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Signal transducing adapter molecule 1 (STAM-1)

 STAM1_HUMAN             Reviewed;         540 AA.
Q92783; B0YJ99; D3DRU5; Q8N6D9;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 166.
RecName: Full=Signal transducing adapter molecule 1;
Short=STAM-1;
Name=STAM; Synonyms=STAM1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-15;
110-119; 137-154; 215-223; 233-247 AND 364-373, AND TISSUE
SPECIFICITY.
TISSUE=T-cell;
PubMed=8780729; DOI=10.1006/bbrc.1996.1290;
Takeshita T., Arita T., Asao H., Tanaka N., Higuchi M., Kuroda H.,
Kaneko K., Munakata H., Endo Y., Fujita T., Sugamura K.;
"Cloning of a novel signal-transducing adaptor molecule containing an
SH3 domain and ITAM.";
Biochem. Biophys. Res. Commun. 225:1035-1039(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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).
[5]
PROTEIN SEQUENCE OF 189-213, INTERACTION WITH HGS, CLEAVAGE OF
INITIATOR METHIONINE, PHOSPHORYLATION AT TYR-198, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=11687594; DOI=10.1074/jbc.M109992200;
Steen H., Kuster B., Fernandez M., Pandey A., Mann M.;
"Tyrosine phosphorylation mapping of the epidermal growth factor
receptor signaling pathway.";
J. Biol. Chem. 277:1031-1039(2002).
[6]
INTERACTION WITH HGS.
PubMed=9407053; DOI=10.1074/jbc.272.52.32785;
Asao H., Sasaki Y., Arita T., Tanaka N., Endo K., Kasai H.,
Takeshita T., Endo Y., Fujita T., Sugamura K.;
"Hrs is associated with STAM, a signal-transducing adaptor molecule.
Its suppressive effect on cytokine-induced cell growth.";
J. Biol. Chem. 272:32785-32791(1997).
[7]
INTERACTION WITH STAMBP.
PubMed=10383417; DOI=10.1074/jbc.274.27.19129;
Tanaka N., Kaneko K., Asao H., Kasai H., Endo Y., Fujita T.,
Takeshita T., Sugamura K.;
"Possible involvement of a novel STAM-associated molecule 'AMSH' in
intracellular signal transduction mediated by cytokines.";
J. Biol. Chem. 274:19129-19135(1999).
[8]
INTERACTION WITH HGS, AND IDENTIFICATION IN A COMPLEX WITH HGS AND
EPS15.
PubMed=12551915; DOI=10.1074/jbc.M210843200;
Bache K.G., Raiborg C., Mehlum A., Stenmark H.;
"STAM and Hrs are subunits of a multivalent ubiquitin-binding complex
on early endosomes.";
J. Biol. Chem. 278:12513-12521(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
INTERACTION WITH PDGFRB, AND PHOSPHORYLATION AT TYR-381 AND TYR-384.
PubMed=20494825; DOI=10.1016/j.cellsig.2010.05.004;
Wardega P., Heldin C.H., Lennartsson J.;
"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects
cell proliferation but not migration.";
Cell. Signal. 22:1363-1368(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
INTERACTION WITH LITAF, IDENTIFICATION IN A COMPLEX WITH HGS AND
LITAF, AND SUBCELLULAR LOCATION.
PubMed=23166352; DOI=10.1083/jcb.201204137;
Lee S.M., Chin L.S., Li L.;
"Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the
ESCRT machinery in endosomal trafficking.";
J. Cell Biol. 199:799-816(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
INTERACTION WITH DTX3L, IDENTIFICATION IN A COMPLEX WITH DTX3L; HGS
AND ITCH, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=24790097; DOI=10.1091/mbc.E13-10-0612;
Holleman J., Marchese A.;
"The ubiquitin ligase deltex-3l regulates endosomal sorting of the G
protein-coupled receptor CXCR4.";
Mol. Biol. Cell 25:1892-1904(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-276, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[18]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 301-377 IN COMPLEX WITH
STAM, SUBUNIT, AND INTERACTION WITH STAM.
PubMed=19278655; DOI=10.1016/j.str.2009.01.012;
Ren X., Kloer D.P., Kim Y.C., Ghirlando R., Saidi L.F., Hummer G.,
Hurley J.H.;
"Hybrid structural model of the complete human ESCRT-0 complex.";
Structure 17:406-416(2009).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 4-143 IN COMPLEX WITH
UBIQUITIN, DOMAIN VHS, AND SUBUNIT.
PubMed=20150893; DOI=10.1038/emboj.2010.6;
Ren X., Hurley J.H.;
"VHS domains of ESCRT-0 cooperate in high-avidity binding to
polyubiquitinated cargo.";
EMBO J. 29:1045-1054(2010).
[20]
VARIANT [LARGE SCALE ANALYSIS] ASP-212.
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: Involved in intracellular signal transduction mediated
by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation,
it plays a role in signaling leading to DNA synthesis and MYC
induction. May also play a role in T-cell development. Involved in
down-regulation of receptor tyrosine kinase via multivesicular
body (MVBs) when complexed with HGS (ESCRT-0 complex). The ESCRT-0
complex binds ubiquitin and acts as sorting machinery that
recognizes ubiquitinated receptors and transfers them to further
sequential lysosomal sorting/trafficking processes.
-!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or
STAM2 and HGS (PubMed:11687594, PubMed:9407053, PubMed:19278655).
Probably part of a complex at least composed of HSG, STAM and
EPS15 (PubMed:12551915). Found in a complex with HGS and E3 ligase
ITCH and DTX3L (PubMed:24790097). Interacts with E3 ligase DTX3L;
the interaction brings together STAM and HSG, promotes their
recruitment to early endosomes and decreases STAM and HGS
ubiquitination by ITCH (PubMed:24790097). Interacts with
STAMBP/AMSH (PubMed:10383417). Interacts with PDGFRB
(PubMed:20494825). Interacts with LITAF; the interaction is direct
(PubMed:23166352). Identified in a complex with HGS and LITAF
(PubMed:23166352). {ECO:0000269|PubMed:10383417,
ECO:0000269|PubMed:11687594, ECO:0000269|PubMed:12551915,
ECO:0000269|PubMed:19278655, ECO:0000269|PubMed:20150893,
ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:23166352,
ECO:0000269|PubMed:24790097, ECO:0000269|PubMed:9407053}.
-!- INTERACTION:
O14964:HGS; NbExp=5; IntAct=EBI-15763634, EBI-740220;
Q99LI8:Hgs (xeno); NbExp=4; IntAct=EBI-15763634, EBI-2119135;
Q13094:LCP2; NbExp=3; IntAct=EBI-752333, EBI-346946;
O95630:STAMBP; NbExp=7; IntAct=EBI-752333, EBI-396676;
P0CG53:UBB (xeno); NbExp=9; IntAct=EBI-752333, EBI-5333021;
P0CG48:UBC; NbExp=6; IntAct=EBI-752333, EBI-3390054;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Early endosome
membrane {ECO:0000269|PubMed:23166352,
ECO:0000269|PubMed:24790097}; Peripheral membrane protein
{ECO:0000305|PubMed:23166352, ECO:0000305|PubMed:24790097};
Cytoplasmic side {ECO:0000305|PubMed:23166352,
ECO:0000305|PubMed:24790097}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92783-1; Sequence=Displayed;
Name=2;
IsoId=Q92783-2; Sequence=VSP_014846, VSP_014847;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:8780729}.
-!- DOMAIN: The VHS domain mediates high-avidity binding to Lys63-
linked and Lys48-linked polyubiquitinated cargos.
{ECO:0000269|PubMed:20150893}.
-!- PTM: Phosphorylated on Tyr-198. Phosphorylated in response to IL2,
IL3, IL4, IL7, CSF2/GM-CSF, EGF and PDGFB. Phosphorylated by
activated PDGFRB. {ECO:0000269|PubMed:11687594,
ECO:0000269|PubMed:20494825}.
-!- PTM: Ubiquitinated by ITCH. {ECO:0000269|PubMed:24790097}.
-!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
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EMBL; U43899; AAC50734.1; -; mRNA.
EMBL; EF445033; ACA06077.1; -; Genomic_DNA.
EMBL; EF445033; ACA06078.1; -; Genomic_DNA.
EMBL; CH471072; EAW86207.1; -; Genomic_DNA.
