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Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B)

 RUNX1_RAT               Reviewed;         450 AA.
Q63046;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 150.
RecName: Full=Runt-related transcription factor 1;
AltName: Full=Acute myeloid leukemia 1 protein;
AltName: Full=Core-binding factor subunit alpha-2;
Short=CBF-alpha-2;
AltName: Full=Oncogene AML-1;
AltName: Full=Polyomavirus enhancer-binding protein 2 alpha B subunit;
Short=PEA2-alpha B;
Short=PEBP2-alpha B;
Name=Runx1; Synonyms=Aml1, Cbfa2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
PubMed=7969143; DOI=10.1128/MCB.14.12.8051;
Zhu X., Yeadon J.E., Burden S.J.;
"AML1 is expressed in skeletal muscle and is regulated by
innervation.";
Mol. Cell. Biol. 14:8051-8057(1994).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND SER-21, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. The alpha subunit binds DNA and appears to have
a role in the development of normal hematopoiesis. Isoform AML-1L
interferes with the transactivation activity of RUNX1. Acts
synergistically with ELF4 to transactivate the IL-3 promoter and
with ELF2 to transactivate the BLK promoter. Inhibits KAT6B-
dependent transcriptional activation. 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 (By similarity). Positively regulates the
expression of RORC in T-helper 17 cells (By similarity).
{ECO:0000250|UniProtKB:Q01196, ECO:0000250|UniProtKB:Q03347}.
-!- SUBUNIT: Heterodimer with CBFB. RUNX1 binds DNA as a monomer and
through the Runt domain. DNA-binding is increased by
heterodimerization. Interacts with TLE1 and ALYREF/THOC4.
Interacts with ELF1, ELF2 and SPI1. Interacts via its Runt domain
with the ELF4 N-terminal region. Interaction with ELF2 isoform 2
(NERF-1a) may act to repress RUNX1-mediated transactivation.
Interacts with KAT6A and KAT6B. Interacts with SUV39H1, leading to
abrogation of transactivating and DNA-binding properties of RUNX1.
Interacts with YAP1 and HIPK2. Interaction with CDK6 prevents
myeloid differentiation, reducing its transcription
transactivation activity. Found in a complex with PRMT5, RUNX1 and
CBFB. Interacts with FOXP3. Interacts with TBX21.
{ECO:0000250|UniProtKB:Q01196, ECO:0000250|UniProtKB:Q03347}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Expressed in skeletal muscle.
{ECO:0000269|PubMed:7969143}.
-!- INDUCTION: Expression increases following denervation.
{ECO:0000269|PubMed:7969143}.
-!- DOMAIN: A proline/serine/threonine rich region at the C-terminus
is necessary for transcriptional activation of target genes.
-!- 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-272 and Ser-275 by HIPK2 when
associated with CBFB and DNA. This phosphorylation promotes
subsequent EP300 phosphorylation (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; L35271; AAA66191.1; -; mRNA.
RefSeq; NP_059021.1; NM_017325.2.
UniGene; Rn.11201; -.
ProteinModelPortal; Q63046; -.
SMR; Q63046; -.
BioGrid; 248410; 1.
ELM; Q63046; -.
STRING; 10116.ENSRNOP00000002313; -.
iPTMnet; Q63046; -.
PhosphoSitePlus; Q63046; -.
PaxDb; Q63046; -.
PRIDE; Q63046; -.
Ensembl; ENSRNOT00000002313; ENSRNOP00000002313; ENSRNOG00000001704.
GeneID; 50662; -.
KEGG; rno:50662; -.
UCSC; RGD:2283; rat.
CTD; 861; -.
RGD; 2283; Runx1.
eggNOG; KOG3982; Eukaryota.
eggNOG; ENOG4111J4Y; LUCA.
GeneTree; ENSGT00390000016964; -.
HOGENOM; HOG000045616; -.
HOVERGEN; HBG060268; -.
InParanoid; Q63046; -.
KO; K08367; -.
PhylomeDB; Q63046; -.
Reactome; R-RNO-549127; Organic cation transport.
