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Myc protein (Diminutive protein) (dMyc1)

 MYC_DROME               Reviewed;         717 AA.
Q9W4S7; O96903; P91665;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
23-MAY-2018, entry version 146.
RecName: Full=Myc protein {ECO:0000312|FlyBase:FBgn0262656};
AltName: Full=Diminutive protein {ECO:0000303|PubMed:8929412};
AltName: Full=dMyc1 {ECO:0000303|PubMed:8929412};
Name=Myc {ECO:0000303|PubMed:8929412,
ECO:0000312|FlyBase:FBgn0262656};
Synonyms=dm {ECO:0000303|PubMed:8929412};
ORFNames=CG10798 {ECO:0000312|FlyBase:FBgn0262656};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF45866.2};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=Oregon-R {ECO:0000269|PubMed:8929412};
PubMed=8929412; DOI=10.1126/science.274.5292.1523;
Gallant P., Shiio Y., Cheng P.F., Parkhurst S.M., Eisenman R.N.;
"Myc and Max homologs in Drosophila.";
Science 274:1523-1527(1996).
[2] {ECO:0000305}
SEQUENCE REVISION TO 274.
Gallant P., Shiio Y., Cheng P.F., Parkhurst S.M., Eisenman R.N.;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo;
PubMed=9037036; DOI=10.1073/pnas.94.4.1235;
Schreiber-Agus N., Stein D., Chen K., Goltz J.S., Stevens L.,
DePinho R.A.;
"Drosophila Myc is oncogenic in mammalian cells and plays a role in
the diminutive phenotype.";
Proc. Natl. Acad. Sci. U.S.A. 94:1235-1240(1997).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5] {ECO:0000305}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[7] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[8]
FUNCTION, AND INTERACTION WITH AGO.
PubMed=15182669; DOI=10.1016/j.cub.2004.04.040;
Moberg K.H., Mukherjee A., Veraksa A., Artavanis-Tsakonas S.,
Hariharan I.K.;
"The Drosophila F box protein archipelago regulates dMyc protein
levels in vivo.";
Curr. Biol. 14:965-974(2004).
[9]
FUNCTION, AND INTERACTION WITH PONT AND REPT.
PubMed=16087886; DOI=10.1073/pnas.0408945102;
Bellosta P., Hulf T., Balla Diop S., Usseglio F., Pradel J.,
Aragnol D., Gallant P.;
"Myc interacts genetically with Tip48/Reptin and Tip49/Pontin to
control growth and proliferation during Drosophila development.";
Proc. Natl. Acad. Sci. U.S.A. 102:11799-11804(2005).
[10]
FUNCTION, INTERACTION WITH LID, AND IDENTIFICATION IN COMPLEX WITH LID
AND ASH2.
PubMed=17311883; DOI=10.1101/gad.1523007;
Secombe J., Li L., Carlos L., Eisenman R.N.;
"The Trithorax group protein Lid is a trimethyl histone H3K4
demethylase required for dMyc-induced cell growth.";
Genes Dev. 21:537-551(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND SER-220, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[12]
FUNCTION, AND INTERACTION WITH AGO AND PUF.
PubMed=24173801; DOI=10.1242/dev.096941;
Li L., Anderson S., Secombe J., Eisenman R.N.;
"The Drosophila ubiquitin-specific protease Puffyeye regulates dMyc-
mediated growth.";
Development 140:4776-4787(2013).
[13]
FUNCTION.
PubMed=24615015; DOI=10.1128/MCB.00658-13;
Hovhanyan A., Herter E.K., Pfannstiel J., Gallant P., Raabe T.;
"Drosophila mbm is a nucleolar myc and casein kinase 2 target required
for ribosome biogenesis and cell growth of central brain
neuroblasts.";
Mol. Cell. Biol. 34:1878-1891(2014).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25999153; DOI=10.1038/srep10339;
Kuo Y., Huang H., Cai T., Wang T.;
"Target of Rapamycin Complex 2 regulates cell growth via Myc in
Drosophila.";
Sci. Rep. 5:10339-10339(2015).
