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SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B)

 SH2B1_HUMAN             Reviewed;         756 AA.
Q9NRF2; A8K2R7; Q96FK3; Q96SX3; Q9NRF1; Q9NRF3; Q9P2P7; Q9Y3Y3;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
10-FEB-2021, entry version 161.
RecName: Full=SH2B adapter protein 1;
AltName: Full=Pro-rich, PH and SH2 domain-containing signaling mediator;
Short=PSM;
AltName: Full=SH2 domain-containing protein 1B;
Name=SH2B1; Synonyms=KIAA1299, SH2B;
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; 2 AND 3), FUNCTION IN JAK2
ACTIVATION, SELF-ASSOCIATION, INTERACTION WITH JAK2; SH2B2; INSR AND IGF1R,
PHOSPHORYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF PHE-29; ALA-34; ALA-38;
PHE-41; ALA-42; TYR-48; PHE-68; PHE-72 AND ARG-555, AND VARIANT ALA-484.
PubMed=15767667; DOI=10.1128/mcb.25.7.2607-2621.2005;
Nishi M., Werner E.D., Oh B.C., Frantz J.D., Dhe-Paganon S., Hansen L.,
Lee J., Shoelson S.E.;
"Kinase activation through dimerization by human SH2-B.";
Mol. Cell. Biol. 25:2607-2621(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-541.
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI. The
complete sequences of 150 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 7:65-73(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Teratocarcinoma, and Tongue;
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 MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
[LARGE SCALE MRNA] OF 144-756 (ISOFORM 3), AND VARIANT ALA-484.
TISSUE=Mammary cancer;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
Myers R.M., Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-756 (ISOFORM 2).
TISSUE=Eye;
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 INSR.
PubMed=9498552; DOI=10.1093/oxfordjournals.jbchem.a021868;
Riedel H., Wang J., Hansen H., Yousaf N.;
"PSM, an insulin-dependent, pro-rich, PH, SH2 domain containing partner of
the insulin receptor.";
J. Biochem. 122:1105-1113(1997).
[8]
FUNCTION, INTERACTION WITH INSR, AND PHOSPHORYLATION.
PubMed=9742218; DOI=10.1042/bj3350103;
Kotani K., Wilden P., Pillay T.S.;
"SH2-Balpha is an insulin-receptor adapter protein and substrate that
interacts with the activation loop of the insulin-receptor kinase.";
Biochem. J. 335:103-109(1998).
[9]
FUNCTION IN PDGF SIGNALING, AND INTERACTION WITH PDGFRA/B.
PubMed=9694882; DOI=10.1074/jbc.273.33.21239;
Rui L., Carter-Su C.;
"Platelet-derived growth factor (PDGF) stimulates the association of SH2-
Bbeta with PDGF receptor and phosphorylation of SH2-Bbeta.";
J. Biol. Chem. 273:21239-21245(1998).
[10]
INTERACTION WITH INSR AND ISR1.
PubMed=10594240; DOI=10.1007/s003359901183;
Nelms K., O'Neill T.J., Li S., Hubbard S.R., Gustafson T.A., Paul W.E.;
"Alternative splicing, gene localization, and binding of SH2-B to the
insulin receptor kinase domain.";
Mamm. Genome 10:1160-1167(1999).
[11]
INTERACTION WITH JAK1; JAK2 AND JAK3, AND PHOSPHORYLATION.
PubMed=11751854; DOI=10.1074/jbc.m109165200;
O'Brien K.B., O'Shea J.J., Carter-Su C.;
"SH2-B family members differentially regulate JAK family tyrosine
kinases.";
J. Biol. Chem. 277:8673-8681(2002).
[12]
FUNCTION IN FGF SIGNALING, AND INTERACTION WITH FGFR3.
PubMed=11827956; DOI=10.1074/jbc.m102777200;
Kong M., Wang C.S., Donoghue D.J.;
"Interaction of fibroblast growth factor receptor 3 and the adapter protein
SH2-B. A role in STAT5 activation.";
J. Biol. Chem. 277:15962-15970(2002).
[13]
FUNCTION IN NGF SIGNALING.
PubMed=14565960; DOI=10.1074/jbc.m310040200;
Wang X., Chen L., Maures T.J., Herrington J., Carter-Su C.;
"SH2-B is a positive regulator of nerve growth factor-mediated activation
of the Akt/Forkhead pathway in PC12 cells.";
J. Biol. Chem. 279:133-141(2004).
[14]
FUNCTION IN GDNF SIGNALING, AND INTERACTION WITH RET.
PubMed=16569669; DOI=10.1242/jcs.02845;
Zhang Y., Zhu W., Wang Y.G., Liu X.J., Jiao L., Liu X., Zhang Z.H.,
Lu C.L., He C.;
"Interaction of SH2-Bbeta with RET is involved in signaling of GDNF-induced
neurite outgrowth.";
J. Cell Sci. 119:1666-1676(2006).
[15]
FUNCTION IN RET SIGNALING, AND INTERACTION WITH PRKAR1A/RET.
PubMed=17471236; DOI=10.1038/sj.onc.1210480;
Donatello S., Fiorino A., Degl'Innocenti D., Alberti L., Miranda C.,
Gorla L., Bongarzone I., Rizzetti M.G., Pierotti M.A., Borrello M.G.;
"SH2B1beta adaptor is a key enhancer of RET tyrosine kinase signaling.";
Oncogene 26:6546-6559(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, 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).
[18]
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).
[19]
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).
[20]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-270, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Adapter protein for several members of the tyrosine kinase
receptor family. Involved in multiple signaling pathways mediated by
Janus kinase (JAK) and receptor tyrosine kinases, including the
receptors of insulin (INS), insulin-like growth factor I (IGF1), nerve
growth factor (NGF), brain-derived neurotrophic factor (BDNF), glial
cell line-derived neurotrophic factor (GDNF), platelet-derived growth
factor (PDGF) and fibroblast growth factors (FGFs). In growth hormone
(GH) signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1,
which in turn is phosphorylated by JAK2 on tyrosine residues. These
phosphotyrosines form potential binding sites for other signaling
proteins. GH also promotes serine/threonine phosphorylation of SH2B1
and these phosphorylated residues may serve to recruit other proteins
to the GHR-JAK2-SH2B1 complexes, such as RAC1. In leptin (LEP)
signaling, binds to and potentiates the activation of JAK2 by globally
enhancing downstream pathways. In response to leptin, binds
simultaneously to both, JAK2 and IRS1 or IRS2, thus mediating formation
of a complex of JAK2, SH2B1 and IRS1 or IRS2. Mediates tyrosine
phosphorylation of IRS1 and IRS2, resulting in activation of the PI 3-
kinase pathway. Acts as positive regulator of NGF-mediated activation
of the Akt/Forkhead pathway; prolongs NGF-induced phosphorylation of
AKT1 on 'Ser-473' and AKT1 enzymatic activity. Enhances the kinase
activity of the cytokine receptor-associated tyrosine kinase JAK2 and
of other receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2,
the mechanism seems to involve dimerization of both, SH2B1 and JAK2.
Enhances RET phosphorylation and kinase activity. Isoforms seem to be
differentially involved in IGF-I and PDGF-induced mitogenesis (By
similarity). {ECO:0000250, ECO:0000269|PubMed:11827956,
ECO:0000269|PubMed:14565960, ECO:0000269|PubMed:15767667,
ECO:0000269|PubMed:16569669, ECO:0000269|PubMed:17471236,
ECO:0000269|PubMed:9694882, ECO:0000269|PubMed:9742218}.
-!- SUBUNIT: Self-associates. Homopentamer (By similarity). Forms a
heteromultimeric complex with SH2B2 (By similarity). Interacts with
SH2B2. Isoform 1 interacts via its SH2 domain with JAK2. Isoform 2
interacts via its SH2 domain and its N-terminus with JAK2; the SH2
domain is required for the major interaction with JAK2 phosphorylated
on tyrosine residues; the N-terminus provides a low-affinity binding to
JAK2 independent of JAK2 phosphorylation. Isoform 3 interacts via its
SH2 domain with JAK2. Isoform 1 interacts via its SH2 domain with INSR;
the interaction requires receptor activation. Isoform 3 interacts via
its SH2 domain with INSR; the interaction requires receptor activation
and requires INSR phosphorylation at 'Tyr-1185'. Isoform 1 interacts
with IGF1R; the interaction requires receptor activation. Isoform 2
interacts with PRKAR1A/RET (PTC2) fusion protein; the interaction
requires RET 'Tyr-905' and Tyr-981'. Isoform 2 interacts via its SH2
domain with FGFR3; the interaction requires FGFR3 'Tyr-724' and 'Tyr-
760'. Isoform 2 interacts with RET; the interaction requires RET kinase
activity and RET 'Tyr-981'. Isoform 2 interacts with RAC1. Isoform 2
interacts with PDGFRA and/or PDGFRB; the interaction requires receptor
activation. Interacts with ISR1 and ISR2. Isoform 3 is probably part of
a complex consisting of INSR, ISR1 and SH2B1. Probably part of a
ternary complex consisting of SH2B1, JAK2 and ISR1 or ISR2. May
interact with FCER1G (By similarity). Interacts (via SH2 domain) with
NTRK1 (phosphorylated) (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q9NRF2; P00533: EGFR; NbExp=4; IntAct=EBI-310491, EBI-297353;
Q9NRF2; P06213: INSR; NbExp=6; IntAct=EBI-310491, EBI-475899;
Q9NRF2; P42227: Stat3; Xeno; NbExp=5; IntAct=EBI-310491, EBI-602878;
Q9NRF2; P52631: Stat3; Xeno; NbExp=2; IntAct=EBI-310491, EBI-10764775;
Q9NRF2-2; P62993: GRB2; NbExp=3; IntAct=EBI-10691662, EBI-401755;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000305}.
Nucleus {ECO:0000250}. Note=Shuttles between the nucleus and the
cytoplasm. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Alpha;
IsoId=Q9NRF2-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q9NRF2-2; Sequence=VSP_032027;
Name=3; Synonyms=Gamma;
IsoId=Q9NRF2-3; Sequence=VSP_032028;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in skeletal
muscle and ovary. {ECO:0000269|PubMed:15767667}.
-!- PTM: Phosphorylated on tyrosine residues in response to receptor kinase
stimulation. Phosphorylated by RET. {ECO:0000269|PubMed:11751854,
ECO:0000269|PubMed:15767667, ECO:0000269|PubMed:9742218}.
-!- SIMILARITY: Belongs to the SH2B adapter family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH10704.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=BAA92537.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
Sequence=BAB55148.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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EMBL; AF227967; AAF73912.1; -; mRNA.
EMBL; AF227968; AAF73913.1; -; mRNA.
EMBL; AF227969; AAF73914.1; -; mRNA.
EMBL; AB037720; BAA92537.1; ALT_INIT; mRNA.
EMBL; AK027488; BAB55148.1; ALT_INIT; mRNA.
EMBL; AK290332; BAF83021.1; -; mRNA.
EMBL; AL049924; CAB43208.1; -; mRNA.
EMBL; AL713760; CAD28530.1; -; mRNA.
EMBL; AC133550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010704; AAH10704.1; ALT_INIT; mRNA.
CCDS; CCDS32424.1; -. [Q9NRF2-2]
CCDS; CCDS53996.1; -. [Q9NRF2-1]
CCDS; CCDS53997.1; -. [Q9NRF2-3]
PIR; T08662; T08662.
RefSeq; NP_001139267.1; NM_001145795.1. [Q9NRF2-1]
RefSeq; NP_001139268.1; NM_001145796.1. [Q9NRF2-2]
RefSeq; NP_001139269.1; NM_001145797.1. [Q9NRF2-3]
RefSeq; NP_001139284.1; NM_001145812.1. [Q9NRF2-2]
RefSeq; NP_001295222.1; NM_001308293.1. [Q9NRF2-1]
RefSeq; NP_001295223.1; NM_001308294.1.
RefSeq; NP_056318.2; NM_015503.2. [Q9NRF2-2]
RefSeq; XP_016878603.1; XM_017023114.1.
RefSeq; XP_016878604.1; XM_017023115.1.
RefSeq; XP_016878605.1; XM_017023116.1.
PDB; 5W3R; X-ray; 1.39 A; A=519-628.
PDBsum; 5W3R; -.
SMR; Q9NRF2; -.
BioGRID; 117455; 20.
IntAct; Q9NRF2; 16.
MINT; Q9NRF2; -.
STRING; 9606.ENSP00000321221; -.
iPTMnet; Q9NRF2; -.
PhosphoSitePlus; Q9NRF2; -.
BioMuta; SH2B1; -.
DMDM; 313104186; -.
jPOST; Q9NRF2; -.
MassIVE; Q9NRF2; -.
MaxQB; Q9NRF2; -.
PaxDb; Q9NRF2; -.
PeptideAtlas; Q9NRF2; -.
PRIDE; Q9NRF2; -.
ProteomicsDB; 82346; -. [Q9NRF2-1]
ProteomicsDB; 82347; -. [Q9NRF2-2]
ProteomicsDB; 82348; -. [Q9NRF2-3]
Antibodypedia; 26583; 279 antibodies.
Ensembl; ENST00000322610; ENSP00000321221; ENSG00000178188. [Q9NRF2-1]
Ensembl; ENST00000337120; ENSP00000337163; ENSG00000178188. [Q9NRF2-2]
Ensembl; ENST00000359285; ENSP00000352232; ENSG00000178188. [Q9NRF2-3]
Ensembl; ENST00000395532; ENSP00000378903; ENSG00000178188. [Q9NRF2-2]
Ensembl; ENST00000618521; ENSP00000481709; ENSG00000178188. [Q9NRF2-1]
GeneID; 25970; -.
KEGG; hsa:25970; -.
UCSC; uc002dri.4; human. [Q9NRF2-1]
CTD; 25970; -.
DisGeNET; 25970; -.
GeneCards; SH2B1; -.
HGNC; HGNC:30417; SH2B1.
HPA; ENSG00000178188; Low tissue specificity.
MalaCards; SH2B1; -.
MIM; 608937; gene.
neXtProt; NX_Q9NRF2; -.
OpenTargets; ENSG00000178188; -.
Orphanet; 261222; Distal 16p11.2 microdeletion syndrome.
Orphanet; 261197; Proximal 16p11.2 microdeletion syndrome.
Orphanet; 329249; Severe early-onset obesity-insulin resistance syndrome due to SH2B1 deficiency.
PharmGKB; PA145148084; -.
VEuPathDB; HostDB:ENSG00000178188.14; -.
eggNOG; ENOG502QT43; Eukaryota.
GeneTree; ENSGT00950000183191; -.
HOGENOM; CLU_014885_4_0_1; -.
InParanoid; Q9NRF2; -.
OMA; SSTLMPF; -.
PhylomeDB; Q9NRF2; -.
TreeFam; TF323184; -.
PathwayCommons; Q9NRF2; -.
Reactome; R-HSA-1170546; Prolactin receptor signaling. [Q9NRF2-2]
Reactome; R-HSA-2586552; Signaling by Leptin. [Q9NRF2-2]
Reactome; R-HSA-982772; Growth hormone receptor signaling. [Q9NRF2-2]
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; Q9NRF2; -.
SIGNOR; Q9NRF2; -.
BioGRID-ORCS; 25970; 33 hits in 877 CRISPR screens.
ChiTaRS; SH2B1; human.
GeneWiki; SH2B1; -.
GenomeRNAi; 25970; -.
Pharos; Q9NRF2; Tbio.
PRO; PR:Q9NRF2; -.
Proteomes; UP000005640; Chromosome 16.
RNAct; Q9NRF2; protein.
Bgee; ENSG00000178188; Expressed in right hemisphere of cerebellum and 217 other tissues.
ExpressionAtlas; Q9NRF2; baseline and differential.
Genevisible; Q9NRF2; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IGI:MGI.
GO; GO:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
CDD; cd10346; SH2_SH2B_family; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR015012; Phe_ZIP.
InterPro; IPR036290; Phe_ZIP_sf.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR030523; SH2B.
InterPro; IPR030521; SH2B1.
InterPro; IPR035057; SH2B1_SH2.
PANTHER; PTHR10872; PTHR10872; 1.
PANTHER; PTHR10872:SF3; PTHR10872:SF3; 1.
Pfam; PF00169; PH; 1.
Pfam; PF08916; Phe_ZIP; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00233; PH; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF109805; SSF109805; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cytoplasm; Membrane; Methylation;
Nucleus; Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1..756
/note="SH2B adapter protein 1"
/id="PRO_0000323593"
DOMAIN 267..376
/note="PH"
DOMAIN 527..625
/note="SH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
REGION 1..555
/note="Interaction with JAK2 (low-affinity binding;
independent of JAK2 phosphorylation)"
/evidence="ECO:0000250"
REGION 24..85
/note="Required for self-association"
REGION 85..196
/note="Interaction with RAC1"
/evidence="ECO:0000250"
REGION 100..243
/note="Required for NGF signaling"
/evidence="ECO:0000250"
REGION 224..233
/note="Required for nuclear localization"
/evidence="ECO:0000250"
MOD_RES 88
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91ZM2"
MOD_RES 96
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648"
MOD_RES 270
/note="Omega-N-methylarginine"
/evidence="ECO:0000244|PubMed:24129315"
MOD_RES 417
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91ZM2"
MOD_RES 420
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91ZM2"
MOD_RES 439
/note="Phosphotyrosine; by JAK1, JAK2 and PDGFR"
/evidence="ECO:0000250|UniProtKB:Q62985"
MOD_RES 494
/note="Phosphotyrosine; by JAK1, JAK2"
/evidence="ECO:0000250|UniProtKB:Q62985"
VAR_SEQ 633..756
/note="EPTTSHDPPQPPEPPSWTDPPQPGAEEASRAPEVAAAAAAAAKERQEKEKAG
GGGVPEELVPVVELVPVVELEEAIAPGSEAQGAGSGGDAGVPPMVQLQQSPLGGDGEEG
GHPRAINNQYSFV -> GREQAGSHAGVCEGDGCHPDASCTLMPFGASDCVTDHLP
(in isoform 2)"
/evidence="ECO:0000303|PubMed:10718198,
ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15767667, ECO:0000303|PubMed:17974005"
/id="VSP_032027"
VAR_SEQ 633..756
/note="EPTTSHDPPQPPEPPSWTDPPQPGAEEASRAPEVAAAAAAAAKERQEKEKAG
GGGVPEELVPVVELVPVVELEEAIAPGSEAQGAGSGGDAGVPPMVQLQQSPLGGDGEEG
GHPRAINNQYSFV -> GEQSRSAGEEVPVHPRSEAGSRLGAMRGCAREMDATPMPPAP
SCPSERVTV (in isoform 3)"
/evidence="ECO:0000303|PubMed:15767667,
ECO:0000303|PubMed:17974005"
/id="VSP_032028"
VARIANT 484
/note="T -> A (in dbSNP:rs7498665)"
/evidence="ECO:0000269|PubMed:15767667,
ECO:0000269|PubMed:17974005"
/id="VAR_039550"
VARIANT 541
/note="V -> A (in dbSNP:rs17850682)"
/evidence="ECO:0000269|PubMed:10718198"
/id="VAR_039551"
MUTAGEN 29
/note="F->R: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
MUTAGEN 34
/note="A->D: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
MUTAGEN 38
/note="A->D: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
MUTAGEN 41
/note="F->A: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
MUTAGEN 42
/note="A->D: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
MUTAGEN 48
/note="Y->A: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
MUTAGEN 68
/note="F->A: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
MUTAGEN 72
/note="F->A: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
MUTAGEN 555
/note="R->A: Abolishes self-association and interaction
with INSR and IGF1R."
/evidence="ECO:0000269|PubMed:15767667"
CONFLICT 197
/note="N -> D (in Ref. 3; BAF83021)"
/evidence="ECO:0000305"
CONFLICT 519
/note="D -> G (in Ref. 3; BAF83021)"
/evidence="ECO:0000305"
HELIX 522..524
/evidence="ECO:0000244|PDB:5W3R"
STRAND 528..531
/evidence="ECO:0000244|PDB:5W3R"
HELIX 534..542
/evidence="ECO:0000244|PDB:5W3R"
HELIX 545..548
/evidence="ECO:0000244|PDB:5W3R"
STRAND 551..556
/evidence="ECO:0000244|PDB:5W3R"
STRAND 558..560
/evidence="ECO:0000244|PDB:5W3R"
STRAND 564..570
/evidence="ECO:0000244|PDB:5W3R"
STRAND 573..581
/evidence="ECO:0000244|PDB:5W3R"
STRAND 587..589
/evidence="ECO:0000244|PDB:5W3R"
STRAND 592..596
/evidence="ECO:0000244|PDB:5W3R"
HELIX 597..606
/evidence="ECO:0000244|PDB:5W3R"
STRAND 614..616
/evidence="ECO:0000244|PDB:5W3R"
SEQUENCE 756 AA; 79366 MW; CF680B57114CB1D3 CRC64;
MNGAPSPEDG ASPSSPPLPP PPPPSWREFC ESHARAAALD FARRFRLYLA SHPQYAGPGA
EAAFSRRFAE LFLQHFEAEV ARASGSLSPP ILAPLSPGAE ISPHDLSLES CRVGGPLAVL
GPSRSSEDLA GPLPSSVSSS STTSSKPKLK KRFSLRSVGR SVRGSVRGIL QWRGTVDPPS
SAGPLETSSG PPVLGGNSNS NSSGGAGTVG RGLVSDGTSP GERWTHRFER LRLSRGGGAL
KDGAGMVQRE ELLSFMGAEE AAPDPAGVGR GGGVAGPPSG GGGQPQWQKC RLLLRSEGEG
GGGSRLEFFV PPKASRPRLS IPCSSITDVR TTTALEMPDR ENTFVVKVEG PSEYIMETVD
AQHVKAWVSD IQECLSPGPC PATSPRPMTL PLAPGTSFLT RENTDSLELS CLNHSESLPS
QDLLLGPSES NDRLSQGAYG GLSDRPSASI SPSSASIAAS HFDSMELLPP ELPPRIPIEE
GPPTGTVHPL SAPYPPLDTP ETATGSFLFQ GEPEGGEGDQ PLSGYPWFHG MLSRLKAAQL
VLTGGTGSHG VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM
LEHFRVHPIP LESGGSSDVV LVSYVPSSQR QQEPTTSHDP PQPPEPPSWT DPPQPGAEEA
SRAPEVAAAA AAAAKERQEK EKAGGGGVPE ELVPVVELVP VVELEEAIAP GSEAQGAGSG
GDAGVPPMVQ LQQSPLGGDG EEGGHPRAIN NQYSFV


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WP1049: G Protein Signaling Pathways
WP232: G Protein Signaling Pathways
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Related Genes :
[Sh2b1 Sh2bpsm1] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[SH2B1 KIAA1299 SH2B] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B)
[Sh2b1 Sh2-b Sh2bpsm1] SH2B adapter protein 1 (FceRI gamma-chain-interacting protein SH2-B) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[Sh2d1b Eat2 Eat2a Sh2d1b1] SH2 domain-containing protein 1B (EWS/FLI1-activated transcript 2) (EAT-2)
[GRB2 ASH] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[SH2D1A DSHP SAP] SH2 domain-containing protein 1A (Duncan disease SH2-protein) (Signaling lymphocytic activation molecule-associated protein) (SLAM-associated protein) (T-cell signal transduction molecule SAP)
[Grb2] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2)
[SH2D2A SCAP TSAD VRAP] SH2 domain-containing protein 2A (SH2 domain-containing adapter protein) (T cell-specific adapter protein) (TSAd) (VEGF receptor-associated protein)
[Grb2 Ash] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[GRB2] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2)
[Blnk Bash Ly57 Slp65] B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Lymphocyte antigen 57) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (Slp-65)
[Inpp5d 7a33 Ship Ship1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (Phosphatidylinositol-4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship)
[BLNK BASH SLP65] B-cell linker protein (B-cell adapter containing a SH2 domain protein) (B-cell adapter containing a Src homology 2 domain protein) (Cytoplasmic adapter protein) (Src homology 2 domain-containing leukocyte protein of 65 kDa) (SLP-65)
[BCAR3 NSP2 SH2D3B UNQ271/PRO308] Breast cancer anti-estrogen resistance protein 3 (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B)
[SHC1 SHC SHCA] SHC-transforming protein 1 (SHC-transforming protein 3) (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[NCK2 GRB4] Cytoplasmic protein NCK2 (Growth factor receptor-bound protein 4) (NCK adaptor protein 2) (Nck-2) (SH2/SH3 adaptor protein NCK-beta)
[INPPL1 SHIP2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[Shc1 Shc ShcA] SHC-transforming protein 1 (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[INPP5D SHIP SHIP1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship) (hp51CN)
[Inpp5d Ship Ship1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Phosphatidylinositol-4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1)
[SHC3 NSHC SHCC] SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (Protein Rai) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3)
[SHB] SH2 domain-containing adapter protein B
[Shc1] SHC-transforming protein 1 (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[Shb] SH2 domain-containing adapter protein B
[NCK1 NCK] Cytoplasmic protein NCK1 (NCK adaptor protein 1) (Nck-1) (SH2/SH3 adaptor protein NCK-alpha)
[Inppl1 Ship2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (AblSH3-binding protein) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[Inppl1 Ship2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[SQSTM1 ORCA OSIL] Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62)
[Socs3 Cis3 Cish3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (Protein EF-10)
[SOCS3 CIS3 SSI3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (STAT-induced STAT inhibitor 3) (SSI-3)

Bibliography :
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