SHB_HUMAN
ID SHB_HUMAN Reviewed; 509 AA.
AC Q15464; B9EGM0; D3DRQ5; Q504U5; Q5VUM8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=SH2 domain-containing adapter protein B;
GN Name=SHB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PDGFRB.
RC TISSUE=Fetal brain;
RX PubMed=8302579;
RA Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L.;
RT "Shb is a ubiquitously expressed Src homology 2 protein.";
RL Oncogene 9:19-27(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH PDGFRB; FGFR1; EPS8 AND V-SRC.
RX PubMed=7537362;
RA Karlsson T., Songyang Z., Landgren E., Lavergne C., Di Fiore P.P.,
RA Anafi M., Pawson T., Cantley L.C., Claesson-Welsh L., Welsh M.;
RT "Molecular interactions of the Src homology 2 domain protein Shb with
RT phosphotyrosine residues, tyrosine kinase receptors and Src homology 3
RT domain proteins.";
RL Oncogene 10:1475-1483(1995).
RN [6]
RP FUNCTION.
RX PubMed=8806685;
RA Karlsson T., Welsh M.;
RT "Apoptosis of NIH3T3 cells overexpressing the Src homology 2 domain protein
RT Shb.";
RL Oncogene 13:955-961(1996).
RN [7]
RP FUNCTION.
RX PubMed=9751119;
RA Karlsson T., Kullander K., Welsh M.;
RT "The Src homology 2 domain protein Shb transmits basic fibroblast growth
RT factor- and nerve growth factor-dependent differentiation signals in PC12
RT cells.";
RL Cell Growth Differ. 9:757-766(1998).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH GRB2; GRAP AND CD3Z, AND
RP MUTAGENESIS OF ARG-435.
RX PubMed=9484780; DOI=10.1038/sj.onc.1201607;
RA Welsh M., Songyang Z., Frantz J.D., Trueb T., Reedquist K.A., Karlsson T.,
RA Miyazaki M., Cantley L.C., Band H., Shoelson S.E.;
RT "Stimulation through the T cell receptor leads to interactions between SHB
RT and several signaling proteins.";
RL Oncogene 16:891-901(1998).
RN [9]
RP PHOSPHORYLATION, AND INTERACTION WITH LAT AND PLCG1.
RX PubMed=10488157; DOI=10.1074/jbc.274.39.28050;
RA Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M.;
RT "Requirement of the Src homology 2 domain protein Shb for T cell receptor-
RT dependent activation of the interleukin-2 gene nuclear factor for
RT activation of T cells element in Jurkat T cells.";
RL J. Biol. Chem. 274:28050-28057(1999).
RN [10]
RP FUNCTION.
RX PubMed=10828022;
RA Dixelius J., Larsson H., Sasaki T., Holmqvist K., Lu L., Engstroem A.,
RA Timpl R., Welsh M., Claesson-Welsh L.;
RT "Endostatin-induced tyrosine kinase signaling through the Shb adaptor
RT protein regulates endothelial cell apoptosis.";
RL Blood 95:3403-3411(2000).
RN [11]
RP FUNCTION, AND INTERACTION WITH PDGFRA.
RX PubMed=10837138; DOI=10.1006/excr.2000.4896;
RA Hooshmand-Rad R., Lu L., Heldin C.-H., Claesson-Welsh L., Welsh M.;
RT "Platelet-derived growth factor-mediated signaling through the Shb adaptor
RT protein: effects on cytoskeletal organization.";
RL Exp. Cell Res. 257:245-254(2000).
RN [12]
RP INTERACTION WITH CRK.
RX PubMed=10964504; DOI=10.1006/excr.2000.4984;
RA Lu L., Anneren C., Reedquist K.A., Bos J.L., Welsh M.;
RT "NGF-dependent neurite outgrowth in PC12 cells overexpressing the Src
RT homology 2-domain protein shb requires activation of the Rap1 pathway.";
RL Exp. Cell Res. 259:370-377(2000).
RN [13]
RP INTERACTION WITH IL2RB; IL2RG; JAK1 AND JAK3.
RX PubMed=12200137; DOI=10.1016/s0006-291x(02)02016-8;
RA Lindholm C.K.;
RT "IL-2 receptor signaling through the Shb adapter protein in T and NK
RT cells.";
RL Biochem. Biophys. Res. Commun. 296:929-936(2002).
RN [14]
RP FUNCTION, INTERACTION WITH ZAP70; LCP2; VAV1 AND GRAP2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12084069; DOI=10.1046/j.1432-1033.2002.03008.x;
RA Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.;
RT "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells.";
RL Eur. J. Biochem. 269:3279-3288(2002).
RN [15]
RP INTERACTION WITH FGFR1.
RX PubMed=12181353; DOI=10.1091/mbc.e02-02-0103;
RA Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M.,
RA Claesson-Welsh L.;
RT "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates
RT the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells.";
RL Mol. Biol. Cell 13:2881-2893(2002).
RN [16]
RP FUNCTION, AND INTERACTION WITH IRS2.
RX PubMed=12520086; DOI=10.1007/bf03402033;
RA Welsh N., Makeeva N., Welsh M.;
RT "Overexpression of the Shb SH2 domain-protein in insulin-producing cells
RT leads to altered signaling through the IRS-1 and IRS-2 proteins.";
RL Mol. Med. 8:695-704(2002).
RN [17]
RP FUNCTION, AND INTERACTION WITH PTK2/FAK1.
RX PubMed=12464388; DOI=10.1016/s0898-6568(02)00076-1;
RA Holmqvist K., Cross M.J., Riley D., Welsh M.;
RT "The Shb adaptor protein causes Src-dependent cell spreading and activation
RT of focal adhesion kinase in murine brain endothelial cells.";
RL Cell. Signal. 15:171-179(2003).
RN [18]
RP FUNCTION, AND INTERACTION WITH KDR.
RX PubMed=15026417; DOI=10.1074/jbc.m312729200;
RA Holmqvist K., Cross M.J., Rolny C., Haegerkvist R., Rahimi N.,
RA Matsumoto T., Claesson-Welsh L., Welsh M.;
RT "The adaptor protein shb binds to tyrosine 1175 in vascular endothelial
RT growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular
RT migration.";
RL J. Biol. Chem. 279:22267-22275(2004).
RN [19]
RP FUNCTION.
RX PubMed=15919073; DOI=10.1016/j.yexcr.2005.04.020;
RA Rolny C., Lu L., Aagren N., Nilsson I., Roe C., Webb G.C., Welsh M.;
RT "Shb promotes blood vessel formation in embryoid bodies by augmenting
RT vascular endothelial growth factor receptor-2 and platelet-derived growth
RT factor receptor-beta signaling.";
RL Exp. Cell Res. 308:381-393(2005).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-307 AND SER-388, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-187, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Adapter protein which regulates several signal transduction
CC cascades by linking activated receptors to downstream signaling
CC components. May play a role in angiogenesis by regulating FGFR1, VEGFR2
CC and PDGFR signaling. May also play a role in T-cell antigen
CC receptor/TCR signaling, interleukin-2 signaling, apoptosis and neuronal
CC cells differentiation by mediating basic-FGF and NGF-induced signaling
CC cascades. May also regulate IRS1 and IRS2 signaling in insulin-
CC producing cells. {ECO:0000269|PubMed:10828022,
CC ECO:0000269|PubMed:10837138, ECO:0000269|PubMed:12084069,
CC ECO:0000269|PubMed:12464388, ECO:0000269|PubMed:12520086,
CC ECO:0000269|PubMed:15026417, ECO:0000269|PubMed:15919073,
CC ECO:0000269|PubMed:8806685, ECO:0000269|PubMed:9484780,
CC ECO:0000269|PubMed:9751119}.
CC -!- SUBUNIT: Interacts with PTPN11 (By similarity). Interacts with
CC phosphorylated 'Tyr-720' of the ligand-activated receptor PDGFRA via
CC its SH2 domain. Interacts with the ligand-activated receptors PDGFRB,
CC FGFR1, KDR/VEGFR2, IL2RB and IL2RG. Interacts with EPS8 and V-SRC.
CC Interacts with GRB2 and GRAP. Interacts with CD3Z. Interacts with
CC tyrosine-phosphorylated LAT upon T-cell antigen receptor activation.
CC Interacts with PLCG1. Interacts with ZAP70, LCP2/SLP-76, VAV1 and
CC GRAP2. Interacts with JAK1 and JAK3. Interacts with PTK2/FAK1.
CC Interacts with CRK/CrKII. Interacts with IRS2. {ECO:0000250,
CC ECO:0000269|PubMed:10488157, ECO:0000269|PubMed:10837138,
CC ECO:0000269|PubMed:10964504, ECO:0000269|PubMed:12084069,
CC ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:12200137,
CC ECO:0000269|PubMed:12464388, ECO:0000269|PubMed:12520086,
CC ECO:0000269|PubMed:15026417, ECO:0000269|PubMed:7537362,
CC ECO:0000269|PubMed:8302579, ECO:0000269|PubMed:9484780}.
CC -!- INTERACTION:
CC Q15464; P00519: ABL1; NbExp=5; IntAct=EBI-4402156, EBI-375543;
CC Q15464; P10721: KIT; NbExp=2; IntAct=EBI-4402156, EBI-1379503;
CC Q15464; P08581: MET; NbExp=4; IntAct=EBI-4402156, EBI-1039152;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Associates with membrane lipid rafts
CC upon TCR stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15464-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15464-2; Sequence=VSP_019846, VSP_019847;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9484780}.
CC -!- DOMAIN: The SH2 domain preferentially binds phosphopeptides with the
CC consensus sequence Y-[TVI]-X-L and mediates interaction with PDGFRA,
CC PDGFRB, FGRFR1, IL2RB, IL2RG, CD3Z and CRK/CrKII.
CC -!- PTM: Phosphorylated upon PDGFRA, PDGFRB, TCR, IL2 receptor, FGFR1 or
CC VEGFR2 activation. {ECO:0000269|PubMed:10488157}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA53091.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X75342; CAA53091.1; ALT_INIT; mRNA.
DR EMBL; AL138752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58254.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58255.1; -; Genomic_DNA.
DR EMBL; BC094765; AAH94765.1; ALT_INIT; mRNA.
DR EMBL; BC136581; AAI36582.1; -; mRNA.
DR EMBL; BC136582; AAI36583.1; -; mRNA.
DR CCDS; CCDS43806.1; -. [Q15464-1]
DR PIR; I38228; I38228.
DR RefSeq; NP_003019.2; NM_003028.2. [Q15464-1]
DR AlphaFoldDB; Q15464; -.
DR SMR; Q15464; -.
DR BioGRID; 112358; 68.
DR IntAct; Q15464; 15.
DR MINT; Q15464; -.
DR STRING; 9606.ENSP00000366936; -.
DR BindingDB; Q15464; -.
DR iPTMnet; Q15464; -.
DR PhosphoSitePlus; Q15464; -.
DR BioMuta; SHB; -.
DR DMDM; 110816415; -.
DR EPD; Q15464; -.
DR jPOST; Q15464; -.
DR MassIVE; Q15464; -.
DR MaxQB; Q15464; -.
DR PaxDb; Q15464; -.
DR PeptideAtlas; Q15464; -.
DR PRIDE; Q15464; -.
DR ProteomicsDB; 60600; -. [Q15464-1]
DR ProteomicsDB; 60601; -. [Q15464-2]
DR Antibodypedia; 4119; 286 antibodies from 30 providers.
DR DNASU; 6461; -.
DR Ensembl; ENST00000377707.4; ENSP00000366936.3; ENSG00000107338.10. [Q15464-1]
DR GeneID; 6461; -.
DR KEGG; hsa:6461; -.
DR MANE-Select; ENST00000377707.4; ENSP00000366936.3; NM_003028.3; NP_003019.2.
DR UCSC; uc004aax.4; human. [Q15464-1]
DR CTD; 6461; -.
DR DisGeNET; 6461; -.
DR GeneCards; SHB; -.
DR HGNC; HGNC:10838; SHB.
DR HPA; ENSG00000107338; Low tissue specificity.
DR MIM; 600314; gene.
DR neXtProt; NX_Q15464; -.
DR OpenTargets; ENSG00000107338; -.
DR PharmGKB; PA35744; -.
DR VEuPathDB; HostDB:ENSG00000107338; -.
DR eggNOG; ENOG502RT81; Eukaryota.
DR GeneTree; ENSGT00940000161591; -.
DR HOGENOM; CLU_029444_0_0_1; -.
DR InParanoid; Q15464; -.
DR OMA; SERKWIG; -.
DR OrthoDB; 1120795at2759; -.
DR PhylomeDB; Q15464; -.
DR TreeFam; TF325799; -.
DR PathwayCommons; Q15464; -.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR SignaLink; Q15464; -.
DR BioGRID-ORCS; 6461; 27 hits in 1082 CRISPR screens.
DR ChiTaRS; SHB; human.
DR GeneWiki; SHB_(gene); -.
DR GenomeRNAi; 6461; -.
DR Pharos; Q15464; Tbio.
DR PRO; PR:Q15464; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15464; protein.
DR Bgee; ENSG00000107338; Expressed in parotid gland and 180 other tissues.
DR Genevisible; Q15464; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045624; P:positive regulation of T-helper cell differentiation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR CDD; cd10389; SH2_SHB; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035040; SHB.
DR InterPro; IPR035045; SHB_SH2.
DR PANTHER; PTHR15127:SF31; PTHR15127:SF31; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Apoptosis; Cell membrane; Cytoplasm;
KW Developmental protein; Differentiation; Isopeptide bond; Membrane;
KW Phosphoprotein; Reference proteome; SH2 domain; Ubl conjugation.
FT CHAIN 1..509
FT /note="SH2 domain-containing adapter protein B"
FT /id="PRO_0000246324"
FT DOMAIN 410..504
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..410
FT /note="Mediates interaction with LAT, PTK2/FAK1, JAK1 and
FT JAK3"
FT /evidence="ECO:0000269|PubMed:10488157,
FT ECO:0000269|PubMed:12200137"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 187
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 280..297
FT /note="EFQRQESVRSQHKGIQLY -> GLQEAWRHSPSGCFPVGP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019846"
FT VAR_SEQ 298..509
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019847"
FT MUTAGEN 435
FT /note="R->K: Loss of interaction with CD3Z. Alters LAT,
FT PLCG1, VAV1 and LCP2 phosphorylation, MAP kinase signaling,
FT Rac1 and JNK activation, intracellular calcium increase,
FT activation of the nuclear factor for activation of T-cells
FT and subsequent interleukin-2 expression which normally
FT occur upon T-cells stimulation."
FT /evidence="ECO:0000269|PubMed:9484780"
FT CONFLICT 91..93
FT /note="DFE -> HFQ (in Ref. 1; CAA53091)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="I -> S (in Ref. 1; CAA53091)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="S -> P (in Ref. 1; CAA53091)"
FT /evidence="ECO:0000305"
SQ 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
