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Transcription factor Maf (Proto-oncogene c-Maf) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog)

 MAF_MOUSE               Reviewed;         370 AA.
P54843; Q3V1Z2; Q4QY62;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 2.
18-JUL-2018, entry version 153.
RecName: Full=Transcription factor Maf;
AltName: Full=Proto-oncogene c-Maf;
AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog;
Name=Maf; Synonyms=Maf2;
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 [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Cerebellum;
PubMed=7799931; DOI=10.1128/MCB.15.1.246;
Kurschner C., Morgan J.I.;
"The maf proto-oncogene stimulates transcription from multiple sites
in a promoter that directs Purkinje neuron-specific gene expression.";
Mol. Cell. Biol. 15:246-254(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=14707122; DOI=10.1074/jbc.M312414200;
Cui W., Tomarev S.I., Piatigorsky J., Chepelinsky A.B., Duncan M.K.;
"Mafs, Prox1, and Pax6 can regulate chicken betaB1-crystallin gene
expression.";
J. Biol. Chem. 279:11088-11095(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
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).
[5]
FUNCTION, HETEROTETRAMER, INTERACTION WITH USF2, AND MUTAGENESIS OF
LEU-334.
PubMed=9070273; DOI=10.1006/bbrc.1997.6097;
Kurschner C., Morgan J.I.;
"USF2/FIP associates with the b-Zip transcription factor, c-Maf, via
its bHLH domain and inhibits c-Maf DNA binding activity.";
Biochem. Biophys. Res. Commun. 231:333-339(1997).
[6]
FUNCTION, AND INTERACTION WITH ETS1 AND MYB.
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).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10403649; DOI=10.1016/S1074-7613(00)80073-4;
Kim J.I., Ho I.-C., Grusby M.J., Glimcher L.H.;
"The transcription factor c-Maf controls the production of
interleukin-4 but not other Th2 cytokines.";
Immunity 10:745-751(1999).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=10383433; DOI=10.1074/jbc.274.27.19254;
Kawauchi S., Takahashi S., Nakajima O., Ogino H., Morita M.,
Nishizawa M., Yasuda K., Yamamoto M.;
"Regulation of lens fiber cell differentiation by transcription factor
c-Maf.";
J. Biol. Chem. 274:19254-19260(1999).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10097114; DOI=10.1073/pnas.96.7.3781;
Kim J.I., Li T., Ho I.C., Grusby M.J., Glimcher L.H.;
"Requirement for the c-Maf transcription factor in crystallin gene
regulation and lens development.";
Proc. Natl. Acad. Sci. U.S.A. 96:3781-3785(1999).
[10]
FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=10603348;
Ring B.Z., Cordes S.P., Overbeek P.A., Barsh G.S.;
"Regulation of mouse lens fiber cell development and differentiation
by the Maf gene.";
Development 127:307-317(2000).
[11]
FUNCTION, AND INTERACTION WITH CREBBP AND EP300.
PubMed=11943779; DOI=10.1074/jbc.M201821200;
Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.;
"CREB-binding protein/p300 co-activation of crystallin gene
expression.";
J. Biol. Chem. 277:24081-24089(2002).
[12]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=14512017; DOI=10.1016/S0012-1606(03)00324-5;
MacLean H.E., Kim J.I., Glimcher M.J., Wang J., Kronenberg H.M.,
Glimcher L.H.;
"Absence of transcription factor c-maf causes abnormal terminal
differentiation of hypertrophic chondrocytes during endochondral bone
development.";
Dev. Biol. 262:51-63(2003).
[13]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=15249232; DOI=10.1016/j.bbrc.2004.05.222;
Imaki J., Tsuchiya K., Mishima T., Onodera H., Kim J.I., Yoshida K.,
Ikeda H., Sakai M.;
"Developmental contribution of c-maf in the kidney: distribution and
developmental study of c-maf mRNA in normal mice kidney and
histological study of c-maf knockout mice kidney and liver.";
Biochem. Biophys. Res. Commun. 320:1323-1327(2004).
[14]
FUNCTION, AND INTERACTION WITH MYB.
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).
[15]
FUNCTION, MUTAGENESIS OF SER-15 AND SER-70, DNA-BINDING, AND TISSUE
SPECIFICITY.
PubMed=17897790; DOI=10.1016/j.gene.2007.08.010;
Mahoney K.M., Petrovic N., Schacke W., Shapiro L.H.;
"CD13/APN transcription is regulated by the proto-oncogene c-Maf via
an atypical response element.";
Gene 403:178-187(2007).
