AC T09921
XX
ID T09921
XX
DT 18.01.2006 (created); anu.
DT 20.05.2014 (updated); asv.
CO Copyright (C), QIAGEN.
XX
FA c-Myb
XX
SY c-Myb; MYB; MYB PROTO-ONCOGENE PROTEIN.
XX
OS mouse, Mus musculus
OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae; murinae
XX
GE G000488 Myb.
XX
CL C0022; trp; 3.5.1.1.1.1.
XX
SZ 636 AA; 71.4 kDa (cDNA) (calc.), 75 kDa (SDS)
XX
SQ MARRPRHSIYSSDEDDEDIEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGT
SQ DDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAK
SQ HLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNA
SQ IKNHWNSTMRRKVEQEGYLQEPSKASQTPVATSFQKNNHLMGFGHASPPSQLSPSGQSSV
SQ NSEYPYYHIAEAQNISSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELEL
SQ LLMSTENELKGQQALPTQNHTCSYPGWHSTSIVDQTRPHGDSAPVSCLGEHHATPSLPAD
SQ PGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHESSGLDAPTLP
SQ STPLIGHKLTPCRDQTVKTQKENSIFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPL
SQ KMLPQTPSHAVEDLQDVIKRESDESGIVAEFQESGPPLLKKIKQEVESPTEKSGNFFCSN
SQ HWAENSLSTQLFSQASPVADAPNILTSSVLMTPVSEDEDNVLKAFTVPKNRPLVGPLQPC
SQ SGAWEPASCGKTEDQMTASGPARKYVNAFSARTLVM
XX
SC translated from EMBL:BC011513
XX
FT 35 86 
PS50090; MYB_3.
FT 39 88 
SM00717; sant.
FT 40 86 
PF00249; Myb-like DNA-binding domain.
FT 56 582 
PF00478; IMP dehydrogenase / GMP reductase dom.
FT 87 138 
PS50090; MYB_3.
FT 91 140 
SM00717; sant.
FT 92 138 
PF00249; Myb-like DNA-binding domain.
FT 139 189 
PS50090; MYB_3.
FT 143 191 
SM00717; sant.
FT 144 189 
PF00249; Myb-like DNA-binding domain.
FT 223 313 PF07988; Mitotic protein Wos2.
FT 275 325 transcription activation domain [4].
XX
IN T00581 C/EBPbeta; human, Homo sapiens.
IN T00526 MyoD; mouse, Mus musculus.
XX
MX M00004 V$CMYB_01.
MX M01821 V$CMYB_Q5.
MX M02883 V$MYB_03.
MX M02779 V$MYB_05.
MX M00773 V$MYB_Q3.
MX M07299 V$MYB_Q4.
MX M00913 V$MYB_Q5_01.
MX M08890 V$MYB_Q5_02.
MX M00183 V$MYB_Q6.
XX
BS R32837.
BS R02100.
BS R02392.
BS R31102.
BS R29667.
BS R01431.
BS R21711.
BS R21712.
BS R21713.
BS R21714.
BS R21719.
BS R21723.
BS R03999.
BS R04000.
BS R04001.
BS R04002.
BS R08124.
BS R38135.
BS R38136.
BS R61902.
BS R20714.
BS R01849.
XX
DR TRANSPATH: MO000057321.
DR EMBL: BC011513;
DR EMBL: K03547;
DR EMBL: M12848;
DR EMBL: M13989;
DR EMBL: M20210;
DR EMBL: M21169;
DR EMBL: X02774;
DR EMBL: X04099;
DR EMBL: X04100;
DR EMBL: X04101;
DR EMBL: X04102;
DR EMBL: X04103;
DR EMBL: X04104;
DR EMBL: X16389;
DR EMBL: X16390;
DR UniProtKB: P06876;
DR PDB: 1IDY.
DR PDB: 1IDZ.
DR PDB: 1MBE.
DR PDB: 1MBF.
DR PDB: 1MBG.
DR PDB: 1MBH.
DR PDB: 1MBJ.
DR PDB: 1MBK.
DR PDB: 1MSE.
DR PDB: 1MSF.
XX
RN [1]; RE0047992.
RX PUBMED: 11792321.
RA Tahirov T. H., Sato K., Ichikawa-Iwata E., Sasaki M., Inoue-Bungo T., Shiina M., Kimura K., Takata S., Fujikawa A., Morii H., Kumasaka T., Yamamoto M., Ishii S., Ogata K.
RT Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a promoter.
RL Cell 108:57-70 (2002).
RN [2]; RE0048003.
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 myeloid gene during differentiation.
RL Mol. Cell. Biol. 18:2729-2737 (1998).
RN [3]; RE0048027.
RX PUBMED: 16055116.
RA Kaspar P., Pajer P., Sedlak D., Tamaoki T., Dvorak M.
RT c-Myb inhibits myogenic differentiation through repression of MyoD.
RL Exp. Cell Res. 309:419-428 (2005).
RN [4]; RE0002390.
RX PUBMED: 2668947.
RA Sakura H., Kanei-Ishii C., Nagase T., Nakagoshi H., Gonda T. J.
RT Delineation of three functional domains of the transcriptional activator encoded by the c-myb protooncogene
RL Proc. Natl. Acad. Sci. USA 86:5758-5762 (1989).
XX
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