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Insulin receptor substrate 4 (IRS-4) (160 kDa phosphotyrosine protein) (py160) (Phosphoprotein of 160 kDa) (pp160)

 IRS4_HUMAN              Reviewed;        1257 AA.
O14654;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
05-DEC-2018, entry version 160.
RecName: Full=Insulin receptor substrate 4;
Short=IRS-4;
AltName: Full=160 kDa phosphotyrosine protein;
Short=py160;
AltName: Full=Phosphoprotein of 160 kDa;
Short=pp160;
Name=IRS4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 100-117; 233-240;
613-618; 836-843 AND 844-852, AND PHOSPHORYLATION.
TISSUE=Kidney;
PubMed=9261155; DOI=10.1074/jbc.272.34.21403;
Lavan B.E., Fantin V.R., Chang E.T., Lane W.S., Keller S.R.,
Lienhard G.E.;
"A novel 160-kDa phosphotyrosine protein in insulin-treated embryonic
kidney cells is a new member of the insulin receptor substrate
family.";
J. Biol. Chem. 272:21403-21407(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GRB2 AND PIK3R1, AND
PHOSPHORYLATION.
PubMed=9553137; DOI=10.1074/jbc.273.17.10726;
Fantin V.R., Sparling J.D., Slot J.W., Keller S.R., Lienhard G.E.,
Lavan B.E.;
"Characterization of insulin receptor substrate 4 in human embryonic
kidney 293 cells.";
J. Biol. Chem. 273:10726-10732(1998).
[5]
INTERACTION WITH CRK AND CRKL.
PubMed=9614078; DOI=10.1074/jbc.273.24.14780;
Koval A.P., Karas M., Zick Y., LeRoith D.;
"Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-
like growth factor-I receptor-mediated signal transduction.";
J. Biol. Chem. 273:14780-14787(1998).
[6]
FUNCTION.
PubMed=10531310; DOI=10.1074/jbc.274.44.31179;
Qu B.-H., Karas M., Koval A., LeRoith D.;
"Insulin receptor substrate-4 enhances insulin-like growth factor-I-
induced cell proliferation.";
J. Biol. Chem. 274:31179-31184(1999).
[7]
FUNCTION, AND INTERACTION WITH GRB2 AND PIK3R1.
PubMed=10594015; DOI=10.1128/MCB.20.1.126-138.2000;
Uchida T., Myers M.G. Jr., White M.F.;
"IRS-4 mediates protein kinase B signaling during insulin stimulation
without promoting antiapoptosis.";
Mol. Cell. Biol. 20:126-138(2000).
[8]
INTERACTION WITH CRK, AND MUTAGENESIS OF TYR-700; TYR-717; TYR-743 AND
TYR-779.
PubMed=11316748; DOI=10.1210/endo.142.5.8135;
Karas M., Koval A.P., Zick Y., LeRoith D.;
"The insulin-like growth factor I receptor-induced interaction of
insulin receptor substrate-4 and Crk-II.";
Endocrinology 142:1835-1840(2001).
[9]
INTERACTION WITH NISCH.
PubMed=11912194; DOI=10.1074/jbc.M111838200;
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.;
"Insulin receptor substrate 4 associates with the protein IRAS.";
J. Biol. Chem. 277:19439-19447(2002).
[10]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12639902; DOI=10.1210/en.2002-220723;
Schreyer S., Ledwig D., Rakatzi I., Kloeting I., Eckel J.;
"Insulin receptor substrate-4 is expressed in muscle tissue without
acting as a substrate for the insulin receptor.";
Endocrinology 144:1211-1218(2003).
[11]
PHOSPHORYLATION AT TYR-921, INTERACTION WITH SHC1; GRB2; PHOSPHOLIPASE
C-GAMMA AND PHOSPHATIDYLINOSITOL 3-KINASE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15316024; DOI=10.1074/jbc.M404537200;
Hinsby A.M., Olsen J.V., Mann M.;
"Tyrosine phosphoproteomics of fibroblast growth factor signaling: a
role for insulin receptor substrate-4.";
J. Biol. Chem. 279:46438-46447(2004).
[12]
INTERACTION WITH PPP4C, INDUCTION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15331607; DOI=10.1074/jbc.M408067200;
Mihindukulasuriya K.A., Zhou G., Qin J., Tan T.-H.;
"Protein phosphatase 4 interacts with and down-regulates insulin
receptor substrate 4 following tumor necrosis factor-alpha
stimulation.";
