RUNX3_HUMAN
ID RUNX3_HUMAN Reviewed; 415 AA.
AC Q13761; B1AJV5; Q12969; Q13760;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Runt-related transcription factor 3;
DE AltName: Full=Acute myeloid leukemia 2 protein;
DE AltName: Full=Core-binding factor subunit alpha-3;
DE Short=CBF-alpha-3;
DE AltName: Full=Oncogene AML-2;
DE AltName: Full=Polyomavirus enhancer-binding protein 2 alpha C subunit;
DE Short=PEA2-alpha C;
DE Short=PEBP2-alpha C;
DE AltName: Full=SL3-3 enhancer factor 1 alpha C subunit;
DE AltName: Full=SL3/AKV core-binding factor alpha C subunit;
GN Name=RUNX3; Synonyms=AML2, CBFA3, PEBP2A3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7622058; DOI=10.1016/0378-1119(95)00060-j;
RA Bae S.-C., Takahashi E., Zhang Y.-W., Ogawa E., Shigesada K., Namba Y.,
RA Satake M., Ito Y.;
RT "Cloning, mapping and expression of PEBP2 alpha C, a third gene encoding
RT the mammalian Runt domain.";
RL Gene 159:245-248(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7835892; DOI=10.1006/geno.1994.1519;
RA Levanon D., Negreanu V., Bernstein Y., Bar-Am I., Avivi L., Groner Y.;
RT "AML1, AML2, and AML3, the human members of the runt domain gene-family:
RT cDNA structure, expression, and chromosomal localization.";
RL Genomics 23:425-432(1994).
RN [3]
RP SEQUENCE REVISION.
RA Groner Y.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-148.
RX PubMed=7607690; DOI=10.1016/0888-7543(95)80185-o;
RA Wijmenga C., Speck N.A., Dracopoli N.C., Hofker M.H., Liu P., Collins F.S.;
RT "Identification of a new murine runt domain-containing gene, Cbfa3, and
RT localization of the human homolog, CBFA3, to chromosome 1p35-pter.";
RL Genomics 26:611-614(1995).
RN [8]
RP INTERACTION WITH TLE1.
RX PubMed=9751710; DOI=10.1073/pnas.95.20.11590;
RA Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D.,
RA Stifani S., Paroush Z., Groner Y.;
RT "Transcriptional repression by AML1 and LEF-1 is mediated by the
RT TLE/Groucho corepressors.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998).
RN [9]
RP INTERACTION WITH SUV39H1.
RX PubMed=16652147; DOI=10.1038/sj.onc.1209591;
RA Reed-Inderbitzin E., Moreno-Miralles I., Vanden-Eynden S.K., Xie J.,
RA Lutterbach B., Durst-Goodwin K.L., Luce K.S., Irvin B.J., Cleary M.L.,
RA Brandt S.J., Hiebert S.W.;
RT "RUNX1 associates with histone deacetylases and SUV39H1 to repress
RT transcription.";
RL Oncogene 25:5777-5786(2006).
RN [10]
RP INTERACTION WITH FOXP3.
RX PubMed=17377532; DOI=10.1038/nature05673;
RA Ono M., Yaguchi H., Ohkura N., Kitabayashi I., Nagamura Y., Nomura T.,
RA Miyachi Y., Tsukada T., Sakaguchi S.;
RT "Foxp3 controls regulatory T-cell function by interacting with
RT AML1/Runx1.";
RL Nature 446:685-689(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP FUNCTION, INTERACTION WITH ZFHX3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20599712; DOI=10.1016/j.bbrc.2010.06.090;
RA Mabuchi M., Kataoka H., Miura Y., Kim T.S., Kawaguchi M., Ebi M.,
RA Tanaka M., Mori Y., Kubota E., Mizushima T., Shimura T., Mizoshita T.,
RA Tanida S., Kamiya T., Asai K., Joh T.;
RT "Tumor suppressor, AT motif binding factor 1 (ATBF1), translocates to the
RT nucleus with runt domain transcription factor 3 (RUNX3) in response to TGF-
RT beta signal transduction.";
RL Biochem. Biophys. Res. Commun. 398:321-325(2010).