-!- FUNCTION: Participates in the regulation of gene transcription
(PubMed:8929412, PubMed:16087886, PubMed:24173801,
PubMed:24615015, PubMed:25999153). Binds DNA in a non-specific
manner, yet also specifically recognizes the core sequence
CAC[GA]TG (PubMed:8929412). Seems to activate the transcription of
growth-related genes; required for cellular proliferation and
growth (PubMed:16087886, PubMed:25999153). Functions in the TORC2-
mediated regulation of cell growth, acting downstream of the TORC2
complex (PubMed:25999153). Inhibits the demethylase activity of
Lid (PubMed:17311883). Activates transcription of mbm
(PubMed:24615015). Able to induce the SCF E3 ubiquitin-protein
ligase member archipelago (ago) which functions in its degradation
(PubMed:15182669, PubMed:24173801). It may therefore create a
negative feedback loop with ago that is regulated by the ubiquitin
hydrolase puf (PubMed:24173801). {ECO:0000269|PubMed:15182669,
ECO:0000269|PubMed:16087886, ECO:0000269|PubMed:17311883,
ECO:0000269|PubMed:24173801, ECO:0000269|PubMed:24615015,
ECO:0000269|PubMed:25999153, ECO:0000269|PubMed:8929412}.
-!- FUNCTION: Transcription factor that binds DNA in a non-specific
manner, yet also specifically recognizes the core sequence 5'-
CAC[GA]TG-3'. Activates the transcription of growth-related genes.
{ECO:0000250|UniProtKB:P01106}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein (PubMed:8929412). Binds DNA as a heterodimer with Max
(PubMed:8929412). Interacts with ago (PubMed:15182669,
PubMed:24173801). Interacts with lid (PubMed:17311883). Part of a
complex containing lid, Myc and ash2 (PubMed:17311883). Component
of a complex with pont and rept (PubMed:16087886). Interacts with
puf (PubMed:24173801). {ECO:0000269|PubMed:15182669,
ECO:0000269|PubMed:16087886, ECO:0000269|PubMed:17311883,
ECO:0000269|PubMed:24173801, ECO:0000269|PubMed:8929412}.
-!- INTERACTION:
Q9VZF4:ago; NbExp=2; IntAct=EBI-120162, EBI-138334;
P16371:gro; NbExp=3; IntAct=EBI-120162, EBI-153866;
P16371-2:gro; NbExp=3; IntAct=EBI-120162, EBI-15661898;
P91664:Max; NbExp=3; IntAct=EBI-120162, EBI-193577;
Q9VH07:pont; NbExp=4; IntAct=EBI-120162, EBI-234957;
Q9V3K3:rept; NbExp=4; IntAct=EBI-120162, EBI-192924;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25999153}.
Cytoplasm {ECO:0000269|PubMed:25999153}. Note=Transolcation from
the cytoplasm to the nucleus may be promoted by the TORC2 complex
(Lst8 and rictor). {ECO:0000269|PubMed:25999153}.
-!- TISSUE SPECIFICITY: Low levels detected throughout embryo before
cellular blastoderm formation, particularly concentrated in pole
plasm. Zygotic expression detected during cellular blastoderm
stage in endodermal anlagen of anterior and posterior midgut at
both poles. After gastrulation, expression detected in
invaginating ventral furrow of mesoderm. Continued expression in
anterior and posterior midgut and mesoderm during germband
extension. During late germ-band retraction, expression remains
detectable in fusing midgut and presumed developing somatic
musculature. {ECO:0000269|PubMed:8929412,
ECO:0000269|PubMed:9037036}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
embryos. {ECO:0000269|PubMed:8929412, ECO:0000269|PubMed:9037036}.
-!- PTM: Probably targeted for ubiquitination by the SFC ubiquitin
ligase complex member ago, leading to its proteasomal degradation.
{ECO:0000305|PubMed:15182669}.
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EMBL; U77370; AAB39842.2; -; mRNA.
EMBL; U81384; AAD00517.1; -; mRNA.
EMBL; AE014298; AAF45866.2; -; Genomic_DNA.
EMBL; AL121800; CAD24780.1; -; Genomic_DNA.
EMBL; AY058627; AAL13856.1; -; mRNA.
RefSeq; NP_001259204.1; NM_001272275.1.
RefSeq; NP_525062.2; NM_080323.4.
UniGene; Dm.4239; -.
ProteinModelPortal; Q9W4S7; -.
SMR; Q9W4S7; -.
BioGrid; 57835; 166.
DIP; DIP-18847N; -.
IntAct; Q9W4S7; 16.
MINT; Q9W4S7; -.
STRING; 7227.FBpp0303995; -.
iPTMnet; Q9W4S7; -.
PaxDb; Q9W4S7; -.
PRIDE; Q9W4S7; -.
EnsemblMetazoa; FBtr0070525; FBpp0070501; FBgn0262656.
EnsemblMetazoa; FBtr0331605; FBpp0303995; FBgn0262656.
GeneID; 31310; -.
KEGG; dme:Dmel_CG10798; -.
UCSC; CG10798-RA; d. melanogaster.
CTD; 4609; -.
FlyBase; FBgn0262656; Myc.
eggNOG; ENOG410IPD1; Eukaryota.
eggNOG; ENOG410XXWA; LUCA.
GeneTree; ENSGT00510000046414; -.
InParanoid; Q9W4S7; -.
KO; K04377; -.
OMA; PEFRHNV; -.
OrthoDB; EOG091G0YBS; -.
PhylomeDB; Q9W4S7; -.
Reactome; R-DME-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
Reactome; R-DME-9018519; Estrogen-dependent gene expression.
SignaLink; Q9W4S7; -.
ChiTaRS; Myc; fly.
GenomeRNAi; 31310; -.
PRO; PR:Q9W4S7; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0262656; -.
ExpressionAtlas; Q9W4S7; baseline and differential.
Genevisible; Q9W4S7; DM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
GO; GO:0008283; P:cell proliferation; IEP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:FlyBase.
GO; GO:0031670; P:cellular response to nutrient; IDA:FlyBase.
GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEP:UniProtKB.
GO; GO:0009880; P:embryonic pattern specification; IGI:FlyBase.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:FlyBase.
GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:FlyBase.
GO; GO:0022008; P:neurogenesis; IGI:FlyBase.
GO; GO:0017126; P:nucleologenesis; IMP:FlyBase.
GO; GO:0030307; P:positive regulation of cell growth; TAS:FlyBase.
GO; GO:0045793; P:positive regulation of cell size; IMP:UniProtKB.
GO; GO:0048639; P:positive regulation of developmental growth; IMP:FlyBase.
GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase.
GO; GO:0050769; P:positive regulation of neurogenesis; IMP:FlyBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
GO; GO:0010506; P:regulation of autophagy; IMP:FlyBase.
GO; GO:0044719; P:regulation of imaginal disc-derived wing size; IMP:FlyBase.
GO; GO:0046620; P:regulation of organ growth; IMP:FlyBase.
GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IDA:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0090062; P:regulation of trehalose metabolic process; IMP:FlyBase.
GO; GO:0042594; P:response to starvation; IMP:FlyBase.
GO; GO:0006360; P:transcription by RNA polymerase I; IDA:FlyBase.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Activator; Coiled coil; Complete proteome; Cytoplasm; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 717 Myc protein.
/FTId=PRO_0000127322.
DOMAIN 625 677 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
COILED 679 711 {ECO:0000255}.
COMPBIAS 361 377 Asn-rich.
COMPBIAS 465 608 Ser-rich.
MOD_RES 217 217 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 353 353 G -> D (in Ref. 3; AAD00517).
{ECO:0000305}.
CONFLICT 362 362 N -> S (in Ref. 3; AAD00517).
{ECO:0000305}.
