-dependent phosphorylation of the RUNX2 transcription factor by cdc2 regulates endothelial cell proliferation."
Qiao M., Shapiro P., Fosbrink M., Rus H., Kumar R., Passaniti A.
J. Biol. Chem. 281:7118-7128(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCNB1, PHOSPHORYLATION AT SER-451 BY CDK1, MUTAGENESIS OF SER-451.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Metaphyseal dysplasia with maxillary hypoplasia and brachydactyly is caused by a duplication in RUNX2."
FORGE Canada Consortium
Moffatt P., Ben Amor M., Glorieux F.H., Roschger P., Klaushofer K., Schwartzentruber J.A., Paterson A.D., Hu P., Marshall C., Fahiminiya S., Majewski J., Beaulieu C.L., Boycott K.M., Rauch F.
Am. J. Hum. Genet. 92:252-258(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MDMHB.
[11]"Missense mutations abolishing DNA binding of the osteoblast-specific transcription factor OSF2/CBFA1 in cleidocranial dysplasia."
Lee B., Thirunavukkarasu K., Zhou L., Pastore L., Baldini A., Hecht J., Geoffroy V., Ducy P., Karsenty G.
Nat. Genet. 16:307-310(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLCD ARG-175 AND ASN-191.
[12]"Mutation analysis of core binding factor A1 in patients with cleidocranial dysplasia."
Quack I., Vonderstrass B., Stock M., Aylsworth A.S., Becker A., Brueton L., Lee P.J., Majewski F., Mulliken J.B., Suri M., Zenker M., Mundlos S., Otto F.
Am. J. Hum. Genet. 65:1268-1278(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLCD ARG-113; ARG-118; CYS-121; ARG-123; ARG-205; GLN-225; TRP-225 AND SER-511.
[13]"CBFA1 mutation analysis and functional correlation with phenotypic variability in cleidocranial dysplasia."
Zhou G., Chen Y., Zhou L., Thirunavukkarasu K., Hecht J., Chitayat D., Gelb B.D., Pirinen S., Berry S.A., Greenberg C.R., Karsenty G., Lee B.
Hum. Mol. Genet. 8:2311-2316(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLCD ASN-133 DEL; GLN-169; ARG-175; GLN-190; ASN-191; CYS-193; PHE-199; ALA-200; ARG-209 AND GLN-225.
[14]"PEBP2alphaA/CBFA1 mutations in Japanese cleidocranial dysplasia patients."
Zhang Y.-W., Yasui N., Kakazu N., Abe T., Takada K., Imai S., Sato M., Nomura S., Ochi T., Okuzumi S., Nogami H., Nagai T., Ohashi H., Ito Y.
Gene 244:21-28(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLCD SER-197.
[15]"A novel CBFA1 mutation (R190W) in an Italian family with cleidocranial dysplasia."
Giannotti A., Tessa A., Patrono C., De Florio L., Velardo M., Dionisi-Vici C., Bertini E., Santorelli F.M.
Hum. Mutat. 16:277-277(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLCD TRP-190.
[16]"Functional analysis of RUNX2 mutations in Japanese patients with cleidocranial dysplasia demonstrates novel genotype-phenotype correlations."
Yoshida T., Kanegane H., Osato M., Yanagida M., Miyawaki T., Ito Y., Shigesada K.
Am. J. Hum. Genet. 71:724-738(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLCD TRP-190; SER-197; ASN-218; ILE-220; TRP-225 AND GLN-225, CHARACTERIZATION OF VARIANTS CLCD TRP-190; SER-197; ASN-218; ILE-220; TRP-225 AND GLN-225.
[17]"New mutations in the CBFA1 gene in two Mexican patients with cleidocranial dysplasia."
Machuca-Tzili L., Monroy-Jaramillo N., Gonzalez-del Angel A., Kofman-Alfaro S.
Clin. Genet. 61:349-353(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLCD LEU-53.
[18]"Cleidocranial dysplasia with decreased bone density and biochemical findings of hypophosphatasia."
Morava E., Karteszi J., Weisenbach J., Caliebe A., Mundlos S., Mehes K.
Eur. J. Pediatr. 161:619-622(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLCD PRO-169.
[19]"Mutations in the RUNX2 gene in patients with cleidocranial dysplasia."
Otto F., Kanegane H., Mundlos S.
Hum. Mutat. 19:209-216(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLCD GLY-156; PRO-169; TRP-190; LYS-201; TRP-225; GLN-225 AND VAL-362.
[20]"Four novel RUNX2 mutations including a splice donor site result in the cleidocranial dysplasia phenotype."
Kim H.-J., Nam S.-H., Kim H.-J., Park H.-S., Ryoo H.-M., Kim S.-Y., Cho T.-J., Kim S.-G., Bae S.-C., Kim I.-S., Stein J.L., van Wijnen A.J., Stein G.S., Lian J.B., Choi J.-Y.
J. Cell. Physiol. 207:114-122(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLCD GLY-131 AND GLN-225.
[21]"A novel RUNX2 mutation (T420I) in Chinese patients with cleidocranial dysplasia."
Wang G.X., Sun R.P., Song F.L.
Genet. Mol. Res. 9:41-47(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLCD ILE-420.
[22]"Deletions of the RUNX2 gene are present in about 10% of individuals with cleidocranial dysplasia."
Ott C.E., Leschik G., Trotier F., Brueton L., Brunner H.G., Brussel W., Guillen-Navarro E., Haase C., Kohlhase J., Kotzot D., Lane A., Lee-Kirsch M.A., Morlot S., Simon M.E.H., Steichen-Gersdorf E., Tegay D.H., Peters H., Mundlos S., Klopocki E.
Hum. Mutat. 31:E1587-E1593(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLCD ASN-118; SER-131; CYS-131; PRO-136; ASP-156; VAL-175; LYS-175; SER-187; GLN-193; ILE-200; HIS-209; PRO-211; GLN-218; GLU-218; LEU-225; GLY-228; ARG-233; ASN-287 AND ASN-420.
[23]"RUNX2 mutations in cleidocranial dysplasia patients."
Ryoo H.M., Kang H.Y., Lee S.K., Lee K.E., Kim J.W.
Oral Dis. 16:55-60(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLCD TRP-225.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF001450 expand/collapse EMBL AC list , AF001443, AF001444, AF001445, AF001446, AF001447, AF001448, AF001449 Genomic DNA. Translation: AAB65159.2.
AF001450 expand/collapse EMBL AC list , AF001444, AF001445, AF001446, AF001447, AF001448, AF001449 Genomic DNA. Translation: AAB65158.1.
AL161907, AL096865, AL358135 Genomic DNA. Translation: CAI19638.1.
AL161907, AL096865, AL358135 Genomic DNA. Translation: CAI19639.1.
AL358135, AL096865, AL161907 Genomic DNA. Translation: CAI13528.1.
AL358135, AL096865, AL161907 Genomic DNA. Translation: CAI13531.1.
AL096865, AL161907, AL358135 Genomic DNA. Translation: CAI19925.1.
AL096865, AL161907, AL358135 Genomic DNA. Translation: CAI19931.1.
AF053952 mRNA. Translation: AAC78624.1.
AF053949 Genomic DNA. Translation: AAC77441.1.
L40992 mRNA. Translation: AAA89072.1.
RefSeqNP_001015051.3. NM_001015051.3.
NP_001019801.3. NM_001024630.3.
UniGeneHs.535845.

3D structure databases

ProteinModelPortalQ13950.
SMRQ13950. Positions 112-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107308. 43 interactions.
DIPDIP-36707N.
IntActQ13950. 5 interactions.
MINTMINT-219985.
STRING9606.ENSP00000352514.

PTM databases

PhosphoSiteQ13950.

Polymorphism databases

DMDM17368460.

Proteomic databases

PaxDbQ13950.
PRIDEQ13950.

Protocols and materials databases

DNASU860.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359524; ENSP00000352514; ENSG00000124813. [Q13950-2]
ENST00000371436; ENSP00000360491; ENSG00000124813. [Q13950-3]
ENST00000371438; ENSP00000360493; ENSG00000124813. [Q13950-1]
ENST00000465038; ENSP00000420707; ENSG00000124813. [Q13950-1]
GeneID860.
KEGGhsa:860.
UCSCuc003oxt.3. human. [Q13950-2]
uc011dvx.2. human. [Q13950-1]
uc011dvy.2. human. [Q13950-3]

Organism-specific databases

CTD860.
GeneCardsGC06P045295.
HGNCHGNC:10472. RUNX2.
HPACAB008374.
CAB062561.
HPA022040.
MIM119600. phenotype.
156510. phenotype.
600211. gene.
neXtProtNX_Q13950.
Orphanet1452. Cleidocranial dysplasia.
2504. Metaphyseal dysplasia - maxillary hypoplasia - brachydacty.
PharmGKBPA34885.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG123889.
HOGENOMHOG000045616.
HOVERGENHBG060268.
InParanoidQ13950.
KOK09278.
PhylomeDBQ13950.
TreeFamTF321496.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkQ13950.

Gene expression databases

ArrayExpressQ13950.
BgeeQ13950.
CleanExHS_RUNX2.
GenevestigatorQ13950.

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.
IPR016554. TF_Runt-rel_RUNX.
[Graphical view]
PANTHERPTHR11950. PTHR11950. 1 hit.
PfamPF00853. Runt. 1 hit.
PF08504. RunxI. 1 hit.
[Graphical view]
PIRSFPIRSF009374. TF_Runt-rel_RUNX. 1 hit.
PRINTSPR00967. ONCOGENEAML1.
SUPFAMSSF49417. SSF49417. 1 hit.
PROSITEPS51062. RUNT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRUNX2.
GenomeRNAi860.
NextBio3572.
PROQ13950.
SOURCESearch...

Entry information

Entry nameRUNX2_HUMAN
AccessionPrimary (citable) accession number: Q13950
Secondary accession number(s): O14614, O14615, O95181
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 2, 2001
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM