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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.
16-OCT-2019, entry version 133.
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:
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; 2.
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 10 organ(s), highest expression level in skeletal muscle tissue.
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; 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.
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; Complete proteome; Cytoplasm; Membrane;
Methylation; Nucleus; Phosphoprotein; Reference proteome; SH2 domain.
CHAIN 1 756 SH2B adapter protein 1.
/FTId=PRO_0000323611.
DOMAIN 247 376 PH.
DOMAIN 527 625 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 1 555 Interaction with JAK2 (low-affinity
binding; independent of JAK2
phosphorylation).
REGION 24 85 Required for self-association.
{ECO:0000250}.
REGION 85 196 Interaction with RAC1.
{ECO:0000269|PubMed:11786545}.
REGION 100 243 Required for NGF signaling.
REGION 224 233 Required for nuclear localization.
MOD_RES 88 88 Phosphoserine.
{ECO:0000250|UniProtKB:Q91ZM2}.
MOD_RES 96 96 Phosphoserine; by MAPK1 or MAPK3; in
vitro. {ECO:0000269|PubMed:10473609}.
MOD_RES 270 270 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9NRF2}.
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:0000269|PubMed:12551917}.
MOD_RES 494 494 Phosphotyrosine; by JAK1, JAK2.
{ECO:0000269|PubMed:12551917}.
VAR_SEQ 632 756 ERSTSRDPTQPSEPPPWTDPPHPGAEEASGAPEVAAATAAA
AKERQEKEKAGGGGVQEELVPMAELVPMAELEEAIAPGTEA
QGGAGSSGDLEVSLMVQLQQLPLGGNGEEGGHPRAINNQYS
FV -> GREQAGSHAGVCEGDRCYPDASSTFLPFGASDCVT
EHFP (in isoform 2).
{ECO:0000303|PubMed:9343427}.
/FTId=VSP_032045.
MUTAGEN 96 96 S->A: Reduces in vitro phosphorylation by
MAPK1 and/or MAPK3.
{ECO:0000269|PubMed:10473609}.
MUTAGEN 231 231 L->A: Abolishes nuclear localization;
when associated with A-233.
{ECO:0000269|PubMed:15082760}.
MUTAGEN 233 233 L->A: Abolishes nuclear localization;
when associated with A-231.
{ECO:0000269|PubMed:15082760}.
MUTAGEN 439 439 Y->F: Fails to enhance GH-induced
membrane ruffling; when associated with
F-494. {ECO:0000269|PubMed:12551917}.
MUTAGEN 439 439 Y->F: Reduces phosphorylation by JAK1,
JAK2 and PDGFRA.
{ECO:0000269|PubMed:12551917}.
MUTAGEN 494 494 Y->F: Fails to enhance GH-induced
membrane ruffling; when associated with
F-439. {ECO:0000269|PubMed:12551917}.
MUTAGEN 494 494 Y->F: Reduces phosphorylation by JAK1 and
JAK2. {ECO:0000269|PubMed:12551917}.
MUTAGEN 555 555 R->E: Reduces interaction with JAK2 and
abolishes JAK2 kinase activity; reduces
GH-stimulated cell motility; abolishes
interaction with PDGFRA.
{ECO:0000269|PubMed:10377387,
ECO:0000269|PubMed:10757801}.
CONFLICT 211 211 R -> K (in Ref. 2; AAC04575).
{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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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