Runt-related transcription factor 2

Preferred order of sections

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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	607 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. 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	BMP 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 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-dependent Inferred from direct assay PubMed 18804520. Source: UniProtKB odontogenesis of dentin-containing tooth Inferred from mutant phenotype PubMed 15136142 PubMed 15668330. Source: MGI osteoblast development Inferred from genetic interaction PubMed 18986983. 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 12434156 PubMed 15030764 PubMed 15107406 PubMed 15150273 PubMed 15990875 PubMed 18487609 PubMed 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 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 stem cell differentiation Inferred from direct assay PubMed 17693062. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 15225881 PubMed 17182356. Source: MGI nuclear chromatin Inferred from direct assay PubMed 17352693. Source: BHF-UCL transcription factor complex Inferred from direct assay Ref.11. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro chromatin binding Inferred from direct assay PubMed 15537544 PubMed 18487609. Source: MGI sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 12551949 PubMed 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
DDX5	P17844	2	EBI-6119991,EBI-351962	From a different organism.
Ddx5	Q6AYI1	2	EBI-903354,EBI-931635	From a different organism.
Hdac4	Q6NZM9	3	EBI-903354,EBI-646397
Twist2	Q9D030	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 607

607

Runt-related transcription factor 2

PRO_0000174660

Regions

Domain

187 – 315

129

Runt

Region

1 – 88

88

Interaction with IFI204

Region

242 – 258

17

Required for interaction with FOXO1

Region

422 – 525

104

Interaction with KAT6A By similarity

Region

460 – 554

95

Interaction with KAT6B By similarity

Compositional bias

128 – 156

29

Poly-Gln

Compositional bias

158 – 175

18

Poly-Ala

Compositional bias

323 – 607

285

Pro/Ser/Thr-rich

Amino acid modifications

Modified residue

537

1

Phosphoserine; by CDK1 By similarity

Natural variations

Alternative sequence

1 – 98

98

MLHSP…QSFFW → MRIPV in isoform 3 and isoform 4.

VSP_005940

Alternative sequence

1 – 79

79

Missing in isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9.

VSP_005939

Alternative sequence

47 – 57

11

Missing in isoform 2.

VSP_005941

Alternative sequence

156

1

Missing in isoform 3 and isoform 4.

VSP_005942

Alternative sequence

316 – 373

58

Missing in isoform 6 and isoform 9.

VSP_005943

Alternative sequence

399 – 400

2

PS → LS in isoform 4.

VSP_005944

Alternative sequence

401 – 607

207

Missing in isoform 4.

VSP_005945

Alternative sequence

427 – 439

13

DDDTA…FCLWP → GFCGTTTTTTTKL in isoform 7.

VSP_005946

Alternative sequence

428 – 607

180

DDTAT…VWRPY → SEPSTLDSQSSTTLFLSSEE PGPSTAALPSPSSSCEPQPF SPSPMLPPLLQPLSTASTVP APCVPRRTGLYTIVTSSPEA APHLVDWMPSCPTATSPGVR GKDHERPQTMMAPAPALASE RGHSQHAGPARDDHAEHPGT SPKPCAPPAAAATLEASVGD ILVELRTMNGHLDIIAKALT KLASSLVPQSQPVPEAPDAN in isoform 8 and isoform 9.

VSP_005947

Alternative sequence

440 – 607

168

Missing in isoform 7.

VSP_005948

Experimental info

Sequence conflict

266

1

A → S in AAC78626. Ref.4

Sequence conflict

280

1

G → S in AAC78626. Ref.4

Sequence conflict

373

1

D → N in AAC78626. Ref.4

Sequence conflict

375

1

R → T in AAC78626. Ref.4

Sequence conflict

396

1

M → L in AAC78626. Ref.4

Sequence conflict

459

1

P → L in AAC78626. Ref.4

Sequence conflict

472

1

R → P in AAC78626. Ref.4

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified November 2, 2001. Version 2. Checksum: E87A4497ED19EE0E Show »	FASTA	607	66,205
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 »	FASTA	596	65,154
10 20 30 40 50 60 MLHSPHKQPQ NHKCGANFLQ EDCKKALAFK WLISAGHYQP PRPTESFKAA SSIYNRGHKF 70 80 90 100 110 120 YLEKKGGTMA SNSLFSAVTP CQQSFFWDPS TSRRFSPPSS SLQPGKMSDV SPVVAAQQQQ 130 140 150 160 170 180 QQQQQQQQQQ QQQQQQQQQQ QQQQQEAAAA AAAAAAAAAA AAAAVPRLRP PHDNRTMVEI 190 200 210 220 230 240 IADHPAELVR TDSPNFLCSV LPSHWRCNKT LPVAFKVVAL GEVPDGTVVT VMAGNDENYS 250 260 270 280 290 300 AELRNASAVM KNQVARFNDL RFVGRSGRGK SFTLTITVFT NPPQVATYHR AIKVTVDGPR 310 320 330 340 350 360 EPRRHRQKLD DSKPSLFSDR LSDLGRIPHP SMRVGVPPQN PRPSLNSAPS PFNPQGQSQI 370 380 390 400 410 420 TDPRQAQSSP PWSYDQSYPS YLSQMTSPSI HSTTPLSSTR GTGLPAITDV PRRISDDDTA 430 440 450 460 470 480 TSDFCLWPSS LSKKSQAGAS ELGPFSDPRQ FPSISSLTES RFSNPRMHYP ATFTYTPPVT 490 500 510 520 530 540 SGMSLGMSAT THYHTYLPPP YPGSSQSQSG PFQTSSTPYL YYGTSSASYQ FPMVPGGDRS 550 560 570 580 590 PSRMVPPCTT TSNGSTLLNP NLPNQNDGVD ADGSHSSSPT VLNSSGRMDE SVWRPY « Hide
Isoform 3 (PEBP2-alpha A1) [UniParc]. Checksum: EAF92506819B2D28 Show »	FASTA	513	55,752
10 20 30 40 50 60 MRIPVDPSTS RRFSPPSSSL QPGKMSDVSP VVAAQQQQQQ QQQQQQQQQQ QQQQQQQQQQ 70 80 90 100 110 120 QQEAAAAAAA AAAAAAAAAA AVPRLRPPHD NRTMVEIIAD HPAELVRTDS PNFLCSVLPS 130 140 150 160 170 180 HWRCNKTLPV AFKVVALGEV PDGTVVTVMA GNDENYSAEL RNASAVMKNQ VARFNDLRFV 190 200 210 220 230 240 GRSGRGKSFT LTITVFTNPP QVATYHRAIK VTVDGPREPR RHRQKLDDSK PSLFSDRLSD 250 260 270 280 290 300 LGRIPHPSMR VGVPPQNPRP SLNSAPSPFN PQGQSQITDP RQAQSSPPWS YDQSYPSYLS 310 320 330 340 350 360 QMTSPSIHST TPLSSTRGTG LPAITDVPRR ISDDDTATSD FCLWPSSLSK KSQAGASELG 370 380 390 400 410 420 PFSDPRQFPS ISSLTESRFS NPRMHYPATF TYTPPVTSGM SLGMSATTHY HTYLPPPYPG 430 440 450 460 470 480 SSQSQSGPFQ TSSTPYLYYG TSSASYQFPM VPGGDRSPSR MVPPCTTTSN GSTLLNPNLP 490 500 510 NQNDGVDADG SHSSSPTVLN SSGRMDESVW RPY « Hide
Isoform 4 (PEBP2-alpha A2) [UniParc]. Checksum: 0CF6BFF4B8CD4DBB Show »	FASTA	306	33,599
10 20 30 40 50 60 MRIPVDPSTS RRFSPPSSSL QPGKMSDVSP VVAAQQQQQQ QQQQQQQQQQ QQQQQQQQQQ 70 80 90 100 110 120 QQEAAAAAAA AAAAAAAAAA AVPRLRPPHD NRTMVEIIAD HPAELVRTDS PNFLCSVLPS 130 140 150 160 170 180 HWRCNKTLPV AFKVVALGEV PDGTVVTVMA GNDENYSAEL RNASAVMKNQ VARFNDLRFV 190 200 210 220 230 240 GRSGRGKSFT LTITVFTNPP QVATYHRAIK VTVDGPREPR RHRQKLDDSK PSLFSDRLSD 250 260 270 280 290 300 LGRIPHPSMR VGVPPQNPRP SLNSAPSPFN PQGQSQITDP RQAQSSPPWS YDQSYPSYLS QMTSLS « Hide
Isoform 5 (G1) [UniParc]. Checksum: 1675D3EA1CB5D4EE Show »	FASTA	528	57,417
10 20 30 40 50 60 MASNSLFSAV TPCQQSFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ QQQQQQQQQQ 70 80 90 100 110 120 QQQQQQQQQQ QQQQQQQEAA AAAAAAAAAA AAAAAAVPRL RPPHDNRTMV EIIADHPAEL 130 140 150 160 170 180 VRTDSPNFLC SVLPSHWRCN KTLPVAFKVV ALGEVPDGTV VTVMAGNDEN YSAELRNASA 190 200 210 220 230 240 VMKNQVARFN DLRFVGRSGR GKSFTLTITV FTNPPQVATY HRAIKVTVDG PREPRRHRQK 250 260 270 280 290 300 LDDSKPSLFS DRLSDLGRIP HPSMRVGVPP QNPRPSLNSA PSPFNPQGQS QITDPRQAQS 310 320 330 340 350 360 SPPWSYDQSY PSYLSQMTSP SIHSTTPLSS TRGTGLPAIT DVPRRISDDD TATSDFCLWP 370 380 390 400 410 420 SSLSKKSQAG ASELGPFSDP RQFPSISSLT ESRFSNPRMH YPATFTYTPP VTSGMSLGMS 430 440 450 460 470 480 ATTHYHTYLP PPYPGSSQSQ SGPFQTSSTP YLYYGTSSAS YQFPMVPGGD RSPSRMVPPC 490 500 510 520 TTTSNGSTLL NPNLPNQNDG VDADGSHSSS PTVLNSSGRM DESVWRPY « Hide
Isoform 6 (G2) [UniParc]. Checksum: E77D395B48886713 Show »	FASTA	470	51,032
10 20 30 40 50 60 MASNSLFSAV TPCQQSFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ QQQQQQQQQQ 70 80 90 100 110 120 QQQQQQQQQQ QQQQQQQEAA AAAAAAAAAA AAAAAAVPRL RPPHDNRTMV EIIADHPAEL 130 140 150 160 170 180 VRTDSPNFLC SVLPSHWRCN KTLPVAFKVV ALGEVPDGTV VTVMAGNDEN YSAELRNASA 190 200 210 220 230 240 VMKNQVARFN DLRFVGRSGR GKSFTLTITV FTNPPQVATY HRAIKVTVDG PREPRRPRQA 250 260 270 280 290 300 QSSPPWSYDQ SYPSYLSQMT SPSIHSTTPL SSTRGTGLPA ITDVPRRISD DDTATSDFCL 310 320 330 340 350 360 WPSSLSKKSQ AGASELGPFS DPRQFPSISS LTESRFSNPR MHYPATFTYT PPVTSGMSLG 370 380 390 400 410 420 MSATTHYHTY LPPPYPGSSQ SQSGPFQTSS TPYLYYGTSS ASYQFPMVPG GDRSPSRMVP 430 440 450 460 470 PCTTTSNGST LLNPNLPNQN DGVDADGSHS SSPTVLNSSG RMDESVWRPY « Hide
Isoform 7 (U1) [UniParc]. Checksum: 38F2DE7E6AC8747C Show »	FASTA	360	39,277
10 20 30 40 50 60 MASNSLFSAV TPCQQSFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ QQQQQQQQQQ 70 80 90 100 110 120 QQQQQQQQQQ QQQQQQQEAA AAAAAAAAAA AAAAAAVPRL RPPHDNRTMV EIIADHPAEL 130 140 150 160 170 180 VRTDSPNFLC SVLPSHWRCN KTLPVAFKVV ALGEVPDGTV VTVMAGNDEN YSAELRNASA 190 200 210 220 230 240 VMKNQVARFN DLRFVGRSGR GKSFTLTITV FTNPPQVATY HRAIKVTVDG PREPRRHRQK 250 260 270 280 290 300 LDDSKPSLFS DRLSDLGRIP HPSMRVGVPP QNPRPSLNSA PSPFNPQGQS QITDPRQAQS 310 320 330 340 350 360 SPPWSYDQSY PSYLSQMTSP SIHSTTPLSS TRGTGLPAIT DVPRRISGFC GTTTTTTTKL « Hide
Isoform 8 (Y1) [UniParc]. Checksum: C05C800013B5A912 Show »	FASTA	548	58,669
10 20 30 40 50 60 MASNSLFSAV TPCQQSFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ QQQQQQQQQQ 70 80 90 100 110 120 QQQQQQQQQQ QQQQQQQEAA AAAAAAAAAA AAAAAAVPRL RPPHDNRTMV EIIADHPAEL 130 140 150 160 170 180 VRTDSPNFLC SVLPSHWRCN KTLPVAFKVV ALGEVPDGTV VTVMAGNDEN YSAELRNASA 190 200 210 220 230 240 VMKNQVARFN DLRFVGRSGR GKSFTLTITV FTNPPQVATY HRAIKVTVDG PREPRRHRQK 250 260 270 280 290 300 LDDSKPSLFS DRLSDLGRIP HPSMRVGVPP QNPRPSLNSA PSPFNPQGQS QITDPRQAQS 310 320 330 340 350 360 SPPWSYDQSY PSYLSQMTSP SIHSTTPLSS TRGTGLPAIT DVPRRISDSE PSTLDSQSST 370 380 390 400 410 420 TLFLSSEEPG PSTAALPSPS SSCEPQPFSP SPMLPPLLQP LSTASTVPAP CVPRRTGLYT 430 440 450 460 470 480 IVTSSPEAAP HLVDWMPSCP TATSPGVRGK DHERPQTMMA PAPALASERG HSQHAGPARD 490 500 510 520 530 540 DHAEHPGTSP KPCAPPAAAA TLEASVGDIL VELRTMNGHL DIIAKALTKL ASSLVPQSQP VPEAPDAN « Hide
Isoform 9 (Y2) [UniParc]. Checksum: 86043D899DFA524F Show »	FASTA	490	52,285
10 20 30 40 50 60 MASNSLFSAV TPCQQSFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ QQQQQQQQQQ 70 80 90 100 110 120 QQQQQQQQQQ QQQQQQQEAA AAAAAAAAAA AAAAAAVPRL RPPHDNRTMV EIIADHPAEL 130 140 150 160 170 180 VRTDSPNFLC SVLPSHWRCN KTLPVAFKVV ALGEVPDGTV VTVMAGNDEN YSAELRNASA 190 200 210 220 230 240 VMKNQVARFN DLRFVGRSGR GKSFTLTITV FTNPPQVATY HRAIKVTVDG PREPRRPRQA 250 260 270 280 290 300 QSSPPWSYDQ SYPSYLSQMT SPSIHSTTPL SSTRGTGLPA ITDVPRRISD SEPSTLDSQS 310 320 330 340 350 360 STTLFLSSEE PGPSTAALPS PSSSCEPQPF SPSPMLPPLL QPLSTASTVP APCVPRRTGL 370 380 390 400 410 420 YTIVTSSPEA APHLVDWMPS CPTATSPGVR GKDHERPQTM MAPAPALASE RGHSQHAGPA 430 440 450 460 470 480 RDDHAEHPGT SPKPCAPPAA AATLEASVGD ILVELRTMNG HLDIIAKALT KLASSLVPQS 490 QPVPEAPDAN « Hide

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.
IPI	IPI00124426. IPI00222181. IPI00222182. IPI00222183. IPI00222187. IPI00222191. IPI00282089. IPI00466044. IPI00974967.
PIR	A48233.
RefSeq	NP_001139510.1. NM_001146038.2. NP_001258556.1. NM_001271627.1. NP_033950.2. NM_009820.5.
UniGene	Mm.391013. Mm.391017.
3D structure databases
ProteinModelPortal	Q08775.
SMR	Q08775. Positions 198-311.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q08775. 9 interactions.
PTM databases
PhosphoSite	Q08775.
Proteomic databases
PaxDb	Q08775.
PRIDE	Q08775.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000113571; ENSMUSP00000109201; ENSMUSG00000039153. ENSMUST00000159943; ENSMUSP00000124918; ENSMUSG00000039153. ENSMUST00000160673; ENSMUSP00000123743; ENSMUSG00000039153.
GeneID	12393.
KEGG	mmu:12393.
UCSC	uc008cpy.2. mouse. uc008cpz.2. mouse. uc008cqa.2. mouse. uc008cqc.2. mouse.
Organism-specific databases
CTD	860.
MGI	MGI:99829. Runx2.
Phylogenomic databases
eggNOG	NOG123889.
GeneTree	ENSGT00390000016964.
HOVERGEN	HBG060268.
InParanoid	Q08775.
KO	K09278.
OMA	XVVALGE.
OrthoDB	EOG4WDDDC.
Enzyme and pathway databases
Reactome	REACT_78136. Gene Expression.
Gene expression databases
ArrayExpress	Q08775.
Bgee	Q08775.
CleanEx	MM_RUNX2.
Genevestigator	Q08775.
GermOnline	ENSMUSG00000039153. Mus musculus.
Family and domain databases
Gene3D	2.60.40.720. 1 hit.
InterPro	IPR000040. AML1_Runt. IPR008967. p53-like_TF_DNA-bd. IPR012346. p53/RUNT-type_TF_DNA-bd. IPR013524. Runt_dom. IPR013711. RunxI_c_dom. [Graphical view]
PANTHER	PTHR11950. PTHR11950. 1 hit.
Pfam	PF00853. Runt. 1 hit. PF08504. RunxI. 1 hit. [Graphical view]
PRINTS	PR00967. ONCOGENEAML1.
SUPFAM	SSF49417. P53_like_DNA_bnd. 1 hit.
PROSITE	PS51062. RUNT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1681609.
ChiTaRS	RUNX2. mouse.
NextBio	281136.
SOURCE	Search...

Entry information

Entry name

RUNX2_MOUSE

Accession

Primary (citable) accession number: Q08775
Secondary accession number(s): O35183

Q9Z2J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	November 2, 2001
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents