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SH2B adapter protein 1 (FceRI gamma-chain-interacting protein SH2-B) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)

 SH2B1_RAT               Reviewed;         756 AA.
Q62985; O55072;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-APR-2020, entry version 136.
RecName: Full=SH2B adapter protein 1;
AltName: Full=FceRI gamma-chain-interacting protein SH2-B;
AltName: Full=SH2 domain-containing protein 1B;
AltName: Full=SH2-B PH domain-containing signaling mediator 1;
Name=Sh2b1; Synonyms=Sh2-b, Sh2bpsm1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH FCER1G.
TISSUE=Mast cell;
PubMed=9636306; DOI=10.1038/nbt1295-1474;
Osborne M.A., Dalton S., Kochan J.P.;
"The yeast tribrid system -- genetic detection of trans-phosphorylated
ITAM-SH2-interactions.";
Biotechnology (N.Y.) 13:1474-1478(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION, AND
INTERACTION WITH JAK2.
TISSUE=Kidney;
PubMed=9343427; DOI=10.1128/mcb.17.11.6633;
Rui L., Mathews L.S., Hotta K., Gustafson T.A., Carter-Su C.;
"Identification of SH2-Bbeta as a substrate of the tyrosine kinase JAK2
involved in growth hormone signaling.";
Mol. Cell. Biol. 17:6633-6644(1997).
[3]
TISSUE SPECIFICITY.
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).
[4]
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).
[5]
FUNCTION IN NGF SIGNALING, INTERACTION WITH NTRK1, AND PHOSPHORYLATION.
PubMed=9856458; DOI=10.1016/s0896-6273(00)80620-0;
Qian X., Riccio A., Zhang Y., Ginty D.D.;
"Identification and characterization of novel substrates of Trk receptors
in developing neurons.";
Neuron 21:1017-1029(1998).
[6]
FUNCTION IN NGF SIGNALING, PHOSPHORYLATION AT SER-96, AND MUTAGENESIS OF
SER-96.
PubMed=10473609; DOI=10.1074/jbc.274.37.26485;
Rui L., Herrington J., Carter-Su C.;
"SH2-B, a membrane-associated adapter, is phosphorylated on multiple
serines/threonines in response to nerve growth factor by kinases within the
MEK/ERK cascade.";
J. Biol. Chem. 274:26485-26492(1999).
[7]
FUNCTION IN JAK2 ACTIVATION, AND MUTAGENESIS OF ARG-555.
PubMed=10377387; DOI=10.1073/pnas.96.13.7172;
Rui L., Carter-Su C.;
"Identification of SH2-bbeta as a potent cytoplasmic activator of the
tyrosine kinase Janus kinase 2.";
Proc. Natl. Acad. Sci. U.S.A. 96:7172-7177(1999).
[8]
FUNCTION, INTERACTION WITH JAK2, AND MUTAGENESIS OF ARG-555.
PubMed=10757801; DOI=10.1128/mcb.20.9.3168-3177.2000;
Rui L., Gunter D.R., Herrington J., Carter-Su C.;
"Differential binding to and regulation of JAK2 by the SH2 domain and N-
terminal region of SH2-bbeta.";
Mol. Cell. Biol. 20:3168-3177(2000).
[9]
FUNCTION, SUBUNIT, AND INTERACTION WITH SH2B2.
PubMed=11238898; DOI=10.1128/mcb.21.5.1613-1620.2001;
Qian X., Ginty D.D.;
"SH2-B and APS are multimeric adapters that augment TrkA signaling.";
Mol. Cell. Biol. 21:1613-1620(2001).
[10]
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).
[11]
FUNCTION IN ACTIN REORGANIZATION, AND INTERACTION WITH RAC1.
PubMed=11786545; DOI=10.1074/jbc.m111138200;
Diakonova M., Gunter D.R., Herrington J., Carter-Su C.;
"SH2-Bbeta is a Rac-binding protein that regulates cell motility.";
J. Biol. Chem. 277:10669-10677(2002).
[12]
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]
PHOSPHORYLATION AT TYR-439 AND TYR-494, AND MUTAGENESIS OF TYR-439 AND
TYR-494.
PubMed=12551917; DOI=10.1074/jbc.m210765200;
O'Brien K.B., Argetsinger L.S., Diakonova M., Carter-Su C.;
"YXXL motifs in SH2-Bbeta are phosphorylated by JAK2, JAK1, and platelet-
derived growth factor receptor and are required for membrane ruffling.";
J. Biol. Chem. 278:11970-11978(2003).
[14]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-231 AND LEU-233.
PubMed=15082760; DOI=10.1128/mcb.24.9.3633-3647.2004;
Chen L., Carter-Su C.;
"Adapter protein SH2-B beta undergoes nucleocytoplasmic shuttling:
implications for nerve growth factor induction of neuronal
differentiation.";
Mol. Cell. Biol. 24:3633-3647(2004).
[15]
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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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:10377387,
ECO:0000269|PubMed:10473609, ECO:0000269|PubMed:10757801,
ECO:0000269|PubMed:11238898, ECO:0000269|PubMed:11786545,
ECO:0000269|PubMed:16569669, ECO:0000269|PubMed:9343427,
ECO:0000269|PubMed:9856458}.
-!- SUBUNIT: Self-associates. Homopentamer. Forms a heteromultimeric
complex with SH2B2. 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 1 interacts via its SH2 domain with INSR; the
interaction requires receptor activation. Isoform 1 interacts with
IGF1R; the interaction requires receptor activation. Isoform 2
interacts via its SH2 domain with FGFR3. Isoform 2 interacts with RET;
the interaction requires RET kinase activity. Isoform 2 interacts with
RAC1. Isoform 2 interacts with PDGFRA and/or PDGFRB; the interaction
requires receptor activation. Interacts with ISR1 and ISR2. 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 (By
similarity). May interact with FCER1G. Interacts (via SH2 domain) with
NTRK1 (phosphorylated). {ECO:0000250, ECO:0000269|PubMed:10757801,
ECO:0000269|PubMed:11238898, ECO:0000269|PubMed:11751854,
ECO:0000269|PubMed:11786545, ECO:0000269|PubMed:11827956,
ECO:0000269|PubMed:16569669, ECO:0000269|PubMed:9343427,
ECO:0000269|PubMed:9636306, ECO:0000269|PubMed:9694882,
ECO:0000269|PubMed:9856458}.
-!- INTERACTION:
Q62985; P07949: RET; Xeno; NbExp=3; IntAct=EBI-7395583, EBI-2480756;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15082760}. Membrane
{ECO:0000305|PubMed:15082760}. Nucleus {ECO:0000269|PubMed:15082760}.
Note=Shuttles between the nucleus and the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q62985-1; Sequence=Displayed;
Name=2;
IsoId=Q62985-2; Sequence=VSP_032045;
-!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed. Expressed in
epididymal adipose tissue, liver and skeletal muscle.
{ECO:0000269|PubMed:9742218}.
-!- PTM: Phosphorylated on tyrosine residues in response to treatment with
growth hormone (GH), IFN-gamma (IFNG), BDNF, PDGF and FGF.
Phosphorylated on tyrosine residues by JAK2 and JAK1. Phosphorylated on
multiple serine and threonine residues in response to treatment with
NGF. Phosphorylated on serine residues. {ECO:0000269|PubMed:10473609,
ECO:0000269|PubMed:11751854, ECO:0000269|PubMed:12551917,
ECO:0000269|PubMed:9343427, ECO:0000269|PubMed:9856458}.
-!- SIMILARITY: Belongs to the SH2B adapter family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; U57391; AAC52601.1; -; mRNA.
EMBL; AF047577; AAC04575.1; -; mRNA.
RefSeq; NP_001041645.1; NM_001048180.1.
RefSeq; NP_604451.2; NM_134456.3. [Q62985-1]
RefSeq; XP_006230415.1; XM_006230353.3. [Q62985-1]
RefSeq; XP_006230416.1; XM_006230354.3. [Q62985-1]
SMR; Q62985; -.
BioGrid; 250140; 5.
IntAct; Q62985; 37.
MINT; Q62985; -.
STRING; 10116.ENSRNOP00000066048; -.
iPTMnet; Q62985; -.
PaxDb; Q62985; -.
PRIDE; Q62985; -.
Ensembl; ENSRNOT00000074274; ENSRNOP00000066048; ENSRNOG00000049181. [Q62985-1]
GeneID; 89817; -.
KEGG; rno:89817; -.
CTD; 25970; -.
RGD; 620132; Sh2b1.
eggNOG; ENOG410IMWK; Eukaryota.
eggNOG; ENOG41102PH; LUCA.
GeneTree; ENSGT00950000183191; -.
InParanoid; Q62985; -.
KO; K12459; -.
OMA; MLEHFRM; -.
OrthoDB; 556279at2759; -.
PhylomeDB; Q62985; -.
Reactome; R-RNO-1170546; Prolactin receptor signaling.
