Q03347
uniprot
Q03347
canonical
amino_acid_sequence
MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDGGPALASKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDARQIQPSPPWSYDQSYQYLGSITSSSVHPATPISPGRASGMTSLSAELSSRLSTAPDLTAFGDPRQFPTLPSISDPRMHYPGAFTYSPPVTSGIGIGMSAMSSASRYHTYLPPPYPGSSQAQAGPFQTGSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGAALLNPSLPSQSDVVETEGSHSNSPTNMPPARLEEAVWRPY
uniprot
proteins
disease_involvement
DISEASE: Note=Mice with an Runx1 lacking the DNA-binding region are found to die between embryonic days 11.5 to 12.5 due to hemorrhaging in the central nervous system. This hemorrhaging is preceded by necrosis and hematopoiesis is blocked (PubMed:8622955). {ECO:0000269|PubMed:8622955}.
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. Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter. 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 (PubMed:18258917). CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (PubMed:23481257). 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 (PubMed:21151104). {ECO:0000250|UniProtKB:Q01196, ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:18258917, ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:23481257, ECO:0000305}.; FUNCTION: Isoform 4 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:0000269|PubMed:11203699}.
uniprot
proteins
mass_dalton
48610
uniprot
proteins
mutagenesis
MUTAGEN 80; /note="R->A: Interferes with DNA-binding."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 109; /note="N->A: Interferes with heterodimerization."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 113; /note="Y->A: Interferes with heterodimerization."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 142; /note="R->A: Interferes with DNA-binding."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 144; /note="K->M: Interferes with DNA-binding."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 149; /note="T->A: Interferes with heterodimerization."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 170; /note="V->A: No effect."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 171; /note="D->A: Interferes with DNA-binding."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 174; /note="R->A: Interferes with DNA-binding."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 177; /note="R->A: Interferes with DNA-binding."; /evidence="ECO:0000269|PubMed:11257229"; MUTAGEN 249; /note="S->A: Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:16917507"; MUTAGEN 276; /note="S->A: Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:16917507"; MUTAGEN 447..451; /note="Missing: Inhibits repression of ZBTB7B expression."; /evidence="ECO:0000269|PubMed:18258917, ECO:0000269|PubMed:23481257
uniprot
proteins
post_translational_modification
PTM: Phosphorylated in its C-terminus upon IL-6 treatment. Phosphorylation enhances interaction with KAT6A (By similarity). {ECO:0000250}.; PTM: Methylated. {ECO:0000250}.; 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:16917507}.
uniprot
proteins
pubmed
10903914
uniprot
proteins
pubmed
11203699
uniprot
proteins
pubmed
11243869
uniprot
proteins
pubmed
11257229
uniprot
proteins
pubmed
11375505
uniprot
proteins
pubmed
12217689
uniprot
proteins
pubmed
16917507
uniprot
proteins
pubmed
17377532
uniprot
proteins
pubmed
18258917
uniprot
proteins
pubmed
21151104
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22193545
uniprot
proteins
pubmed
23481257
uniprot
proteins
pubmed
8164679
uniprot
proteins
pubmed
8437866
uniprot
proteins
pubmed
8565077
uniprot
proteins
pubmed
8622955
uniprot
proteins
sequence_length
451
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17377532}.
uniprot
proteins