Reactome; R-RNO-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
Reactome; R-RNO-8931987; RUNX1 regulates estrogen receptor mediated transcription.
Reactome; R-RNO-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-RNO-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-RNO-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
Reactome; R-RNO-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
Reactome; R-RNO-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
PRO; PR:Q63046; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001704; -.
ExpressionAtlas; Q63046; baseline and differential.
Genevisible; Q63046; RN.
GO; GO:0016513; C:core-binding factor complex; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:RGD.
GO; GO:0002062; P:chondrocyte differentiation; IBA:GO_Central.
GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
GO; GO:0043371; P:negative regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
GO; GO:0001503; P:ossification; IBA:GO_Central.
GO; GO:0030728; P:ovulation; IEP:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
GO; GO:0030854; P:positive regulation of granulocyte differentiation; ISS:UniProtKB.
GO; GO:2000872; P:positive regulation of progesterone secretion; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:RGD.
GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.60.40.720; -; 1.
Gene3D; 4.10.770.10; -; 1.
InterPro; IPR000040; AML1_Runt.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
InterPro; IPR013524; Runt_dom.
InterPro; IPR027384; Runx_central_dom_sf.
InterPro; IPR013711; RunxI_C_dom.
InterPro; IPR016554; TF_Runt-rel_RUNX.
PANTHER; PTHR11950; PTHR11950; 1.
Pfam; PF00853; Runt; 1.
Pfam; PF08504; RunxI; 1.
PIRSF; PIRSF009374; TF_Runt-rel_RUNX; 1.
PRINTS; PR00967; ONCOGENEAML1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS51062; RUNT; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; DNA-binding; Methylation;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 450 Runt-related transcription factor 1.
/FTId=PRO_0000174657.
DOMAIN 50 178 Runt. {ECO:0000255|PROSITE-
ProRule:PRU00399}.
REGION 80 84 Interaction with DNA. {ECO:0000250}.
REGION 135 143 Interaction with DNA. {ECO:0000250}.
REGION 168 177 Interaction with DNA. {ECO:0000250}.
REGION 290 369 Interaction with KAT6A. {ECO:0000250}.
REGION 306 398 Interaction with KAT6B. {ECO:0000250}.
REGION 360 400 Interaction with FOXP3.
{ECO:0000250|UniProtKB:Q01196}.
COMPBIAS 187 450 Pro/Ser/Thr-rich.
BINDING 112 112 Chloride 1. {ECO:0000255|PROSITE-
ProRule:PRU00399}.
BINDING 116 116 Chloride 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00399}.
BINDING 139 139 Chloride 2. {ECO:0000255|PROSITE-
ProRule:PRU00399}.
BINDING 170 170 Chloride 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00399}.
MOD_RES 14 14 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 24 24 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 43 43 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 249 249 Phosphoserine; by HIPK2.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 267 267 Phosphoserine.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 272 272 Phosphothreonine; by HIPK2.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 275 275 Phosphoserine; by HIPK2.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 295 295 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01196}.
MOD_RES 433 433 Phosphoserine.
{ECO:0000250|UniProtKB:Q01196}.
SEQUENCE 450 AA; 48556 MW; 4B53AD706D487AC3 CRC64;
MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGAAL ASKLRSGDRS MVEVLADHPG
ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG TLVTVMAGND ENYSAELRNA
TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI TVFTNPPQVA TYHRAIKITV DGPREPRRHR
QKLDDQTKPG SLSFSERLSE LEQLRRTAMR VSPHHPAPTP NPRASLNHST AFNPQPQSQM
QDARQIQPSP PWSYDQSYQY LGSITSSVHP ATPISPGRAS GMTSLSAELS SRLSTAPDLT
AFGDPRQFPT LPSISDPRMH YPGAFTYSPP VTSGIGIGMS AMSSTSRYHT YLPPPYPGSS
QAQAGPFQTG SPSYHLYYGT SAGSYQFSMV GGERSPPRIL PPCTNASTGA ALLNPSLPSQ
SDVVETEGSH SNSPTNMPPA RLEEAVWRPY


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