Reactome; R-RNO-982772; Growth hormone receptor signaling.
Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
PRO; PR:Q62985; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000049181; Expressed in skeletal muscle tissue and 9 other tissues.
ExpressionAtlas; Q62985; baseline and differential.
Genevisible; Q62985; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:RGD.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:RGD.
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;
Alternative splicing; Cytoplasm; Membrane; Methylation; Nucleus;
Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1..756
/note="SH2B adapter protein 1"
/id="PRO_0000323611"
DOMAIN 247..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)"
REGION 24..85
/note="Required for self-association"
/evidence="ECO:0000250"
REGION 85..196
/note="Interaction with RAC1"
/evidence="ECO:0000269|PubMed:11786545"
REGION 100..243
/note="Required for NGF signaling"
REGION 224..233
/note="Required for nuclear localization"
MOD_RES 88
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91ZM2"
MOD_RES 96
/note="Phosphoserine; by MAPK1 or MAPK3; in vitro"
/evidence="ECO:0000269|PubMed:10473609"
MOD_RES 270
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:Q9NRF2"
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:0000269|PubMed:12551917"
MOD_RES 494
/note="Phosphotyrosine; by JAK1, JAK2"
/evidence="ECO:0000269|PubMed:12551917"
VAR_SEQ 632..756
/note="ERSTSRDPTQPSEPPPWTDPPHPGAEEASGAPEVAAATAAAAKERQEKEKAG
GGGVQEELVPMAELVPMAELEEAIAPGTEAQGGAGSSGDLEVSLMVQLQQLPLGGNGEE
GGHPRAINNQYSFV -> GREQAGSHAGVCEGDRCYPDASSTFLPFGASDCVTEHFP
(in isoform 2)"
/evidence="ECO:0000303|PubMed:9343427"
/id="VSP_032045"
MUTAGEN 96
/note="S->A: Reduces in vitro phosphorylation by MAPK1
and/or MAPK3."
/evidence="ECO:0000269|PubMed:10473609"
MUTAGEN 231
/note="L->A: Abolishes nuclear localization; when
associated with A-233."
/evidence="ECO:0000269|PubMed:15082760"
MUTAGEN 233
/note="L->A: Abolishes nuclear localization; when
associated with A-231."
/evidence="ECO:0000269|PubMed:15082760"
MUTAGEN 439
/note="Y->F: Fails to enhance GH-induced membrane ruffling;
when associated with F-494."
/evidence="ECO:0000269|PubMed:12551917"
MUTAGEN 439
/note="Y->F: Reduces phosphorylation by JAK1, JAK2 and
PDGFRA."
/evidence="ECO:0000269|PubMed:12551917"
MUTAGEN 494
/note="Y->F: Fails to enhance GH-induced membrane ruffling;
when associated with F-439."
/evidence="ECO:0000269|PubMed:12551917"
MUTAGEN 494
/note="Y->F: Reduces phosphorylation by JAK1 and JAK2."
/evidence="ECO:0000269|PubMed:12551917"
MUTAGEN 555
/note="R->E: Reduces interaction with JAK2 and abolishes
JAK2 kinase activity; reduces GH-stimulated cell motility;
abolishes interaction with PDGFRA."
