MYB_HUMAN
ID MYB_HUMAN Reviewed; 640 AA.
AC P10242; E9PI07; E9PLZ5; E9PNA4; E9PNL6; E9PRS2; P78391; P78392; P78525;
AC P78526; Q14023; Q14024; Q708E4; Q708E7; Q9UE83;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Transcriptional activator Myb;
DE AltName: Full=Proto-oncogene c-Myb;
GN Name=MYB;
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=3540945; DOI=10.1073/pnas.83.24.9636;
RA Majello B., Kenyon L.C., Dalla-Favera R.;
RT "Human c-myb protooncogene: nucleotide sequence of cDNA and organization of
RT the genomic locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9636-9640(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=2202948;
RA Westin E.H., Gorse K.M., Clarke M.F.;
RT "Alternative splicing of the human c-myb gene.";
RL Oncogene 5:1117-1124(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
RX PubMed=15169551; DOI=10.1186/1471-2164-5-33;
RA Close J.P., Game L., Clark B., Bergounioux J., Gerovassili A., Thein S.L.;
RT "Genome annotation of a 1.5 Mb region of human chromosome 6q23 encompassing
RT a quantitative trait locus for fetal hemoglobin expression in adults.";
RL BMC Genomics 5:33-33(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 6).
RC TISSUE=Liver, and Placenta;
RA Westin E.H., Gorse K.M.;
RT "Characterization of the complete sequence structure of the human c-myb
RT gene.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gaillard C., Perbal B.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 8; 9; 10 AND 11), AND ALTERNATIVE
RP SPLICING.
RA O'Rourke J.P. Jr., Ness S.A.;
RT "Complex RNA splicing produces multiple forms of c-Myb with distinct
RT transcriptional activities.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1).
RX PubMed=8302584;
RA Jacobs S.M., Gorse K.M., Westin E.H.;
RT "Identification of a second promoter in the human c-myb proto-oncogene.";
RL Oncogene 9:227-235(1994).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=1944282; DOI=10.1128/mcb.11.12.6166-6176.1991;
RA Nicolaides N.C., Gualdi R., Casadevall C., Manzella L., Calabretta B.;
RT "Positive autoregulation of c-myb expression via Myb binding sites in the
RT 5' flanking region of the human c-myb gene.";
RL Mol. Cell. Biol. 11:6166-6176(1991).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-640 (ISOFORMS 1 AND 12).
RX PubMed=3014652; DOI=10.1126/science.3014652;
RA Slamon D.J., Boone T.C., Murdock D.C., Keith D.E., Press M.F., Larson R.A.,
RA Souza L.M.;
RT "Studies of the human c-myb gene and its product in human acute
RT leukemias.";
RL Science 233:347-351(1986).
RN [13]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=2687764;
RA Dasgupta P., Reddy E.P.;
RT "Identification of alternatively spliced transcripts for human c-myb:
RT molecular cloning and sequence analysis of human c-myb exon 9A sequences.";
RL Oncogene 4:1419-1423(1989).
RN [14]
RP DOMAIN.
RX PubMed=2189102;
RA Kalkbrenner F., Guehmann S., Moelling K.;
RT "Transcriptional activation by human c-myb and v-myb genes.";
RL Oncogene 5:657-661(1990).
RN [15]
RP INTERACTION WITH SIAH1, AND DEGRADATION.
RX PubMed=10747903; DOI=10.1074/jbc.m000372200;
RA Tanikawa J., Ichikawa-Iwata E., Kanei-Ishii C., Nakai A., Matsuzawa S.,
RA Reed J.C., Ishii S.;
RT "p53 suppresses the c-Myb-induced activation of heat shock transcription
RT factor 3.";
RL J. Biol. Chem. 275:15578-15585(2000).
RN [16]
RP PHOSPHORYLATION BY HIPK1, INTERACTION WITH HIPK1, AND SUBCELLULAR LOCATION.
RX PubMed=19646965; DOI=10.1016/j.bbrc.2009.07.139;
RA Matre V., Nordgaard O., Alm-Kristiansen A.H., Ledsaak M., Gabrielsen O.S.;
RT "HIPK1 interacts with c-Myb and modulates its activity through
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 388:150-154(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-480, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP INDUCTION.
