SNTB2_HUMAN - dbPTM
SNTB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNTB2_HUMAN
UniProt AC Q13425
Protein Name Beta-2-syntrophin
Gene Name SNTB2
Organism Homo sapiens (Human).
Sequence Length 540
Subcellular Localization Membrane. Cytoplasmic vesicle, secretory vesicle membrane
Peripheral membrane protein. Cell junction. Cytoplasm, cytoskeleton. Membrane-associated. In muscle, it is exclusively localized at the neuromuscular junction (By similarity). In insulinoma c
Protein Description Adapter 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..
Protein Sequence MRVAAATAAAGAGPAMAVWTRATKAGLVELLLRERWVRVVAELSGESLSLTGDAAAAELEPALGPAAAAFNGLPNGGGAGDSLPGSPSRGLGPPSPPAPPRGPAGEAGASPPVRRVRVVKQEAGGLGISIKGGRENRMPILISKIFPGLAADQSRALRLGDAILSVNGTDLRQATHDQAVQALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGAAPQSPSFSGSEDSGSPKHQNSTKDRKIIPLKMCFAARNLSMPDLENRLIELHSPDSRNTLILRCKDTATAHSWFVAIHTNIMALLPQVLAELNAMLGATSTAGGSKEVKHIAWLAEQAKLDGGRQQWRPVLMAVTEKDLLLYDCMPWTRDAWASPCHSYPLVATRLVHSGSGCRSPSLGSDLTFATRTGSRQGIEMHLFRVETHRDLSSWTRILVQGCHAAAELIKEVSLGCMLNGQEVRLTIHYENGFTISRENGGSSSILYRYPFERLKMSADDGIRNLYLDFGGPEGELTMDLHSCPKPIVFVLHTFLSAKVTRMGLLV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MRVAAATAAAGAGP
-CCHHHHHHHCCCCC		16.4724719451
20PhosphorylationGPAMAVWTRATKAGL
CCHHHHHHHHHHHHH		12.1124043423
23PhosphorylationMAVWTRATKAGLVEL
HHHHHHHHHHHHHHH		20.3824719451
24UbiquitinationAVWTRATKAGLVELL
HHHHHHHHHHHHHHH		39.20-
44PhosphorylationVRVVAELSGESLSLT
HHHHHHHHCCCEEEC		31.8320068231
47PhosphorylationVAELSGESLSLTGDA
HHHHHCCCEEECCCH		27.1220068231
49PhosphorylationELSGESLSLTGDAAA
HHHCCCEEECCCHHH		32.9120068231
51PhosphorylationSGESLSLTGDAAAAE
HCCCEEECCCHHHHH		29.6420068231
82PhosphorylationNGGGAGDSLPGSPSR
CCCCCCCCCCCCCCC		35.2320068231
86PhosphorylationAGDSLPGSPSRGLGP
CCCCCCCCCCCCCCC		20.1220068231
88PhosphorylationDSLPGSPSRGLGPPS
CCCCCCCCCCCCCCC		40.4520068231
95PhosphorylationSRGLGPPSPPAPPRG
CCCCCCCCCCCCCCC		46.8019664994
110PhosphorylationPAGEAGASPPVRRVR
CCCCCCCCCCCEEEE		28.9019664994
129PhosphorylationEAGGLGISIKGGREN
CCCCCCEEEECCCCC		19.2230266825
131UbiquitinationGGLGISIKGGRENRM
CCCCEEEECCCCCCC		48.82-
143PhosphorylationNRMPILISKIFPGLA
CCCEEEEEHHCCCCC		19.09-
165PhosphorylationRLGDAILSVNGTDLR
HHHCEEEEECCCCHH		13.8627134283
169PhosphorylationAILSVNGTDLRQATH
EEEEECCCCHHHHCH		27.0224670416
184UbiquitinationDQAVQALKRAGKEVL
HHHHHHHHHCCCCCE		43.12-
184MethylationDQAVQALKRAGKEVL
HHHHHHHHHCCCCCE		43.12115980777
188UbiquitinationQALKRAGKEVLLEVK
HHHHHCCCCCEEEEE		43.60-
201PhosphorylationVKFIREVTPYIKKPS
EEEHHHHCCCCCCCC		12.9617924679
203PhosphorylationFIREVTPYIKKPSLV
EHHHHCCCCCCCCCC		18.9228102081
205AcetylationREVTPYIKKPSLVSD
HHHCCCCCCCCCCCC		53.4312435265
206UbiquitinationEVTPYIKKPSLVSDL
HHCCCCCCCCCCCCC		30.22-
206AcetylationEVTPYIKKPSLVSDL
HHCCCCCCCCCCCCC		30.2212435275
208PhosphorylationTPYIKKPSLVSDLPW
CCCCCCCCCCCCCCC		50.7323927012
211PhosphorylationIKKPSLVSDLPWEGA
CCCCCCCCCCCCCCC		38.4323927012
222PhosphorylationWEGAAPQSPSFSGSE
CCCCCCCCCCCCCCC		22.8122167270
224PhosphorylationGAAPQSPSFSGSEDS
CCCCCCCCCCCCCCC		36.9722167270
226PhosphorylationAPQSPSFSGSEDSGS
CCCCCCCCCCCCCCC		45.8330266825
