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Transcriptional activator Myb (Proto-oncogene c-Myb)

 MYB_MOUSE               Reviewed;         636 AA.
P06876; E9QMG8; Q61929;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 183.
RecName: Full=Transcriptional activator Myb;
AltName: Full=Proto-oncogene c-Myb;
Name=Myb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=3010282; DOI=10.1073/pnas.83.10.3204;
Bender T.P., Kuehl W.M.;
"Murine myb protooncogene mRNA: cDNA sequence and evidence for 5'
heterogeneity.";
Proc. Natl. Acad. Sci. U.S.A. 83:3204-3208(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2998780;
Gonda T.J., Gough N.M., Dunn A.R., de Blaquiere J.;
"Nucleotide sequence of cDNA clones of the murine myb proto-
oncogene.";
EMBO J. 4:2003-2008(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3608990;
Watson R.J., Dyson P.J., McMahon J.;
"Multiple c-myb transcript cap sites are variously utilized in cells
of mouse haemopoietic origin.";
EMBO J. 6:1643-1651(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3033638; DOI=10.1073/pnas.84.10.3171;
Rosson D., Dugan D., Reddy E.P.;
"Aberrant splicing events that are induced by proviral integration:
implications for myb oncogene activation.";
Proc. Natl. Acad. Sci. U.S.A. 84:3171-3175(1987).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
PubMed=2481264; DOI=10.1093/nar/17.23.9593;
Sobieszczuk P.W., Gonda T.J., Dunn A.R.;
"Structure and biological activity of the transcriptional initiation
sequences of the murine c-myb oncogene.";
Nucleic Acids Res. 17:9593-9611(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 72-636.
PubMed=3023843; DOI=10.1128/MCB.6.2.380;
Shen-Ong G.L.C., Morse H.C. III, Potter M., Mushinski F.;
"Two modes of c-myb activation in virus-induced mouse myeloid
tumors.";
Mol. Cell. Biol. 6:380-392(1986).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-401.
PubMed=3016644; DOI=10.1093/nar/14.13.5309;
Lavu S., Reddy E.P.;
"Structural organization and nucleotide sequence of mouse c-myb
oncogene: activation in ABPL tumors is due to viral integration in an
intron which results in the deletion of the 5' coding sequences.";
Nucleic Acids Res. 14:5309-5320(1986).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-402.
PubMed=3014527; DOI=10.1073/pnas.83.14.5010;
Weinstein Y., Ihle J.N., Lavu S., Reddy P.E.;
"Truncation of the c-myb gene by a retroviral integration in an
interleukin 3-dependent myeloid leukemia cell line.";
Proc. Natl. Acad. Sci. U.S.A. 83:5010-5014(1986).
[11]
DOMAIN C-TERMINAL.
PubMed=2670562;
Gonda T.J., Buckmaster C., Ramsay R.G.;
"Activation of c-myb by carboxy-terminal truncation: relationship to
transformation of murine haemopoietic cells in vitro.";
EMBO J. 8:1777-1783(1989).
[12]
NEGATIVE REGULATORY DOMAIN.
PubMed=1923521;
Hu Y., Ramsay R.G., Kanei-Ishii C., Ishii S., Gonda T.J.;
"Transformation by carboxyl-deleted Myb reflects increased
transactivating capacity and disruption of a negative regulatory
domain.";
Oncogene 6:1549-1553(1991).
[13]
DOMAIN LEUCINE-ZIPPER, AND NEGATIVE AUTOREGULATION.
PubMed=8408047;
Nomura T., Sakai N., Sarai A., Sudo T., Kanei-Ishii C., Ramsay R.G.,
Favier D., Gonda T.J., Ishii S.;
"Negative autoregulation of c-Myb activity by homodimer formation
through the leucine zipper.";
J. Biol. Chem. 268:21914-21923(1993).
[14]
INTERACTION WITH MYBBP1A1.
PubMed=9447996; DOI=10.1128/MCB.18.2.989;
Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A.,
Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A.,
Ishii S., Gonda T.J.;
"Molecular cloning reveals that the p160 Myb-binding protein is a
novel, predominantly nucleolar protein which may play a role in
transactivation by Myb.";
Mol. Cell. Biol. 18:989-1002(1998).
[15]
INTERACTION WITH MAF.
PubMed=9566892; DOI=10.1128/MCB.18.5.2729;
Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.;
"c-Maf interacts with c-Myb to regulate transcription of an early
myeloid gene during differentiation.";
Mol. Cell. Biol. 18:2729-2737(1998).
