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SH3 domain-containing kinase-binding protein 1 (CD2-binding protein 3) (CD2BP3) (Cbl-interacting protein of 85 kDa) (Human Src family kinase-binding protein 1) (HSB-1)

 SH3K1_HUMAN             Reviewed;         665 AA.
Q96B97; B7Z1D5; Q5JPT4; Q5JPT5; Q8IWX6; Q8IX98; Q96RN4; Q9NYR0;
23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
23-MAY-2003, sequence version 2.
05-JUL-2017, entry version 161.
RecName: Full=SH3 domain-containing kinase-binding protein 1;
AltName: Full=CD2-binding protein 3;
Short=CD2BP3;
AltName: Full=Cbl-interacting protein of 85 kDa;
AltName: Full=Human Src family kinase-binding protein 1;
Short=HSB-1;
Name=SH3KBP1; Synonyms=CIN85;
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), AND INTERACTION WITH CBL.
PubMed=10679202; DOI=10.1006/bbrc.2000.2147;
Take H., Watanabe S., Takeda K., Yu Z.-X., Iwata N., Kajigaya S.;
"Cloning and characterization of a novel adaptor protein, CIN85, that
interacts with c-Cbl.";
Biochem. Biophys. Res. Commun. 268:321-328(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=T-cell;
PubMed=12618476; DOI=10.1093/intimm/dxg032;
Tibaldi E.V., Reinherz E.L.;
"CD2BP3, CIN85 and the structurally related adaptor protein CMS bind
to the same CD2 cytoplasmic segment but elicit divergent functional
activities.";
Int. Immunol. 15:313-329(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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=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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adrenal cortex, and Uterus;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 262-665, AND VARIANT LEU-382.
PubMed=11474197;
Narita T., Amano F., Yoshizaki K., Nishimoto N., Nishimura T.,
Tajima T., Namiki H., Taniyama T.;
"Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in
situ hybridization.";
Cytogenet. Cell Genet. 93:133-134(2001).
[7]
INTERACTION WITH BLNK; CRK; BCAR1; PIK3R3; GRB2 AND SOS1, AND
SELF-ASSOCIATION.
PubMed=11071869; DOI=10.1006/bbrc.2000.3760;
Watanabe S., Take H., Takeda K., Yu Z.X., Iwata N., Kajigaya S.;
"Characterization of the CIN85 adaptor protein and identification of
components involved in CIN85 complexes.";
Biochem. Biophys. Res. Commun. 278:167-174(2000).
[8]
INTERACTION WITH CBLB AND ENDOPHILINS, LACK OF INTERACTION WITH CBLC,
FUNCTION IN RECEPTOR INTERNALIZATION, AND SUBCELLULAR LOCATION.
PubMed=12177062; DOI=10.1074/jbc.M205535200;
Szymkiewicz I., Kowanetz K., Soubeyran P., Dinarina A., Lipkowitz S.,
Dikic I.;
"CIN85 participates in Cbl-b-mediated down-regulation of receptor
tyrosine kinases.";
J. Biol. Chem. 277:39666-39672(2002).
[9]
FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH EGFR; SH3GL1;
SH3GL2; SH3GL3 AND CBL, AND SUBCELLULAR LOCATION.
PubMed=11894095; DOI=10.1038/416183a;
Soubeyran P., Kowanetz K., Szymkiewicz I., Langdon W.Y., Dikic I.;
"Cbl-CIN85-endophilin complex mediates ligand-induced downregulation
of EGF receptors.";
Nature 416:183-187(2002).
[10]
FUNCTION IN RECEPTOR INTERNALIZATION, AND INTERACTION WITH SH3GL1;
SH3GL2; SH3GL3; CBL AND MET.
PubMed=11894096; DOI=10.1038/416187a;
Petrelli A., Gilestro G.F., Lanzardo S., Comoglio P.M., Migone N.,
Giordano S.;
"The endophilin-CIN85-Cbl complex mediates ligand-dependent
downregulation of c-Met.";
Nature 416:187-190(2002).