J. Biol. Chem. 279:46588-46594(2004).
[13]
INTERACTION WITH PTK6, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15870689; DOI=10.1038/sj.onc.1208721;
Qiu H., Zappacosta F., Su W., Annan R.S., Miller W.T.;
"Interaction between Brk kinase and insulin receptor substrate-4.";
Oncogene 24:5656-5664(2005).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17408801; DOI=10.1016/j.jhep.2007.01.031;
Cuevas E.P., Escribano O., Chiloeches A., Ramirez Rubio S.,
Roman I.D., Fernandez-Moreno M.D., Guijarro L.G.;
"Role of insulin receptor substrate-4 in IGF-I-stimulated HEPG2
proliferation.";
J. Hepatol. 46:1089-1098(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
VARIANTS [LARGE SCALE ANALYSIS] VAL-20; GLU-215 AND ARG-557.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Acts as an interface between multiple growth factor
receptors possessing tyrosine kinase activity, such as insulin
receptor, IGF1R and FGFR1, and a complex network of intracellular
signaling molecules containing SH2 domains. Involved in the IGF1R
mitogenic signaling pathway. Promotes the AKT1 signaling pathway
and BAD phosphorylation during insulin stimulation without
activation of RPS6KB1 or the inhibition of apoptosis. Interaction
with GRB2 enhances insulin-stimulated mitogen-activated protein
kinase activity. May be involved in nonreceptor tyrosine kinase
signaling in myoblasts. Plays a pivotal role in the
proliferation/differentiation of hepatoblastoma cell through EPHB2
activation upon IGF1 stimulation. May play a role in the signal
transduction in response to insulin and to a lesser extent in
response to IL4 and GH on mitogenesis. Plays a role in growth,
reproduction and glucose homeostasis. May act as negative
regulators of the IGF1 signaling pathway by suppressing the
function of IRS1 and IRS2. {ECO:0000269|PubMed:10531310,
ECO:0000269|PubMed:10594015, ECO:0000269|PubMed:12639902,
ECO:0000269|PubMed:17408801, ECO:0000269|PubMed:9553137}.
-!- SUBUNIT: Interacts with SOCS6 in response to stimulation with
either insulin or IGF1 (By similarity). Interacts with CRK and
CRKL. Interaction with CRK is stronger than with CRKL. Interacts
with CRK via the phosphorylated YXXM motifs. Interacts with GRB2
and PIK3R1. Interacts with PLC-gamma, SHC1, PTK6, PPP4C and NISCH.
{ECO:0000250, ECO:0000269|PubMed:10594015,
ECO:0000269|PubMed:11316748, ECO:0000269|PubMed:11912194,
ECO:0000269|PubMed:15316024, ECO:0000269|PubMed:15331607,
ECO:0000269|PubMed:15870689, ECO:0000269|PubMed:9553137,
ECO:0000269|PubMed:9614078}.
-!- INTERACTION:
P46108:CRK; NbExp=8; IntAct=EBI-356594, EBI-886;
P00533:EGFR; NbExp=2; IntAct=EBI-356594, EBI-297353;
Q15185:PTGES3; NbExp=2; IntAct=EBI-356594, EBI-1049387;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9553137};
Peripheral membrane protein {ECO:0000269|PubMed:9553137};
Cytoplasmic side {ECO:0000269|PubMed:9553137}.
-!- TISSUE SPECIFICITY: Expressed in myoblasts. Expressed in liver and
hepatocellular carcinoma. {ECO:0000269|PubMed:12639902,
ECO:0000269|PubMed:17408801}.
-!- INDUCTION: Down-regulated by PPP4C in a phosphatase activity-
dependent manner. {ECO:0000269|PubMed:15331607}.
-!- PTM: Phosphorylated on tyrosine residues in response to both
insulin and IGF1 signaling. Phosphorylated on Tyr-921 in response
to FGF2 signaling. Phosphorylation of Tyr-921 is required for
GRB2, phospholipase C-gamma and phosphatidylinositol 3-kinase
interaction. {ECO:0000269|PubMed:15316024,
ECO:0000269|PubMed:9261155, ECO:0000269|PubMed:9553137}.
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EMBL; AF007567; AAC51738.1; -; mRNA.
EMBL; AL035425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471120; EAX02682.1; -; Genomic_DNA.
CCDS; CCDS14544.1; -.
RefSeq; NP_003595.1; NM_003604.2.
UniGene; Hs.407141; -.
UniGene; Hs.460872; -.
ProteinModelPortal; O14654; -.
BioGrid; 114048; 118.
IntAct; O14654; 99.
MINT; O14654; -.
STRING; 9606.ENSP00000361202; -.
iPTMnet; O14654; -.
PhosphoSitePlus; O14654; -.
BioMuta; IRS4; -.
EPD; O14654; -.
MaxQB; O14654; -.
PaxDb; O14654; -.
PeptideAtlas; O14654; -.
PRIDE; O14654; -.
ProteomicsDB; 48151; -.
DNASU; 8471; -.
Ensembl; ENST00000372129; ENSP00000361202; ENSG00000133124.
GeneID; 8471; -.
KEGG; hsa:8471; -.
UCSC; uc004eoc.3; human.
CTD; 8471; -.
DisGeNET; 8471; -.
EuPathDB; HostDB:ENSG00000133124.11; -.
GeneCards; IRS4; -.
HGNC; HGNC:6128; IRS4.
HPA; HPA017372; -.
MIM; 300904; gene.
neXtProt; NX_O14654; -.
OpenTargets; ENSG00000133124; -.
PharmGKB; PA29923; -.
eggNOG; ENOG410IXEK; Eukaryota.
eggNOG; ENOG410Z9EP; LUCA.
GeneTree; ENSGT00940000160883; -.
HOGENOM; HOG000113104; -.
HOVERGEN; HBG107140; -.
InParanoid; O14654; -.
KO; K17446; -.
OMA; MFMAPGA; -.
OrthoDB; EOG091G02EF; -.
PhylomeDB; O14654; -.
TreeFam; TF325994; -.
Reactome; R-HSA-2428928; IRS-related events triggered by IGF1R.
SignaLink; O14654; -.
SIGNOR; O14654; -.
GeneWiki; IRS4; -.
GenomeRNAi; 8471; -.
PRO; PR:O14654; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000133124; Expressed in 23 organ(s), highest expression level in adenohypophysis.
CleanEx; HS_IRS4; -.
Genevisible; O14654; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005158; F:insulin receptor binding; IBA:GO_Central.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IBA:GO_Central.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd01204; PTB_IRS; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR039011; IRS.
InterPro; IPR002404; IRS_PTB.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR10614; PTHR10614; 1.
Pfam; PF02174; IRS; 1.
PRINTS; PR00628; INSULINRSI.
SMART; SM00233; PH; 1.
SMART; SM00310; PTBI; 1.
PROSITE; PS51064; IRS_PTB; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transducer.
CHAIN 1 1257 Insulin receptor substrate 4.
/FTId=PRO_0000314678.
DOMAIN 78 199 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 231 335 IRS-type PTB. {ECO:0000255|PROSITE-
ProRule:PRU00389}.
REGION 678 800 CRK-binding.
REGION 895 897 GRB2-binding.
MOTIF 487 490 YXXM motif 1.
MOTIF 700 703 YXXM motif 2.
MOTIF 717 720 YXXM motif 3.
MOTIF 743 746 YXXM motif 4.
MOTIF 779 782 YXXM motif 5.
MOTIF 828 831 YXXM motif 6.
MOTIF 921 924 YXXM motif 7.
COMPBIAS 18 28 Poly-Ala.
COMPBIAS 124 137 Ala-rich.
COMPBIAS 218 226 Poly-Ala.
COMPBIAS 628 639 Pro-rich.
COMPBIAS 1094 1212 Ala-rich.
MOD_RES 921 921 Phosphotyrosine.
{ECO:0000269|PubMed:15316024}.
VARIANT 20 20 A -> V (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_038042.
VARIANT 34 34 L -> F (in dbSNP:rs1801162).
/FTId=VAR_051078.
VARIANT 215 215 G -> E (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_038043.
VARIANT 508 508 N -> K (in dbSNP:rs34287560).
/FTId=VAR_051079.
VARIANT 557 557 G -> R (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_038044.
VARIANT 879 879 H -> D (in dbSNP:rs1801164).
/FTId=VAR_051080.
VARIANT 1230 1230 D -> Y (in dbSNP:rs28546943).
/FTId=VAR_061669.
MUTAGEN 700 700 Y->F: No effect. Reduces interaction with
CRK by 50%; when associated with F-717.
Abolishes interaction with CRK; when
associated with F-717; F-743 and F-779.
{ECO:0000269|PubMed:11316748}.
MUTAGEN 717 717 Y->F: No effect. Reduces interaction with
CRK by 50%; when associated with F-700.
Abolishes interaction with CRK; when
associated with F-700; F-743 and F-779.
{ECO:0000269|PubMed:11316748}.
MUTAGEN 743 743 Y->F: No effect. Reduces interaction with
CRK by 50%; when associated with F-779.
Abolishes interaction with CRK; when
associated with F-700; F-717 and F-779.
{ECO:0000269|PubMed:11316748}.
MUTAGEN 779 779 Y->F: No effect. Reduces interaction with
CRK by 50%; when associated with F-743.
Abolishes interaction with CRK; when
associated with F-700; F-717 and F-743.
{ECO:0000269|PubMed:11316748}.