CONFLICT 365 365 S -> K (in Ref. 3; AAD00517).
{ECO:0000305}.
CONFLICT 369 373 NNKLK -> IKNNN (in Ref. 3; AAD00517).
{ECO:0000305}.
SEQUENCE 717 AA; 79308 MW; D6A74CF5D4B80150 CRC64;
MALYRSDPYS IMDDQLFSNI SIFDMDNDLY DMDKLLSSST IQSDLEKIED MESVFQDYDL
EEDMKPEIRN IDCMWPAMSS CLTSGNGNGI ESGNSAASSY SETGAVSLAM VSGSTNLYSA
YQRSQTTDNT QSNQQHVVNS AENMPVIIKK ELADLDYTVC QKRLRLSGGD KKSQIQDEVH
LIPPGGSLLR KRNNQDIIRK SGELSGSDSI KYQRPDTPHS LTDEVAASEF RHNVDLRACV
MGSNNISLTG NDSDVNYIKQ ISRELQNTGK DPLPVRYIPP INDVLDVLNQ HSNSTGGQQQ
LNQQQLDEQQ QAIDIATGRN TVDSPPTTGS DSDSDDGEPL NFDLRHHRTS KSGSNASITT
NNNNSNNKNN KLKNNSNGML HMMHITDHSY TRCNDMVDDG PNLETPSDSD EEIDVVSYTD
KKLPTNPSCH LMGALQFQMA HKISIDHMKQ KPRYNNFNLP YTPASSSPVK SVANSRYPSP
SSTPYQNCSS ASPSYSPLSV DSSNVSSSSS SSSSQSSFTT SSSNKGRKRS SLKDPGLLIS
SSSVYLPGVN NKVTHSSMMS KKSRGKKVVG TSSGNTSPIS SGQDVDAMDR NWQRRSGGIA
TSTSSNSSVH RKDFVLGFDE ADTIEKRNQH NDMERQRRIG LKNLFEALKK QIPTIRDKER
APKVNILREA AKLCIQLTQE EKELSMQRQL LSLQLKQRQD TLASYQMELN ESRSVSG


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18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
EIAAB32247 ADP-ribosylation factor-like protein 6-interacting protein 5,Aip-5,ARL-6-interacting protein 5,ARL6IP5,Cytoskeleton-related vitamin A-responsive protein,Dermal papilla-derived protein 11,DERP11,Glutam
E1773h ELISA kit G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
E1773h ELISA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB29586 Mouse,Mus musculus,p53-induced gene 11 protein,Pig11,Tp53i11,Transformation related protein 53 inducible protein 11,Trp53i11,Tumor protein p53-inducible protein 11
EIAAB43486 Mouse,Mus musculus,Protein TAP1,Protein TRUSS,Rabex-5_Rin2-interacting protein,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.002 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.01 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.1 mg
EIAAB43485 C20orf188,Homo sapiens,Human,Protein TAP1,Protein TRUSS,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp4-associated protein,TR
EIAAB33912 E3 ubiquitin-protein ligase RBBP6,Mouse,Mus musculus,P2pr,p53-associated cellular protein of testis,Pact,Proliferation potential-related protein,Protein P2P-R,Rbbp6,Retinoblastoma-binding protein 6
EIAAB38162 Homo sapiens,Human,MAP,Merlin-associated protein,RabGAPLP,RABGAPLP,Rab-GTPase-activating protein-like protein,RUN and TBC1 domain-containing protein 3,RUTBC3,SGSM3,Small G protein signaling modulator
EIAAB29908 Cap1,Contraception-associated protein 1,Fertility protein SP22,Park7,Parkinson disease protein 7 homolog,Protein CAP1,Protein DJ-1,Rat,Rattus norvegicus
EIAAB31031 DDXBP1,DEAD_H box-binding protein 1,E3 SUMO-protein ligase PIAS1,GBP,Gu-binding protein,Homo sapiens,Human,PIAS1,Protein inhibitor of activated STAT protein 1,RNA helicase II-binding protein


 

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