true2002-10-102024-03-27220SNTB2_HUMANThe three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives.Ahn A.H.Feener C.A.Gussoni E.Yoshida M.Ozawa E.Kunkel L.M.doi:10.1074/jbc.271.5.27241996J. Biol. Chem.2712724-2730NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)INTERACTION WITH DMD; DTNA AND UTRNMuscleThe receptor tyrosine phosphatase-like protein ICA512 binds the PDZ domains of beta2-syntrophin and nNOS in pancreatic beta-cells.Ort T.Maksimova E.Dirkx R.Kachinsky A.M.Berghs S.Froehner S.C.Solimena M.doi:10.1078/0171-9335-000952000Eur. J. Cell Biol.79621-630NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)INTERACTION WITH PTPRNBrainThe status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)Mammary glandThe neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses.Garcia R.A.Vasudevan K.Buonanno A.doi:10.1073/pnas.97.7.35962000Proc. Natl. Acad. Sci. U.S.A.973596-3601INTERACTION WITH ERBB4Dephosphorylation of beta2-syntrophin and Ca2+/mu-calpain-mediated cleavage of ICA512 upon stimulation of insulin secretion.Ort T.Voronov S.Guo J.Zawalich K.Froehner S.C.Zawalich W.Solimena M.doi:10.1093/emboj/20.15.40132001EMBO J.204013-4023INTERACTION WITH PTPRNAn unappreciated role for RNA surveillance.Hillman R.T.Green R.E.Brenner S.E.doi:10.1186/gb-2004-5-2-r82004Genome Biol.5R8.1-R8.16SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S)Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V.Blagoev B.Gnad F.Macek B.Kumar C.Mortensen P.Mann M.doi:10.1016/j.cell.2006.09.0262006Cell127635-648PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Cervix carcinomaCombining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T.Yi W.Lu B.Park S.K.Xu T.Lee J.-D.Yates J.R. IIIdoi:10.1021/pr07054412008J. Proteome Res.71346-1351PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H.Olsen J.V.Bairlein M.Gnad F.Oppermann F.S.Korner R.Greff Z.Keri G.Stemmann O.Mann M.doi:10.1016/j.molcel.2008.07.0072008Mol. Cell31438-448PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]A quantitative atlas of mitotic phosphorylation.Dephoure N.Zhou C.Villen J.Beausoleil S.A.Bakalarski C.E.Elledge S.J.Gygi S.P.doi:10.1073/pnas.08051391052008Proc. Natl. Acad. Sci. U.S.A.10510762-10767PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-233 AND SER-393IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S.Helbig A.O.Slijper M.Krijgsveld J.Heck A.J.Mohammed S.doi:10.1021/ac90043092009Anal. Chem.814493-4501IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V.Lundgren D.H.Hwang S.-I.Rezaul K.Wu L.Eng J.K.Rodionov V.Han D.K.doi:10.1126/scisignal.20000072009Sci. Signal.2RA46IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Leukemic T-cellQuantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.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.doi:10.1126/scisignal.20004752010Sci. Signal.3RA3PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110; SER-222 AND SER-393IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.Burkard T.R.Planyavsky M.Kaupe I.Breitwieser F.P.Buerckstuemmer T.Bennett K.L.Superti-Furga G.Colinge J.doi:10.1186/1752-0509-5-172011BMC Syst. Biol.517IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T.Prokhorova T.A.Akimov V.Henningsen J.Johansen P.T.Kratchmarova I.Kassem M.Mann M.Olsen J.V.Blagoev B.doi:10.1126/scisignal.20015702011Sci. Signal.4RS3IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Toward a comprehensive characterization of a human cancer cell phosphoproteome.Zhou H.Di Palma S.Preisinger C.Peng M.Polat A.N.Heck A.J.Mohammed S.doi:10.1021/pr300630k2013J. Proteome Res.12260-271PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110; SER-129; SER-222; SER-393 AND SER-395IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]ErythroleukemiaAn enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y.Song C.Cheng K.Dong M.Wang F.Huang J.Sun D.Wang L.Ye M.Zou H.doi:10.1016/j.jprot.2013.11.0142014J. Proteomics96253-262PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110 AND SER-211IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]LiverLRP4 third beta-propeller domain mutations cause novel congenital myasthenia by compromising agrin-mediated MuSK signaling in a position-specific manner.Ohkawara B.Cabrera-Serrano M.Nakata T.Milone M.Asai N.Ito K.Ito M.Masuda A.Ito Y.Engel A.G.Ohno K.doi:10.1093/hmg/ddt5782014Hum. Mol. Genet.231856-1868VARIANT ARG-3762.00A/B/C/D=112-200148661 site, 1 O-linked glycan (1 site)179 antibodies from 21 providershumanSNTB2Low tissue specificitygeneEukaryota9 hits in 1149 CRISPR screenshumanTbioProteinExpressed in tibia and 197 other cell types or tissuesbaseline and differentialPDZ_signalingPHsplit_syntrophinPleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)PDZPDZ_sfPH-like_dom_sfPH_domainPHsplit_syntrophinSyntrophinBETA-2-SYNTROPHINSYNTROPHINPDZPHPH_17PDZPHPDZ domain-likePH domain-likePDZPH_DOMAINHSBeta-2-syntrophin59 kDa dystrophin-associated protein A1 basic component 2Syntrophin-3SNT3Syntrophin-likeSNTLSNTB2D16S2531ESNT2B2SNTLAdapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN.Monomer and homodimer (Probable). Interacts with the other members of the syntrophin family: SNTA1 and SNTB1; and with the sodium channel proteins SCN4A and SCN5A. Interacts with SAST, MAST205, microtubules and microtubule-associated proteins (By similarity). Interacts with the dystrophin protein DMD and related proteins DTNA and UTRN, and with the neuroregulin receptor ERBB4. Interacts with PTPRN when phosphorylated, protecting PTPRN from protein cleavage by CAPN1. Dephosphorylation upon insulin stimulation disrupts the interaction with PTPRN and results in the cleavage of PTPRN. Interacts with DTNB (By similarity).Membrane-associated. In muscle, it is exclusively localized at the neuromuscular junction (By similarity). In insulinoma cell line, it is enriched in secretory granules.Ubiquitous. Isoform 1 is the predominant isoform. Weak level of isoform 2 is present in all tested tissues, except in liver and heart where it is highly expressed.The PH 1 domain mediates the oligomerization in a calcium dependent manner.The PDZ domain binds to the last three or four amino acids of ion channels and receptor proteins. The association with dystrophin or related proteins probably leaves the PDZ domain available to recruit proteins to the membrane (By similarity).The SU domain binds calmodulin in a calcium-dependent manner.Phosphorylated. Partially dephosphorylated upon insulin stimulation.Lacks domains required for interaction with dystrophin related proteins. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.Belongs to the syntrophin family.Beta-2-syntrophin579501540PDZ115198PH 1163300PH 2325437SU484Disordered73114Disordered220240Calmodulin-binding518Pro residues89106Phosphoserine95Phosphoserine110Phosphoserine129Phosphoserine211Phosphoserine222Phosphoserine233Phosphoserine393Phosphoserine395In isoform 2.QN266267In isoform 2.268R376E424113119127133134136138145150154161166176184188196false16false3false2ADRA1DCASKDMD1996-11-01157950c12cd9db7689a23fece50927a373d51f1Beta2-syntrophin58MRVAAATAAAGAGPAMAVWTRATKAGLVELLLRERWVRVVAELSGESLSLTGDAAAAELEPALGPAAAAFNGLPNGGGAGDSLPGSPSRGLGPPSPPAPPRGPAGEAGASPPVRRVRVVKQEAGGLGISIKGGRENRMPILISKIFPGLAADQSRALRLGDAILSVNGTDLRQATHDQAVQALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGAAPQSPSFSGSEDSGSPKHQNSTKDRKIIPLKMCFAARNLSMPDLENRLIELHSPDSRNTLILRCKDTATAHSWFVAIHTNIMALLPQVLAELNAMLGATSTAGGSKEVKHIAWLAEQAKLDGGRQQWRPVLMAVTEKDLLLYDCMPWTRDAWASPCHSYPLVATRLVHSGSGCRSPSLGSDLTFATRTGSRQGIEMHLFRVETHRDLSSWTRILVQGCHAAAELIKEVSLGCMLNGQEVRLTIHYENGFTISRENGGSSSILYRYPFERLKMSADDGIRNLYLDFGGPEGELTMDLHSCPKPIVFVLHTFLSAKVTRMGLLV2Beta2-syntrophin28MRVAAATAAAGAGPAMAVWTRATKAGLVELLLRERWVRVVAELSGESLSLTGDAAAAELEPALGPAAAAFNGLPNGGGAGDSLPGSPSRGLGPPSPPAPPRGPAGEAGASPPVRRVRVVKQEAGGLGISIKGGRENRMPILISKIFPGLAADQSRALRLGDAILSVNGTDLRQATHDQAVQALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGAAPQSPSFSGSEDSGSPKHQNSTKDRKIIPLKMCFAARNLSMPDLENRQNtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue