RUNX1
entrez
861
canonical
uniprot
Q01196
canonical
ensembl
ENSG00000159216
resolver
ensp
ENSP00000300305
resolver
ensp
ENSP00000340690
resolver
ensp
ENSP00000351123
resolver
ensp
ENSP00000382184
resolver
ensp
ENSP00000501943
resolver
ensp
ENSP00000552586
resolver
genesymbol
RUNX1
resolver
genesymbol_syn
AML1
resolver
genesymbol_syn
CBFA2
resolver
hgnc
HGNC:10471
resolver
uniprot
A8MV94
resolver
uniprot
B2RMS4
resolver
uniprot
D3DSG1
resolver
uniprot
O60472
resolver
uniprot
O60473
resolver
uniprot
O76047
resolver
uniprot
O76089
resolver
uniprot
Q13081
resolver
uniprot
Q13755
resolver
uniprot
Q13756
resolver
uniprot
Q13757
resolver
uniprot
Q13758
resolver
uniprot
Q13759
resolver
uniprot
Q15341
resolver
uniprot
Q15343
resolver
uniprot
Q16122
resolver
uniprot
Q16284
resolver
uniprot
Q16285
resolver
uniprot
Q16286
resolver
uniprot
Q16346
resolver
uniprot
Q16347
resolver
uniprot
Q92479
resolver
uniprot_entry
RUNX1_HUMAN
resolver
uniprot_sec
A8MV94
resolver
uniprot_sec
B2RMS4
resolver
uniprot_sec
D3DSG1
resolver
uniprot_sec
O60472
resolver
uniprot_sec
O60473
resolver
uniprot_sec
O76047
resolver
uniprot_sec
O76089
resolver
uniprot_sec
Q13081
resolver
uniprot_sec
Q13755
resolver
uniprot_sec
Q13756
resolver
uniprot_sec
Q13757
resolver
uniprot_sec
Q13758
resolver
uniprot_sec
Q13759
resolver
uniprot_sec
Q15341
resolver
uniprot_sec
Q15343
resolver
uniprot_sec
Q16122
resolver
uniprot_sec
Q16284
resolver
uniprot_sec
Q16285
resolver
uniprot_sec
Q16286
resolver
uniprot_sec
Q16346
resolver
uniprot_sec
Q16347
resolver
uniprot_sec
Q92479
resolver
amino_acid_sequence
MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPPYPGSSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNSPTNMAPSARLEEAVWRPY
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause of M2 type acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with RUNX1T1.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause of therapy-related myelodysplastic syndrome (T-MDS). Translocation t(3;21)(q26;q22) with EAP or MECOM.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22) with EAP or MECOM.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is found in childhood acute lymphoblastic leukemia (ALL). Translocation t(12;21)(p13;q22) with TEL. The translocation fuses the 3'-end of TEL to the alternate 5'-exon of AML-1H.; DISEASE: Note=A chromosomal aberration involving RUNX1 is found in acute leukemia. Translocation t(11,21)(q13;q22) that forms a MACROD1-RUNX1 fusion protein.; DISEASE: Familial platelet disorder with associated myeloid malignancy (FPDMM) [MIM:601399]: Autosomal dominant disease characterized by qualitative and quantitative platelet defects, and propensity to develop acute myelogenous leukemia. {ECO:0000269|PubMed:10508512}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is found in therapy-related myeloid malignancies. Translocation t(16;21)(q24;q22) that forms a RUNX1-CBFA2T3 fusion protein.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause of chronic myelomonocytic leukemia. Inversion inv(21)(q21;q22) with USP16.; DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is found in acute myeloid leukemia. Translocation t(20;21)(q11;q22) with CBFA2T2. {ECO:0000269|PubMed:20520637}.
uniprot
proteins
function
FUNCTION: Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis (PubMed:17431401). Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter (PubMed:10207087, PubMed:14970218). Inhibits KAT6B-dependent transcriptional activation (By similarity). Involved in lineage commitment of immature T cell precursors. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells (PubMed:17377532). Positively regulates the expression of RORC in T-helper 17 cells (By similarity). {ECO:0000250|UniProtKB:Q03347, ECO:0000269|PubMed:10207087, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:14970218, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:17431401, ECO:0000305}.; FUNCTION: Isoform AML-1G shows higher binding activities for target genes and binds TCR-beta-E2 and RAG-1 target site with threefold higher affinity than other isoforms. It is less effective in the context of neutrophil terminal differentiation. {ECO:0000250|UniProtKB:Q03347}.; FUNCTION: Isoform AML-1L interferes with the transactivation activity of RUNX1. {ECO:0000269|PubMed:9199349}.