[11]
UBIQUITINATION BY CBL AND CBLB.
PubMed=12218189; DOI=10.1073/pnas.192462299;
Haglund K., Shimokawa N., Szymkiewicz I., Dikic I.;
"Cbl-directed monoubiquitination of CIN85 is involved in regulation of
ligand-induced degradation of EGF receptors.";
Proc. Natl. Acad. Sci. U.S.A. 99:12191-12196(2002).
[12]
INTERACTION WITH DAB2, AND IDENTIFICATION IN A COMPLEX WITH DAB2 AND
CLATHRIN.
PubMed=14596919; DOI=10.1016/S0014-5793(03)01111-6;
Kowanetz K., Terzic J., Dikic I.;
"Dab2 links CIN85 with clathrin-mediated receptor internalization.";
FEBS Lett. 554:81-87(2003).
[13]
FUNCTION IN CELL ADHESION, AND INTERACTION WITH PDCD6IP; PTK2/FAK1 AND
PTK2B/PYK2.
PubMed=12771190; DOI=10.1242/jcs.00522;
Schmidt M.H., Chen B., Randazzo L.M., Boegler O.;
"SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse
cytoskeletal elements, including FAKs, and modulate cell adhesion.";
J. Cell Sci. 116:2845-2855(2003).
[14]
INTERACTION WITH CD2 AND F-ACTIN CAPPING PROTEIN.
PubMed=12690097; DOI=10.1074/jbc.M302540200;
Hutchings N.J., Clarkson N., Chalkley R., Barclay A.N., Brown M.H.;
"Linking the T cell surface protein CD2 to the actin-capping protein
CAPZ via CMS and CIN85.";
J. Biol. Chem. 278:22396-22403(2003).
[15]
FUNCTION IN RECEPTOR INTERNALIZATION.
PubMed=12734385; DOI=10.1073/pnas.1031790100;
Schmidt M.H., Furnari F.B., Cavenee W.K., Bogler O.;
"Epidermal growth factor receptor signaling intensity determines
intracellular protein interactions, ubiquitination, and
internalization.";
Proc. Natl. Acad. Sci. U.S.A. 100:6505-6510(2003).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND 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).
[17]
FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH ASAP1; ARAP3;
HIP1R; SYNJ2; INPP5D; STAP1 AND EGFR, IDENTIFICATION IN A COMPLEX WITH
ASAP1 AND ARAP3, AND SUBCELLULAR LOCATION.
PubMed=15090612; DOI=10.1091/mbc.E03-09-0683;
Kowanetz K., Husnjak K., Holler D., Kowanetz M., Soubeyran P.,
Hirsch D., Schmidt M.H., Pavelic K., De Camilli P., Randazzo P.A.,
Dikic I.;
"CIN85 associates with multiple effectors controlling intracellular
trafficking of epidermal growth factor receptors.";
Mol. Biol. Cell 15:3155-3166(2004).
[18]
INTERACTION WITH PDCD6IP; EGFR; CBL AND CBLB.
PubMed=15456872; DOI=10.1128/MCB.24.20.8981-8993.2004;
Schmidt M.H., Hoeller D., Yu J., Furnari F.B., Cavenee W.K., Dikic I.,
Bogler O.;
"Alix/AIP1 antagonizes epidermal growth factor receptor downregulation
by the Cbl-SETA/CIN85 complex.";
Mol. Cell. Biol. 24:8981-8993(2004).
[19]
FUNCTION, AND INTERACTION WITH MAP3K4.
PubMed=16256071; DOI=10.1016/j.bbrc.2005.10.032;
Aissouni Y., Zapart G., Iovanna J.L., Dikic I., Soubeyran P.;
"CIN85 regulates the ability of MEKK4 to activate the p38 MAP kinase
pathway.";
Biochem. Biophys. Res. Commun. 338:808-814(2005).
[20]
INTERACTION WITH SPRY2.
PubMed=15962011; DOI=10.1038/sj.embor.7400453;
Haglund K., Schmidt M.H., Wong E.S., Guy G.R., Dikic I.;
"Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth
factor receptor downregulation.";
EMBO Rep. 6:635-641(2005).
[21]
FUNCTION IN APOPTOSIS, AND INTERACTION WITH SRC; LCK; LYN; FGR; FYN;
HCK; TRADD; BIRC2; TRAF1; TRAF2 AND TNFR1.
PubMed=15707590; DOI=10.1016/j.yexcr.2004.11.005;
Narita T., Nishimura T., Yoshizaki K., Taniyama T.;
"CIN85 associates with TNF receptor 1 via Src and modulates TNF-alpha-
induced apoptosis.";
Exp. Cell Res. 304:256-264(2005).
[22]
FUNCTION IN RECEPTOR INTERNALIZATION.
PubMed=16177060; DOI=10.4049/jimmunol.175.7.4208;
Molfetta R., Belleudi F., Peruzzi G., Morrone S., Leone L., Dikic I.,
Piccoli M., Frati L., Torrisi M.R., Santoni A., Paolini R.;
"CIN85 regulates the ligand-dependent endocytosis of the IgE receptor:
a new molecular mechanism to dampen mast cell function.";
J. Immunol. 175:4208-4216(2005).
[23]
INTERACTION WITH ARHGAP17.
PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
Starostine A., Metalnikov P., Pawson T.;
"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
proteins in epithelial cells.";
Cell 125:535-548(2006).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND 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).
[25]
INTERACTION WITH DDN AND MAGI2, AND SUBCELLULAR LOCATION.
PubMed=16751601; DOI=10.1093/jb/mvj105;
Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K.,
Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.;
"CIN85 is localized at synapses and forms a complex with S-SCAM via
dendrin.";
J. Biochem. 139:931-939(2006).
[26]
INTERACTION WITH MVB12A.
PubMed=16895919; DOI=10.1074/jbc.M605693200;
Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E.,
Taniguchi H.;
"CFBP is a novel tyrosine-phosphorylated protein that might function
as a regulator of CIN85/CD2AP.";
J. Biol. Chem. 281:28919-28931(2006).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-436; SER-509;
SER-511; SER-521 AND SER-587, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
INTERACTION WITH MAP3K4 AND ZFP36, AND SUBCELLULAR LOCATION.
PubMed=20221403; DOI=10.1371/journal.pone.0009588;
Kedar V.P., Darby M.K., Williams J.G., Blackshear P.J.;
"Phosphorylation of human tristetraprolin in response to its
interaction with the Cbl interacting protein CIN85.";
PLoS ONE 5:E9588-E9588(2010).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-436 AND
SER-587, 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).
[32]
FUNCTION.
PubMed=21834987; DOI=10.1186/1741-7007-9-54;
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
"Identification and characterization of a set of conserved and new
regulators of cytoskeletal organisation, cell morphology and
migration.";
BMC Biol. 9:54-54(2011).
[33]
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).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; THR-254; SER-436
AND SER-587, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-509 AND
SER-511, AND 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).
[37]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-58 IN COMPLEX WITH CBLB.
PubMed=16228008; DOI=10.1038/nsmb1000;
Jozic D., Cardenes N., Deribe Y.L., Moncalian G., Hoeller D.,
Groemping Y., Dikic I., Rittinger K., Bravo J.;
"Cbl promotes clustering of endocytic adaptor proteins.";
Nat. Struct. Mol. Biol. 12:972-979(2005).
