SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q13950

- RUNX2_HUMAN

UniProt

Q13950 - RUNX2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Runt-related transcription factor 2
Gene
RUNX2, AML3, CBFA1, OSF2, PEBP2A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. 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.1 Publication

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  4. chromatin binding Source: Ensembl
  5. protein binding Source: UniProtKB
  6. sequence-specific DNA binding transcription factor activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

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

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
SignaLinkiQ13950.

Names & Taxonomyi

Protein namesi
Recommended name:
Runt-related transcription factor 2
Alternative name(s):
Acute myeloid leukemia 3 protein
Core-binding factor subunit alpha-1
Short name:
CBF-alpha-1
Oncogene AML-3
Osteoblast-specific transcription factor 2
Short name:
OSF-2
Polyomavirus enhancer-binding protein 2 alpha A subunit
Short name:
PEA2-alpha A
Short name:
PEBP2-alpha A
SL3-3 enhancer factor 1 alpha A subunit
SL3/AKV core-binding factor alpha A subunit
Gene namesi
Name:RUNX2
Synonyms:AML3, CBFA1, OSF2, PEBP2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:10472. RUNX2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nuclear chromatin Source: BHF-UCL
  3. nucleus Source: HPA
  4. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.14 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531Q → L in CLCD. 1 Publication
VAR_064081
Natural varianti84 – 841A → AAAAAAAAAAA in CLCD associated with brachydactyly of hands and feet. 1 Publication
VAR_012130
Natural varianti113 – 1131L → R in CLCD. 1 Publication
VAR_012132
Natural varianti118 – 1181S → N in CLCD. 1 Publication
VAR_064082
Natural varianti118 – 1181S → R in CLCD. 1 Publication
VAR_012133
Natural varianti121 – 1211F → C in CLCD. 1 Publication
VAR_012134
Natural varianti123 – 1231C → R in CLCD. 1 Publication
VAR_012135
Natural varianti131 – 1311R → C in CLCD. 1 Publication
VAR_064083
Natural varianti131 – 1311R → G in CLCD. 1 Publication
VAR_064084
Natural varianti131 – 1311R → S in CLCD. 1 Publication
VAR_064085
Natural varianti133 – 1331Missing in CLCD. 1 Publication
VAR_012136
Natural varianti136 – 1361L → P in CLCD. 1 Publication
VAR_064086
Natural varianti156 – 1561V → D in CLCD. 1 Publication
VAR_064087
Natural varianti156 – 1561V → G in CLCD. 1 Publication
VAR_064088
Natural varianti169 – 1691R → P in CLCD. 2 Publications
VAR_064089
Natural varianti169 – 1691R → Q in CLCD. 1 Publication
VAR_012137
Natural varianti175 – 1751M → K in CLCD. 1 Publication
VAR_064090
Natural varianti175 – 1751M → R in CLCD; abolishes DNA binding. 2 Publications
VAR_012138
Natural varianti175 – 1751M → V in CLCD. 1 Publication
VAR_064091
Natural varianti187 – 1871F → S in CLCD. 1 Publication
VAR_064092
Natural varianti190 – 1901R → Q in CLCD; abolishes DNA binding. 1 Publication
VAR_012139
Natural varianti190 – 1901R → W in CLCD; has severely impaired DNA binding and transactivation. 3 Publications
VAR_012140
Natural varianti191 – 1911S → N in CLCD; abolishes DNA binding. 2 Publications
VAR_012141
Natural varianti193 – 1931R → C in CLCD. 1 Publication
VAR_012142
Natural varianti193 – 1931R → Q in CLCD. 1 Publication
VAR_064093
Natural varianti197 – 1971F → S in CLCD; retains heterodimerization activity together with a trace potential for DNA binding; retains a low but still substantial transactivation activity. 2 Publications
VAR_012143
Natural varianti199 – 1991L → F in CLCD; abolishes DNA binding. 1 Publication
VAR_012144
Natural varianti200 – 2001T → A in CLCD; mild; associated also with isolated dental anomalies; normal DNA binding. 1 Publication
VAR_012145
Natural varianti200 – 2001T → I in CLCD. 1 Publication
VAR_064094
Natural varianti201 – 2011I → K in CLCD. 1 Publication
VAR_064095
Natural varianti205 – 2051T → R in CLCD. 1 Publication
VAR_012146
Natural varianti209 – 2091Q → H in CLCD. 1 Publication
VAR_064096
Natural varianti209 – 2091Q → R in CLCD. 1 Publication
VAR_012147
Natural varianti211 – 2111A → P in CLCD. 1 Publication
VAR_064097
Natural varianti218 – 2181K → E in CLCD. 1 Publication
VAR_064098
Natural varianti218 – 2181K → N in CLCD; has severely impaired DNA binding and transactivation. 1 Publication
VAR_064099
Natural varianti218 – 2181K → Q in CLCD. 1 Publication
VAR_064100
Natural varianti220 – 2201T → I in CLCD; has severely impaired DNA binding and transactivation. 1 Publication
VAR_064101
Natural varianti225 – 2251R → L in CLCD. 1 Publication
VAR_064102
Natural varianti225 – 2251R → Q in CLCD; interferes with nuclear localization; abolishes DNA binding. 5 Publications
VAR_012148
Natural varianti225 – 2251R → W in CLCD; interferes with nuclear localization; has severely impaired DNA binding and transactivation. 4 Publications
VAR_012149
Natural varianti228 – 2281R → G in CLCD. 1 Publication
VAR_064103
Natural varianti233 – 2331K → R in CLCD. 1 Publication
VAR_064104
Natural varianti287 – 2871D → N in CLCD. 1 Publication
VAR_064105
Natural varianti362 – 3621A → V in CLCD. 1 Publication
VAR_064106
Natural varianti420 – 4201T → I in CLCD. 1 Publication
VAR_064107
Natural varianti420 – 4201T → N in CLCD. 1 Publication
VAR_064108
Natural varianti511 – 5111G → S in CLCD; unknown pathological significance. 1 Publication
Corresponds to variant rs11498198 [ dbSNP | Ensembl ].
VAR_012150
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 (1 Publication).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi451 – 4511S → A: Reduced DNA-binding and impaired phosphorylation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi119600. phenotype.
156510. phenotype.
Orphaneti1452. Cleidocranial dysplasia.
2504. Metaphyseal dysplasia - maxillary hypoplasia - brachydacty.
PharmGKBiPA34885.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Runt-related transcription factor 2
PRO_0000174659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei451 – 4511Phosphoserine; by CDK11 Publication

Post-translational modificationi

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-340.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13950.
PaxDbiQ13950.
PRIDEiQ13950.

PTM databases

PhosphoSiteiQ13950.

Expressioni

Tissue specificityi

Specifically expressed in osteoblasts.

Gene expression databases

ArrayExpressiQ13950.
BgeeiQ13950.
CleanExiHS_RUNX2.
GenevestigatoriQ13950.

Organism-specific databases

HPAiCAB008374.
CAB062561.
HPA022040.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The alpha subunit binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Interacts with XRCC6 (Ku70) and XRCC5 (Ku80). Interacts with 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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PIN1Q135267EBI-976402,EBI-714158
SMAD6O435413EBI-976402,EBI-976374

Protein-protein interaction databases

BioGridi107308. 43 interactions.
DIPiDIP-36707N.
IntActiQ13950. 5 interactions.
MINTiMINT-219985.
STRINGi9606.ENSP00000352514.

Structurei

3D structure databases

ProteinModelPortaliQ13950.
SMRiQ13950. Positions 103-252.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 229129Runt
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni242 – 25817Required for interaction with FOXO1 By similarity
Add
BLAST
Regioni336 – 439104Interaction with KAT6A By similarity
Add
BLAST
Regioni374 – 46895Interaction with KAT6B
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 7123Poly-Gln
Add
BLAST
Compositional biasi73 – 8917Poly-Ala
Add
BLAST
Compositional biasi237 – 521285Pro/Ser/Thr-rich
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 Runt domain.

Phylogenomic databases

eggNOGiNOG123889.
HOGENOMiHOG000045616.
HOVERGENiHBG060268.
InParanoidiQ13950.
KOiK09278.
PhylomeDBiQ13950.
TreeFamiTF321496.

Family and domain databases

Gene3Di2.60.40.720. 1 hit.
4.10.770.10. 1 hit.
InterProiIPR000040. AML1_Runt.
IPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR013524. Runt_dom.
IPR027384. Runx_central_dom.
IPR013711. RunxI_C_dom.
IPR016554. TF_Runt-rel_RUNX.
[Graphical view]
PANTHERiPTHR11950. PTHR11950. 1 hit.
PfamiPF00853. Runt. 1 hit.
PF08504. RunxI. 1 hit.
[Graphical view]
PIRSFiPIRSF009374. TF_Runt-rel_RUNX. 1 hit.
PRINTSiPR00967. ONCOGENEAML1.
SUPFAMiSSF49417. SSF49417. 1 hit.
PROSITEiPS51062. RUNT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13950-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MASNSLFSTV TPCQQNFFWD PSTSRRFSPP SSSLQPGKMS DVSPVVAAQQ    50
QQQQQQQQQQ QQQQQQQQQQ QEAAAAAAAA AAAAAAAAAV PRLRPPHDNR 100
TMVEIIADHP AELVRTDSPN FLCSVLPSHW RCNKTLPVAF KVVALGEVPD 150
GTVVTVMAGN DENYSAELRN ASAVMKNQVA RFNDLRFVGR SGRGKSFTLT 200
ITVFTNPPQV ATYHRAIKVT VDGPREPRRH RQKLDDSKPS LFSDRLSDLG 250
RIPHPSMRVG VPPQNPRPSL NSAPSPFNPQ GQSQITDPRQ AQSSPPWSYD 300
QSYPSYLSQM TSPSIHSTTP LSSTRGTGLP AITDVPRRIS DDDTATSDFC 350
LWPSTLSKKS QAGASELGPF SDPRQFPSIS SLTESRFSNP RMHYPATFTY 400
TPPVTSGMSL GMSATTHYHT YLPPPYPGSS QSQSGPFQTS STPYLYYGTS 450
SGSYQFPMVP GGDRSPSRML PPCTTTSNGS TLLNPNLPNQ NDGVDADGSH 500
SSSPTVLNSS GRMDESVWRP Y 521
Length:521
Mass (Da):56,648
Last modified:November 2, 2001 - v2
Checksum:i44C4F3867D6F3EB1
GO
Isoform 2 (identifier: Q13950-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MASNSLFSTVTPCQQNFFW → MRIPV