[16]
FUNCTION, SUBUNIT, INTERACTION WITH PAX6, DNA-BINDING, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=17901057; DOI=10.1074/jbc.M702795200;
Gosmain Y., Avril I., Mamin A., Philippe J.;
"Pax-6 and c-Maf functionally interact with the alpha-cell-specific
DNA element G1 in vivo to promote glucagon gene expression.";
J. Biol. Chem. 282:35024-35034(2007).
[17]
REVIEW, AND FUNCTION.
PubMed=19143053; DOI=10.1038/nrc2460;
Eychene A., Rocques N., Pouponnot C.;
"A new MAFia in cancer.";
Nat. Rev. Cancer 8:683-693(2008).
-!- FUNCTION: Acts as a transcriptional activator or repressor. When
overexpressed, represses anti-oxidant response element (ARE)-
mediated transcription. Involved either as an oncogene or as a
tumor suppressor, depending on the cell context. Binds to the ARE
sites of detoxifying enzyme gene promoters (By similarity).
Involved in embryonic lens fiber cell development. Recruits the
transcriptional coactivators CREBBP and/or EP300 to crystallin
promoters leading to up-regulation of crystallin gene during lens
fiber cell differentiation. Activates the expression of IL4 in T
helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis
by interacting with MYB and decreasing BCL2 expression. Together
with PAX6, transactivates strongly the glucagon gene promoter
through the G1 element. Activates transcription of the CD13
proximal promoter in endothelial cells. Represses transcription of
the CD13 promoter in early stages of myelopoiesis by affecting the
ETS1 and MYB cooperative interaction. Involved in the initial
chondrocyte terminal differentiation and the disappearance of
hypertrophic chondrocytes during endochondral bone development.
Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7
promoter. Binds to the T-MARE (Maf response element) sites of
lens-specific alpha- and beta-crystallin gene promoters. Binds
element G1 on the glucagon promoter. Binds an AT-rich region
adjacent to the TGC motif (atypical Maf response element) in the
CD13 proximal promoter in endothelial cells. It may interact with
additional basic-zipper proteins that determine a subtype of Maf-
responsive element binding. {ECO:0000250,
ECO:0000269|PubMed:10097114, ECO:0000269|PubMed:10383433,
ECO:0000269|PubMed:10403649, ECO:0000269|PubMed:10603348,
ECO:0000269|PubMed:11943779, ECO:0000269|PubMed:14512017,
ECO:0000269|PubMed:17823980, ECO:0000269|PubMed:17897790,
ECO:0000269|PubMed:17901057, ECO:0000269|PubMed:19143053,
ECO:0000269|PubMed:9070273, ECO:0000269|PubMed:9566892}.
-!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip
transcription factors. Binds DNA as a homodimer or as a
heterodimer. Heterotetramer of two MAF and two USF2. Interacts
with PAX6; the interaction is direct. Interacts with MYB;
interaction takes place weakly in normal T-cells and increases in
T-cells following stimulation through the TCR engagement.
Interacts with MYB; the ternary complex formed with MYB and the
CD13 promoter is regulated in response to differentiating signals.
Interacts with USF2; the interaction inhibits its DNA-binding
activity on the L7 promoter. Interacts with CREBBP, EP300 and ETS1
(By similarity). {ECO:0000250}.
-!- INTERACTION:
Q91ZW3:Smarca5; NbExp=2; IntAct=EBI-3842521, EBI-927547;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P54843-1; Sequence=Displayed;
Name=2; Synonyms=Long;
IsoId=P54843-2; Sequence=VSP_036408;
Note=No experimental confirmation available.;
Name=3;
IsoId=P54843-3; Sequence=VSP_036409;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in tubules of the renal cortex and
hepatocytes. Expressed in the lens (at protein level). Expressed
in pancreatic islets and endothelial cells.
{ECO:0000269|PubMed:15249232, ECO:0000269|PubMed:17897790,
ECO:0000269|PubMed:17901057}.
-!- DEVELOPMENTAL STAGE: Expressed in the floor of the diencephalon at
10 dpc (at protein level). Expressed in the midline of the
forebrain and in the eye region at 9 dpc. Expressed in the head
ectoderm destined to become the lens vesicle at 9 and 10 dpc.
Expressed in the lens placode at 10.5 dpc. Expressed in the lens
vesicle in both epithelial and fiber cells at 11 dpc. Expressed in
secondary fiber cells at the equatorial region that divides the
lens into anterior and posterior hemispheres between 11 and 14
dpc. Expressed in the neural tube and in primary fiber cells of
the lens at 11.5 dpc. Expressed in proximal tubules of the cortex
in the kidney at 16 and 17 dpc. Expressed in hypertrophic
chondrocytes at 14.5 to 18.5 dpc. Expressed in the pancreas at
12.5 dpc until the adult stage. {ECO:0000269|PubMed:10383433,
ECO:0000269|PubMed:10603348, ECO:0000269|PubMed:14512017,
ECO:0000269|PubMed:15249232, ECO:0000269|PubMed:17901057}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
Ubiquitination is triggered by glucocorticoids (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated by GSK3 and MAPK13 on serine and threonine
residues (By similarity). The phosphorylation status can serve to
either stimulate or inhibit transcription. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Knockout mice lacking this gene exhibit
small eyes or microphthalmia with an absence of normal lens
structures, an abnormal chondrocyte development, with terminal
differentiation of hypertrophic chondrocytes initially delayed,
followed by a subsequent expansion of the hypertrophic chondrocyte
domain in the growth plates of embryonic and postnatal long bones.
They also show a lack of IL4 production.
{ECO:0000269|PubMed:10097114, ECO:0000269|PubMed:10383433,
ECO:0000269|PubMed:10403649, ECO:0000269|PubMed:10603348,
ECO:0000269|PubMed:14512017}.
-!- SIMILARITY: Belongs to the bZIP family. Maf subfamily.
{ECO:0000305}.
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EMBL; S74567; AAB32820.1; -; mRNA.
EMBL; AY560005; AAY81957.1; -; mRNA.
EMBL; AK132165; BAE21007.1; -; mRNA.
EMBL; AC113301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS40486.1; -. [P54843-1]
RefSeq; NP_001020748.2; NM_001025577.2. [P54843-1]
UniGene; Mm.275549; -.
UniGene; Mm.439772; -.
UniGene; Mm.488377; -.
ProteinModelPortal; P54843; -.
SMR; P54843; -.
BioGrid; 201281; 2.
IntAct; P54843; 3.
MINT; P54843; -.
STRING; 10090.ENSMUSP00000104732; -.
iPTMnet; P54843; -.
PhosphoSitePlus; P54843; -.
MaxQB; P54843; -.
PaxDb; P54843; -.
PRIDE; P54843; -.
Ensembl; ENSMUST00000069009; ENSMUSP00000067704; ENSMUSG00000055435. [P54843-3]
Ensembl; ENSMUST00000109104; ENSMUSP00000104732; ENSMUSG00000055435. [P54843-1]
GeneID; 17132; -.
KEGG; mmu:17132; -.
UCSC; uc009noe.2; mouse. [P54843-3]
UCSC; uc009nof.1; mouse. [P54843-1]
CTD; 4094; -.
MGI; MGI:96909; Maf.
eggNOG; KOG4196; Eukaryota.
eggNOG; ENOG41102C7; LUCA.
GeneTree; ENSGT00550000074549; -.
HOGENOM; HOG000261683; -.
HOVERGEN; HBG000313; -.
InParanoid; P54843; -.
KO; K09035; -.
OMA; DRSINQC; -.
OrthoDB; EOG091G0H46; -.
PhylomeDB; P54843; -.
TreeFam; TF325689; -.
ChiTaRS; Maf; mouse.
PRO; PR:P54843; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000055435; -.
Genevisible; P54843; MM.
GO; GO:0005737; C:cytoplasm; 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:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0048468; P:cell development; IMP:MGI.
GO; GO:0001816; P:cytokine production; IDA:MGI.
GO; GO:0048839; P:inner ear development; IDA:MGI.
GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
GO; GO:0070306; P:lens fiber cell differentiation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR028573; Maf/V-MAF.
InterPro; IPR013592; Maf_TF_N.
InterPro; IPR008917; TF_DNA-bd_sf.
InterPro; IPR024874; Transciption_factor_Maf_fam.
PANTHER; PTHR10129; PTHR10129; 1.
PANTHER; PTHR10129:SF9; PTHR10129:SF9; 1.
Pfam; PF03131; bZIP_Maf; 1.
Pfam; PF08383; Maf_N; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; DNA-binding;
Isopeptide bond; Nucleus; Proto-oncogene; Reference proteome;
Repressor; Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation.
CHAIN 1 370 Transcription factor Maf.
/FTId=PRO_0000076492.
DOMAIN 285 348 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 126 370 Represses ARE-mediated transcription.
{ECO:0000250}.
REGION 285 310 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 313 334 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 126 251 Gly-rich.
COMPBIAS 132 224 Ala-rich.
COMPBIAS 180 194 His-rich.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O75444}.
CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O75444}.
CROSSLNK 328 328 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O75444}.
VAR_SEQ 370 370 M -> MCVCVCALFIL (in isoform 2).
{ECO:0000303|PubMed:14707122}.
/FTId=VSP_036408.
VAR_SEQ 370 370 M -> MYPRDSSTSVM (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_036409.
MUTAGEN 15 15 S->A: Inhibition on transcriptional
activation on CD13 proximal promoter in
endothelial cells.
{ECO:0000269|PubMed:17897790}.
MUTAGEN 70 70 S->A: No effect on transcriptional
activation on CD13 proximal promoter.
Increases liver specific transactivation
on the IL-4 promoter.
{ECO:0000269|PubMed:17897790}.
MUTAGEN 334 334 L->P: Abolishes interaction with USF2.
{ECO:0000269|PubMed:9070273}.
CONFLICT 202 202 A -> T (in Ref. 1; AAB32820).
{ECO:0000305}.
CONFLICT 208 211 ASAS -> SSSN (in Ref. 1; AAB32820).
{ECO:0000305}.
CONFLICT 223 224 SA -> NT (in Ref. 1; AAB32820).
{ECO:0000305}.
CONFLICT 231 231 G -> D (in Ref. 1; AAB32820).
{ECO:0000305}.
CONFLICT 248 248 A -> S (in Ref. 1; AAB32820).
{ECO:0000305}.
SEQUENCE 370 AA; 38435 MW; 1E8722C8287AAAC9 CRC64;
MASELAMNNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM
STPCSSVPPS PSFSAPSPGS GSEQKAHLED YYWMTGYPQQ LNPEALGFSP EDAVEALISN
SHQLQGGFDG YARGAQQLAA AAGAGAGASL GGSGEEMGPA AAVVSAVIAA AAAQSGAAPH
YHHHHHHAAG HHHHPTAGAP GAAGGASASA SGAGGAGGGG PASAGGGGGG GGGGGTAGAG
GALHPHHAAG GLHFDDRFSD EQLVTMSVRE LNRQLRGVSK EEVIRLKQKR RTLKNRGYAQ
SCRFKRVQQR HVLESEKNQL LQQVDHLKQE ISRLVRERDA YKEKYEKLVS NGFRENGSSS
DNPSSPEFFM


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15-288-21143 Transcription factor AP-1 - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
15-288-21143 Transcription factor AP-1 - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
E1292p ELISA kit Activator protein 1,AP1,JUN,Pig,Proto-oncogene c-Jun,Sus scrofa,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292p ELISA Activator protein 1,AP1,JUN,Pig,Proto-oncogene c-Jun,Sus scrofa,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
U1292p CLIA Activator protein 1,AP1,JUN,Pig,Proto-oncogene c-Jun,Sus scrofa,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
U1292r CLIA Activator protein 1,AP1,Jun,Proto-oncogene c-Jun,Rat,Rattus norvegicus,Rjg-9,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292r ELISA kit Activator protein 1,AP1,Jun,Proto-oncogene c-Jun,Rat,Rattus norvegicus,Rjg-9,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
U1292b CLIA Activator protein 1,AP1,Bos taurus,Bovine,JUN,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292b ELISA kit Activator protein 1,AP1,Bos taurus,Bovine,JUN,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292b ELISA Activator protein 1,AP1,Bos taurus,Bovine,JUN,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292r ELISA Activator protein 1,AP1,Jun,Proto-oncogene c-Jun,Rat,Rattus norvegicus,Rjg-9,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
DL-MAF-Hu Human V-Maf Musculoaponeurotic Fibrosarcoma Oncogene Homolog (MAF) ELISA Kit 96T
U1292m CLIA Activator protein 1,AH119,AP1,Jun,Jun A,Mouse,Mus musculus,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292m ELISA Activator protein 1,AH119,AP1,Jun,Jun A,Mouse,Mus musculus,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292h ELISA Activator protein 1,AP1,Homo sapiens,Human,JUN,p39,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292m ELISA kit Activator protein 1,AH119,AP1,Jun,Jun A,Mouse,Mus musculus,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
E1292h ELISA kit Activator protein 1,AP1,Homo sapiens,Human,JUN,p39,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
U1292h CLIA Activator protein 1,AP1,Homo sapiens,Human,JUN,p39,Proto-oncogene c-Jun,Transcription factor AP-1,V-jun avian sarcoma virus 17 oncogene homolog 96T
MAFA MAF Gene v-maf musculoaponeurotic fibrosarcoma oncogene homolog (avian)


 

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