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SH2 domain-containing adapter protein B

 SHB_HUMAN               Reviewed;         509 AA.
Q15464; B9EGM0; D3DRQ5; Q504U5; Q5VUM8;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
25-JUL-2006, sequence version 2.
25-OCT-2017, entry version 136.
RecName: Full=SH2 domain-containing adapter protein B;
Name=SHB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
INTERACTION WITH PDGFRB.
TISSUE=Fetal brain;
PubMed=8302579;
Welsh M., Mares J., Karlsson T., Lavergne C., Breant B.,
Claesson-Welsh L.;
"Shb is a ubiquitously expressed Src homology 2 protein.";
Oncogene 9:19-27(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Testis;
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).
[5]
INTERACTION WITH PDGFRB; FGFR1; EPS8 AND V-SRC.
PubMed=7537362;
Karlsson T., Songyang Z., Landgren E., Lavergne C., Di Fiore P.P.,
Anafi M., Pawson T., Cantley L.C., Claesson-Welsh L., Welsh M.;
"Molecular interactions of the Src homology 2 domain protein Shb with
phosphotyrosine residues, tyrosine kinase receptors and Src homology 3
domain proteins.";
Oncogene 10:1475-1483(1995).
[6]
FUNCTION.
PubMed=8806685;
Karlsson T., Welsh M.;
"Apoptosis of NIH3T3 cells overexpressing the Src homology 2 domain
protein Shb.";
Oncogene 13:955-961(1996).
[7]
FUNCTION.
PubMed=9751119;
Karlsson T., Kullander K., Welsh M.;
"The Src homology 2 domain protein Shb transmits basic fibroblast
growth factor- and nerve growth factor-dependent differentiation
signals in PC12 cells.";
Cell Growth Differ. 9:757-766(1998).
[8]
FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH GRB2; GRAP AND CD3Z,
AND MUTAGENESIS OF ARG-435.
PubMed=9484780; DOI=10.1038/sj.onc.1201607;
Welsh M., Songyang Z., Frantz J.D., Trueb T., Reedquist K.A.,
Karlsson T., Miyazaki M., Cantley L.C., Band H., Shoelson S.E.;
"Stimulation through the T cell receptor leads to interactions between
SHB and several signaling proteins.";
Oncogene 16:891-901(1998).
[9]
PHOSPHORYLATION, AND INTERACTION WITH LAT AND PLCG1.
PubMed=10488157; DOI=10.1074/jbc.274.39.28050;
Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M.;
"Requirement of the Src homology 2 domain protein Shb for T cell
receptor-dependent activation of the interleukin-2 gene nuclear factor
for activation of T cells element in Jurkat T cells.";
J. Biol. Chem. 274:28050-28057(1999).
[10]
FUNCTION.
PubMed=10828022;
Dixelius J., Larsson H., Sasaki T., Holmqvist K., Lu L., Engstroem A.,
Timpl R., Welsh M., Claesson-Welsh L.;
"Endostatin-induced tyrosine kinase signaling through the Shb adaptor
protein regulates endothelial cell apoptosis.";
Blood 95:3403-3411(2000).
[11]
FUNCTION, AND INTERACTION WITH PDGFRA.
PubMed=10837138; DOI=10.1006/excr.2000.4896;
Hooshmand-Rad R., Lu L., Heldin C.-H., Claesson-Welsh L., Welsh M.;
"Platelet-derived growth factor-mediated signaling through the Shb
adaptor protein: effects on cytoskeletal organization.";
Exp. Cell Res. 257:245-254(2000).
[12]
INTERACTION WITH CRK.
PubMed=10964504; DOI=10.1006/excr.2000.4984;
Lu L., Anneren C., Reedquist K.A., Bos J.L., Welsh M.;
"NGF-dependent neurite outgrowth in PC12 cells overexpressing the Src
homology 2-domain protein shb requires activation of the Rap1
pathway.";
Exp. Cell Res. 259:370-377(2000).
[13]
INTERACTION WITH IL2RB; IL2RG; JAK1 AND JAK3.
PubMed=12200137; DOI=10.1016/S0006-291X(02)02016-8;
Lindholm C.K.;
"IL-2 receptor signaling through the Shb adapter protein in T and NK
cells.";
Biochem. Biophys. Res. Commun. 296:929-936(2002).
[14]
FUNCTION, INTERACTION WITH ZAP70; LCP2; VAV1 AND GRAP2, AND
SUBCELLULAR LOCATION.
PubMed=12084069; DOI=10.1046/j.1432-1033.2002.03008.x;
Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.;
"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.";
Eur. J. Biochem. 269:3279-3288(2002).
[15]
INTERACTION WITH FGFR1.
PubMed=12181353; DOI=10.1091/mbc.E02-02-0103;
Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M.,
Claesson-Welsh L.;
"The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and
regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in
endothelial cells.";
Mol. Biol. Cell 13:2881-2893(2002).
[16]
FUNCTION, AND INTERACTION WITH IRS2.
PubMed=12520086;
Welsh N., Makeeva N., Welsh M.;
"Overexpression of the Shb SH2 domain-protein in insulin-producing
cells leads to altered signaling through the IRS-1 and IRS-2
proteins.";
Mol. Med. 8:695-704(2002).
[17]
FUNCTION, AND INTERACTION WITH PTK2/FAK1.
PubMed=12464388; DOI=10.1016/S0898-6568(02)00076-1;
Holmqvist K., Cross M.J., Riley D., Welsh M.;
"The Shb adaptor protein causes Src-dependent cell spreading and
activation of focal adhesion kinase in murine brain endothelial
cells.";
Cell. Signal. 15:171-179(2003).
[18]
FUNCTION, AND INTERACTION WITH KDR.
PubMed=15026417; DOI=10.1074/jbc.M312729200;
Holmqvist K., Cross M.J., Rolny C., Haegerkvist R., Rahimi N.,
Matsumoto T., Claesson-Welsh L., Welsh M.;
"The adaptor protein shb binds to tyrosine 1175 in vascular
endothelial growth factor (VEGF) receptor-2 and regulates VEGF-
dependent cellular migration.";
J. Biol. Chem. 279:22267-22275(2004).
[19]
FUNCTION.
PubMed=15919073; DOI=10.1016/j.yexcr.2005.04.020;
Rolny C., Lu L., Aagren N., Nilsson I., Roe C., Webb G.C., Welsh M.;
"Shb promotes blood vessel formation in embryoid bodies by augmenting
vascular endothelial growth factor receptor-2 and platelet-derived
growth factor receptor-beta signaling.";
Exp. Cell Res. 308:381-393(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, 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).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-307 AND
SER-388, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
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).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-187, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Adapter protein which regulates several signal
transduction cascades by linking activated receptors to downstream
signaling components. May play a role in angiogenesis by
regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role
in T-cell antigen receptor/TCR signaling, interleukin-2 signaling,
apoptosis and neuronal cells differentiation by mediating basic-
FGF and NGF-induced signaling cascades. May also regulate IRS1 and
IRS2 signaling in insulin-producing cells.
{ECO:0000269|PubMed:10828022, ECO:0000269|PubMed:10837138,
ECO:0000269|PubMed:12084069, ECO:0000269|PubMed:12464388,
ECO:0000269|PubMed:12520086, ECO:0000269|PubMed:15026417,
ECO:0000269|PubMed:15919073, ECO:0000269|PubMed:8806685,
ECO:0000269|PubMed:9484780, ECO:0000269|PubMed:9751119}.
-!- SUBUNIT: Interacts with PTPN11 (By similarity). Interacts with
phosphorylated 'Tyr-720' of the ligand-activated receptor PDGFRA
via its SH2 domain. Interacts with the ligand-activated receptors
PDGFRB, FGFR1, KDR/VEGFR2, IL2RB and IL2RG. Interacts with EPS8
and V-SRC. Interacts with GRB2 and GRAP. Interacts with CD3Z.
Interacts with tyrosine-phosphorylated LAT upon T-cell antigen
receptor activation. Interacts with PLCG1. Interacts with ZAP70,
LCP2/SLP-76, VAV1 and GRAP2. Interacts with JAK1 and JAK3.
Interacts with PTK2/FAK1. Interacts with CRK/CrKII. Interacts with
IRS2. {ECO:0000250, ECO:0000269|PubMed:10488157,
ECO:0000269|PubMed:10837138, ECO:0000269|PubMed:10964504,
ECO:0000269|PubMed:12084069, ECO:0000269|PubMed:12181353,
ECO:0000269|PubMed:12200137, ECO:0000269|PubMed:12464388,
ECO:0000269|PubMed:12520086, ECO:0000269|PubMed:15026417,
ECO:0000269|PubMed:7537362, ECO:0000269|PubMed:8302579,
ECO:0000269|PubMed:9484780}.
-!- INTERACTION:
P00519:ABL1; NbExp=5; IntAct=EBI-4402156, EBI-375543;
P10721:KIT; NbExp=2; IntAct=EBI-4402156, EBI-1379503;
P08581:MET; NbExp=4; IntAct=EBI-4402156, EBI-1039152;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
membrane protein; Cytoplasmic side. Note=Associates with membrane
lipid rafts upon TCR stimulation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15464-1; Sequence=Displayed;
Name=2;
IsoId=Q15464-2; Sequence=VSP_019846, VSP_019847;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:9484780}.
-!- DOMAIN: The SH2 domain preferentially binds phosphopeptides with
the consensus sequence Y-[TVI]-X-L and mediates interaction with
PDGFRA, PDGFRB, FGRFR1, IL2RB, IL2RG, CD3Z and CRK/CrKII.
-!- PTM: Phosphorylated upon PDGFRA, PDGFRB, TCR, IL2 receptor, FGFR1
or VEGFR2 activation. {ECO:0000269|PubMed:10488157}.
-!- SEQUENCE CAUTION:
Sequence=AAH94765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA53091.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X75342; CAA53091.1; ALT_INIT; mRNA.
EMBL; AL583849; CAH73120.1; -; Genomic_DNA.
EMBL; AL138752; CAH73120.1; JOINED; Genomic_DNA.
EMBL; AL161448; CAH73120.1; JOINED; Genomic_DNA.
EMBL; AL161448; CAH73192.1; -; Genomic_DNA.
EMBL; AL138752; CAH73192.1; JOINED; Genomic_DNA.
EMBL; AL583849; CAH73192.1; JOINED; Genomic_DNA.
EMBL; AL138752; CAI13876.1; -; Genomic_DNA.
EMBL; AL161448; CAI13876.1; JOINED; Genomic_DNA.
EMBL; AL583849; CAI13876.1; JOINED; Genomic_DNA.
EMBL; CH471071; EAW58254.1; -; Genomic_DNA.
EMBL; CH471071; EAW58255.1; -; Genomic_DNA.
EMBL; BC094765; AAH94765.1; ALT_INIT; mRNA.
EMBL; BC136581; AAI36582.1; -; mRNA.
EMBL; BC136582; AAI36583.1; -; mRNA.
CCDS; CCDS43806.1; -. [Q15464-1]
PIR; I38228; I38228.
RefSeq; NP_003019.2; NM_003028.2. [Q15464-1]
UniGene; Hs.521482; -.
ProteinModelPortal; Q15464; -.
SMR; Q15464; -.
BioGrid; 112358; 21.
IntAct; Q15464; 9.
MINT; MINT-7046528; -.
STRING; 9606.ENSP00000366936; -.
BindingDB; Q15464; -.
iPTMnet; Q15464; -.
PhosphoSitePlus; Q15464; -.
BioMuta; SHB; -.
DMDM; 110816415; -.
EPD; Q15464; -.
MaxQB; Q15464; -.
PaxDb; Q15464; -.
PeptideAtlas; Q15464; -.
PRIDE; Q15464; -.
Ensembl; ENST00000377707; ENSP00000366936; ENSG00000107338. [Q15464-1]
GeneID; 6461; -.
KEGG; hsa:6461; -.
UCSC; uc004aax.4; human. [Q15464-1]
CTD; 6461; -.
DisGeNET; 6461; -.
EuPathDB; HostDB:ENSG00000107338.9; -.
GeneCards; SHB; -.
H-InvDB; HIX0008049; -.
H-InvDB; HIX0079163; -.
H-InvDB; HIX0189186; -.
HGNC; HGNC:10838; SHB.
HPA; CAB010161; -.
HPA; HPA049911; -.
HPA; HPA052108; -.
MIM; 600314; gene.
neXtProt; NX_Q15464; -.
OpenTargets; ENSG00000107338; -.
PharmGKB; PA35744; -.
eggNOG; ENOG410IGWI; Eukaryota.
eggNOG; ENOG410XQJ2; LUCA.
GeneTree; ENSGT00390000015203; -.
GeneTree; ENSGT00900000142236; -.
HOGENOM; HOG000038038; -.
HOVERGEN; HBG066172; -.
InParanoid; Q15464; -.
OMA; RPDYREQ; -.
OrthoDB; EOG091G0I06; -.
PhylomeDB; Q15464; -.
TreeFam; TF325799; -.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
SignaLink; Q15464; -.
ChiTaRS; SHB; human.
GeneWiki; SHB_(gene); -.
GenomeRNAi; 6461; -.
PRO; PR:Q15464; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000107338; -.
CleanEx; HS_SHB; -.
Genevisible; Q15464; HS.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
GO; GO:1900194; P:negative regulation of oocyte maturation; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0045624; P:positive regulation of T-helper cell differentiation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd10389; SH2_SHB; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR035040; SHB.
InterPro; IPR035045; SHB_SH2.
PANTHER; PTHR15127:SF31; PTHR15127:SF31; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Apoptosis; Cell membrane;
Complete proteome; Cytoplasm; Developmental protein; Differentiation;
Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
SH2 domain; Ubl conjugation.
CHAIN 1 509 SH2 domain-containing adapter protein B.
/FTId=PRO_0000246324.
DOMAIN 410 504 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 1 410 Mediates interaction with LAT, PTK2/FAK1,
JAK1 and JAK3.
{ECO:0000269|PubMed:10488157,
ECO:0000269|PubMed:12200137}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
CROSSLNK 187 187 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 280 297 EFQRQESVRSQHKGIQLY -> GLQEAWRHSPSGCFPVGP
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019846.
VAR_SEQ 298 509 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_019847.
MUTAGEN 435 435 R->K: Loss of interaction with CD3Z.
Alters LAT, PLCG1, VAV1 and LCP2
phosphorylation, MAP kinase signaling,
Rac1 and JNK activation, intracellular
calcium increase, activation of the
nuclear factor for activation of T-cells
and subsequent interleukin-2 expression
which normally occur upon T-cells
stimulation.
{ECO:0000269|PubMed:9484780}.
CONFLICT 91 93 DFE -> HFQ (in Ref. 1; CAA53091).
{ECO:0000305}.
CONFLICT 347 347 I -> S (in Ref. 1; CAA53091).
{ECO:0000305}.
CONFLICT 445 445 S -> P (in Ref. 1; CAA53091).
{ECO:0000305}.
SEQUENCE 509 AA; 55042 MW; 15C392A6EEB761D6 CRC64;
MAKWLNKYFS LGNSKTKSPP QPPRPDYREQ RRRGERPSQP PQAVPQASSA ASASCGPATA
SCFSASSGSL PDDSGSTSDL IRAYRAQKER DFEDPYNGPG SSLRKLRAMC RLDYCGGSGE
PGGVQRAFSA SSASGAAGCC CASSGAGAAA SSSSSSGSPH LYRSSSERRP ATPAEVRYIS
PKHRLIKVES AAGGGAGDPL GGACAGGRTW SPTACGGKKL LNKCAASAAE ESGAGKKDKV
TIADDYSDPF DAKNDLKSKA GKGESAGYME PYEAQRIMTE FQRQESVRSQ HKGIQLYDTP
YEPEGQSVDS DSESTVSPRL RESKLPQDDD RPADEYDQPW EWNRVTIPAL AAQFNGNEKR
QSSPSPSRDR RRQLRAPGGG FKPIKHGSPE FCGILGERVD PAVPLEKQIW YHGAISRGDA
ENLLRLCKEC SYLVRNSQTS KHDYSLSLRS NQGFMHMKLA KTKEKYVLGQ NSPPFDSVPE
VIHYYTTRKL PIKGAEHLSL LYPVAVRTL


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