Show »
Length:507
Mass (Da):55,054
Checksum:i7228C267328DE1DC
GO
Isoform 3 (identifier: Q13950-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:499
Mass (Da):54,249
Checksum:i4BA956230C96EB2E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531Q → L in CLCD. 1 Publication
VAR_064081
Natural varianti78 – 836Missing.
VAR_012131
Natural varianti84 – 841A → AAAAAAAAAAA in CLCD associated with brachydactyly of hands and feet. 1 Publication
VAR_012130
Natural varianti113 – 1131L → R in CLCD. 1 Publication
VAR_012132
Natural varianti118 – 1181S → N in CLCD. 1 Publication
VAR_064082
Natural varianti118 – 1181S → R in CLCD. 1 Publication
VAR_012133
Natural varianti121 – 1211F → C in CLCD. 1 Publication
VAR_012134
Natural varianti123 – 1231C → R in CLCD. 1 Publication
VAR_012135
Natural varianti131 – 1311R → C in CLCD. 1 Publication
VAR_064083
Natural varianti131 – 1311R → G in CLCD. 1 Publication
VAR_064084
Natural varianti131 – 1311R → S in CLCD. 1 Publication
VAR_064085
Natural varianti133 – 1331Missing in CLCD. 1 Publication
VAR_012136
Natural varianti136 – 1361L → P in CLCD. 1 Publication
VAR_064086
Natural varianti156 – 1561V → D in CLCD. 1 Publication
VAR_064087
Natural varianti156 – 1561V → G in CLCD. 1 Publication
VAR_064088
Natural varianti169 – 1691R → P in CLCD. 2 Publications
VAR_064089
Natural varianti169 – 1691R → Q in CLCD. 1 Publication
VAR_012137
Natural varianti175 – 1751M → K in CLCD. 1 Publication
VAR_064090
Natural varianti175 – 1751M → R in CLCD; abolishes DNA binding. 2 Publications
VAR_012138
Natural varianti175 – 1751M → V in CLCD. 1 Publication
VAR_064091
Natural varianti187 – 1871F → S in CLCD. 1 Publication
VAR_064092
Natural varianti190 – 1901R → Q in CLCD; abolishes DNA binding. 1 Publication
VAR_012139
Natural varianti190 – 1901R → W in CLCD; has severely impaired DNA binding and transactivation. 3 Publications
VAR_012140
Natural varianti191 – 1911S → N in CLCD; abolishes DNA binding. 2 Publications
VAR_012141
Natural varianti193 – 1931R → C in CLCD. 1 Publication
VAR_012142
Natural varianti193 – 1931R → Q in CLCD. 1 Publication
VAR_064093
Natural varianti197 – 1971F → S in CLCD; retains heterodimerization activity together with a trace potential for DNA binding; retains a low but still substantial transactivation activity. 2 Publications
VAR_012143
Natural varianti199 – 1991L → F in CLCD; abolishes DNA binding. 1 Publication
VAR_012144
Natural varianti200 – 2001T → A in CLCD; mild; associated also with isolated dental anomalies; normal DNA binding. 1 Publication
VAR_012145
Natural varianti200 – 2001T → I in CLCD. 1 Publication
VAR_064094
Natural varianti201 – 2011I → K in CLCD. 1 Publication
VAR_064095
Natural varianti205 – 2051T → R in CLCD. 1 Publication
VAR_012146
Natural varianti209 – 2091Q → H in CLCD. 1 Publication
VAR_064096
Natural varianti209 – 2091Q → R in CLCD. 1 Publication
VAR_012147
Natural varianti211 – 2111A → P in CLCD. 1 Publication
VAR_064097
Natural varianti218 – 2181K → E in CLCD. 1 Publication
VAR_064098
Natural varianti218 – 2181K → N in CLCD; has severely impaired DNA binding and transactivation. 1 Publication
VAR_064099
Natural varianti218 – 2181K → Q in CLCD. 1 Publication
VAR_064100
Natural varianti220 – 2201T → I in CLCD; has severely impaired DNA binding and transactivation. 1 Publication
VAR_064101
Natural varianti225 – 2251R → L in CLCD. 1 Publication
VAR_064102
Natural varianti225 – 2251R → Q in CLCD; interferes with nuclear localization; abolishes DNA binding. 5 Publications
VAR_012148
Natural varianti225 – 2251R → W in CLCD; interferes with nuclear localization; has severely impaired DNA binding and transactivation. 4 Publications
VAR_012149
Natural varianti228 – 2281R → G in CLCD. 1 Publication
VAR_064103
Natural varianti233 – 2331K → R in CLCD. 1 Publication
VAR_064104
Natural varianti287 – 2871D → N in CLCD. 1 Publication
VAR_064105
Natural varianti362 – 3621A → V in CLCD. 1 Publication
VAR_064106
Natural varianti420 – 4201T → I in CLCD. 1 Publication
VAR_064107
Natural varianti420 – 4201T → N in CLCD. 1 Publication
VAR_064108
Natural varianti511 – 5111G → S in CLCD; unknown pathological significance. 1 Publication
Corresponds to variant rs11498198 [ dbSNP | Ensembl ].
VAR_012150

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1919MASNS…QNFFW → MRIPV in isoform 2.
VSP_005937Add
BLAST
Alternative sequencei341 – 36222Missing in isoform 3.
VSP_005938Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161N → S in AAC77441. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43467.2. [Q13950-1]
CCDS43468.2. [Q13950-3]
RefSeqiNP_001015051.3. NM_001015051.3. [Q13950-3]
NP_001019801.3. NM_001024630.3. [Q13950-1]
XP_006715294.1. XM_006715231.1. [Q13950-2]
UniGeneiHs.535845.