RN [13]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH SRC; FYN AND
RP LCK.
RX PubMed=20100835; DOI=10.1074/jbc.m109.071381;
RA Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H.,
RA Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.;
RT "Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the
RT protein in the cytoplasm.";
RL J. Biol. Chem. 285:10122-10129(2010).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Forms the heterodimeric complex core-binding factor (CBF)
CC with CBFB. RUNX members modulate the transcription of their target
CC genes through recognizing the core consensus binding sequence 5'-
CC TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory
CC regions via their runt domain, while CBFB is a non-DNA-binding
CC regulatory subunit that allosterically enhances the sequence-specific
CC DNA-binding capacity of RUNX. The heterodimers bind to the core site of
CC a number of enhancers and promoters, including murine leukemia virus,
CC polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF
CC promoters (By similarity). May be involved in the control of cellular
CC proliferation and/or differentiation. In association with ZFHX3, up-
CC regulates CDKN1A promoter activity following TGF-beta stimulation
CC (PubMed:20599712). CBF complexes repress ZBTB7B transcription factor
CC during cytotoxic (CD8+) T cell development. They bind to RUNX-binding
CC sequence within the ZBTB7B locus acting as transcriptional silencer and
CC allowing for cytotoxic T cell differentiation. CBF complexes binding to
CC the transcriptional silencer is essential for recruitment of nuclear
CC protein complexes that catalyze epigenetic modifications to establish
CC epigenetic ZBTB7B silencing (By similarity).
CC {ECO:0000250|UniProtKB:Q64131, ECO:0000269|PubMed:20599712}.
CC -!- SUBUNIT: Heterodimer with CBFB. RUNX3 binds DNA as a monomer and
CC through the Runt domain. DNA-binding is increased by heterodimerization
CC (By similarity). Interacts with TLE1 and SUV39H1 (PubMed:9751710 and
CC PubMed:16652147). The tyrosine phosphorylated form (via runt domain)
CC interacts with SRC (via protein kinase domain)(PubMed:20100835).
CC Interacts with FYN and LCK (PubMed:20100835). Interacts with FOXP3
CC (PubMed:17377532). Interacts with ZFHX3 (PubMed:20599712). Interacts
CC with TBX21 (By similarity). {ECO:0000250|UniProtKB:Q64131,
CC ECO:0000269|PubMed:16652147, ECO:0000269|PubMed:17377532,
CC ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20599712,
CC ECO:0000269|PubMed:9751710}.
CC -!- INTERACTION:
CC Q13761; P25440: BRD2; NbExp=8; IntAct=EBI-925990, EBI-2874802;
CC Q13761; P35222: CTNNB1; NbExp=12; IntAct=EBI-925990, EBI-491549;
CC Q13761; Q09472: EP300; NbExp=7; IntAct=EBI-925990, EBI-447295;
CC Q13761; P56524: HDAC4; NbExp=9; IntAct=EBI-925990, EBI-308629;
CC Q13761; Q9UQL6: HDAC5; NbExp=5; IntAct=EBI-925990, EBI-715576;
CC Q13761; Q9NQB0: TCF7L2; NbExp=14; IntAct=EBI-925990, EBI-924724;
CC Q13761; Q04724: TLE1; NbExp=3; IntAct=EBI-925990, EBI-711424;
CC Q13761-2; Q13951: CBFB; NbExp=3; IntAct=EBI-12145465, EBI-718750;
CC Q13761-2; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-12145465, EBI-11978177;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00399,
CC ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20599712}. Cytoplasm
CC {ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20599712}. Note=The
CC tyrosine phosphorylated form localizes to the cytoplasm. Translocates
CC from the cytoplasm to the nucleus following TGF-beta stimulation.
CC {ECO:0000269|PubMed:20599712}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13761-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13761-2; Sequence=VSP_005949;
CC -!- TISSUE SPECIFICITY: Expressed in gastric cancer tissues (at protein
CC level). {ECO:0000269|PubMed:20599712}.
CC -!- DOMAIN: A proline/serine/threonine rich region at the C-terminus is
CC necessary for transcriptional activation of target genes.
CC -!- PTM: Phosphorylated on tyrosine residues by SRC. Phosphorylated by LCK
CC and FYN. {ECO:0000269|PubMed:20100835}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z35278; CAA84541.1; -; mRNA.
DR EMBL; X79550; CAA56093.2; -; mRNA.
DR EMBL; AL023096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW95148.1; -; Genomic_DNA.
DR EMBL; BC013362; AAH13362.1; -; mRNA.
DR EMBL; U14520; AAA86465.1; -; Genomic_DNA.
DR CCDS; CCDS257.1; -. [Q13761-1]
DR CCDS; CCDS30633.1; -. [Q13761-2]
DR PIR; B55563; B55563.
DR PIR; S60078; S60078.
DR RefSeq; NP_001026850.1; NM_001031680.2. [Q13761-2]
DR RefSeq; NP_001307601.1; NM_001320672.1. [Q13761-2]
DR RefSeq; NP_004341.1; NM_004350.2. [Q13761-1]
DR RefSeq; XP_005246081.1; XM_005246024.4. [Q13761-2]
DR PDB; 5W69; X-ray; 2.80 A; I/J/K/L=133-141.
DR PDBsum; 5W69; -.
DR AlphaFoldDB; Q13761; -.
DR SMR; Q13761; -.
DR BioGRID; 107312; 66.
DR ELM; Q13761; -.
DR IntAct; Q13761; 22.
DR MINT; Q13761; -.
DR STRING; 9606.ENSP00000382800; -.
DR GlyGen; Q13761; 11 sites, 1 O-linked glycan (11 sites).
DR iPTMnet; Q13761; -.
DR PhosphoSitePlus; Q13761; -.
DR SwissPalm; Q13761; -.
DR BioMuta; RUNX3; -.
DR DMDM; 17368453; -.
DR EPD; Q13761; -.
DR jPOST; Q13761; -.
DR MassIVE; Q13761; -.
DR MaxQB; Q13761; -.
DR PaxDb; Q13761; -.
DR PeptideAtlas; Q13761; -.
DR PRIDE; Q13761; -.
DR ProteomicsDB; 59677; -. [Q13761-1]
DR ProteomicsDB; 59678; -. [Q13761-2]
DR Antibodypedia; 1124; 706 antibodies from 43 providers.
DR DNASU; 864; -.
DR Ensembl; ENST00000308873.11; ENSP00000308051.6; ENSG00000020633.19. [Q13761-1]
DR Ensembl; ENST00000338888.3; ENSP00000343477.3; ENSG00000020633.19. [Q13761-2]
DR Ensembl; ENST00000399916.5; ENSP00000382800.1; ENSG00000020633.19. [Q13761-2]
DR GeneID; 864; -.
DR KEGG; hsa:864; -.
DR MANE-Select; ENST00000308873.11; ENSP00000308051.6; NM_004350.3; NP_004341.1.
DR UCSC; uc001bjq.4; human. [Q13761-1]
DR CTD; 864; -.
DR DisGeNET; 864; -.
DR GeneCards; RUNX3; -.
DR HGNC; HGNC:10473; RUNX3.
DR HPA; ENSG00000020633; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 600210; gene.
DR neXtProt; NX_Q13761; -.
DR OpenTargets; ENSG00000020633; -.
DR PharmGKB; PA34886; -.
DR VEuPathDB; HostDB:ENSG00000020633; -.
DR eggNOG; KOG3982; Eukaryota.
DR GeneTree; ENSGT00940000156598; -.
DR HOGENOM; CLU_032910_3_0_1; -.
DR InParanoid; Q13761; -.
DR OMA; TQGLWPE; -.
DR PhylomeDB; Q13761; -.
DR TreeFam; TF321496; -.
DR PathwayCommons; Q13761; -.
DR Reactome; R-HSA-4411364; Binding of TCF/LEF:CTNNB1 to target gene promoters.
DR Reactome; R-HSA-8941855; RUNX3 regulates CDKN1A transcription.
DR Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
DR Reactome; R-HSA-8951430; RUNX3 regulates WNT signaling.
DR Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
DR Reactome; R-HSA-8951911; RUNX3 regulates RUNX1-mediated transcription.
DR Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-HSA-8952158; RUNX3 regulates BCL2L11 (BIM) transcription.
DR SignaLink; Q13761; -.
DR SIGNOR; Q13761; -.
DR BioGRID-ORCS; 864; 13 hits in 1092 CRISPR screens.
DR ChiTaRS; RUNX3; human.
DR GeneWiki; RUNX3; -.
DR GenomeRNAi; 864; -.
DR Pharos; Q13761; Tbio.
DR PRO; PR:Q13761; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13761; protein.
DR Bgee; ENSG00000020633; Expressed in granulocyte and 162 other tissues.
DR ExpressionAtlas; Q13761; baseline and differential.
DR Genevisible; Q13761; HS.
DR GO; GO:0000785; C:chromatin; ISS:BHF-UCL.
DR GO; GO:0016513; C:core-binding factor complex; TAS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISS:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; IBA:GO_Central.
DR GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
DR GO; GO:0043371; P:negative regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
DR GO; GO:0048935; P:peripheral nervous system neuron development; TAS:BHF-UCL.
DR GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0071559; P:response to transforming growth factor beta; IDA:UniProtKB.
DR Gene3D; 2.60.40.720; -; 1.
DR InterPro; IPR000040; AML1_Runt.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR013524; Runt_dom.
DR InterPro; IPR013711; RunxI_C_dom.
DR InterPro; IPR016554; TF_Runt-rel_RUNX.
DR PANTHER; PTHR11950; PTHR11950; 1.
DR Pfam; PF00853; Runt; 1.
DR Pfam; PF08504; RunxI; 1.
DR PIRSF; PIRSF009374; TF_Runt-rel_RUNX; 1.
DR PRINTS; PR00967; ONCOGENEAML1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS51062; RUNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..415
FT /note="Runt-related transcription factor 3"
FT /id="PRO_0000174662"
FT DOMAIN 54..182
FT /note="Runt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT CROSSLNK 192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..5
FT /note="MRIPV -> MASNSIFDSFPTYSPTFIR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005949"
FT CONFLICT 249
FT /note="D -> V (in Ref. 2; CAA56093)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="P -> S (in Ref. 2; CAA56093)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="P -> S (in Ref. 2; CAA56093)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="T -> S (in Ref. 2; CAA56093)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="MH -> IY (in Ref. 2; CAA56093)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="P -> T (in Ref. 2; CAA56093)"
FT /evidence="ECO:0000305"
FT CONFLICT 297..298
FT /note="MP -> IS (in Ref. 2; CAA56093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 44356 MW; 593FBFB3C4639BBD CRC64;
MRIPVDPSTS RRFTPPSPAF PCGGGGGKMG ENSGALSAQA AVGPGGRARP EVRSMVDVLA
DHAGELVRTD SPNFLCSVLP SHWRCNKTLP VAFKVVALGD VPDGTVVTVM AGNDENYSAE
LRNASAVMKN QVARFNDLRF VGRSGRGKSF TLTITVFTNP TQVATYHRAI KVTVDGPREP
RRHRQKLEDQ TKPFPDRFGD LERLRMRVTP STPSPRGSLS TTSHFSSQPQ TPIQGTSELN
PFSDPRQFDR SFPTLPTLTE SRFPDPRMHY PGAMSAAFPY SATPSGTSIS SLSVAGMPAT
SRFHHTYLPP PYPGAPQNQS GPFQANPSPY HLYYGTSSGS YQFSMVAGSS SGGDRSPTRM
LASCTSSAAS VAAGNLMNPS LGGQSDGVEA DGSHSNSPTA LSTPGRMDEA VWRPY