uniprot
proteins
mass_dalton
48737
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="S->R: Loss of heterodimerization and reduced EP300 phosphorylation induction."; /evidence="ECO:0000269|PubMed:18695000"; MUTAGEN 80; /note="R->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 83; /note="K->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260, ECO:0000269|PubMed:18695000"; MUTAGEN 83; /note="K->E: Strongly reduces DNA-binding, impaired phosphorylation and reduced EP300 phosphorylation induction."; /evidence="ECO:0000269|PubMed:11276260, ECO:0000269|PubMed:18695000"; MUTAGEN 84; /note="T->A: No effect on DNA binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 106; /note="M->V: Disrupts interaction of AML1-MTG8/ETO with CBFB, no effect on AML1-MTG8/ETO-mediated transformation activity."; /evidence="ECO:0000269|PubMed:19202074"; MUTAGEN 107; /note="A->T: Loss of heterodimerization. Disrupts interactionof AML1-MTG8/ETO with CBFB, no effect on AML1-MTG8/ETO-mediated transformation activity."; /evidence="ECO:0000269|PubMed:10404214, ECO:0000269|PubMed:19202074"; MUTAGEN 108; /note="G->R: Loss of heterodimerization and impaired phosphorylation."; /evidence="ECO:0000269|PubMed:10404214, ECO:0000269|PubMed:18695000"; MUTAGEN 135; /note="R->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 139; /note="R->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 140; /note="S->G: Disrupts AML1-MTG8/ETODNA-binding, decreases AML1-MTG8/ETO transforming activity."; /evidence="ECO:0000269|PubMed:19202074"; MUTAGEN 142; /note="R->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 145..453; /note="Missing: No DNA-binding."; MUTAGEN 167; /note="K->A: Reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 169; /note="T->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 171; /note="D->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 174; /note="R->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 177; /note="R->A: Strongly reduces DNA-binding."; /evidence="ECO:0000269|PubMed:11276260"; MUTAGEN 249; /note="S->A: Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:18695000"; MUTAGEN 273; /note="T->A: Reduced phosphorylation; when associated with A-276."; /evidence="ECO:0000269|PubMed:18695000"; MUTAGEN 276; /note="S->A: Reduced phosphorylation; when associated with A-273."; /evidence="ECO:0000269|PubMed:18695000
uniprot
proteins
post_translational_modification
PTM: Phosphorylated in its C-terminus upon IL-6 treatment. Phosphorylation enhances interaction with KAT6A.; PTM: Methylated. {ECO:0000269|PubMed:12917624}.; PTM: Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when associated with CBFB and DNA. This phosphorylation promotes subsequent EP300 phosphorylation. {ECO:0000269|PubMed:18695000}.
uniprot
proteins
pubmed
10207087
uniprot
proteins
pubmed
10404214
uniprot
proteins
pubmed
10508512
uniprot
proteins
pubmed
10545320
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
10856244
uniprot
proteins
pubmed
11276260
uniprot
proteins
pubmed
11742995
uniprot
proteins
pubmed
11965546
uniprot
proteins
pubmed
12217689
uniprot
proteins
pubmed
12377125
uniprot
proteins
pubmed
12917624
uniprot
proteins
pubmed
1423235
uniprot
proteins
pubmed
14970218
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1560822
uniprot
proteins
pubmed
16652147
uniprot
proteins
pubmed
1720541
uniprot
proteins
pubmed
17377532
uniprot
proteins
pubmed
17431401
uniprot
proteins
pubmed
17532767
uniprot
proteins
pubmed
18280240
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18695000
uniprot
proteins
pubmed
18925961
uniprot
proteins
pubmed
19202074
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20520637
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25134913
uniprot
proteins
pubmed
28533407
uniprot
proteins
pubmed
7533526
uniprot
proteins
pubmed
7541640
uniprot
proteins
pubmed
7651838
uniprot
proteins
pubmed
7761424
uniprot
proteins
pubmed
7780150
uniprot
proteins
pubmed
7795214
uniprot
proteins
pubmed
7835892
uniprot
proteins
pubmed
7891692
uniprot
proteins
pubmed
7919324
uniprot
proteins
pubmed
8313895
uniprot
proteins
pubmed
8334990
uniprot
proteins
pubmed
8353289
uniprot
proteins
pubmed
8395054
uniprot
proteins
pubmed
8413232
uniprot
proteins
pubmed
8490181
uniprot
proteins
pubmed
8634147
uniprot
proteins
pubmed
8700862
uniprot
proteins
pubmed
9119228
uniprot
proteins
pubmed
9199349
uniprot
proteins
pubmed
9596646
uniprot
proteins
pubmed
9751710
uniprot
proteins
sequence_length
453
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus.
uniprot
proteins