228PhosphorylationQSPSFSGSEDSGSPK
CCCCCCCCCCCCCCC		36.7130266825
231PhosphorylationSFSGSEDSGSPKHQN
CCCCCCCCCCCCCCC		36.8022167270
233PhosphorylationSGSEDSGSPKHQNST
CCCCCCCCCCCCCCC		34.4322167270
235UbiquitinationSEDSGSPKHQNSTKD
CCCCCCCCCCCCCCC		60.56-
235AcetylationSEDSGSPKHQNSTKD
CCCCCCCCCCCCCCC		60.5612435285
239PhosphorylationGSPKHQNSTKDRKII
CCCCCCCCCCCCCEE		30.2023927012
240PhosphorylationSPKHQNSTKDRKIIP
CCCCCCCCCCCCEEE		44.5123927012
249UbiquitinationDRKIIPLKMCFAARN
CCCEEEHHHHHHHCC		28.41-
258 (in isoform 2)Phosphorylation-31.6420068231
258O-linked_GlycosylationCFAARNLSMPDLENR
HHHHCCCCCCHHHHH		31.6430379171
258PhosphorylationCFAARNLSMPDLENR
HHHHCCCCCCHHHHH		31.6420068231
271PhosphorylationNRLIELHSPDSRNTL
HHEEEECCCCCCCEE		42.9220068231
274PhosphorylationIELHSPDSRNTLILR
EEECCCCCCCEEEEE		30.7120068231
277PhosphorylationHSPDSRNTLILRCKD
CCCCCCCEEEEEECC		17.6720068231
337UbiquitinationAWLAEQAKLDGGRQQ
HHHHHHHCCCCCHHC		46.97-
360PhosphorylationTEKDLLLYDCMPWTR
CCCCEEEECCCCCCC		13.6830108239
366PhosphorylationLYDCMPWTRDAWASP
EECCCCCCCCCCCCC		16.8930108239
387PhosphorylationVATRLVHSGSGCRSP
EEEEEEECCCCCCCC		27.4623927012
389PhosphorylationTRLVHSGSGCRSPSL
EEEEECCCCCCCCCC		37.4223401153
393PhosphorylationHSGSGCRSPSLGSDL
ECCCCCCCCCCCCCC		23.9419664994
395PhosphorylationGSGCRSPSLGSDLTF
CCCCCCCCCCCCCEE		46.7629255136
398PhosphorylationCRSPSLGSDLTFATR
CCCCCCCCCCEEEEC		34.4430266825
401PhosphorylationPSLGSDLTFATRTGS
CCCCCCCEEEECCCC		19.0630266825
404PhosphorylationGSDLTFATRTGSRQG
CCCCEEEECCCCCCC		25.2723927012
406PhosphorylationDLTFATRTGSRQGIE
CCEEEECCCCCCCEE		34.8422210691
408PhosphorylationTFATRTGSRQGIEMH
EEEECCCCCCCEEEE		22.3322210691
476PhosphorylationISRENGGSSSILYRY
EEECCCCCCEEEEEC		23.4728857561
477PhosphorylationSRENGGSSSILYRYP
EECCCCCCEEEEECC		25.3628857561
478PhosphorylationRENGGSSSILYRYPF
ECCCCCCEEEEECCH		20.5026471730
481PhosphorylationGGSSSILYRYPFERL
CCCCEEEEECCHHHH		13.3626471730
489UbiquitinationRYPFERLKMSADDGI
ECCHHHHCCCCCCCC		36.712190698
489 (in isoform 1)Ubiquitination-36.7121906983
511PhosphorylationGGPEGELTMDLHSCP
CCCCCEEEEEHHHCC		12.3418691976
516PhosphorylationELTMDLHSCPKPIVF
EEEEEHHHCCCCEEE		39.1418691976
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SNTB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNTB2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SNTB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DMD_HUMANDMDphysical
8576247
UTRO_HUMANUTRNphysical
8576247
MAST2_HUMANMAST2physical
10404183
MAST1_HUMANMAST1physical
10404183
ABCA1_HUMANABCA1physical
12054535
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNTB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110 AND SER-393,AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110 AND SER-395,AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110; SER-222 ANDSER-393, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-110, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-222 ANDSER-393, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-110; SER-233 ANDSER-393, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201, AND MASSSPECTROMETRY.

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