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Signal transducing adapter molecule 2 (STAM-2) (Hrs-binding protein)

 STAM2_HUMAN             Reviewed;         525 AA.
O75886; A8K8A0; D3DPA1; Q7LDQ0; Q9UF58;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
20-JUN-2018, entry version 174.
RecName: Full=Signal transducing adapter molecule 2;
Short=STAM-2;
AltName: Full=Hrs-binding protein;
Name=STAM2; Synonyms=HBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
INTERACTION WITH JAK2 AND JAK3.
TISSUE=Fetal brain;
PubMed=10899310; DOI=10.1016/S0014-5793(00)01760-9;
Endo K., Takeshita T., Kasai H., Sasaki Y., Tanaka N., Asao H.,
Kikuchi K., Yamada M., Chenb M., O'Shea J.J., Sugamura K.;
"STAM2, a new member of the STAM family, binding to the Janus
kinases.";
FEBS Lett. 477:55-61(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
INTERACTION WITH HGS AND UBIQUITIN, IDENTIFICATION IN A COMPLEX WITH
HSG AND EPS15, AND SUBCELLULAR LOCATION.
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[9]
INTERACTION WITH CBX5.
PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
"The mammalian heterochromatin protein 1 binds diverse nuclear
proteins through a common motif that targets the chromoshadow
domain.";
Biochem. Biophys. Res. Commun. 331:929-937(2005).
[10]
INTERACTION WITH VPS37C.
PubMed=15509564; DOI=10.1074/jbc.M410384200;
Eastman S.W., Martin-Serrano J., Chung W., Zang T., Bieniasz P.D.;
"Identification of human VPS37C, a component of endosomal sorting
complex required for transport-I important for viral budding.";
J. Biol. Chem. 280:628-636(2005).
[11]
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).
[12]
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).
[13]
STRUCTURE BY NMR OF 1-269.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the VHS and SH3 domains of human signal
transducing adaptor molecule 2.";
Submitted (NOV-2005) to the PDB data bank.
-!- 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 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or
STAM2 and HGS. Part of a complex at least composed of HSG, STAM2
and EPS15. Interacts with JAK2 and JAK3. Interacts with
ubiquitinated proteins and the deubiquitinating enzyme USP8/UBPY
(By similarity). Interacts (via the via the PxVxL motif) with
CBX5; the interaction is direct. Interacts with VPS37C. Interacts
with ubiquitin; the interaction is direct. Interacts (via UIM
domain) with UBQLN1 (via ubiquitin-like domain) (By similarity).
{ECO:0000250|UniProtKB:O88811, ECO:0000269|PubMed:10899310,
ECO:0000269|PubMed:12551915, ECO:0000269|PubMed:15509564,
ECO:0000269|PubMed:15882967}.
-!- INTERACTION:
Q8WU02:-; NbExp=3; IntAct=EBI-373258, EBI-747182;
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-373258, EBI-743598;
Q96B67:ARRDC3; NbExp=5; IntAct=EBI-373258, EBI-2875665;
Q15038:DAZAP2; NbExp=6; IntAct=EBI-373258, EBI-724310;
Q9P2K6:KLHL42; NbExp=5; IntAct=EBI-373258, EBI-739890;
Q969R5:L3MBTL2; NbExp=3; IntAct=EBI-373258, EBI-739909;
Q13094:LCP2; NbExp=8; IntAct=EBI-373258, EBI-346946;
Q99732:LITAF; NbExp=9; IntAct=EBI-373258, EBI-725647;
Q96CS7:PLEKHB2; NbExp=5; IntAct=EBI-373258, EBI-373552;
Q13671:RIN1; NbExp=4; IntAct=EBI-373258, EBI-366017;
Q9H788:SH2D4A; NbExp=3; IntAct=EBI-373258, EBI-747035;
Q9H788-2:SH2D4A; NbExp=3; IntAct=EBI-373258, EBI-10308083;
O95630:STAMBP; NbExp=4; IntAct=EBI-373258, EBI-396676;
O60220:TIMM8A; NbExp=8; IntAct=EBI-373258, EBI-1049822;
Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-373258, EBI-741480;
A5D8V6:VPS37C; NbExp=5; IntAct=EBI-373258, EBI-2559305;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
membrane {ECO:0000269|PubMed:12551915}; Peripheral membrane
protein {ECO:0000269|PubMed:12551915}; Cytoplasmic side
{ECO:0000269|PubMed:12551915}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=STAM2A;
IsoId=O75886-1; Sequence=Displayed;
Name=2; Synonyms=STAM2B;
IsoId=O75886-2; Sequence=VSP_014848;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10899310}.
-!- DOMAIN: The VHS and UIM domains mediate the interaction with
ubiquitinated proteins.
-!- DOMAIN: The SH3 domain mediates the interaction with USP8.
-!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
required for interaction with chromoshadow domains. This motif
requires additional residues -7, -6, +4 and +5 of the central Val
which contact the chromoshadow domain.
-!- PTM: Phosphorylated in response to IL-2, GM-CSF, EGF and PDGF.
-!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
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EMBL; AF042273; AAC63963.1; -; mRNA.
EMBL; AF042274; AAC63964.1; -; mRNA.
EMBL; AL133600; CAB63735.1; -; mRNA.
EMBL; AK292265; BAF84954.1; -; mRNA.
EMBL; AK292847; BAF85536.1; -; mRNA.
EMBL; AC079790; AAY14712.1; -; Genomic_DNA.
EMBL; CH471058; EAX11490.1; -; Genomic_DNA.
EMBL; CH471058; EAX11492.1; -; Genomic_DNA.
EMBL; BC028740; AAH28740.1; -; mRNA.
CCDS; CCDS2196.1; -. [O75886-1]
PIR; T43437; T43437.
RefSeq; NP_005834.4; NM_005843.5. [O75886-1]
UniGene; Hs.17200; -.
PDB; 1X2Q; NMR; -; A=195-269.
PDB; 1X5B; NMR; -; A=1-150.
PDB; 2L0T; NMR; -; B=1-150.
PDB; 5CRV; X-ray; 2.00 A; C/D=350-370.
PDB; 5IXF; NMR; -; A=162-265.
PDBsum; 1X2Q; -.
PDBsum; 1X5B; -.
PDBsum; 2L0T; -.
PDBsum; 5CRV; -.
PDBsum; 5IXF; -.
ProteinModelPortal; O75886; -.
SMR; O75886; -.
BioGrid; 115548; 64.
CORUM; O75886; -.
IntAct; O75886; 41.
MINT; O75886; -.
STRING; 9606.ENSP00000263904; -.
iPTMnet; O75886; -.
PhosphoSitePlus; O75886; -.
BioMuta; STAM2; -.
EPD; O75886; -.
MaxQB; O75886; -.
PaxDb; O75886; -.
PeptideAtlas; O75886; -.
PRIDE; O75886; -.
ProteomicsDB; 50243; -.
ProteomicsDB; 50244; -. [O75886-2]
DNASU; 10254; -.
Ensembl; ENST00000263904; ENSP00000263904; ENSG00000115145. [O75886-1]
GeneID; 10254; -.
KEGG; hsa:10254; -.
UCSC; uc002tyc.4; human. [O75886-1]
CTD; 10254; -.
DisGeNET; 10254; -.
EuPathDB; HostDB:ENSG00000115145.9; -.
GeneCards; STAM2; -.
HGNC; HGNC:11358; STAM2.
HPA; HPA035528; -.
HPA; HPA035529; -.
MIM; 606244; gene.
neXtProt; NX_O75886; -.
OpenTargets; ENSG00000115145; -.
PharmGKB; PA36180; -.
eggNOG; KOG2199; Eukaryota.
eggNOG; ENOG410XTSY; LUCA.
GeneTree; ENSGT00920000149088; -.
HOGENOM; HOG000231952; -.
HOVERGEN; HBG053175; -.
InParanoid; O75886; -.
KO; K04705; -.
OMA; HGGNYMG; -.
OrthoDB; EOG091G0H1Y; -.
PhylomeDB; O75886; -.
TreeFam; TF315007; -.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
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).
SIGNOR; O75886; -.
ChiTaRS; STAM2; human.
EvolutionaryTrace; O75886; -.
GeneWiki; STAM2; -.
GenomeRNAi; 10254; -.
PRO; PR:O75886; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115145; -.
CleanEx; HS_STAM2; -.
Genevisible; O75886; HS.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0033565; C:ESCRT-0 complex; TAS:ParkinsonsUK-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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.
CDD; cd11963; SH3_STAM2; 1.
Gene3D; 1.25.40.90; -; 1.
InterPro; IPR008942; ENTH_VHS.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035675; STAM2_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; SM00726; UIM; 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;
Endosome; Membrane; Phosphoprotein; Protein transport;
Reference proteome; SH3 domain; Transport.
CHAIN 1 525 Signal transducing adapter molecule 2.
/FTId=PRO_0000190147.
DOMAIN 16 144 VHS. {ECO:0000255|PROSITE-
ProRule:PRU00218}.
DOMAIN 165 184 UIM. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 202 261 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 360 377 ITAM.
REGION 219 220 Interaction with USP8. {ECO:0000250}.
REGION 334 368 Interaction with HGS. {ECO:0000250}.
MOTIF 54 67 PxVxL motif.
VAR_SEQ 343 525 Missing (in isoform 2).
{ECO:0000303|PubMed:10899310}.
/FTId=VSP_014848.
CONFLICT 81 83 HLE -> RLG (in Ref. 2; CAB63735).
{ECO:0000305}.
CONFLICT 254 254 N -> D (in Ref. 2; CAB63735).
{ECO:0000305}.
CONFLICT 266 266 A -> V (in Ref. 2; CAB63735).
{ECO:0000305}.
HELIX 10 16 {ECO:0000244|PDB:1X5B}.
HELIX 26 38 {ECO:0000244|PDB:1X5B}.
STRAND 39 41 {ECO:0000244|PDB:1X5B}.
HELIX 42 54 {ECO:0000244|PDB:1X5B}.
HELIX 59 75 {ECO:0000244|PDB:1X5B}.
