ID MYB_MOUSE Reviewed; 636 AA. AC P06876; Q61929; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 05-APR-2011, entry version 123. DE RecName: Full=Transcriptional activator Myb; DE AltName: Full=Proto-oncogene c-Myb; GN Name=Myb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=86205865; PubMed=3010282; DOI=10.1073/pnas.83.10.3204; RA Bender T.P., Kuehl W.M.; RT "Murine myb protooncogene mRNA: cDNA sequence and evidence for 5' RT heterogeneity."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3204-3208(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86055758; PubMed=2998780; RA Gonda T.J., Gough N.M., Dunn A.R., de Blaquiere J.; RT "Nucleotide sequence of cDNA clones of the murine myb proto- RT oncogene."; RL EMBO J. 4:2003-2008(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3608990; RA Watson R.J., Dyson P.J., McMahon J.; RT "Multiple c-myb transcript cap sites are variously utilized in cells RT of mouse haemopoietic origin."; RL EMBO J. 6:1643-1651(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87204099; PubMed=3033638; DOI=10.1073/pnas.84.10.3171; RA Rosson D., Dugan D., Reddy E.P.; RT "Aberrant splicing events that are induced by proviral integration: RT implications for myb oncogene activation."; RL Proc. Natl. Acad. Sci. U.S.A. 84:3171-3175(1987). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47. RX MEDLINE=90098830; PubMed=2481264; DOI=10.1093/nar/17.23.9593; RA Sobieszczuk P.W., Gonda T.J., Dunn A.R.; RT "Structure and biological activity of the transcriptional initiation RT sequences of the murine c-myb oncogene."; RL Nucleic Acids Res. 17:9593-9611(1989). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 72-636. RX MEDLINE=87064321; PubMed=3023843; RA Shen-Ong G.L.C., Morse H.C. III, Potter M., Mushinski F.; RT "Two modes of c-myb activation in virus-induced mouse myeloid RT tumors."; RL Mol. Cell. Biol. 6:380-392(1986). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-401. RX MEDLINE=86286545; PubMed=3016644; DOI=10.1093/nar/14.13.5309; RA Lavu S., Reddy E.P.; RT "Structural organization and nucleotide sequence of mouse c-myb RT oncogene: activation in ABPL tumors is due to viral integration in an RT intron which results in the deletion of the 5' coding sequences."; RL Nucleic Acids Res. 14:5309-5320(1986). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-402. RX MEDLINE=86259723; PubMed=3014527; DOI=10.1073/pnas.83.14.5010; RA Weinstein Y., Ihle J.N., Lavu S., Reddy P.E.; RT "Truncation of the c-myb gene by a retroviral integration in an RT interleukin 3-dependent myeloid leukemia cell line."; RL Proc. Natl. Acad. Sci. U.S.A. 83:5010-5014(1986). RN [10] RP DOMAIN C-TERMINAL. RX MEDLINE=89356652; PubMed=2670562; RA Gonda T.J., Buckmaster C., Ramsay R.G.; RT "Activation of c-myb by carboxy-terminal truncation: relationship to RT transformation of murine haemopoietic cells in vitro."; RL EMBO J. 8:1777-1783(1989). RN [11] RP NEGATIVE REGULATORY DOMAIN. RX MEDLINE=92019822; PubMed=1923521; RA Hu Y., Ramsay R.G., Kanei-Ishii C., Ishii S., Gonda T.J.; RT "Transformation by carboxyl-deleted Myb reflects increased RT transactivating capacity and disruption of a negative regulatory RT domain."; RL Oncogene 6:1549-1553(1991). RN [12] RP DOMAIN LEUCINE-ZIPPER, AND NEGATIVE AUTOREGULATION. RX