-!- FUNCTION: Adapter protein involved in regulating diverse signal
transduction pathways. Involved in the regulation of endocytosis
and lysosomal degradation of ligand-induced receptor tyrosine
kinases, including EGFR and MET/hepatocyte growth factor receptor,
through a association with CBL and endophilins. The association
with CBL, and thus the receptor internalization, may inhibited by
an interaction with PDCD6IP and/or SPRY2. Involved in regulation
of ligand-dependent endocytosis of the IgE receptor. Attenuates
phosphatidylinositol 3-kinase activity by interaction with its
regulatory subunit (By similarity). May be involved in regulation
of cell adhesion; promotes the interaction between TTK2B and
PDCD6IP. May be involved in the regulation of cellular stress
response via the MAPK pathways through its interaction with
MAP3K4. Is involved in modulation of tumor necrosis factor
mediated apoptosis. Plays a role in the regulation of cell
morphology and cytoskeletal organization. Required in the control
of cell shape and migration. {ECO:0000250,
ECO:0000269|PubMed:11894095, ECO:0000269|PubMed:11894096,
ECO:0000269|PubMed:12177062, ECO:0000269|PubMed:12734385,
ECO:0000269|PubMed:12771190, ECO:0000269|PubMed:15090612,
ECO:0000269|PubMed:15707590, ECO:0000269|PubMed:16177060,
ECO:0000269|PubMed:16256071, ECO:0000269|PubMed:21834987}.
-!- SUBUNIT: Can self-associate and form homotetramers. Interacts with
CD2, F-actin capping protein, PIK3R3, GRB2, EGFR, MET, BLNK,
MAP3K4, PDCD6IP, SPRY2, ARHGAP17, ARHGAP27, MAGI2, CRK, BCAR1,
SOS1, ASAP1, ARAP3, HIP1R, SYNJ2, INPP5D and STAP1. Interacts with
CBL and CBLB, but does not interact with CBLC. Two molecules of
SH3KBP1 seem to bind through their respective SH3 1 domain to one
molecule of CBLB. The interaction with CBL or CBLB and EGFR is
increased upon EGF stimulation. The interaction with CBL is
attenuated by PDCD6IP. Interacts through its proline-rich region
with the SH3 domain of endophilins SH3GL1, SH3GL2 and SH3GL3. The
SH3KBP1-endophilin complex seems to associate with a complex
containing the phosphorylated receptor (EGFR or MET) and
phosphorylated CBL. Probably associates with ASAP1 and
phosphorylated EGFR. Probably part of a complex consisting of at
least SH3KBP1, ASAP1 and ARAP3. Interacts with focal adhesion
kinases PTK2/FAK1 AND PTK2B/PYK2, probably as a dimer. Interacts
with DAB2 and probably associates with chathrin through its
interaction with DAB2. Part of a complex consisting of SH3KBP1,
DAB2, and clathrin heavy chain. DAB2 and clathrin dissociate from
SH3KBP1 following growth factor treatment, enabling interaction
with CBL. Interacts with DDN and probably associates with MAGI2
through its interaction with DDN. Interacts with the SH3 domains
of SRC tyrosine-protein kinases SRC, LCK, LYN, FGR, FYN and HCK.
Interacts with TRADD, BIRC2, TRAF1, TRAF2 and TNFR1, and the
association with a TNFR1-associated complex upon stimulation with
TNF-alpha seems to be mediated by SRC. Interacts (via SH3 domains)
with SHKBP1 (via PXXXPR motifs) (By similarity). Interaction with
CBL is abolished in the presence of SHKBP1 (By similarity).
Interacts (via SH3 domains) with ZFP36 (via extreme C-terminal
region) (PubMed:20221403). Interacts with MAP3K4; this interaction
enhances the association with ZFP36 (PubMed:20221403).
{ECO:0000250|UniProtKB:Q8R550, ECO:0000269|PubMed:10679202,
ECO:0000269|PubMed:11071869, ECO:0000269|PubMed:11894095,
ECO:0000269|PubMed:11894096, ECO:0000269|PubMed:12177062,
ECO:0000269|PubMed:12690097, ECO:0000269|PubMed:12771190,
ECO:0000269|PubMed:14596919, ECO:0000269|PubMed:15090612,
ECO:0000269|PubMed:15456872, ECO:0000269|PubMed:15707590,
ECO:0000269|PubMed:15962011, ECO:0000269|PubMed:16228008,
ECO:0000269|PubMed:16256071, ECO:0000269|PubMed:16678097,
ECO:0000269|PubMed:16751601, ECO:0000269|PubMed:16895919,
ECO:0000269|PubMed:20221403}.
-!- INTERACTION:
Q8WWN8:ARAP3; NbExp=2; IntAct=EBI-346595, EBI-4402732;
Q9ULH1:ASAP1; NbExp=8; IntAct=EBI-346595, EBI-346622;
P52907:CAPZA1; NbExp=2; IntAct=EBI-346595, EBI-355586;
P22681:CBL; NbExp=18; IntAct=EBI-346595, EBI-518228;
Q13191:CBLB; NbExp=21; IntAct=EBI-346595, EBI-744027;
P06729:CD2; NbExp=3; IntAct=EBI-346595, EBI-3912464;
P98078:Dab2 (xeno); NbExp=9; IntAct=EBI-346595, EBI-1391846;
O94850:DDN; NbExp=5; IntAct=EBI-346595, EBI-5240523;
P50570:DNM2; NbExp=5; IntAct=EBI-346595, EBI-346547;
P39052:Dnm2 (xeno); NbExp=4; IntAct=EBI-346595, EBI-349613;
Q86UU5:GGN; NbExp=4; IntAct=EBI-346595, EBI-10259069;
Q9JKY5:Hip1r (xeno); NbExp=3; IntAct=EBI-346595, EBI-642457;
Q92835:INPP5D; NbExp=6; IntAct=EBI-346595, EBI-1380477;
Q9Y6R4:MAP3K4; NbExp=5; IntAct=EBI-346595, EBI-448104;
P78314:SH3BP2; NbExp=8; IntAct=EBI-346595, EBI-727062;
Q99962:SH3GL2; NbExp=2; IntAct=EBI-346595, EBI-77938;
O43597:SPRY2; NbExp=2; IntAct=EBI-346595, EBI-742487;
Q13501:SQSTM1; NbExp=4; IntAct=EBI-346595, EBI-307104;
Q9ULZ2:STAP1; NbExp=4; IntAct=EBI-346595, EBI-6083058;
O15056:SYNJ2; NbExp=3; IntAct=EBI-346595, EBI-310513;
P0CG48:UBC; NbExp=6; IntAct=EBI-346595, EBI-3390054;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20221403}.
Cytoplasm, cytoskeleton. Cytoplasmic vesicle membrane; Peripheral
membrane protein. Cell junction, synapse, synaptosome. Cell
junction, focal adhesion {ECO:0000250}. Note=Localized in
endocytic vesicles containing clustered receptors. Colocalizes
with ASAP1 in vesicular structures. Colocalized with actin
microfilaments and focal adhesions (By similarity). Colocalized
with MAGI2 in synaptosomes. Translocation to EGFR containing
vesicles upon EGF stimulation is inhibited in the presence of
SH3KBP1 (By similarity). Colocalizes with ZFP36 in the cytoplasm
(PubMed:20221403). {ECO:0000250|UniProtKB:Q8R550,
ECO:0000269|PubMed:20221403}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96B97-1; Sequence=Displayed;
Note=Interacts with CBL.;
Name=2;
IsoId=Q96B97-2; Sequence=VSP_007504;
Note=Interacts with CD2 cytoplasmic tail and does not interact
with F-actin.;
Name=3;
IsoId=Q96B97-3; Sequence=VSP_044655, VSP_044656;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Also expressed in some
cancer cell lines.
-!- PTM: Monoubiquitinated by CBL and CBLB after EGF stimulation;
probably on its C-terminus.
-!- SEQUENCE CAUTION:
Sequence=AAH50663.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF230904; AAF37854.1; -; mRNA.
EMBL; AF542051; AAN77231.1; -; mRNA.
EMBL; AK293234; BAH11470.1; -; mRNA.