SEQUENCE 1257 AA; 133768 MW; 4D512D65A7A80374 CRC64;
MASCSFTRDQ ATRRLRGAAA AAAAALAAVV TTPLLSSGTP TALIGTGSSC PGAMWLSTAT
GSRSDSESEE EDLPVGEEVC KRGYLRKQKH GHRRYFVLKL ETADAPARLE YYENARKFRH
SVRAAAAAAA AAASGAAIPP LIPPRRVITL YQCFSVSQRA DARYRHLIAL FTQDEYFAMV
AENESEQESW YLLLSRLILE SKRRRCGTLG AQPDGEPAAL AAAAAAEPPF YKDVWQVIVK
PRGLGHRKEL SGVFRLCLTD EEVVFVRLNT EVASVVVQLL SIRRCGHSEQ YFFLEVGRST
VIGPGELWMQ VDDCVVAQNM HELFLEKMRA LCADEYRARC RSYSISIGAH LLTLLSARRH
LGLVPLEPGG WLRRSRFEQF CHLRAIGDGE DEMLFTRRFV TPSEPVAHSR RGRLHLPRGR
RSRRAVSVPA SFFRRLAPSP ARPRHPAEAP NNGARLSSEV SGSGSGNFGE EGNPQGKEDQ
EGSGGDYMPM NNWGSGNGRG SGGGQGSNGQ GSSSHSSGGN QCSGEGQGSR GGQGSNGQGS
GGNQCSRDGQ GTAGGHGSGG GQRPGGGHGS GGGQGPGDGH GSGGGKNSGG GKGSGSGKGS
DGDGERGKSL KKRSYFGKLT QSKQQQMPPP PPPPPPPPPA GGTGGKGKSG GRFRLYFCVD
RGATKECKEA KEVKDAEIPE GAARGPHRAR AFDEDEDDPY VPMRPGVATP LVSSSDYMPM
APQNVSASKK RHSRSPFEDS RGYMMMFPRV SPPPAPSPPK APDTNKEDDS KDNDSESDYM
FMAPGAGAIP KNPRNPQGGS SSKSWSSYFS LPNPFRSSPL GQNDNSEYVP MLPGKFLGRG
LDKEVSYNWD PKDAASKPSG EGSFSKPGDG GSPSKPSDHE PPKNKAKRPN RLSFITKGYK
IKPKPQKPTH EQREADSSSD YVNMDFTKRE SNTPAPSTQG LPDSWGIIAE PRQSAFSNYV
NVEFGVPFPN PANDLSDLLR AIPRANPLSL DSARWPLPPL PLSATGSNAI EEEGDYIEVI
FNSAMTPAMA LADSAIRYDA ETGRIYVVDP FSECCMDISL SPSRCSEPPP VARLLQEEEQ
ERRRPQSRSQ SFFAAARAAV SAFPTDSLER DLSPSSAPAV ASAAEPTLAL SQVVAAASAL
AAAPGIGAAA AAAGFDSASA RWFQPVANAA DAEAVRGAQD VAGGSNPGAH NPSANLARGD
NQAGGAAAAA AAPEPPPRSR RVPRPPERED SDNDDDTHVR MDFARRDNQF DSPKRGR


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E02I0403 Rat Insulin receptor substrate 1 ELISA 96T/kit
E02I0406 Rat Insulin receptor substrate 2 ELISA 96T/kit
YHB0581Ra Rat Insulin receptor substrate 1,IRS-1 ELISA Kit 96T
YHB0581Ra Rat Insulin receptor substrate 1,IRS-1 ELISA Kit 48T
EH822 Insulin receptor substrate 2 Elisa Kit 96T
E0919Ra Rat Insulin receptor substrate 1,IRS-1 ELISA Kit 96T
201-20-7104 IRS P53{Insulin receptor substrate P53}rabbit.pAb 0.2ml
E13I0406 Anserine Insulin receptor substrate 2 96 Tests/kit
3521P IRS-1 _ Insulin receptor substrate-1 Peptide 0.05 mg
E05I0406 Guinea Insulin receptor substrate 2 96 Tests/kit
E0918Ra Rat Insulin receptor substrate 1,IRS-1 ELISA Kit 48T
E02I0403 Rat Insulin receptor substrate 1 ELISA, IRS-1
CSB-E14318r Rat insulin receptor substrate-1(IRS-1) ELISA Kit 96T
E07I0406 Porcine Insulin receptor substrate 2 96 Tests/kit
E03I0406 Mouse Insulin receptor substrate 2 96 Tests/kit
E06I0406 Goat Insulin receptor substrate 2 96 Tests/kit
E02I0406 Rat Insulin receptor substrate 2 ELISA, IRS-2


 

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