Genome annotation databases

EnsembliENST00000359524; ENSP00000352514; ENSG00000124813. [Q13950-2]
ENST00000371436; ENSP00000360491; ENSG00000124813. [Q13950-3]
ENST00000371438; ENSP00000360493; ENSG00000124813. [Q13950-1]
ENST00000465038; ENSP00000420707; ENSG00000124813. [Q13950-1]
GeneIDi860.
KEGGihsa:860.
UCSCiuc003oxt.3. human. [Q13950-2]
uc011dvx.2. human. [Q13950-1]
uc011dvy.2. human. [Q13950-3]

Polymorphism databases

DMDMi17368460.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43467.2. [Q13950-1 ]
CCDS43468.2. [Q13950-3 ]
RefSeqi NP_001015051.3. NM_001015051.3. [Q13950-3 ]
NP_001019801.3. NM_001024630.3. [Q13950-1 ]
XP_006715294.1. XM_006715231.1. [Q13950-2 ]
UniGenei Hs.535845.

3D structure databases

ProteinModelPortali Q13950.
SMRi Q13950. Positions 103-252.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107308. 43 interactions.
DIPi DIP-36707N.
IntActi Q13950. 5 interactions.
MINTi MINT-219985.
STRINGi 9606.ENSP00000352514.

PTM databases

PhosphoSitei Q13950.

Polymorphism databases

DMDMi 17368460.

Proteomic databases

MaxQBi Q13950.
PaxDbi Q13950.
PRIDEi Q13950.

Protocols and materials databases

DNASUi 860.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359524 ; ENSP00000352514 ; ENSG00000124813 . [Q13950-2 ]
ENST00000371436 ; ENSP00000360491 ; ENSG00000124813 . [Q13950-3 ]
ENST00000371438 ; ENSP00000360493 ; ENSG00000124813 . [Q13950-1 ]
ENST00000465038 ; ENSP00000420707 ; ENSG00000124813 . [Q13950-1 ]
GeneIDi 860.
KEGGi hsa:860.
UCSCi uc003oxt.3. human. [Q13950-2 ]
uc011dvx.2. human. [Q13950-1 ]
uc011dvy.2. human. [Q13950-3 ]

Organism-specific databases

CTDi 860.
GeneCardsi GC06P045295.
GeneReviewsi RUNX2.
HGNCi HGNC:10472. RUNX2.
HPAi CAB008374.
CAB062561.
HPA022040.
MIMi 119600. phenotype.
156510. phenotype.
600211. gene.
neXtProti NX_Q13950.
Orphaneti 1452. Cleidocranial dysplasia.
2504. Metaphyseal dysplasia - maxillary hypoplasia - brachydacty.
PharmGKBi PA34885.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG123889.
HOGENOMi HOG000045616.
HOVERGENi HBG060268.
InParanoidi Q13950.
KOi K09278.
PhylomeDBi Q13950.
TreeFami TF321496.

Enzyme and pathway databases

Reactomei REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
SignaLinki Q13950.

Miscellaneous databases

GeneWikii RUNX2.
GenomeRNAii 860.
NextBioi 3572.
PROi Q13950.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13950.
Bgeei Q13950.
CleanExi HS_RUNX2.
Genevestigatori Q13950.

Family and domain databases

Gene3Di 2.60.40.720. 1 hit.
4.10.770.10. 1 hit.
InterProi IPR000040. AML1_Runt.
IPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR013524. Runt_dom.
IPR027384. Runx_central_dom.
IPR013711. RunxI_C_dom.
IPR016554. TF_Runt-rel_RUNX.
[Graphical view ]
PANTHERi PTHR11950. PTHR11950. 1 hit.
Pfami PF00853. Runt. 1 hit.
PF08504. RunxI. 1 hit.
[Graphical view ]
PIRSFi PIRSF009374. TF_Runt-rel_RUNX. 1 hit.
PRINTSi PR00967. ONCOGENEAML1.
SUPFAMi SSF49417. SSF49417. 1 hit.
PROSITEi PS51062. RUNT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiRUNX2_HUMAN
AccessioniPrimary (citable) accession number: Q13950
Secondary accession number(s): O14614, O14615, O95181
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 2, 2001
Last modified: September 3, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi