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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.
18-JUL-2018, entry version 142.
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:
P00533:EGFR; NbExp=2; IntAct=EBI-310491, EBI-297353;
P06213:INSR; NbExp=6; IntAct=EBI-310491, EBI-475899;
P42227:Stat3 (xeno); NbExp=5; IntAct=EBI-310491, EBI-602878;
P52631:Stat3 (xeno); NbExp=2; IntAct=EBI-310491, EBI-10764775;
-!- 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=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA92537.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB55148.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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. [Q9NRF2-1]
RefSeq; XP_016878604.1; XM_017023115.1. [Q9NRF2-1]
RefSeq; XP_016878605.1; XM_017023116.1. [Q9NRF2-1]
UniGene; Hs.15744; -.
PDB; 5W3R; X-ray; 1.39 A; A=519-628.
PDBsum; 5W3R; -.
ProteinModelPortal; Q9NRF2; -.
SMR; Q9NRF2; -.
BioGrid; 117455; 19.
IntAct; Q9NRF2; 15.
MINT; Q9NRF2; -.
STRING; 9606.ENSP00000321221; -.
iPTMnet; Q9NRF2; -.
PhosphoSitePlus; Q9NRF2; -.
BioMuta; SH2B1; -.
DMDM; 313104186; -.
EPD; Q9NRF2; -.
MaxQB; Q9NRF2; -.
PaxDb; Q9NRF2; -.
PeptideAtlas; Q9NRF2; -.
PRIDE; Q9NRF2; -.
ProteomicsDB; 82346; -.
ProteomicsDB; 82347; -. [Q9NRF2-2]
ProteomicsDB; 82348; -. [Q9NRF2-3]
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; -.
EuPathDB; HostDB:ENSG00000178188.14; -.
GeneCards; SH2B1; -.
H-InvDB; HIX0017272; -.
HGNC; HGNC:30417; SH2B1.
HPA; HPA076175; -.
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; -.
eggNOG; ENOG410IMWK; Eukaryota.
eggNOG; ENOG41102PH; LUCA.
GeneTree; ENSGT00530000063355; -.
HOVERGEN; HBG006707; -.
InParanoid; Q9NRF2; -.
KO; K12459; -.
OMA; GDRWTHR; -.
OrthoDB; EOG091G04RI; -.
PhylomeDB; Q9NRF2; -.
TreeFam; TF323184; -.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
Reactome; R-HSA-2586552; Signaling by Leptin.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; Q9NRF2; -.
SIGNOR; Q9NRF2; -.
GeneWiki; SH2B1; -.
GenomeRNAi; 25970; -.
PRO; PR:Q9NRF2; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000178188; -.
CleanEx; HS_SH2B1; -.
ExpressionAtlas; Q9NRF2; baseline and differential.
Genevisible; Q9NRF2; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
GO; GO:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; Complete proteome; Cytoplasm;
Membrane; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; SH2 domain.
CHAIN 1 756 SH2B adapter protein 1.
/FTId=PRO_0000323593.
DOMAIN 267 376 PH.
DOMAIN 527 625 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 1 555 Interaction with JAK2 (low-affinity
binding; independent of JAK2
phosphorylation). {ECO:0000250}.
REGION 24 85 Required for self-association.
REGION 85 196 Interaction with RAC1. {ECO:0000250}.
REGION 100 243 Required for NGF signaling.
{ECO:0000250}.
REGION 224 233 Required for nuclear localization.
{ECO:0000250}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZM2}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648}.
MOD_RES 270 270 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZM2}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZM2}.
MOD_RES 439 439 Phosphotyrosine; by JAK1, JAK2 and PDGFR.
{ECO:0000250|UniProtKB:Q62985}.
MOD_RES 494 494 Phosphotyrosine; by JAK1, JAK2.
{ECO:0000250|UniProtKB:Q62985}.
VAR_SEQ 633 756 EPTTSHDPPQPPEPPSWTDPPQPGAEEASRAPEVAAAAAAA
AKERQEKEKAGGGGVPEELVPVVELVPVVELEEAIAPGSEA
QGAGSGGDAGVPPMVQLQQSPLGGDGEEGGHPRAINNQYSF
V -> GREQAGSHAGVCEGDGCHPDASCTLMPFGASDCVTD
HLP (in isoform 2).
{ECO:0000303|PubMed:10718198,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15767667,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_032027.
VAR_SEQ 633 756 EPTTSHDPPQPPEPPSWTDPPQPGAEEASRAPEVAAAAAAA
AKERQEKEKAGGGGVPEELVPVVELVPVVELEEAIAPGSEA
QGAGSGGDAGVPPMVQLQQSPLGGDGEEGGHPRAINNQYSF
V -> GEQSRSAGEEVPVHPRSEAGSRLGAMRGCAREMDAT
PMPPAPSCPSERVTV (in isoform 3).
{ECO:0000303|PubMed:15767667,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_032028.
VARIANT 484 484 T -> A (in dbSNP:rs7498665).
{ECO:0000269|PubMed:15767667,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_039550.
VARIANT 541 541 V -> A (in dbSNP:rs17850682).
{ECO:0000269|PubMed:10718198}.
/FTId=VAR_039551.
MUTAGEN 29 29 F->R: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
MUTAGEN 34 34 A->D: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
MUTAGEN 38 38 A->D: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
MUTAGEN 41 41 F->A: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
MUTAGEN 42 42 A->D: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
MUTAGEN 48 48 Y->A: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
MUTAGEN 68 68 F->A: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
MUTAGEN 72 72 F->A: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
MUTAGEN 555 555 R->A: Abolishes self-association and
interaction with INSR and IGF1R.
{ECO:0000269|PubMed:15767667}.
CONFLICT 197 197 N -> D (in Ref. 3; BAF83021).
{ECO:0000305}.
CONFLICT 519 519 D -> G (in Ref. 3; BAF83021).
{ECO:0000305}.
HELIX 522 524 {ECO:0000244|PDB:5W3R}.
STRAND 528 531 {ECO:0000244|PDB:5W3R}.
HELIX 534 542 {ECO:0000244|PDB:5W3R}.
HELIX 545 548 {ECO:0000244|PDB:5W3R}.
STRAND 551 556 {ECO:0000244|PDB:5W3R}.
STRAND 558 560 {ECO:0000244|PDB:5W3R}.
STRAND 564 570 {ECO:0000244|PDB:5W3R}.
STRAND 573 581 {ECO:0000244|PDB:5W3R}.
STRAND 587 589 {ECO:0000244|PDB:5W3R}.
STRAND 592 596 {ECO:0000244|PDB:5W3R}.
HELIX 597 606 {ECO:0000244|PDB:5W3R}.
STRAND 614 616 {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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