RX PubMed=23166356; DOI=10.1084/jem.20121387;
RA Basso K., Schneider C., Shen Q., Holmes A.B., Setty M., Leslie C.,
RA Dalla-Favera R.;
RT "BCL6 positively regulates AID and germinal center gene expression via
RT repression of miR-155.";
RL J. Exp. Med. 209:2455-2465(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND THR-534, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-480, 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: Transcriptional activator; DNA-binding protein that
CC specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important
CC role in the control of proliferation and differentiation of
CC hematopoietic progenitor cells.
CC -!- SUBUNIT: Binds MYBBP1A. Interacts with HIPK2, MAF and NLK (By
CC similarity). Binds to HIPK1. {ECO:0000250, ECO:0000269|PubMed:10747903,
CC ECO:0000269|PubMed:19646965}.
CC -!- INTERACTION:
CC P10242; Q00610: CLTC; NbExp=4; IntAct=EBI-298355, EBI-354967;
CC P10242; O15083: ERC2; NbExp=2; IntAct=EBI-298355, EBI-2684336;
CC P10242; Q9H074-2: PAIP1; NbExp=3; IntAct=EBI-298355, EBI-12101100;
CC P10242; P63165: SUMO1; NbExp=3; IntAct=EBI-298355, EBI-80140;
CC P10242; P61956: SUMO2; NbExp=3; IntAct=EBI-298355, EBI-473220;
CC P10242; P17542: TAL1; NbExp=2; IntAct=EBI-298355, EBI-1753878;
CC P10242; O60293: ZFC3H1; NbExp=2; IntAct=EBI-298355, EBI-746701;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:19646965}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1;
CC IsoId=P10242-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10242-2; Sequence=VSP_003293;
CC Name=3;
CC IsoId=P10242-3; Sequence=VSP_003294, VSP_003295;
CC Name=4;
CC IsoId=P10242-4; Sequence=VSP_003296;
CC Name=5;
CC IsoId=P10242-5; Sequence=VSP_003297, VSP_003298;
CC Name=6;
CC IsoId=P10242-6; Sequence=VSP_003299;
CC Name=7;
CC IsoId=P10242-7; Sequence=VSP_003293, VSP_003296;
CC Name=8;
CC IsoId=P10242-8; Sequence=VSP_046660;
CC Name=9;
CC IsoId=P10242-9; Sequence=VSP_046658;
CC Name=10;
CC IsoId=P10242-10; Sequence=VSP_046661;
CC Name=11;
CC IsoId=P10242-11; Sequence=VSP_046659;
CC Name=12;
CC IsoId=P10242-12; Sequence=VSP_053389;
CC -!- INDUCTION: Negatively regulated by microRNA-155 (miR-155).
CC {ECO:0000269|PubMed:23166356}.
CC -!- DOMAIN: Comprised of 3 domains; an N-terminal DNA-binding domain, a
CC centrally located transcriptional activation domain and a C-terminal
CC domain involved in transcriptional repression.
CC {ECO:0000269|PubMed:2189102}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent
CC proteasomal degradation. {ECO:0000305}.
CC -!- PTM: Phosphorylated by NLK on multiple sites, which induces proteasomal
CC degradation. {ECO:0000250}.
CC -!- PTM: Phosphorylated by HIPK1. This phosphorylation reduces MYB
CC transcription factor activity but not MYB protein levels.
CC {ECO:0000269|PubMed:19646965}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MYBID41466ch6q23.html";
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DR EMBL; M15024; AAA52032.1; -; mRNA.
DR EMBL; X52125; CAA36371.1; -; mRNA.
DR EMBL; AJ606319; CAE55170.1; -; mRNA.
DR EMBL; AJ606320; CAE55171.1; -; mRNA.
DR EMBL; AJ616791; CAF04482.1; -; mRNA.
DR EMBL; AJ616791; CAF04479.1; -; mRNA.
DR EMBL; U22376; AAB49034.1; -; Genomic_DNA.
DR EMBL; U22376; AAB49035.1; -; Genomic_DNA.
DR EMBL; U22376; AAB49036.1; -; Genomic_DNA.
DR EMBL; U22376; AAB49037.1; -; Genomic_DNA.
DR EMBL; U22376; AAB49038.1; -; Genomic_DNA.
DR EMBL; U22376; AAB49039.1; -; Genomic_DNA.
DR EMBL; AF104863; AAC96326.1; -; mRNA.
DR EMBL; AY787443; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY787447; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY787448; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY787461; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY787468; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL023693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47969.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47973.1; -; Genomic_DNA.
DR EMBL; BC064955; AAH64955.1; -; mRNA.
DR EMBL; M13665; AAA52030.1; -; mRNA.
DR EMBL; M13666; AAA52031.1; -; mRNA.
DR EMBL; X17469; CAA35503.1; -; mRNA.
DR CCDS; CCDS47481.1; -. [P10242-4]
DR CCDS; CCDS47482.1; -. [P10242-2]
DR CCDS; CCDS5174.1; -. [P10242-1]
DR CCDS; CCDS55058.1; -. [P10242-7]
DR CCDS; CCDS55059.1; -. [P10242-8]
DR CCDS; CCDS55060.1; -. [P10242-10]
DR CCDS; CCDS55061.1; -. [P10242-11]
DR CCDS; CCDS55062.1; -. [P10242-9]
DR PIR; A26661; TVHUMB.
DR RefSeq; NP_001123644.1; NM_001130172.1. [P10242-2]
DR RefSeq; NP_001123645.1; NM_001130173.1. [P10242-4]
DR RefSeq; NP_001155128.1; NM_001161656.1. [P10242-7]
DR RefSeq; NP_001155129.1; NM_001161657.1. [P10242-11]
DR RefSeq; NP_001155130.1; NM_001161658.1. [P10242-8]
DR RefSeq; NP_001155131.1; NM_001161659.1. [P10242-10]
DR RefSeq; NP_001155132.1; NM_001161660.1. [P10242-9]
DR RefSeq; NP_005366.2; NM_005375.3. [P10242-1]
DR AlphaFoldDB; P10242; -.
DR SMR; P10242; -.
DR BioGRID; 110687; 181.
DR ComplexPortal; CPX-504; c-Myb-C/EBPbeta complex.
DR DIP; DIP-1057N; -.
DR ELM; P10242; -.
DR IntAct; P10242; 97.
DR MINT; P10242; -.
DR iPTMnet; P10242; -.
DR PhosphoSitePlus; P10242; -.
DR BioMuta; MYB; -.
DR DMDM; 2815504; -.
DR EPD; P10242; -.
DR jPOST; P10242; -.
DR MassIVE; P10242; -.
DR MaxQB; P10242; -.
DR PaxDb; P10242; -.
DR PeptideAtlas; P10242; -.
DR PRIDE; P10242; -.
DR ProteomicsDB; 20651; -.
DR ProteomicsDB; 21951; -.
DR ProteomicsDB; 22356; -.
DR ProteomicsDB; 22452; -.
DR ProteomicsDB; 23398; -.
DR ProteomicsDB; 52578; -. [P10242-1]
DR ProteomicsDB; 52579; -. [P10242-2]
DR ProteomicsDB; 52580; -. [P10242-3]
DR ProteomicsDB; 52581; -. [P10242-4]
DR ProteomicsDB; 52582; -. [P10242-5]
DR ProteomicsDB; 52583; -. [P10242-6]
DR Antibodypedia; 4486; 946 antibodies from 43 providers.
DR DNASU; 4602; -.
DR Ensembl; ENST00000341911.10; ENSP00000339992.5; ENSG00000118513.20. [P10242-4]
DR Ensembl; ENST00000367812.6; ENSP00000356786.2; ENSG00000118513.20. [P10242-6]
DR Ensembl; ENST00000367814.8; ENSP00000356788.4; ENSG00000118513.20. [P10242-1]
DR Ensembl; ENST00000442647.7; ENSP00000410825.2; ENSG00000118513.20. [P10242-2]
DR Ensembl; ENST00000525369.5; ENSP00000435938.1; ENSG00000118513.20. [P10242-11]
DR Ensembl; ENST00000525477.5; ENSP00000437081.1; ENSG00000118513.20. [P10242-3]
DR Ensembl; ENST00000525514.5; ENSP00000435578.1; ENSG00000118513.20. [P10242-3]
DR Ensembl; ENST00000528774.5; ENSP00000434723.1; ENSG00000118513.20. [P10242-7]
DR Ensembl; ENST00000529586.5; ENSP00000437264.1; ENSG00000118513.20. [P10242-3]
DR Ensembl; ENST00000533384.5; ENSP00000432811.1; ENSG00000118513.20. [P10242-5]
DR Ensembl; ENST00000533624.5; ENSP00000436605.1; ENSG00000118513.20. [P10242-9]
DR Ensembl; ENST00000533808.5; ENSP00000435293.1; ENSG00000118513.20. [P10242-5]
DR Ensembl; ENST00000533837.5; ENSP00000434639.1; ENSG00000118513.20. [P10242-5]
DR Ensembl; ENST00000534044.5; ENSP00000435055.1; ENSG00000118513.20. [P10242-10]
DR Ensembl; ENST00000534121.5; ENSP00000432851.1; ENSG00000118513.20. [P10242-8]
DR GeneID; 4602; -.
DR KEGG; hsa:4602; -.
DR MANE-Select; ENST00000341911.10; ENSP00000339992.5; NM_001130173.2; NP_001123645.1. [P10242-4]
DR UCSC; uc003qfh.4; human. [P10242-1]
DR CTD; 4602; -.
DR DisGeNET; 4602; -.
DR GeneCards; MYB; -.
DR HGNC; HGNC:7545; MYB.
DR HPA; ENSG00000118513; Group enriched (bone marrow, breast, intestine, lymphoid tissue).
DR MalaCards; MYB; -.
DR MIM; 189990; gene.
DR neXtProt; NX_P10242; -.
DR OpenTargets; ENSG00000118513; -.
DR Orphanet; 86849; Acute basophilic leukemia.
DR Orphanet; 251671; Angiocentric glioma.
DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR PharmGKB; PA31345; -.
DR VEuPathDB; HostDB:ENSG00000118513; -.
DR eggNOG; KOG0048; Eukaryota.
DR GeneTree; ENSGT00940000156248; -.
DR HOGENOM; CLU_015440_2_1_1; -.
DR InParanoid; P10242; -.
DR OMA; YNYISET; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; P10242; -.
DR TreeFam; TF326257; -.
DR PathwayCommons; P10242; -.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P10242; -.
DR SIGNOR; P10242; -.
DR BioGRID-ORCS; 4602; 113 hits in 1111 CRISPR screens.
DR ChiTaRS; MYB; human.
DR GeneWiki; MYB_(gene); -.
DR GenomeRNAi; 4602; -.
DR Pharos; P10242; Tbio.
DR PRO; PR:P10242; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P10242; protein.
DR Bgee; ENSG00000118513; Expressed in mucosa of sigmoid colon and 124 other tissues.
DR ExpressionAtlas; P10242; baseline and differential.
DR Genevisible; P10242; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0061515; P:myeloid cell development; IC:ComplexPortal.
DR GO; GO:1901533; P:negative regulation of hematopoietic progenitor cell differentiation; IMP:ARUK-UCL.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045624; P:positive regulation of T-helper cell differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR015395; C-myb_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR012642; Tscrpt_reg_Wos2-domain.
DR Pfam; PF09316; Cmyb_C; 1.
DR Pfam; PF07988; LMSTEN; 1.
DR Pfam; PF00249; Myb_DNA-binding; 3.
DR SMART; SM00717; SANT; 3.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..640
FT /note="Transcriptional activator Myb"
FT /id="PRO_0000197048"
FT DOMAIN 35..86
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 87..142
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 143..193
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 63..86
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 115..138
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 166..189
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 90..193
FT /note="Interaction with HIPK2 and NLK"
FT /evidence="ECO:0000250"
FT REGION 275..327
FT /note="Transcription activation domain (PubMed:2189102)"
FT /evidence="ECO:0000269|PubMed:2189102"
FT REGION 328..465
FT /note="Negative regulatory domain"
FT /evidence="ECO:0000250"
FT REGION 336..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..397
FT /note="Leucine-zipper"
FT MOD_RES 471
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 282..316
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_046658"
FT VAR_SEQ 314..316
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15169551,
FT ECO:0000303|PubMed:2202948, ECO:0000303|Ref.6"
FT /id="VSP_003293"
FT VAR_SEQ 317..640
FT /note="TQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGEHHSTPSLPADPGSLPEES
FT ASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHENSDLEMPSLTSTPLIGH
FT KLTVTTPFHRDQTVKTQKENTVFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKM
FT LPQTPSHLVEDLQDVIKQESDESGIVAEFQENGPPLLKKIKQEVESPTDKSGNFFCSHH
FT WEGDSLNTQLFTQTSPVADAPNILTSSVLMAPASEDEDNVLKAFTVPKNRSLASPLQPC
FT SSTWEPASCGKMEEQMTSSSQARKYVNAFSARTLVM -> VRLSSCA (in isoform
FT 12)"
FT /evidence="ECO:0000303|PubMed:3014652"
FT /id="VSP_053389"
FT VAR_SEQ 317..401
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_046659"
FT VAR_SEQ 317..350
FT /note="TQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGE -> LCGPLLNSDIFSDW
FT AANWDGSLCFATYIVNQQRQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003294"
FT VAR_SEQ 351..640
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003295"
FT VAR_SEQ 386..401
FT /note="VKNLLEFAETLQFIDS -> DSSSWCDLSSFEFFEEADFSPSQHHTGKALQL
FT QQREGNGTKPAGEPSPRVNKRMLSESSLDPPKVLPPARHSTIPLVILRKKRGQASPLAT
FT GDCSSFIFADVSSSTPKRSPVKSLPFSPSQ (in isoform 8)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_046660"
FT VAR_SEQ 401
FT /note="S -> SDSSSWCDLSSFEFFEEADFSPSQHHTGKALQLQQREGNGTKPAGEP
FT SPRVNKRMLSESSLDPPKVLPPARHSTIPLVILRKKRGQASPLATGDCSSFIFADVSSS
FT TPKRSPVKSLPFSPSQ (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15169551, ECO:0000303|Ref.6"
FT /id="VSP_003296"
FT VAR_SEQ 402
FT /note="F -> M (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003297"
FT VAR_SEQ 403..640
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003298"
FT VAR_SEQ 530..566
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_046661"
FT VAR_SEQ 567..640
FT /note="NILTSSVLMAPASEDEDNVLKAFTVPKNRSLASPLQPCSSTWEPASCGKMEE
FT QMTSSSQARKYVNAFSARTLVM -> TGVQWHDFGSLQPLPPGFKRFSCLSLPRSWDYR
FT HPPPRPANFEFLVETGFLHVGQAGLELLTSGDLPASASQSARITGVSHRARPEYSYKLR
FT FNGTSIRR (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003299"
FT VARIANT 336
FT /note="T -> I (in dbSNP:rs2229999)"
FT /id="VAR_050188"
FT VARIANT 422
FT /note="T -> N (in dbSNP:rs2230000)"
FT /id="VAR_050189"
FT CONFLICT 511
FT /note="I -> F (in Ref. 1; AAA52032 and 6; AY787447/
FT AY787448)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="A -> R (in Ref. 1; AAA52032 and 6; AY787447/
FT AY787448)"
FT /evidence="ECO:0000305"
FT CONFLICT P10242-4:433
FT /note="L -> F (in Ref. 8; CAA35503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 72341 MW; FD5E6694020426ED CRC64;
MARRPRHSIY SSDEDDEDFE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT
DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK
HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA
IKNHWNSTMR RKVEQEGYLQ ESSKASQPAV ATSFQKNSHL MGFAQAPPTA QLPATGQPTV
NNDYSYYHIS EAQNVSSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL
LLMSTENELK GQQVLPTQNH TCSYPGWHST TIADHTRPHG DSAPVSCLGE HHSTPSLPAD
PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SFLNTSSNHE NSDLEMPSLT
STPLIGHKLT VTTPFHRDQT VKTQKENTVF RTPAIKRSIL ESSPRTPTPF KHALAAQEIK
YGPLKMLPQT PSHLVEDLQD VIKQESDESG IVAEFQENGP PLLKKIKQEV ESPTDKSGNF
FCSHHWEGDS LNTQLFTQTS PVADAPNILT SSVLMAPASE DEDNVLKAFT VPKNRSLASP
LQPCSSTWEP ASCGKMEEQM TSSSQARKYV NAFSARTLVM