EMBL; CH471072; EAW86209.1; -; Genomic_DNA.
EMBL; BC030586; AAH30586.1; -; mRNA.
CCDS; CCDS7122.1; -. [Q92783-1]
PIR; JC4916; JC4916.
RefSeq; NP_003464.1; NM_003473.3. [Q92783-1]
UniGene; Hs.335391; -.
PDB; 2L0A; NMR; -; A=207-267.
PDB; 3F1I; X-ray; 2.30 A; C/S=301-377.
PDB; 3LDZ; X-ray; 2.60 A; A/B/C/D=4-143.
PDBsum; 2L0A; -.
PDBsum; 3F1I; -.
PDBsum; 3LDZ; -.
ProteinModelPortal; Q92783; -.
SMR; Q92783; -.
BioGrid; 113722; 69.
CORUM; Q92783; -.
DIP; DIP-37761N; -.
IntAct; Q92783; 17.
MINT; Q92783; -.
STRING; 9606.ENSP00000366746; -.
iPTMnet; Q92783; -.
PhosphoSitePlus; Q92783; -.
SwissPalm; Q92783; -.
BioMuta; STAM; -.
DMDM; 71153545; -.
EPD; Q92783; -.
MaxQB; Q92783; -.
PaxDb; Q92783; -.
PeptideAtlas; Q92783; -.
PRIDE; Q92783; -.
Ensembl; ENST00000377524; ENSP00000366746; ENSG00000136738. [Q92783-1]
GeneID; 8027; -.
KEGG; hsa:8027; -.
UCSC; uc001ipj.3; human. [Q92783-1]
CTD; 8027; -.
DisGeNET; 8027; -.
EuPathDB; HostDB:ENSG00000136738.14; -.
GeneCards; STAM; -.
HGNC; HGNC:11357; STAM.
HPA; CAB034399; -.
HPA; HPA043882; -.
MIM; 601899; gene.
neXtProt; NX_Q92783; -.
OpenTargets; ENSG00000136738; -.
PharmGKB; PA36179; -.
eggNOG; KOG2199; Eukaryota.
eggNOG; ENOG410XTSY; LUCA.
GeneTree; ENSGT00870000136415; -.
HOGENOM; HOG000231952; -.
HOVERGEN; HBG053175; -.
InParanoid; Q92783; -.
KO; K04705; -.
OMA; GIMEQAY; -.
OrthoDB; EOG091G0H1Y; -.
PhylomeDB; Q92783; -.
TreeFam; TF315007; -.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
SignaLink; Q92783; -.
SIGNOR; Q92783; -.
ChiTaRS; STAM; human.
EvolutionaryTrace; Q92783; -.
GeneWiki; Signal_transducing_adaptor_molecule; -.
GenomeRNAi; 8027; -.
PRO; PR:Q92783; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000136738; -.
CleanEx; HS_STAM; -.
ExpressionAtlas; Q92783; baseline and differential.
Genevisible; Q92783; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0033565; C:ESCRT-0 complex; IDA:UniProtKB.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:1903551; P:regulation of extracellular exosome assembly; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd11964; SH3_STAM1; 1.
Gene3D; 1.25.40.90; -; 1.
InterPro; IPR008942; ENTH_VHS.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035657; STAM1_SH3.
InterPro; IPR003903; UIM_dom.
InterPro; IPR002014; VHS_dom.
Pfam; PF00018; SH3_1; 1.
Pfam; PF02809; UIM; 1.
Pfam; PF00790; VHS; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SMART; SM00288; VHS; 1.
SUPFAM; SSF48464; SSF48464; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS50330; UIM; 1.
PROSITE; PS50179; VHS; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Endosome; Isopeptide bond; Membrane;
Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
SH3 domain; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11687594,
ECO:0000269|PubMed:8780729}.
CHAIN 2 540 Signal transducing adapter molecule 1.
/FTId=PRO_0000190145.
DOMAIN 16 143 VHS. {ECO:0000255|PROSITE-
ProRule:PRU00218}.
DOMAIN 171 190 UIM. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 210 269 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 370 387 ITAM.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 198 198 Phosphotyrosine.
{ECO:0000269|PubMed:11687594}.
MOD_RES 381 381 Phosphotyrosine.
{ECO:0000269|PubMed:20494825}.