MEDLINE=94012781; PubMed=8408047; RA Nomura T., Sakai N., Sarai A., Sudo T., Kanei-Ishii C., Ramsay R.G., RA Favier D., Gonda T.J., Ishii S.; RT "Negative autoregulation of c-Myb activity by homodimer formation RT through the leucine zipper."; RL J. Biol. Chem. 268:21914-21923(1993). RN [13] RP INTERACTION WITH MYBBP1A1. RX PubMed=9447996; RA Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., RA Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., RA Ishii S., Gonda T.J.; RT "Molecular cloning reveals that the p160 Myb-binding protein is a RT novel, predominantly nucleolar protein which may play a role in RT transactivation by Myb."; RL Mol. Cell. Biol. 18:989-1002(1998). RN [14] RP INTERACTION WITH MAF. RX PubMed=9566892; RA Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.; RT "c-Maf interacts with c-Myb to regulate transcription of an early RT myeloid gene during differentiation."; RL Mol. Cell. Biol. 18:2729-2737(1998). RN [15] RP INTERACTION WITH HIPK2 AND NLK. RX PubMed=15082531; DOI=10.1101/gad.1170604; RA Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T., RA Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E., RA Kim Y., Matsumoto K., Ishii S.; RT "Wnt-1 signal induces phosphorylation and degradation of c-Myb protein RT via TAK1, HIPK2, and NLK."; RL Genes Dev. 18:816-829(2004). RN [16] RP INTERACTION WITH MAF. RX PubMed=17823980; DOI=10.1002/eji.200636979; RA Peng S., Lalani S., Leavenworth J.W., Ho I.-C., Pauza M.E.; RT "c-Maf interacts with c-Myb to down-regulate Bcl-2 expression and RT increase apoptosis in peripheral CD4 cells."; RL Eur. J. Immunol. 37:2868-2880(2007). RN [17] RP STRUCTURE BY NMR OF 142-193. RX MEDLINE=92335311; PubMed=1631139; DOI=10.1073/pnas.89.14.6428; RA Ogata K., Hojo H., Aimoto S., Nakai T., Nakamura H., Sarai A., RA Ishii S., Nishimura Y.; RT "Solution structure of a DNA-binding unit of Myb: a helix-turn-helix- RT related motif with conserved tryptophans forming a hydrophobic core."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6428-6432(1992). RN [18] RP STRUCTURE BY NMR OF 89-192. RX MEDLINE=93373918; PubMed=8365401; RX DOI=10.1111/j.1432-1033.1993.tb18126.x; RA Jamin N., Gabrielsen O.S., Gilles N., Lirsac P.-N., Toma F.; RT "Secondary structure of the DNA-binding domain of the c-Myb RT oncoprotein in solution. A multidimensional double and triple RT heteronuclear NMR study."; RL Eur. J. Biochem. 216:147-154(1993). RN [19] RP STRUCTURE BY NMR OF 38-89; 90-141 AND 142-193. RX MEDLINE=95316681; PubMed=7796266; DOI=10.1038/nsb0495-309; RA Ogata K., Morikawa S., Nakamura H., Hojo H., Yoshimura S., Zhang R., RA Aimoto S., Ametani Y., Hirata Z., Sarai A., Ishii S., Nishimura Y.; RT "Comparison of the free and DNA-complexed forms of the DNA-binding RT domain from c-Myb."; RL Nat. Struct. Biol. 2:309-320(1995). RN [20] RP STRUCTURE BY NMR OF 140-193. RX MEDLINE=97098437; PubMed=8942977; DOI=10.1073/pnas.93.24.13583; RA Furukawa K., Oda M., Nakamura H.; RT "A small engineered protein lacks structural uniqueness by increasing RT the side-chain conformational entropy."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13583-13588(1996). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-193 IN COMPLEX WITH HUMAN RP CEBPB. RX MEDLINE=21652535; PubMed=11792321; DOI=10.1016/S0092-8674(01)00636-5; RA Tahirov T.H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T., RA Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T., RA Yamamoto M., Ishii S., Ogata K.; RT "Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a RT promoter."; RL Cell 108:57-70(2002). CC -!- FUNCTION: Transcriptional activator; DNA-binding protein that CC specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an CC important role in the control of proliferation and differentiation CC of hematopoietic progenitor cells. CC -!- SUBUNIT: Interacts with HIPK2, MAF, MYBBP1A and NLK. CC -!- INTERACTION: CC Q9QZR5:Hipk2; NbExp=1; IntAct=EBI-366934, EBI-366905; CC O54949:Nlk; NbExp=1; IntAct=EBI-366934, EBI-366894; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DOMAIN: Comprised of 3 domains; an N-terminal DNA-binding domain, CC a centrally located transcriptional activation domain and a C- CC terminal domain involved in transcriptional repression. CC -!- DOMAIN: C-terminal truncated mutants display increased CC transactivation. CC -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its CC subsequent proteasomal degradation (By similarity). CC -!- PTM: Phosphorylated by NLK on multiple sites, which induces CC proteasomal degradation. CC -!- SIMILARITY: Contains 3 HTH myb-type DNA-binding domains. 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; M21169; AAA39782.1; -; Genomic_DNA. DR EMBL; M12848; AAB59713.1; -; mRNA. DR EMBL; M20210; AAA39783.1; -; Genomic_DNA. DR EMBL; X02774; CAA26552.1; -; mRNA. DR EMBL; BC011513; AAH11513.1; -; mRNA. DR EMBL; X04099; CAA27724.1; -; Genomic_DNA. DR EMBL; X04100; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X04101; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X04102; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X04103; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X04104; CAA27724.1; JOINED; Genomic_DNA. DR EMBL; X16389; CAA34425.1; -; Genomic_DNA. DR EMBL; X16390; CAA34426.1; -; Genomic_DNA. DR EMBL; M13989; AAA39787.1; -; Genomic_DNA. DR EMBL; K03547; AAA39786.1; -; Genomic_DNA. DR IPI; IPI00323266; -. DR PIR; A25285; TVMSMB. DR RefSeq; NP_001185843.1; NM_001198914.1. DR RefSeq; NP_034978.3; NM_010848.3. DR UniGene; Mm.52109; -. DR PDB; 1GUU; X-ray; 1.60 A; A=38-89. DR PDB; 1GV2; X-ray; 1.68 A; A=89-193. DR PDB; 1GV5; X-ray; 1.58 A; A=90-141. DR PDB; 1GVD; X-ray; 1.45 A; A=90-141. DR PDB; 1H88; X-ray; 2.80 A; C=37-193. DR PDB; 1H89; X-ray; 2.45 A; C=37-193. DR PDB; 1IDY; NMR; -; A=141-193. DR PDB; 1IDZ; NMR; -; A=141-193. DR PDB; 1MBE; NMR; -; A=38-89. DR PDB; 1MBF; NMR; -; A=38-89. DR PDB; 1MBG; NMR; -; A=90-141. DR PDB; 1MBH; NMR; -; A=90-141. DR PDB; 1MBJ; NMR; -; A=142-193. DR PDB; 1MBK; NMR; -; A=142-193. DR PDB; 1MSE; NMR; -; C=90-193. DR PDB; 1MSF; NMR; -; C=90-193. DR PDB; 1SB0; NMR; -; B=291-315. DR PDB; 2AGH; NMR; -; A=291-315. DR PDBsum; 1GUU; -. DR PDBsum; 1GV2; -. DR PDBsum; 1GV5; -. DR PDBsum; 1GVD; -. DR PDBsum; 1H88; -. DR PDBsum; 1H89; -. DR PDBsum; 1IDY; -. DR PDBsum; 1IDZ; -. DR PDBsum; 1MBE; -. DR PDBsum; 1MBF; -. DR PDBsum; 1MBG; -. DR PDBsum; 1MBH; -. DR PDBsum; 1MBJ; -. DR PDBsum; 1MBK; -. DR PDBsum; 1MSE; -. DR PDBsum; 1MSF; -. DR PDBsum; 1SB0; -. DR PDBsum; 2AGH; -. DR ProteinModelPortal; P06876; -. DR SMR; P06876; 38-193. DR IntAct; P06876; 3. DR STRING; P06876; -. DR PhosphoSite; P06876; -. DR PRIDE; P06876; -. DR Ensembl; ENSMUST00000020158; ENSMUSP00000020158; ENSMUSG00000019982. DR GeneID; 17863; -. DR KEGG; mmu:17863; -. DR UCSC; uc007eog.1; mouse. DR CTD; 17863; -. DR MGI; MGI:97249; Myb. DR eggNOG; roNOG13688; -. DR HOVERGEN; HBG007964; -. DR OrthoDB; EOG4H9XKD; -. DR NextBio; 292625; -. DR ArrayExpress; P06876; -. DR Bgee; P06876; -. DR CleanEx; MM_MYB; -. DR Genevestigator; P06876; -. DR GermOnline; ENSMUSG00000019982; Mus musculus. DR GO; GO:0005654; C:nucleoplasm; EXP:Reactome. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI. DR GO; GO:0030528; F:transcription regulator activity; IEA:InterPro. DR GO; GO:0006816; P:calcium ion transport; IMP:MGI. DR GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:MGI. DR InterPro; IPR015395; C-myb_C. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR014778; Myb_DNA-bd. DR InterPro; IPR015495; Myb_trans_fac. DR InterPro; IPR001005; SANT_DNA-bd. DR InterPro; IPR017930; Tscrpt_reg_HTH_Myb-type. DR InterPro; IPR012642; Tscrpt_reg_Wos2-domain. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 3. DR PANTHER; PTHR10641; Myb_transfac; 1. DR Pfam; PF09316; Cmyb_C; 1. DR Pfam; PF00249; Myb_DNA-binding; 3. DR Pfam; PF07988; Wos2; 1. DR SMART; SM00717; SANT; 3. DR SUPFAM; SSF46689; Homeodomain_like; 2. DR PROSITE; PS51294; HTH_MYB; 3. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; DNA-binding; Nucleus; KW Proto-oncogene; Repeat; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1 636 Transcriptional activator Myb. FT /FTId=PRO_0000197049. FT DOMAIN 35 86 HTH myb-type 1. FT DOMAIN 87 142 HTH myb-type 2. FT DOMAIN 143 193 HTH myb-type 3. FT DOMAIN 375 396 Leucine-zipper. FT DNA_BIND 63 86 H-T-H motif (By similarity). FT DNA_BIND 115 138 H-T-H motif. FT DNA_BIND 166 189 H-T-H motif. FT REGION 90 193 Interaction with HIPK2 and NLK. FT REGION 275 327 Transcriptional activation domain (By FT similarity). FT REGION 328 460 Negative regulatory domain. FT MOD_RES 467 467 N6-acetyllysine (By similarity). FT MOD_RES 476 476 N6-acetyllysine (By similarity). FT CONFLICT 105 105 E -> K (in Ref. 2; CAA26552). FT CONFLICT 201 201 E -> K (in Ref. 2; CAA26552). FT CONFLICT 267 267 V -> A (in Ref. 1; AAB59713). FT CONFLICT 402 402 F -> V (in Ref. 9; AAA39786). FT CONFLICT 411 411 S -> N (in Ref. 2; CAA26552). FT CONFLICT 500 500 R -> Q (in Ref. 1; AAB59713). FT CONFLICT 525 525 E -> A (in Ref. 2; CAA26552). FT HELIX 45 58 FT HELIX 63 68 FT HELIX 75 86 FT HELIX 97 110 FT HELIX 115 119 FT HELIX 127 136 FT HELIX 149 162 FT HELIX 166 170 FT HELIX 178 188 FT HELIX 292 311 SQ SEQUENCE 636 AA; 71450 MW; 0DC19B2A84726ECE CRC64; MARRPRHSIY SSDEDDEDIE MCDHDYDGLL PKSGKRHLGK TRWTREEDEK LKKLVEQNGT DDWKVIANYL PNRTDVQCQH RWQKVLNPEL IKGPWTKEED QRVIELVQKY GPKRWSVIAK HLKGRIGKQC RERWHNHLNP EVKKTSWTEE EDRIIYQAHK RLGNRWAEIA KLLPGRTDNA IKNHWNSTMR RKVEQEGYLQ EPSKASQTPV ATSFQKNNHL MGFGHASPPS QLSPSGQSSV NSEYPYYHIA EAQNISSHVP YPVALHVNIV NVPQPAAAAI QRHYNDEDPE KEKRIKELEL LLMSTENELK GQQALPTQNH TCSYPGWHST SIVDQTRPHG DSAPVSCLGE HHATPSLPAD PGSLPEESAS PARCMIVHQG TILDNVKNLL EFAETLQFID SFLNTSSNHE SSGLDAPTLP STPLIGHKLT PCRDQTVKTQ KENSIFRTPA IKRSILESSP RTPTPFKHAL AAQEIKYGPL KMLPQTPSHA VEDLQDVIKR ESDESGIVAE FQESGPPLLK KIKQEVESPT EKSGNFFCSN HWAENSLSTQ LFSQASPVAD APNILTSSVL MTPVSEDEDN VLKAFTVPKN RPLVGPLQPC SGAWEPASCG KTEDQMTASG PARKYVNAFS ARTLVM //