EMBL; AK293237; BAH11471.1; -; mRNA.
EMBL; AL732423; CAI40277.1; -; Genomic_DNA.
EMBL; AL732325; CAI40277.1; JOINED; Genomic_DNA.
EMBL; AL732327; CAI40277.1; JOINED; Genomic_DNA.
EMBL; AL732423; CAI40278.1; -; Genomic_DNA.
EMBL; AL732327; CAI40278.1; JOINED; Genomic_DNA.
EMBL; AL732327; CAI40511.1; -; Genomic_DNA.
EMBL; AL732325; CAI40511.1; JOINED; Genomic_DNA.
EMBL; AL732423; CAI40511.1; JOINED; Genomic_DNA.
EMBL; AL732327; CAI40512.1; -; Genomic_DNA.
EMBL; AL732423; CAI40512.1; JOINED; Genomic_DNA.
EMBL; AL732325; CAI41254.1; -; Genomic_DNA.
EMBL; AL732327; CAI41254.1; JOINED; Genomic_DNA.
EMBL; AL732423; CAI41254.1; JOINED; Genomic_DNA.
EMBL; AL732409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL772197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015806; AAH15806.1; -; mRNA.
EMBL; BC050663; AAH50663.1; ALT_SEQ; mRNA.
EMBL; AF329267; AAK95587.1; -; mRNA.
EMBL; AF329268; AAO13348.1; -; mRNA.
CCDS; CCDS14193.1; -. [Q96B97-1]
CCDS; CCDS35213.1; -. [Q96B97-2]
CCDS; CCDS55383.1; -. [Q96B97-3]
PIR; JC7191; JC7191.
RefSeq; NP_001019837.1; NM_001024666.2. [Q96B97-2]
RefSeq; NP_001171889.1; NM_001184960.1. [Q96B97-3]
RefSeq; NP_114098.1; NM_031892.2. [Q96B97-1]
RefSeq; XP_016884958.1; XM_017029469.1.
UniGene; Hs.726365; -.
PDB; 2BZ8; X-ray; 2.00 A; A/B=1-58.
PDB; 2K6D; NMR; -; A=267-328.
PDB; 2K9G; NMR; -; A=262-333.
PDB; 2N64; NMR; -; A/B/C=594-665.
PDB; 2O2O; NMR; -; A=92-168.
PDB; 2YDL; X-ray; 2.05 A; A=270-328.
PDB; 5ABS; X-ray; 1.74 A; A=599-662.
PDBsum; 2BZ8; -.
PDBsum; 2K6D; -.
PDBsum; 2K9G; -.
PDBsum; 2N64; -.
PDBsum; 2O2O; -.
PDBsum; 2YDL; -.
PDBsum; 5ABS; -.
ProteinModelPortal; Q96B97; -.
SMR; Q96B97; -.
BioGrid; 119029; 274.
DIP; DIP-31803N; -.
IntAct; Q96B97; 57.
MINT; MINT-233697; -.
STRING; 9606.ENSP00000380921; -.
iPTMnet; Q96B97; -.
PhosphoSitePlus; Q96B97; -.
BioMuta; SH3KBP1; -.
DMDM; 31077034; -.
EPD; Q96B97; -.
MaxQB; Q96B97; -.
PaxDb; Q96B97; -.
PeptideAtlas; Q96B97; -.
PRIDE; Q96B97; -.
DNASU; 30011; -.
Ensembl; ENST00000379698; ENSP00000369020; ENSG00000147010. [Q96B97-2]
Ensembl; ENST00000379716; ENSP00000369039; ENSG00000147010. [Q96B97-3]
Ensembl; ENST00000397821; ENSP00000380921; ENSG00000147010. [Q96B97-1]
GeneID; 30011; -.
KEGG; hsa:30011; -.
UCSC; uc004czl.4; human. [Q96B97-1]
CTD; 30011; -.
DisGeNET; 30011; -.
GeneCards; SH3KBP1; -.
HGNC; HGNC:13867; SH3KBP1.
HPA; CAB021892; -.
HPA; HPA003351; -.
HPA; HPA003355; -.
MIM; 300374; gene.
neXtProt; NX_Q96B97; -.
OpenTargets; ENSG00000147010; -.
PharmGKB; PA37822; -.
eggNOG; KOG4348; Eukaryota.
eggNOG; ENOG410XQBY; LUCA.
GeneTree; ENSGT00530000063594; -.
HOGENOM; HOG000231405; -.
HOVERGEN; HBG057824; -.
InParanoid; Q96B97; -.
KO; K12470; -.
OMA; EDKEEHV; -.
OrthoDB; EOG091G041Q; -.
PhylomeDB; Q96B97; -.
TreeFam; TF350191; -.
Reactome; R-HSA-182971; EGFR downregulation.
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-8866376; Reelin signalling pathway.
Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; Q96B97; -.
SIGNOR; Q96B97; -.
ChiTaRS; SH3KBP1; human.
EvolutionaryTrace; Q96B97; -.
GeneWiki; SH3KBP1; -.
GenomeRNAi; 30011; -.
PRO; PR:Q96B97; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000147010; -.
CleanEx; HS_SH3KBP1; -.
ExpressionAtlas; Q96B97; baseline and differential.
Genevisible; Q96B97; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
InterPro; IPR001452; SH3_domain.
Pfam; PF14604; SH3_9; 3.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 3.
SUPFAM; SSF50044; SSF50044; 3.
PROSITE; PS50002; SH3; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell junction;
Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Endocytosis; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH3 domain; SH3-binding; Synapse;
Synaptosome; Ubl conjugation.
CHAIN 1 665 SH3 domain-containing kinase-binding
protein 1.
/FTId=PRO_0000097728.
DOMAIN 1 58 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 98 157 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 267 328 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 602 664 {ECO:0000255}.
COMPBIAS 327 428 Pro-rich.
MOD_RES 156 156 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R550}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R550}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 254 254 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 521 521 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 587 587 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 54 MVEAIVEFDYQAQHDDELTISVGEIITNIRKEDGGWWEGQI
NGRRGLFPDNFVR -> MEVSAAKAPSAADLSEI (in
isoform 2). {ECO:0000303|PubMed:12618476,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_007504.
VAR_SEQ 1 4 MVEA -> MGEE (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044655.
VAR_SEQ 5 242 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044656.
VARIANT 382 382 P -> L. {ECO:0000269|PubMed:11474197}.
/FTId=VAR_015667.
CONFLICT 288 288 I -> T (in Ref. 3; BAH11471).
{ECO:0000305}.
CONFLICT 426 426 V -> A (in Ref. 3; BAH11471).
{ECO:0000305}.
CONFLICT 570 570 A -> V (in Ref. 5; AAH15806).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:2BZ8}.
STRAND 25 30 {ECO:0000244|PDB:2BZ8}.
TURN 33 35 {ECO:0000244|PDB:2BZ8}.
STRAND 36 41 {ECO:0000244|PDB:2BZ8}.
STRAND 44 49 {ECO:0000244|PDB:2BZ8}.
HELIX 50 52 {ECO:0000244|PDB:2BZ8}.
STRAND 53 55 {ECO:0000244|PDB:2BZ8}.
STRAND 102 105 {ECO:0000244|PDB:2O2O}.
STRAND 113 115 {ECO:0000244|PDB:2O2O}.
STRAND 124 126 {ECO:0000244|PDB:2O2O}.
HELIX 130 132 {ECO:0000244|PDB:2O2O}.
STRAND 149 153 {ECO:0000244|PDB:2O2O}.
TURN 161 164 {ECO:0000244|PDB:2O2O}.
STRAND 270 276 {ECO:0000244|PDB:2YDL}.
STRAND 283 285 {ECO:0000244|PDB:2K6D}.
STRAND 293 299 {ECO:0000244|PDB:2YDL}.
STRAND 301 303 {ECO:0000244|PDB:2K9G}.
STRAND 306 311 {ECO:0000244|PDB:2YDL}.
STRAND 314 319 {ECO:0000244|PDB:2YDL}.
HELIX 320 322 {ECO:0000244|PDB:2YDL}.
STRAND 323 325 {ECO:0000244|PDB:2YDL}.
HELIX 605 661 {ECO:0000244|PDB:5ABS}.
SEQUENCE 665 AA; 73126 MW; 3BD350FCDB14BD4C CRC64;
MVEAIVEFDY QAQHDDELTI SVGEIITNIR KEDGGWWEGQ INGRRGLFPD NFVREIKKEM
KKDPLTNKAP EKPLHEVPSG NSLLSSETIL RTNKRGERRR RRCQVAFSYL PQNDDELELK
VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN FIKELSGESD ELGISQDEQL SKSSLRETTG
SESDGGDSSS TKSEGANGTV ATAAIQPKKV KGVGFGDIFK DKPIKLRPRS IEVENDFLPV
EKTIGKKLPA TTATPDSSKT EMDSRTKSKD YCKVIFPYEA QNDDELTIKE GDIVTLINKD
CIDVGWWEGE LNGRRGVFPD NFVKLLPPDF EKEGNRPKKP PPPSAPVIKQ GAGTTERKHE
IKKIPPERPE MLPNRTEEKE RPEREPKLDL QKPSVPAIPP KKPRPPKTNS LSRPGALPPR
RPERPVGPLT HTRGDSPKID LAGSSLSGIL DKDLSDRSND IDLEGFDSVV SSTEKLSHPT
TSRPKATGRR PPSQSLTSSS LSSPDIFDSP SPEEDKEEHI SLAHRGVDAS KKTSKTVTIS
QVSDNKASLP PKPGTMAAGG GGPAPLSSAA PSPLSSSLGT AGHRANSPSL FGTEGKPKME
PAASSQAAVE ELRTQVRELR SIIETMKDQQ KREIKQLLSE LDEEKKIRLR LQMEVNDIKK
ALQSK


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E1394h ELISA kit Calcium- and integrin-binding protein,Calcium and integrin-binding protein 1,Calmyrin,CIB,CIB,CIB1,CIBP,DNA-PKcs-interacting protein,Homo sapiens,Human,Kinase-interacting protein,KIP,KIP,PR 96T
EIAAB26847 Amyloid beta A4 protein-binding family A member 2-binding protein,APBA2BP,Homo sapiens,Human,NECAB3,Nek2-interacting protein 1,Neuronal calcium-binding protein 3,NIP1,N-terminal EF-hand calcium-bindin
EIAAB12528 CAP-binding protein complex-interacting protein 1,DJ-1-binding protein,DJBP,DJBP,EFCAB6,EF-hand calcium-binding domain-containing protein 6,Homo sapiens,Human,KIAA1672
EIAAB29754 Homo sapiens,HSPC218,Human,PABP-interacting protein 2,PAIP2,PAIP-2,PAIP2A,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2
18-003-42203 Mitogen-activated protein kinase kinase kinase 7-interacting protein 2 - TAK1-binding protein 2 Polyclonal 0.05 mg Aff Pur
EIAAB29748 Homo sapiens,Human,KIAA1155,PABP-interacting protein 2B,PAIP2B,PAIP-2B,Poly(A)-binding protein-interacting protein 2B,Polyadenylate-binding protein-interacting protein 2B
18-003-43089 Oligodendrocyte transcription factor 2 - Oligo2; Basic helix-loop-helix protein class B 1; Protein kinase C-binding protein RACK17; Protein kinase C-binding protein 2 Polyclonal 0.05 mg Aff Pur
EIAAB29749 Homo sapiens,Human,PABP-interacting protein 1,PAIP1,PAIP-1,Poly(A)-binding protein-interacting protein 1,Polyadenylate-binding protein-interacting protein 1


 

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