MOD_RES 384 384 Phosphotyrosine.
{ECO:0000269|PubMed:20494825}.
CROSSLNK 276 276 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 392 403 YYMQSSGVSGSQ -> GSGPTIRKPSPS (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_014846.
VAR_SEQ 404 540 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014847.
VARIANT 212 212 G -> D (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036348.
CONFLICT 267 267 D -> Y (in Ref. 4; AAH30586).
{ECO:0000305}.
HELIX 10 16 {ECO:0000244|PDB:3LDZ}.
STRAND 21 23 {ECO:0000244|PDB:3LDZ}.
HELIX 26 36 {ECO:0000244|PDB:3LDZ}.
HELIX 42 54 {ECO:0000244|PDB:3LDZ}.
HELIX 59 75 {ECO:0000244|PDB:3LDZ}.
HELIX 78 84 {ECO:0000244|PDB:3LDZ}.
HELIX 87 99 {ECO:0000244|PDB:3LDZ}.
HELIX 102 119 {ECO:0000244|PDB:3LDZ}.
HELIX 123 125 {ECO:0000244|PDB:3LDZ}.
HELIX 127 137 {ECO:0000244|PDB:3LDZ}.
STRAND 213 219 {ECO:0000244|PDB:2L0A}.
STRAND 236 244 {ECO:0000244|PDB:2L0A}.
STRAND 247 251 {ECO:0000244|PDB:2L0A}.
STRAND 256 258 {ECO:0000244|PDB:2L0A}.
STRAND 264 266 {ECO:0000244|PDB:2L0A}.
HELIX 304 315 {ECO:0000244|PDB:3F1I}.
HELIX 327 375 {ECO:0000244|PDB:3F1I}.
SEQUENCE 540 AA; 59180 MW; 8D6F07FAE538F36F CRC64;
MPLFATNPFD QDVEKATSEM NTAEDWGLIL DICDKVGQSR TGPKDCLRSI MRRVNHKDPH
VAMQALTLLG ACVSNCGKIF HLEVCSRDFA SEVSNVLNKG HPKVCEKLKA LMVEWTDEFK
NDPQLSLISA MIKNLKEQGV TFPAIGSQAA EQAKASPALV AKDPGTVANK KEEEDLAKAI
ELSLKEQRQQ STTLSTLYPS TSSLLTNHQH EGRKVRAIYD FEAAEDNELT FKAGEIITVL
DDSDPNWWKG ETHQGIGLFP SNFVTADLTA EPEMIKTEKK TVQFSDDVQV ETIEPEPEPA
FIDEDKMDQL LQMLQSTDPS DDQPDLPELL HLEAMCHQMG PLIDEKLEDI DRKHSELSEL
NVKVMEALSL YTKLMNEDPM YSMYAKLQNQ PYYMQSSGVS GSQVYAGPPP SGAYLVAGNA
QMSHLQSYSL PPEQLSSLSQ AVVPPSANPA LPSQQTQAAY PNTMVSSVQG NTYPSQAPVY
SPPPAATAAA ATADVTLYQN AGPNMPQVPN YNLTSSTLPQ PGGSQQPPQP QQPYSQKALL


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E1833h Mouse ELISA Kit FOR Signal transducing adapter molecule 2 96T
H0950 Signal transducing adapter molecule 2 (STAM2), Rat, ELISA Kit 96T
CSB-EL022793RA Rat Signal transducing adapter molecule 2(STAM2) ELISA kit 96T
H0947 Signal transducing adapter molecule 2 (STAM2), Chicken, ELISA Kit 96T
CSB-EL022793HU Human Signal transducing adapter molecule 2(STAM2) ELISA kit 96T
CSB-EL022793RA Rat Signal transducing adapter molecule 2(STAM2) ELISA kit SpeciesRat 96T
CSB-EL022793MO Mouse Signal transducing adapter molecule 2(STAM2) ELISA kit 96T
H0949 Signal transducing adapter molecule 2 (STAM2), Mouse, ELISA Kit 96T
CSB-EL022793CH Chicken Signal transducing adapter molecule 2(STAM2) ELISA kit 96T
H0948 Signal transducing adapter molecule 2 (STAM2), Human, ELISA Kit 96T


 

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