/evidence="ECO:0000269|PubMed:10377387,
ECO:0000269|PubMed:10757801"
CONFLICT 211
/note="R -> K (in Ref. 2; AAC04575)"
/evidence="ECO:0000305"
SEQUENCE 756 AA; 79637 MW; D4FCF3086CF3DFE0 CRC64;
MNGAPSPEDG VFPSPPALPP PPPPSWQEFC ESHARAAALD LARRFRLYLA SHPQYAEPGA
EAAFSGRFAE LFLQHFEAEV ARASGSLSPP VLAPLSPGVE IPPSHDLSLE SCRVGGPLAV
LGPSRSSEDL AGPLPSSVSS STTSSKPKLK KRFSLRSVGR SVRGSVRGIL QWRGAVESPS
QAGPLETTSG PPVLGGNSNS NSSGGAGTVG RALANDGTSP GERWTHRFER LRLSRGGGTL
RDGAGVIQRE ELLSFMGAEE AAPDPAGVGR GGGAAGLTSG GGGQPQWQKC RLLLRSEGEG
GGGSRLEFFV PPKASRPRLS IPCSTITDVR TATALEMPDR ENTFVVKVEG PSEYILETTD
ALHVKAWVSD IQECLSPGPC PAISPRPMTL PLAPGTSFLT KDNTESLELP CLNHSESLPS
QDLLLGPSES NDRLSQGAYG GLSDRPSASF SPSSASIAAS HFDSMELLPP ELPPRIPIEE
GPPAGTVHPL STPYPPLDTP EAATGSFLFQ GEAEGGEGDQ PLSGYPWFHG MLSRLKAAQL
VLEGGTSSHG VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM
LEHFRVHPIP LESGGSSDVV LVSYVPSQRQ QERSTSRDPT QPSEPPPWTD PPHPGAEEAS
GAPEVAAATA AAAKERQEKE KAGGGGVQEE LVPMAELVPM AELEEAIAPG TEAQGGAGSS
GDLEVSLMVQ LQQLPLGGNG EEGGHPRAIN NQYSFV


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EIAAB38183 Homo sapiens,Human,SCAP,SH2 domain-containing adapter protein,SH2 domain-containing protein 2A,SH2D2A,T cell-specific adapter protein,TSAd,TSAD,VEGF receptor-associated protein,VRAP
EIAAB11725 Adapter protein containing PH domain, PTB domain and leucine zipper motif 2,Appl2,DCC-interacting protein 13-beta,Dip13b,Dip13-beta,Dip3b,Mouse,Mus musculus
EIAAB11724 Adapter protein containing PH domain, PTB domain and leucine zipper motif 2,APPL2,DCC-interacting protein 13-beta,DIP13B,Dip13-beta,Homo sapiens,Human
EIAAB11722 Adapter protein containing PH domain, PTB domain and leucine zipper motif 1,Appl1,DCC-interacting protein 13-alpha,Dip13a,Dip13-alpha,Kiaa1428,Mouse,Mus musculus
EIAAB11723 Adapter protein containing PH domain, PTB domain and leucine zipper motif 1,APPL,APPL1,DCC-interacting protein 13-alpha,DIP13A,Dip13-alpha,Homo sapiens,Human,KIAA1428
U1600c CLIA BASH,B-cell adapter SH2 domain-containing protein,B-cell linker protein,BLNK,Chicken,Cytoplasmic adapter protein,Gallus gallus,SLP-65,Src homology 2 domain-containing leukocyte protein of 65 kDa 96T
Pathways :
WP1654: gamma-Hexachlorocyclohexane degradation
WP2292: Chemokine signaling pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1049: G Protein Signaling Pathways
WP73: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1673: Naphthalene and anthracene degradation
WP211: BMP signaling pathway
WP2199: Seed Development
WP931: G Protein Signaling Pathways
WP2032: TSH signaling pathway
WP813: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP2272: Pathogenic Escherichia coli infection
WP1502: Mitochondrial biogenesis
WP1665: Limonene and pinene degradation
WP232: G Protein Signaling Pathways
WP35: G Protein Signaling Pathways
WP2203: TSLP Signaling Pathway
WP1493: Carbon assimilation C4 pathway
WP1692: Protein export
WP1657: Glycerolipid metabolism
WP1663: Homologous recombination
WP346: Protein Modifications
WP1713: Two-component system

Related Genes :
[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)
[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)
[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)
[Grb2] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (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)
[NCK1 NCK] Cytoplasmic protein NCK1 (NCK adaptor protein 1) (Nck-1) (SH2/SH3 adaptor protein NCK-alpha)
[Grb2 Ash] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[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)
[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)
[Shc1 Shc ShcA] SHC-transforming protein 1 (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[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)
[SH2D2A SCAP TSAD VRAP] SH2 domain-containing protein 2A (SH2 domain-containing adapter protein) (T cell-specific adapter protein) (TSAd) (VEGF receptor-associated protein)
[Shb] SH2 domain-containing adapter protein B
[Shc1] SHC-transforming protein 1 (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[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)
[SHB] SH2 domain-containing adapter protein B
[BCAR3 NSP2 SH2D3B UNQ271/PRO308] Breast cancer anti-estrogen resistance protein 3 (Novel SH2-containing protein 2) (SH2 domain-containing protein 3B)
[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)
[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) (Protein 51C) (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)
[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)
[NCK2 GRB4] Cytoplasmic protein NCK2 (Growth factor receptor-bound protein 4) (NCK adaptor protein 2) (Nck-2) (SH2/SH3 adaptor protein NCK-beta)
[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)
[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)
[LCP2] Lymphocyte cytosolic protein 2 (SH2 domain-containing leukocyte protein of 76 kDa) (SLP-76 tyrosine phosphoprotein) (SLP76)
[Socs3 Cis3 Cish3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (Protein EF-10)

Bibliography :
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