HELIX 78 84 {ECO:0000244|PDB:1X5B}.
HELIX 87 98 {ECO:0000244|PDB:1X5B}.
HELIX 103 119 {ECO:0000244|PDB:1X5B}.
TURN 120 122 {ECO:0000244|PDB:1X5B}.
TURN 124 126 {ECO:0000244|PDB:2L0T}.
HELIX 127 137 {ECO:0000244|PDB:1X5B}.
TURN 138 140 {ECO:0000244|PDB:1X5B}.
STRAND 199 201 {ECO:0000244|PDB:5IXF}.
STRAND 205 211 {ECO:0000244|PDB:1X2Q}.
STRAND 217 219 {ECO:0000244|PDB:1X2Q}.
STRAND 228 233 {ECO:0000244|PDB:1X2Q}.
STRAND 237 244 {ECO:0000244|PDB:1X2Q}.
STRAND 247 251 {ECO:0000244|PDB:1X2Q}.
HELIX 253 255 {ECO:0000244|PDB:1X2Q}.
STRAND 256 258 {ECO:0000244|PDB:1X2Q}.
HELIX 352 357 {ECO:0000244|PDB:5CRV}.
HELIX 359 365 {ECO:0000244|PDB:5CRV}.
SEQUENCE 525 AA; 58164 MW; 408D484544DD9403 CRC64;
MPLFTANPFE QDVEKATNEY NTTEDWSLIM DICDKVGSTP NGAKDCLKAI MKRVNHKVPH
VALQALTLLG ACVANCGKIF HLEVCSRDFA TEVRAVIKNK AHPKVCEKLK SLMVEWSEEF
QKDPQFSLIS ATIKSMKEEG ITFPPAGSQT VSAAAKNGTS SNKNKEDEDI AKAIELSLQE
QKQQHTETKS LYPSSEIQLN NKVARKVRAL YDFEAVEDNE LTFKHGEIII VLDDSDANWW
KGENHRGIGL FPSNFVTTNL NIETEAAAVD KLNVIDDDVE EIKKSEPEPV YIDEDKMDRA
LQVLQSIDPT DSKPDSQDLL DLEDICQQMG PMIDEKLEEI DRKHSELSEL NVKVLEALEL
YNKLVNEAPV YSVYSKLHPP AHYPPASSGV PMQTYPVQSH GGNYMGQSIH QVTVAQSYSL
GPDQIGPLRS LPPNVNSSVT AQPAQTSYLS TGQDTVSNPT YMNQNSNLQS ATGTTAYTQQ
MGMSVDMSSY QNTTSNLPQL AGFPVTVPAH PVAQQHTNYH QQPLL


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EIAAB40216 HBP,Homo sapiens,Hrs-binding protein,Human,Signal transducing adapter molecule 2,STAM2,STAM-2
EIAAB40212 Mouse,Mus musculus,Signal transducing adapter molecule 1,Stam,Stam1,STAM-1
EIAAB40213 Homo sapiens,Human,Signal transducing adapter molecule 1,STAM,STAM1,STAM-1
CSB-EL022792HU Human Signal transducing adapter molecule 1(STAM) ELISA kit 96T
H0946 Signal transducing adapter molecule 1 (STAM), Mouse, ELISA Kit 96T
CSB-EL022792MO Mouse Signal transducing adapter molecule 1(STAM) ELISA kit 96T
H0945 Signal transducing adapter molecule 1 (STAM), Human, ELISA Kit 96T
CSB-EL022792MO Mouse Signal transducing adapter molecule 1(STAM) ELISA kit SpeciesMouse 96T
EIAAB40217 Rat,Rattus norvegicus,Signal transducing adapter molecule 2,Stam2,STAM-2
CSB-EL022792HU Human Signal transducing adapter molecule 1(STAM) ELISA kit SpeciesHuman 96T
STAM1_MOUSE ELISA Kit FOR Signal transducing adapter molecule 1; organism: Mouse; gene name: Stam 96T
EIAAB40214 Chicken,EAST,Epidermal growth factor receptor-associated protein with SH3 and TAM domain,Gallus gallus,Signal transducing adapter molecule 2,STAM2,STAM-2
STAM STAM Gene signal transducing adaptor molecule (SH3 domain and ITAM motif) 1
201-20-5617 STAM{signal transducing adaptor molecule (SH3 domain and ITAM motif) 1}rabbit.pAb 0.2ml
CSB-EL022793RA Rat Signal transducing adapter molecule 2(STAM2) ELISA kit 96T
E1833h Mouse ELISA Kit FOR Signal transducing adapter molecule 2 96T
H0950 Signal transducing adapter molecule 2 (STAM2), Rat, ELISA Kit 96T
H0949 Signal transducing adapter molecule 2 (STAM2), Mouse, ELISA Kit 96T
H0948 Signal transducing adapter molecule 2 (STAM2), Human, 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-EL022793CH Chicken Signal transducing adapter molecule 2(STAM2) ELISA kit 96T
CSB-EL022793MO Mouse Signal transducing adapter molecule 2(STAM2) ELISA kit 96T


 

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