SNTB1_HUMAN - dbPTM
SNTB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNTB1_HUMAN
UniProt AC Q13884
Protein Name Beta-1-syntrophin
Gene Name SNTB1
Organism Homo sapiens (Human).
Sequence Length 538
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 MAVAAAAAAAGPAGAGGGRAQRSGLLEVLVRDRWHKVLVNLSEDALVLSSEEGAAAYNGIGTATNGSFCRGAGAGHPGAGGAQPPDSPAGVRTAFTDLPEQVPESISNQKRGVKVLKQELGGLGISIKGGKENKMPILISKIFKGLAADQTQALYVGDAILSVNGADLRDATHDEAVQALKRAGKEVLLEVKYMREATPYVKKGSPVSEIGWETPPPESPRLGGSTSDPPSSQSFSFHRDRKSIPLKMCYVTRSMALADPENRQLEIHSPDAKHTVILRSKDSATAQAWFSAIHSNVNDLLTRVIAEVREQLGKTGIAGSREIRHLGWLAEKVPGESKKQWKPALVVLTEKDLLIYDSMPRRKEAWFSPVHTYPLLATRLVHSGPGKGSPQAGVDLSFATRTGTRQGIETHLFRAETSRDLSHWTRSIVQGCHNSAELIAEISTACTYKNQECRLTIHYENGFSITTEPQEGAFPKTIIQSPYEKLKMSSDDGIRMLYLDFGGKDGEIQLDLHSCPKPIVFIIHSFLSAKITRLGLVA
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------MAVAAAAAA
------CHHHHHHHH		10.3125944712
23PhosphorylationGGGRAQRSGLLEVLV
CCHHHHHCCCHHHHH		23.0124425749
49PhosphorylationSEDALVLSSEEGAAA
CCCEEEECCCCCHHH		28.3728348404
50PhosphorylationEDALVLSSEEGAAAY
CCEEEECCCCCHHHH		35.1928348404
57PhosphorylationSEEGAAAYNGIGTAT
CCCCHHHHCCCCCCC		14.8122817900
64PhosphorylationYNGIGTATNGSFCRG
HCCCCCCCCCCCCCC		39.6924719451
67PhosphorylationIGTATNGSFCRGAGA
CCCCCCCCCCCCCCC		24.2028348404
87PhosphorylationGGAQPPDSPAGVRTA
CCCCCCCCCCCCCCC		23.5629255136
93PhosphorylationDSPAGVRTAFTDLPE
CCCCCCCCCCCCCCH		24.5825627689
105PhosphorylationLPEQVPESISNQKRG
CCHHCCHHHHHCCHH		25.8324275569
126PhosphorylationELGGLGISIKGGKEN
HHCCCCEEEECCCCC		19.2225072903
134MethylationIKGGKENKMPILISK
EECCCCCCCCHHHHH		47.33-
134UbiquitinationIKGGKENKMPILISK
EECCCCCCCCHHHHH		47.33-
134TrimethylationIKGGKENKMPILISK
EECCCCCCCCHHHHH		47.33-
181UbiquitinationDEAVQALKRAGKEVL
HHHHHHHHHCCCHHE		43.1224816145
185UbiquitinationQALKRAGKEVLLEVK
HHHHHCCCHHEEEEE		43.60-
193PhosphorylationEVLLEVKYMREATPY
HHEEEEEEHHHHCCC		13.43-
198PhosphorylationVKYMREATPYVKKGS
EEEHHHHCCCCCCCC		15.4828102081
200PhosphorylationYMREATPYVKKGSPV
EHHHHCCCCCCCCCC		22.1328102081
205PhosphorylationTPYVKKGSPVSEIGW
CCCCCCCCCCHHCCC		30.8925159151
208PhosphorylationVKKGSPVSEIGWETP
CCCCCCCHHCCCCCC		27.2125159151
214PhosphorylationVSEIGWETPPPESPR
CHHCCCCCCCCCCCC		34.2928355574
219PhosphorylationWETPPPESPRLGGST
CCCCCCCCCCCCCCC		22.5425159151
225PhosphorylationESPRLGGSTSDPPSS
CCCCCCCCCCCCCCC		23.9623401153
226PhosphorylationSPRLGGSTSDPPSSQ
CCCCCCCCCCCCCCC		40.1925159151
227PhosphorylationPRLGGSTSDPPSSQS
CCCCCCCCCCCCCCC		50.2225159151
231PhosphorylationGSTSDPPSSQSFSFH
CCCCCCCCCCCCCCC		46.5329116813
232PhosphorylationSTSDPPSSQSFSFHR
CCCCCCCCCCCCCCC		35.3023401153
234PhosphorylationSDPPSSQSFSFHRDR
CCCCCCCCCCCCCCC		25.4728355574
236PhosphorylationPPSSQSFSFHRDRKS
CCCCCCCCCCCCCCC		25.9529116813
243PhosphorylationSFHRDRKSIPLKMCY
CCCCCCCCCCCEEEE		30.2724719451
250PhosphorylationSIPLKMCYVTRSMAL
CCCCEEEEEEHHHHC		11.0227762562
295PhosphorylationAWFSAIHSNVNDLLT
HHHHHHHHCHHHHHH		36.0420068231
314UbiquitinationEVREQLGKTGIAGSR
HHHHHHCCCCCCCCH		52.77-
315PhosphorylationVREQLGKTGIAGSRE
HHHHHCCCCCCCCHH		31.83-
320PhosphorylationGKTGIAGSREIRHLG
CCCCCCCCHHHHHHH		20.0924719451
356PhosphorylationTEKDLLIYDSMPRRK
ECCCEEEEECCCCCC		11.2630257219
358PhosphorylationKDLLIYDSMPRRKEA
CCEEEEECCCCCCCC		17.4530257219
383PhosphorylationLATRLVHSGPGKGSP
HHEEECCCCCCCCCC		38.9223401153
387MalonylationLVHSGPGKGSPQAGV
ECCCCCCCCCCCCCC		60.3926320211
389PhosphorylationHSGPGKGSPQAGVDL
CCCCCCCCCCCCCCC		19.8219664994
397PhosphorylationPQAGVDLSFATRTGT
CCCCCCCEEECCCCC		14.3623401153
400PhosphorylationGVDLSFATRTGTRQG
CCCCEEECCCCCCCC		27.1023401153
418PhosphorylationHLFRAETSRDLSHWT
EEEEEECCCCHHHHH		18.4626437602
443PhosphorylationAELIAEISTACTYKN
HHHHHHHHHHCCCCC		11.0624719451
444PhosphorylationELIAEISTACTYKNQ
HHHHHHHHHCCCCCC		31.2624719451
447PhosphorylationAEISTACTYKNQECR
HHHHHHCCCCCCEEE		34.7624719451
477PhosphorylationQEGAFPKTIIQSPYE
CCCCCCCCCCCCHHH		24.4522115753
481PhosphorylationFPKTIIQSPYEKLKM
CCCCCCCCHHHHHCC		21.0222115753
483PhosphorylationKTIIQSPYEKLKMSS
CCCCCCHHHHHCCCC		30.8322817900
489PhosphorylationPYEKLKMSSDDGIRM
HHHHHCCCCCCCEEE		29.0922115753
490PhosphorylationYEKLKMSSDDGIRML
HHHHCCCCCCCEEEE		35.9022115753
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNTB1_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 SNTB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DMD_HUMANDMDphysical
7844150
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 SNTB1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-19, AND ACETYLATION AT ALA-2.
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-219, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-219 AND SER-389,AND MASS SPECTROMETRY.

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