[16]
INTERACTION WITH HIPK2 AND NLK.
PubMed=15082531; DOI=10.1101/gad.1170604;
Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T.,
Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E.,
Kim Y., Matsumoto K., Ishii S.;
"Wnt-1 signal induces phosphorylation and degradation of c-Myb protein
via TAK1, HIPK2, and NLK.";
Genes Dev. 18:816-829(2004).
[17]
INTERACTION WITH MAF.
PubMed=17823980; DOI=10.1002/eji.200636979;
Peng S., Lalani S., Leavenworth J.W., Ho I.-C., Pauza M.E.;
"c-Maf interacts with c-Myb to down-regulate Bcl-2 expression and
increase apoptosis in peripheral CD4 cells.";
Eur. J. Immunol. 37:2868-2880(2007).
[18]
STRUCTURE BY NMR OF 142-193.
PubMed=1631139; DOI=10.1073/pnas.89.14.6428;
Ogata K., Hojo H., Aimoto S., Nakai T., Nakamura H., Sarai A.,
Ishii S., Nishimura Y.;
"Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-
related motif with conserved tryptophans forming a hydrophobic core.";
Proc. Natl. Acad. Sci. U.S.A. 89:6428-6432(1992).
[19]
STRUCTURE BY NMR OF 89-192.
PubMed=8365401; DOI=10.1111/j.1432-1033.1993.tb18126.x;
Jamin N., Gabrielsen O.S., Gilles N., Lirsac P.-N., Toma F.;
"Secondary structure of the DNA-binding domain of the c-Myb
oncoprotein in solution. A multidimensional double and triple
heteronuclear NMR study.";
Eur. J. Biochem. 216:147-154(1993).
[20]
STRUCTURE BY NMR OF 38-89; 90-141 AND 142-193.
PubMed=7796266; DOI=10.1038/nsb0495-309;
Ogata K., Morikawa S., Nakamura H., Hojo H., Yoshimura S., Zhang R.,
Aimoto S., Ametani Y., Hirata Z., Sarai A., Ishii S., Nishimura Y.;
"Comparison of the free and DNA-complexed forms of the DNA-binding
domain from c-Myb.";
Nat. Struct. Biol. 2:309-320(1995).
[21]
STRUCTURE BY NMR OF 140-193.
PubMed=8942977; DOI=10.1073/pnas.93.24.13583;
Furukawa K., Oda M., Nakamura H.;
"A small engineered protein lacks structural uniqueness by increasing
the side-chain conformational entropy.";
Proc. Natl. Acad. Sci. U.S.A. 93:13583-13588(1996).
[22]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-193 IN COMPLEX WITH HUMAN
CEBPB.
PubMed=11792321; DOI=10.1016/S0092-8674(01)00636-5;
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.;
"Mechanism of c-Myb-C/EBP beta cooperation from separated sites on a
promoter.";
Cell 108:57-70(2002).
-!- FUNCTION: Transcriptional activator; DNA-binding protein that
specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an
important role in the control of proliferation and differentiation
of hematopoietic progenitor cells.
-!- SUBUNIT: Binds to HIPK1 (By similarity). Interacts with HIPK2,
MAF, MYBBP1A and NLK. {ECO:0000250, ECO:0000269|PubMed:11792321,
ECO:0000269|PubMed:15082531, ECO:0000269|PubMed:17823980,
ECO:0000269|PubMed:9447996, ECO:0000269|PubMed:9566892}.
-!- INTERACTION:
Q9QZR5:Hipk2; NbExp=2; IntAct=EBI-366934, EBI-366905;
P38531:HSF3 (xeno); NbExp=2; IntAct=EBI-366934, EBI-16212976;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- DOMAIN: Comprised of 3 domains; an N-terminal DNA-binding domain,
a centrally located transcriptional activation domain and a C-
terminal domain involved in transcriptional repression.
-!- DOMAIN: C-terminal truncated mutants display increased
transactivation.
-!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its
subsequent proteasomal degradation. {ECO:0000250}.
-!- PTM: Phosphorylated by NLK on multiple sites, which induces
proteasomal degradation.
-!- PTM: Phosphorylated by HIPK1. This phosphorylation reduces MYB
transcription factor activity but not MYB protein levels (By
similarity). {ECO:0000250}.
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EMBL; M21169; AAA39782.1; -; Genomic_DNA.
EMBL; M12848; AAB59713.1; -; mRNA.
EMBL; X02774; CAA26552.1; -; mRNA.
EMBL; M20210; AAA39783.1; -; Genomic_DNA.
EMBL; AC153556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011513; AAH11513.1; -; mRNA.
EMBL; X04099; CAA27724.1; -; Genomic_DNA.
EMBL; X04100; CAA27724.1; JOINED; Genomic_DNA.
EMBL; X04101; CAA27724.1; JOINED; Genomic_DNA.
EMBL; X04102; CAA27724.1; JOINED; Genomic_DNA.
EMBL; X04103; CAA27724.1; JOINED; Genomic_DNA.
EMBL; X04104; CAA27724.1; JOINED; Genomic_DNA.
EMBL; X16389; CAA34425.1; -; Genomic_DNA.
EMBL; X16390; CAA34426.1; -; Genomic_DNA.
EMBL; M13989; AAA39787.1; -; Genomic_DNA.
EMBL; K03547; AAA39786.1; -; Genomic_DNA.
CCDS; CCDS35861.1; -.
PIR; A25285; TVMSMB.
RefSeq; NP_001185843.1; NM_001198914.1.
RefSeq; NP_034978.3; NM_010848.3.
UniGene; Mm.473872; -.
UniGene; Mm.52109; -.
PDB; 1GUU; X-ray; 1.60 A; A=38-89.
PDB; 1GV2; X-ray; 1.68 A; A=89-193.
PDB; 1GV5; X-ray; 1.58 A; A=90-141.
PDB; 1GVD; X-ray; 1.45 A; A=90-141.
PDB; 1H88; X-ray; 2.80 A; C=37-193.
PDB; 1H89; X-ray; 2.45 A; C=37-193.
PDB; 1IDY; NMR; -; A=141-193.
PDB; 1IDZ; NMR; -; A=141-193.
PDB; 1MBE; NMR; -; A=38-89.
PDB; 1MBF; NMR; -; A=38-89.
PDB; 1MBG; NMR; -; A=90-141.
PDB; 1MBH; NMR; -; A=90-141.
PDB; 1MBJ; NMR; -; A=142-193.
PDB; 1MBK; NMR; -; A=142-193.
PDB; 1MSE; NMR; -; C=90-193.
PDB; 1MSF; NMR; -; C=90-193.
PDB; 1SB0; NMR; -; B=291-315.
PDB; 2AGH; NMR; -; A=291-315.
PDBsum; 1GUU; -.
PDBsum; 1GV2; -.
PDBsum; 1GV5; -.
PDBsum; 1GVD; -.
PDBsum; 1H88; -.
PDBsum; 1H89; -.
PDBsum; 1IDY; -.
PDBsum; 1IDZ; -.
PDBsum; 1MBE; -.
PDBsum; 1MBF; -.
PDBsum; 1MBG; -.
PDBsum; 1MBH; -.
PDBsum; 1MBJ; -.
PDBsum; 1MBK; -.
PDBsum; 1MSE; -.
PDBsum; 1MSF; -.
PDBsum; 1SB0; -.
PDBsum; 2AGH; -.
ProteinModelPortal; P06876; -.
SMR; P06876; -.
BioGrid; 201631; 12.
ComplexPortal; CPX-685; c-Myb-C/EBPbeta complex.
DIP; DIP-31713N; -.
ELM; P06876; -.
IntAct; P06876; 3.
STRING; 10090.ENSMUSP00000020158; -.
iPTMnet; P06876; -.
PhosphoSitePlus; P06876; -.
EPD; P06876; -.
PaxDb; P06876; -.
PRIDE; P06876; -.
Ensembl; ENSMUST00000020158; ENSMUSP00000020158; ENSMUSG00000019982.
GeneID; 17863; -.
KEGG; mmu:17863; -.
UCSC; uc007eog.1; mouse.
CTD; 4602; -.
MGI; MGI:97249; Myb.
eggNOG; KOG0048; Eukaryota.
eggNOG; COG5147; LUCA.
GeneTree; ENSGT00390000001038; -.
HOVERGEN; HBG007964; -.
InParanoid; P06876; -.
KO; K09420; -.
TreeFam; TF326257; -.
EvolutionaryTrace; P06876; -.
PRO; PR:P06876; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019982; Expressed in 243 organ(s), highest expression level in thymus.
CleanEx; MM_MYB; -.
ExpressionAtlas; P06876; baseline and differential.
Genevisible; P06876; MM.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001135; F:transcription factor activity, RNA polymerase II transcription factor recruiting; IBA:GO_Central.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0071987; F:WD40-repeat domain binding; IDA:MGI.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0071354; P:cellular response to interleukin-6; IDA:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; ISO:MGI.
GO; GO:0045624; P:positive regulation of T-helper cell differentiation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0048536; P:spleen development; IMP:MGI.
GO; GO:0017145; P:stem cell division; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
CDD; cd00167; SANT; 3.
InterPro; IPR015395; C-myb_C.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017930; Myb_dom.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR012642; Tscrpt_reg_Wos2-domain.
Pfam; PF09316; Cmyb_C; 1.
Pfam; PF07988; LMSTEN; 1.
Pfam; PF00249; Myb_DNA-binding; 3.
SMART; SM00717; SANT; 3.
SUPFAM; SSF46689; SSF46689; 2.
PROSITE; PS51294; HTH_MYB; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Complete proteome; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 636 Transcriptional activator Myb.
/FTId=PRO_0000197049.
DOMAIN 35 86 HTH myb-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DOMAIN 87 142 HTH myb-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DOMAIN 143 193 HTH myb-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 63 86 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 115 138 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 166 189 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
REGION 90 193 Interaction with HIPK2 and NLK.
{ECO:0000269|PubMed:15082531}.
REGION 275 327 Transcriptional activation domain.
{ECO:0000250}.
REGION 328 460 Negative regulatory domain.
REGION 375 396 Leucine-zipper.
MOD_RES 467 467 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10242}.
MOD_RES 476 476 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P10242}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000250|UniProtKB:P10242}.
MOD_RES 530 530 Phosphothreonine.
{ECO:0000250|UniProtKB:P10242}.
CROSSLNK 476 476 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P10242}.
CONFLICT 105 105 E -> K (in Ref. 2; CAA26552).
{ECO:0000305}.
CONFLICT 201 201 E -> K (in Ref. 2; CAA26552).
{ECO:0000305}.
CONFLICT 267 267 V -> A (in Ref. 1; AAB59713).
{ECO:0000305}.
CONFLICT 402 402 F -> V (in Ref. 10; AAA39786).
{ECO:0000305}.
CONFLICT 411 411 S -> N (in Ref. 2; CAA26552).
{ECO:0000305}.
CONFLICT 500 500 Q -> R (in Ref. 2; CAA26552 and 6;
AAH11513). {ECO:0000305}.
CONFLICT 525 525 E -> A (in Ref. 2; CAA26552).
{ECO:0000305}.
HELIX 45 58 {ECO:0000244|PDB:1GUU}.
HELIX 63 68 {ECO:0000244|PDB:1GUU}.
HELIX 75 86 {ECO:0000244|PDB:1GUU}.
STRAND 92 94 {ECO:0000244|PDB:1MBH}.
HELIX 97 110 {ECO:0000244|PDB:1GVD}.
HELIX 115 119 {ECO:0000244|PDB:1GVD}.
HELIX 127 136 {ECO:0000244|PDB:1GVD}.
STRAND 140 142 {ECO:0000244|PDB:1MSE}.
STRAND 144 146 {ECO:0000244|PDB:1MBK}.
HELIX 149 162 {ECO:0000244|PDB:1GV2}.
HELIX 163 165 {ECO:0000244|PDB:1MSF}.
HELIX 166 170 {ECO:0000244|PDB:1GV2}.
STRAND 173 175 {ECO:0000244|PDB:1MBK}.
HELIX 178 188 {ECO:0000244|PDB:1GV2}.
HELIX 189 191 {ECO:0000244|PDB:1IDY}.
HELIX 292 311 {ECO:0000244|PDB:1SB0}.
SEQUENCE 636 AA; 71422 MW; 0C6308E584726D01 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 VEDLQDVIKQ ESDESGIVAE FQESGPPLLK KIKQEVESPT EKSGNFFCSN
HWAENSLSTQ LFSQASPVAD APNILTSSVL MTPVSEDEDN VLKAFTVPKN RPLVGPLQPC
SGAWEPASCG KTEDQMTASG PARKYVNAFS ARTLVM


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31-234 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.1 mg
31-233 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.1 mg
28-797 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.1 mg
28-798 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.05 mg
18-785-210087 c-Jun (Ab-73) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210088 c-Jun (Ab-91) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210088 c-Jun (Ab-91) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210089 c-Jun (Ab-93) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210089 c-Jun (Ab-93) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210090 c-Jun (Ab-170) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210090 c-Jun (Ab-170) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210091 c-Jun (Ab-243) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210091 c-Jun (Ab-243) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg


 

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