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Q13761 (RUNX3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Runt-related transcription factor 3
Alternative name(s):
Acute myeloid leukemia 2 protein
Core-binding factor subunit alpha-3
Short name=CBF-alpha-3
Oncogene AML-2
Polyomavirus enhancer-binding protein 2 alpha C subunit
Short name=PEA2-alpha C
Short name=PEBP2-alpha C
SL3-3 enhancer factor 1 alpha C subunit
SL3/AKV core-binding factor alpha C subunit
Gene names
Name:RUNX3
Synonyms:AML2, CBFA3, PEBP2A3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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, lck, IL-3 and GM-CSF promoters.

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 TLE1 and SUV39H1. The tyrosine phosphorylated form (via runt domain) interacts with SRC (via protein kinase domain). Interacts with FYN and LCK. Ref.8 Ref.9 Ref.11

Subcellular location

Nucleus. Cytoplasm. Note: The tyrosine phosphorylated form localizes to the cytoplasm. Ref.11

Domain

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

Post-translational modification

Phosphorylated on tyrosine residues by SRC. Phosphorylated by LCK and FYN. Ref.11

Sequence similarities

Contains 1 Runt domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from electronic annotation. Source: Ensembl

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

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

peripheral nervous system neuron development

Traceable author statement PubMed 20096094. Source: BHF-UCL

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of transcription, DNA-templated

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

transcription from RNA polymerase II promoter

Traceable author statement Ref.7. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

nuclear chromatin

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

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionATP binding

Non-traceable author statement Ref.2. Source: UniProtKB

RNA polymerase II regulatory region sequence-specific DNA binding

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

protein binding

Inferred from physical interaction Ref.11Ref.8. Source: UniProtKB

sequence-specific DNA binding RNA polymerase II transcription factor activity

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

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.7. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13761-1)

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: Q13761-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MRIPV → MASNSIFDSFPTYSPTFIR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Runt-related transcription factor 3
PRO_0000174662

Regions

Domain54 – 182129Runt
Compositional bias23 – 275Poly-Gly
Compositional bias191 – 415225Pro/Ser/Thr-rich

Amino acid modifications

Modified residue2431Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 55MRIPV → MASNSIFDSFPTYSPTFIR in isoform 2.
VSP_005949

Experimental info

Sequence conflict2491D → V in CAA56093. Ref.2
Sequence conflict2531P → S in CAA56093. Ref.2
Sequence conflict2561P → S in CAA56093. Ref.2
Sequence conflict2591T → S in CAA56093. Ref.2
Sequence conflict268 – 2692MH → IY in CAA56093. Ref.2
Sequence conflict2711P → T in CAA56093. Ref.2
Sequence conflict297 – 2982MP → IS in CAA56093. Ref.2

Sequences

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

Last modified November 1, 1999. Version 2.
Checksum: 593FBFB3C4639BBD

FASTA41544,356
        10         20         30         40         50         60 
MRIPVDPSTS RRFTPPSPAF PCGGGGGKMG ENSGALSAQA AVGPGGRARP EVRSMVDVLA 

        70         80         90        100        110        120 
DHAGELVRTD SPNFLCSVLP SHWRCNKTLP VAFKVVALGD VPDGTVVTVM AGNDENYSAE 

       130        140        150        160        170        180 
LRNASAVMKN QVARFNDLRF VGRSGRGKSF TLTITVFTNP TQVATYHRAI KVTVDGPREP 

       190        200        210        220        230        240 
RRHRQKLEDQ TKPFPDRFGD LERLRMRVTP STPSPRGSLS TTSHFSSQPQ TPIQGTSELN 

       250        260        270        280        290        300 
PFSDPRQFDR SFPTLPTLTE SRFPDPRMHY PGAMSAAFPY SATPSGTSIS SLSVAGMPAT 

       310        320        330        340        350        360 
SRFHHTYLPP PYPGAPQNQS GPFQANPSPY HLYYGTSSGS YQFSMVAGSS SGGDRSPTRM 

       370        380        390        400        410 
LASCTSSAAS VAAGNLMNPS LGGQSDGVEA DGSHSNSPTA LSTPGRMDEA VWRPY 

« Hide

Isoform 2 [UniParc].

Checksum: E9A43E96EDF82389
Show »

FASTA42945,922

References

« Hide 'large scale' references
[1]"Cloning, mapping and expression of PEBP2 alpha C, a third gene encoding the mammalian Runt domain."
Bae S.-C., Takahashi E., Zhang Y.-W., Ogawa E., Shigesada K., Namba Y., Satake M., Ito Y.
Gene 159:245-248(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"AML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localization."
Levanon D., Negreanu V., Bernstein Y., Bar-Am I., Avivi L., Groner Y.
Genomics 23:425-432(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Groner Y.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Skin.
[7]"Identification of a new murine runt domain-containing gene, Cbfa3, and localization of the human homolog, CBFA3, to chromosome 1p35-pter."
Wijmenga C., Speck N.A., Dracopoli N.C., Hofker M.H., Liu P., Collins F.S.
Genomics 26:611-614(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-148.
[8]"Transcriptional repression by AML1 and LEF-1 is mediated by the TLE/Groucho corepressors."
Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D., Stifani S., Paroush Z., Groner Y.
Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TLE1.
[9]"RUNX1 associates with histone deacetylases and SUV39H1 to repress transcription."
Reed-Inderbitzin E., Moreno-Miralles I., Vanden-Eynden S.K., Xie J., Lutterbach B., Durst-Goodwin K.L., Luce K.S., Irvin B.J., Cleary M.L., Brandt S.J., Hiebert S.W.
Oncogene 25:5777-5786(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUV39H1.
[10]"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-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm."
Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.
J. Biol. Chem. 285:10122-10129(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH SRC; FYN AND LCK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35278 mRNA. Translation: CAA84541.1.
X79550 mRNA. Translation: CAA56093.2.
AL023096 Genomic DNA. Translation: CAA18856.1.
AL445471, AL023096 Genomic DNA. Translation: CAC42093.2.
AL023096, AL445471 Genomic DNA. Translation: CAI20422.1.
CH471134 Genomic DNA. Translation: EAW95148.1.
BC013362 mRNA. Translation: AAH13362.1.
U14520 Genomic DNA. Translation: AAA86465.1.
CCDSCCDS257.1. [Q13761-1]
CCDS30633.1. [Q13761-2]
PIRB55563.
S60078.
RefSeqNP_001026850.1. NM_001031680.2. [Q13761-2]
NP_004341.1. NM_004350.2. [Q13761-1]
XP_005246081.1. XM_005246024.2. [Q13761-2]
UniGeneHs.170019.

3D structure databases

ProteinModelPortalQ13761.
SMRQ13761. Positions 56-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107312. 27 interactions.
IntActQ13761. 15 interactions.
MINTMINT-6774046.
STRING9606.ENSP00000343477.

PTM databases

PhosphoSiteQ13761.

Polymorphism databases

DMDM17368453.

Proteomic databases

MaxQBQ13761.
PaxDbQ13761.
PRIDEQ13761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308873; ENSP00000308051; ENSG00000020633. [Q13761-1]
ENST00000338888; ENSP00000343477; ENSG00000020633. [Q13761-2]
ENST00000399916; ENSP00000382800; ENSG00000020633. [Q13761-2]
GeneID864.
KEGGhsa:864.
UCSCuc001bjq.3. human. [Q13761-1]
uc001bjr.3. human. [Q13761-2]

Organism-specific databases

CTD864.
GeneCardsGC01M025226.
HGNCHGNC:10473. RUNX3.
HPACAB025416.
MIM600210. gene.
neXtProtNX_Q13761.
PharmGKBPA34886.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG123889.
HOGENOMHOG000045616.
HOVERGENHBG060268.
KOK09279.
OMAFPYSATP.
OrthoDBEOG7WQ7TV.
PhylomeDBQ13761.
TreeFamTF321496.

Gene expression databases

ArrayExpressQ13761.
BgeeQ13761.
CleanExHS_RUNX3.
GenevestigatorQ13761.

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

GeneWikiRUNX3.
GenomeRNAi864.
NextBio3602.
PROQ13761.
SOURCESearch...

Entry information

Entry nameRUNX3_HUMAN
AccessionPrimary (citable) accession number: Q13761
Secondary accession number(s): B1AJV5, Q12969, Q13760
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 149 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM