Q13950 (RUNX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RUNX2
Synonyms:	AML3, CBFA1, OSF2, PEBP2A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	521 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Interaction with SATB2 results in enhanced DNA binding and transactivation by these transcription factors By similarity. Heterodimer of an alpha and a beta subunit. Interacts with HIVEP3 and HIPK3 By similarity. 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 KAT6A and KAT6B. Binds to cyclin B1 CCNB1. 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 Ref.9
Involvement in disease	Defects in RUNX2 are the cause of cleidocranial dysplasia (CLCD) [MIM:119600]; also known as cleidocranial dysostosis (CCD). CLCD is an 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. Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Sequence similarities	Contains 1 Runt domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.7. Source: UniProtKB osteoblast differentiation Inferred from expression pattern. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.7. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear chromatin Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.7Ref.6. Source: UniProtKB sequence-specific DNA binding transcription factor activity Non-traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMAD6	O43541	3	EBI-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: Phosphorylated on Ser-340.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 521	521	Runt-related transcription factor 2		PRO_0000174659
Regions
	Domain	101 – 229	129	Runt
	Region	336 – 439	104	Interaction with KAT6A By similarity
	Region	374 – 468	95	Interaction with KAT6B
	Compositional bias	49 – 71	23	Poly-Gln
	Compositional bias	73 – 89	17	Poly-Ala
	Compositional bias	237 – 521	285	Pro/Ser/Thr-rich
Amino acid modifications
	Modified residue	451	1	Phosphoserine; by CDK1 Ref.8
Natural variations
	Alternative sequence	1 – 19	19	MASNS…QNFFW → MRIPV in isoform 2.		VSP_005937
	Alternative sequence	341 – 362	22	Missing in isoform 3.		VSP_005938
	Natural variant	53	1	Q → L in CLCD. Ref.16		VAR_064081
	Natural variant	78 – 83	6	Missing.		VAR_012131
	Natural variant	84	1	A → AAAAAAAAAAA in CLCD associated with brachydactyly of hands and feet. Ref.1		VAR_012130
	Natural variant	113	1	L → R in CLCD. Ref.11		VAR_012132
	Natural variant	118	1	S → N in CLCD. Ref.21		VAR_064082
	Natural variant	118	1	S → R in CLCD. Ref.11		VAR_012133
	Natural variant	121	1	F → C in CLCD. Ref.11		VAR_012134
	Natural variant	123	1	C → R in CLCD. Ref.11		VAR_012135
	Natural variant	131	1	R → C in CLCD. Ref.21		VAR_064083
	Natural variant	131	1	R → G in CLCD. Ref.19		VAR_064084
	Natural variant	131	1	R → S in CLCD. Ref.21		VAR_064085
	Natural variant	133	1	Missing in CLCD.		VAR_012136
	Natural variant	136	1	L → P in CLCD. Ref.21		VAR_064086
	Natural variant	156	1	V → D in CLCD. Ref.21		VAR_064087
	Natural variant	156	1	V → G in CLCD. Ref.18		VAR_064088
	Natural variant	169	1	R → P in CLCD. Ref.17 Ref.18		VAR_064089
	Natural variant	169	1	R → Q in CLCD. Ref.12		VAR_012137
	Natural variant	175	1	M → K in CLCD. Ref.21		VAR_064090
	Natural variant	175	1	M → R in CLCD; abolishes DNA binding. Ref.10 Ref.12		VAR_012138
	Natural variant	175	1	M → V in CLCD. Ref.21		VAR_064091
	Natural variant	187	1	F → S in CLCD. Ref.21		VAR_064092
	Natural variant	190	1	R → Q in CLCD; abolishes DNA binding. Ref.12		VAR_012139
	Natural variant	190	1	R → W in CLCD; has severely impaired DNA binding and transactivation. Ref.14 Ref.15 Ref.18		VAR_012140
	Natural variant	191	1	S → N in CLCD; abolishes DNA binding. Ref.10 Ref.12		VAR_012141
	Natural variant	193	1	R → C in CLCD. Ref.12		VAR_012142
	Natural variant	193	1	R → Q in CLCD. Ref.21		VAR_064093
	Natural variant	197	1	F → S in CLCD; retains heterodimerization activity together with a trace potential for DNA binding; retains a low but still substantial transactivation activity. Ref.13 Ref.15		VAR_012143
	Natural variant	199	1	L → F in CLCD; abolishes DNA binding. Ref.12		VAR_012144
	Natural variant	200	1	T → A in CLCD; mild; associated also with isolated dental anomalies; normal DNA binding. Ref.12		VAR_012145
	Natural variant	200	1	T → I in CLCD. Ref.21		VAR_064094
	Natural variant	201	1	I → K in CLCD. Ref.18		VAR_064095
	Natural variant	205	1	T → R in CLCD. Ref.11		VAR_012146
	Natural variant	209	1	Q → H in CLCD. Ref.21		VAR_064096
	Natural variant	209	1	Q → R in CLCD. Ref.12		VAR_012147
	Natural variant	211	1	A → P in CLCD. Ref.21		VAR_064097
	Natural variant	218	1	K → E in CLCD. Ref.21		VAR_064098
	Natural variant	218	1	K → N in CLCD; has severely impaired DNA binding and transactivation. Ref.15		VAR_064099
	Natural variant	218	1	K → Q in CLCD. Ref.21		VAR_064100
	Natural variant	220	1	T → I in CLCD; has severely impaired DNA binding and transactivation. Ref.15		VAR_064101
	Natural variant	225	1	R → L in CLCD. Ref.21		VAR_064102
	Natural variant	225	1	R → Q in CLCD; interferes with nuclear localization; abolishes DNA binding. Ref.11 Ref.12 Ref.15 Ref.18 Ref.19		VAR_012148
	Natural variant	225	1	R → W in CLCD; interferes with nuclear localization; has severely impaired DNA binding and transactivation. Ref.11 Ref.15 Ref.18 Ref.22		VAR_012149
	Natural variant	228	1	R → G in CLCD. Ref.21		VAR_064103
	Natural variant	233	1	K → R in CLCD. Ref.21		VAR_064104
	Natural variant	287	1	D → N in CLCD. Ref.21		VAR_064105
	Natural variant	362	1	A → V in CLCD. Ref.18		VAR_064106
	Natural variant	420	1	T → I in CLCD. Ref.20		VAR_064107
	Natural variant	420	1	T → N in CLCD. Ref.21		VAR_064108
	Natural variant	511	1	G → S in CLCD; could be a polymorphism. Ref.11		VAR_012150
Experimental info
	Mutagenesis	451	1	S → A: Reduced DNA-binding and impaired phosphorylation. Ref.8
	Sequence conflict	16	1	N → S in AAC77441. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Cbfa1a) [UniParc]. Last modified November 2, 2001. Version 2. Checksum: 44C4F3867D6F3EB1	FASTA	521	56,648
	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
	Isoform 2 [UniParc]. Checksum: 7228C267328DE1DC	FASTA	507	55,054
	10 20 30 40 50 60 MRIPVDPSTS RRFSPPSSSL QPGKMSDVSP VVAAQQQQQQ QQQQQQQQQQ QQQQQQQEAA 70 80 90 100 110 120 AAAAAAAAAA AAAAAVPRLR PPHDNRTMVE IIADHPAELV RTDSPNFLCS VLPSHWRCNK 130 140 150 160 170 180 TLPVAFKVVA LGEVPDGTVV TVMAGNDENY SAELRNASAV MKNQVARFND LRFVGRSGRG 190 200 210 220 230 240 KSFTLTITVF TNPPQVATYH RAIKVTVDGP REPRRHRQKL DDSKPSLFSD RLSDLGRIPH 250 260 270 280 290 300 PSMRVGVPPQ NPRPSLNSAP SPFNPQGQSQ ITDPRQAQSS PPWSYDQSYP SYLSQMTSPS 310 320 330 340 350 360 IHSTTPLSST RGTGLPAITD VPRRISDDDT ATSDFCLWPS TLSKKSQAGA SELGPFSDPR 370 380 390 400 410 420 QFPSISSLTE SRFSNPRMHY PATFTYTPPV TSGMSLGMSA TTHYHTYLPP PYPGSSQSQS 430 440 450 460 470 480 GPFQTSSTPY LYYGTSSGSY QFPMVPGGDR SPSRMLPPCT TTSNGSTLLN PNLPNQNDGV 490 500 DADGSHSSSP TVLNSSGRMD ESVWRPY
	Isoform 3 (Cbfa1b) [UniParc]. Checksum: 4BA956230C96EB2E	FASTA	499	54,249
	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 GASELGPFSD PRQFPSISSL 370 380 390 400 410 420 TESRFSNPRM HYPATFTYTP PVTSGMSLGM SATTHYHTYL PPPYPGSSQS QSGPFQTSST 430 440 450 460 470 480 PYLYYGTSSG SYQFPMVPGG DRSPSRMLPP CTTTSNGSTL LNPNLPNQND GVDADGSHSS 490 SPTVLNSSGR MDESVWRPY

References

	« Hide 'large scale' referencesShow '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: 9182765] [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: 9434946] [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. , 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: 14574404] [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: 9651525] [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: 9233771] [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: 12145306] [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: 11965546] [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: 16407259] [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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 (ISOFORM 3), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 9207800] [Abstract] Cited for: VARIANTS CLCD ARG-175 AND ASN-191.
[11]	"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: 10521292] [Abstract] Cited for: VARIANTS CLCD ARG-113; ARG-118; CYS-121; ARG-123; ARG-205; GLN-225; TRP-225 AND SER-511.
[12]	"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: 10545612] [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.
[13]	"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: 10689183] [Abstract] Cited for: VARIANT CLCD SER-197.
[14]	"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: 10980549] [Abstract] Cited for: VARIANT CLCD TRP-190.
[15]	"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: 12196916] [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.
[16]	"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: 12081718] [Abstract] Cited for: VARIANT CLCD LEU-53.
[17]	"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: 12424590] [Abstract] Cited for: VARIANT CLCD PRO-169.
[18]	"Mutations in the RUNX2 gene in patients with cleidocranial dysplasia." Otto F., Kanegane H., Mundlos S. Hum. Mutat. 19:209-216(2002) [PubMed: 11857736] [Abstract] Cited for: VARIANTS CLCD GLY-156; PRO-169; TRP-190; LYS-201; TRP-225; GLN-225 AND VAL-362.
[19]	"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: 16270353] [Abstract] Cited for: VARIANTS CLCD GLY-131 AND GLN-225.
[20]	"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: 20082269] [Abstract] Cited for: VARIANT CLCD ILE-420.
[21]	"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: 20648631] [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.
[22]	"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: 19744171] [Abstract] Cited for: VARIANT CLCD TRP-225.
+	Additional computationally mapped references.

Web resources

GeneReviews

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF001450 , AF001443, AF001444, AF001445, AF001446, AF001447, AF001448, AF001449 Genomic DNA. Translation: AAB65159.2. AF001450 , 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.
IPI	IPI00604427. IPI00946868. IPI01015485.
RefSeq	NP_001015051.3. NM_001015051.3. NP_001019801.3. NM_001024630.3. NP_004339.3. NM_004348.3.
UniGene	Hs.535845.
3D structure databases
ProteinModelPortal	Q13950.
SMR	Q13950. Positions 112-225.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13950. 3 interactions.
STRING	Q13950.
PTM databases
PhosphoSite	Q13950.
Polymorphism databases
DMDM	17368460.
Proteomic databases
PRIDE	Q13950.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000359524; ENSP00000352514; ENSG00000124813. ENST00000371438; ENSP00000360493; ENSG00000124813. ENST00000465038; ENSP00000420707; ENSG00000124813.
GeneID	860.
KEGG	hsa:860.
UCSC	uc003oxt.1. human.
Organism-specific databases
CTD	860.
GeneCards	GC06P045295.
HGNC	HGNC:10472. RUNX2.
HPA	CAB008374. HPA022040.
MIM	119600. phenotype. 600211. gene.
neXtProt	NX_Q13950.
Orphanet	1452. Cleidocranial dysplasia.
PharmGKB	PA34885.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04764.
HOVERGEN	HBG060268.
InParanoid	Q13950.
OrthoDB	EOG47M1XZ.
Enzyme and pathway databases
Pathway_Interaction_DB	fgf_pathway. FGF signaling pathway. smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
Gene expression databases
ArrayExpress	Q13950.
Bgee	Q13950.
CleanEx	HS_RUNX2.
Genevestigator	Q13950.
GermOnline	ENSG00000124813. Homo sapiens.
Family and domain databases
InterPro	IPR013524. AML1/Runt_N. IPR000040. AML1_Runt. IPR008967. p53-like_TF_DNA-bd. IPR012346. p53/RUNT-type_TF_DNA-bd. IPR013711. RunxI. IPR016554. TF_Runt-rel_RUNX. [Graphical view]
Gene3D	G3DSA:2.60.40.720. p53_RUNT_DNA_bd. 1 hit.
KO	K09278.
PANTHER	PTHR11950. AML1_Runt. 1 hit.
Pfam	PF00853. Runt. 1 hit. PF08504. RunxI. 1 hit. [Graphical view]
PIRSF	PIRSF009374. TF_Runt-rel_RUNX. 1 hit.
PRINTS	PR00967. ONCOGENEAML1.
SUPFAM	SSF49417. P53_like_DNA_bnd. 1 hit.
PROSITE	PS51062. RUNT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	3572.
SOURCE	Search...

Entry information

Entry name

RUNX2_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.