SNTB1_MOUSE - dbPTM
SNTB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNTB1_MOUSE
UniProt AC Q99L88
Protein Name Beta-1-syntrophin
Gene Name Sntb1
Organism Mus musculus (Mouse).
Sequence Length 537
Subcellular Localization Cell membrane, sarcolemma
Peripheral membrane protein
Cytoplasmic side . Cell junction . Cytoplasm, cytoskeleton . In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions.
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..
Protein Sequence MAVAAAAVAAPAGGGGARAQRSGLLEVLVRDRWHKVLVNLSEDALVLSCEEGAAAYNGIGAATNGSFCRGSGTGHPVPGVAQAPDSPAGVRTAFTDLPEQVPESISNQKRGVKVLKQELGGLGISIKGGKENKMPILISKIFKGLAADQTQALYVGDAILSVNGADLRDATHDEAVQALKRAGKEVLLEVKYMREATPYVKKGSPVSEIGWETPPPESPRLGGGSAEPLSSQSFSFHRDRKSIPLKMCYVTRNMTLADPENRQLEIHSPDAKHTVILRSKDSATAQAWFSAIHSNAGDLLTRVVADIREQLGKTGIAGSREIRHLGWLAEKVPGESEKQWKPALVVLTEKDLLIYDSMPRRKEAWFSPVHSYPLLATRLVHSGPGKGSPQAGMDLSFATRTGTKQGIETHLFRAEISRDLSHWTRSIVQGCHNSAELTAEITTACTYRNQECRLTIHYDNGFSISTEPQDGAFPKTIIQSPYEKLKMSSDDGIRMLYLDFGGKEGEIQLDLHSCPKPIVFIIHSFLSAKITRLGLVA
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
2Acetylation------MAVAAAAVA
------CHHHHHHHC		10.31-
71PhosphorylationNGSFCRGSGTGHPVP
CCCCCCCCCCCCCCC		17.5221082442
73PhosphorylationSFCRGSGTGHPVPGV
CCCCCCCCCCCCCCE		33.7321082442
86PhosphorylationGVAQAPDSPAGVRTA
CEEECCCCCCCCCCC		18.6525521595
92PhosphorylationDSPAGVRTAFTDLPE
CCCCCCCCCCCCCCH		24.5823984901
95PhosphorylationAGVRTAFTDLPEQVP
CCCCCCCCCCCHHCC		33.8823984901
109UbiquitinationPESISNQKRGVKVLK
CHHHHHCCHHHHHHH		56.2022790023
125PhosphorylationELGGLGISIKGGKEN
HHCCCCEEEECCCCC		19.2223984901
127UbiquitinationGGLGISIKGGKENKM
CCCCEEEECCCCCCC		55.6227667366
140UbiquitinationKMPILISKIFKGLAA
CCCCHHHHHHHCCCC		45.2122790023
180MalonylationDEAVQALKRAGKEVL
HHHHHHHHHCCCHHE		43.1226320211
180UbiquitinationDEAVQALKRAGKEVL
HHHHHHHHHCCCHHE		43.1227667366
184UbiquitinationQALKRAGKEVLLEVK
HHHHHCCCHHEEEEE		43.6022790023
191UbiquitinationKEVLLEVKYMREATP
CHHEEEEEEHHHCCC		24.7722790023
204PhosphorylationTPYVKKGSPVSEIGW
CCCCCCCCCCHHCCC		30.8928833060
207PhosphorylationVKKGSPVSEIGWETP
CCCCCCCHHCCCCCC		27.2128833060
213PhosphorylationVSEIGWETPPPESPR
CHHCCCCCCCCCCCC		34.2925521595
218PhosphorylationWETPPPESPRLGGGS
CCCCCCCCCCCCCCC		22.5425521595
225PhosphorylationSPRLGGGSAEPLSSQ
CCCCCCCCCCCCCCC		32.5022324799
230PhosphorylationGGSAEPLSSQSFSFH
CCCCCCCCCCCEECC		36.7323984901
231PhosphorylationGSAEPLSSQSFSFHR
CCCCCCCCCCEECCC		37.2122817900
233PhosphorylationAEPLSSQSFSFHRDR
CCCCCCCCEECCCCC		25.4728978645
235PhosphorylationPLSSQSFSFHRDRKS
CCCCCCEECCCCCCC		25.9521082442
242PhosphorylationSFHRDRKSIPLKMCY
ECCCCCCCCCCEEEE		30.27-
246UbiquitinationDRKSIPLKMCYVTRN
CCCCCCCEEEEEECC		22.9022790023
272UbiquitinationEIHSPDAKHTVILRS
EEECCCCCCEEEEEC		47.3822790023
280UbiquitinationHTVILRSKDSATAQA
CEEEEECCCCHHHHH		49.6322790023
313MalonylationDIREQLGKTGIAGSR
HHHHHHCCCCCCCCH		52.7726320211
313UbiquitinationDIREQLGKTGIAGSR
HHHHHHCCCCCCCCH		52.7727667366
338UbiquitinationKVPGESEKQWKPALV
CCCCCCHHHCCCEEE		71.4022790023
341UbiquitinationGESEKQWKPALVVLT
CCCHHHCCCEEEEEE		20.2322790023
355PhosphorylationTEKDLLIYDSMPRRK
ECCCEEEEECCCCCC		11.2623140645
357PhosphorylationKDLLIYDSMPRRKEA
CCEEEEECCCCCCCC		17.4523140645
367PhosphorylationRRKEAWFSPVHSYPL
CCCCCCCCCCCCCCE		18.47-
372PhosphorylationWFSPVHSYPLLATRL
CCCCCCCCCEEEEEE		5.30-
382PhosphorylationLATRLVHSGPGKGSP
EEEEECCCCCCCCCC		38.9223737553
386UbiquitinationLVHSGPGKGSPQAGM
ECCCCCCCCCCCCCC		60.3922790023
388PhosphorylationHSGPGKGSPQAGMDL
CCCCCCCCCCCCCCC		19.8225521595
396PhosphorylationPQAGMDLSFATRTGT
CCCCCCCEEEECCCC		14.4723984901
399PhosphorylationGMDLSFATRTGTKQG
CCCCEEEECCCCCCC		27.1023984901
404UbiquitinationFATRTGTKQGIETHL
EEECCCCCCCCEEEE		48.1222790023
484UbiquitinationIIQSPYEKLKMSSDD
CCCCHHHHHCCCCCC		47.7922790023
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 SNTB1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNTB1_MOUSE !!
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 SNTB1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SNTB1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNTB1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-218, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; THR-73; THR-213;SER-218 AND SER-235, AND MASS SPECTROMETRY.

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