STXB1_MOUSE - dbPTM
STXB1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STXB1_MOUSE
UniProt AC O08599
Protein Name Syntaxin-binding protein 1
Gene Name Stxbp1
Organism Mus musculus (Mouse).
Sequence Length 594
Subcellular Localization Cytoplasm, cytosol . Membrane
Peripheral membrane protein.
Protein Description May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions (By similarity)..
Protein Sequence MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIGSTHILTPQKLLDTLKKLNKTDEEISS
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
13UbiquitinationLKAVVGEKIMHDVIK
CHHHHCHHHHHHHHH		39.1322790023
20UbiquitinationKIMHDVIKKVKKKGE
HHHHHHHHHHHHCCC		51.9027667366
42PhosphorylationQLSMRMLSSCCKMTD
HHHHHHHHHHHHCHH		16.40-
43PhosphorylationLSMRMLSSCCKMTDI
HHHHHHHHHHHCHHH		21.41-
70PhosphorylationKRREPLPSLEAVYLI
HCCCCCCCCEEEEEE		46.6629899451
80PhosphorylationAVYLITPSEKSVHSL
EEEEECCCHHHHHHH		49.3529899451
86PhosphorylationPSEKSVHSLISDFKD
CCHHHHHHHHHCCCC		25.8322324799
89PhosphorylationKSVHSLISDFKDPPT
HHHHHHHHCCCCCCC		42.1429899451
92AcetylationHSLISDFKDPPTAKY
HHHHHCCCCCCCCCC		74.4519846845
92UbiquitinationHSLISDFKDPPTAKY
HHHHHCCCCCCCCCC		74.4522790023
98UbiquitinationFKDPPTAKYRAAHVF
CCCCCCCCCEEEEEE		37.4327667366
107PhosphorylationRAAHVFFTDSCPDAL
EEEEEEECCCCHHHH		18.6215572359
110S-palmitoylationHVFFTDSCPDALFNE
EEEECCCCHHHHHHH		3.8328680068
110S-nitrosylationHVFFTDSCPDALFNE
EEEECCCCHHHHHHH		3.8324895380
120UbiquitinationALFNELVKSRAAKVI
HHHHHHHHHHHHHHH		47.0122790023
142PhosphorylationIAFLPYESQVYSLDS
EEEECCCCCCEECCC		21.0715572359
145PhosphorylationLPYESQVYSLDSADS
ECCCCCCEECCCCHH		8.9015572359
146PhosphorylationPYESQVYSLDSADSF
CCCCCCEECCCCHHH		27.1815572359
165UbiquitinationSPHKAQMKNPILERL
CCCHHHCCCHHHHHH		47.7127667366
180S-nitrosylationAEQIATLCATLKEYP
HHHHHHHHHHHHHCC		2.0622588120
184UbiquitinationATLCATLKEYPAVRY
HHHHHHHHHCCCCEE		51.3422790023
196UbiquitinationVRYRGEYKDNALLAQ
CEECCCCCCCHHHHH		39.9622790023
208UbiquitinationLAQLIQDKLDAYKAD
HHHHHHHHHHHHHCC		31.7122790023
225UbiquitinationTMGEGPDKARSQLLI
CCCCCCHHHHHHEEE		49.1622790023
241PhosphorylationDRGFDPSSPVLHELT
ECCCCCCCCHHHHHH		25.15-
269PhosphorylationDVYKYETSGIGEARV
CEEEEECCCCCCEEE		19.2425521595
294UbiquitinationLWIALRHKHIAEVSQ
EEHHHHCHHHHHHCH		30.2122790023
300PhosphorylationHKHIAEVSQEVTRSL
CHHHHHHCHHHHHHH		16.4829899451
306PhosphorylationVSQEVTRSLKDFSSS
HCHHHHHHHHHCCCC		30.3312519779
308UbiquitinationQEVTRSLKDFSSSKR
HHHHHHHHHCCCCCC		58.9522790023
313PhosphorylationSLKDFSSSKRMNTGE
HHHHCCCCCCCCCCC		24.0812519779
314UbiquitinationLKDFSSSKRMNTGEK
HHHCCCCCCCCCCCC		58.5827667366
321UbiquitinationKRMNTGEKTTMRDLS
CCCCCCCCCCHHHHH		51.1127667366
328PhosphorylationKTTMRDLSQMLKKMP
CCCHHHHHHHHHHCH		20.1725521595
333UbiquitinationDLSQMLKKMPQYQKE
HHHHHHHHCHHHHHH		52.4227667366
339UbiquitinationKKMPQYQKELSKYST
HHCHHHHHHHHHHHH		56.5427667366
344PhosphorylationYQKELSKYSTHLHLA
HHHHHHHHHHHHHHH		18.5417203969
345PhosphorylationQKELSKYSTHLHLAE
HHHHHHHHHHHHHHH		17.0617203969
346PhosphorylationKELSKYSTHLHLAED
HHHHHHHHHHHHHHH		25.9315572359
355OxidationLHLAEDCMKHYQGTV
HHHHHHHHHHCCCHH		4.6617203969
361PhosphorylationCMKHYQGTVDKLCRV
HHHHCCCHHHHHHHH		15.2529899451
364UbiquitinationHYQGTVDKLCRVEQD
HCCCHHHHHHHHHHH		45.1922790023
382UbiquitinationGTDAEGEKIKDPMRA
CCCCCCCCCCCHHHH		66.9522790023
384UbiquitinationDAEGEKIKDPMRAIV
CCCCCCCCCHHHHHH		67.8427667366
400PhosphorylationILLDANVSTYDKIRI
HHHCCCCCHHHHHHH		22.5126239621
401PhosphorylationLLDANVSTYDKIRII
HHCCCCCHHHHHHHH		31.3026239621
402PhosphorylationLDANVSTYDKIRIIL
HCCCCCHHHHHHHHH		14.0326239621
441PhosphorylationPEDSEIITNMAHLGV
CCCCHHHHHHHHHCC		25.3029899451
452PhosphorylationHLGVPIVTDSTLRRR
HHCCCEECHHHHHHC		25.5929899451
454PhosphorylationGVPIVTDSTLRRRSK
CCCEECHHHHHHCCC		21.7019060867
455PhosphorylationVPIVTDSTLRRRSKP
CCEECHHHHHHCCCH		27.3921183079
472PhosphorylationKERISEQTYQLSRWT
HHHHHHHHHHHHCCC		14.8025367039
473PhosphorylationERISEQTYQLSRWTP
HHHHHHHHHHHCCCH		13.7225367039
476PhosphorylationSEQTYQLSRWTPIIK
HHHHHHHHCCCHHHH		15.39-
479PhosphorylationTYQLSRWTPIIKDIM
HHHHHCCCHHHHHHH		11.96-
483UbiquitinationSRWTPIIKDIMEDTI
HCCCHHHHHHHHHHH		41.7522790023
497UbiquitinationIEDKLDTKHYPYIST
HHHCCCCCCCCCEEE		40.5922790023
501PhosphorylationLDTKHYPYISTRSSA
CCCCCCCCEEECCCC		10.5929899451
506PhosphorylationYPYISTRSSASFSTT
CCCEEECCCCCCCCC		30.2825619855
507PhosphorylationPYISTRSSASFSTTA
CCEEECCCCCCCCCC		25.3325521595
509PhosphorylationISTRSSASFSTTAVS
EEECCCCCCCCCCCH		22.9824925903
511PhosphorylationTRSSASFSTTAVSAR
ECCCCCCCCCCCHHC		23.5025619855
511O-linked_GlycosylationTRSSASFSTTAVSAR
ECCCCCCCCCCCHHC		23.5022645316
512PhosphorylationRSSASFSTTAVSARY
CCCCCCCCCCCHHCC		19.4325619855
513PhosphorylationSSASFSTTAVSARYG
CCCCCCCCCCHHCCC		24.7025619855
516PhosphorylationSFSTTAVSARYGHWH
CCCCCCCHHCCCCCC		12.4525521595
526UbiquitinationYGHWHKNKAPGEYRS
CCCCCCCCCCCCCCC		61.8427667366
533PhosphorylationKAPGEYRSGPRLIIF
CCCCCCCCCCEEEEE		52.8529899451
574PhosphorylationIGSTHILTPQKLLDT
EECCEECCHHHHHHH		24.079933594
581PhosphorylationTPQKLLDTLKKLNKT
CHHHHHHHHHHHCCC		40.2121183079
588PhosphorylationTLKKLNKTDEEISS-
HHHHHCCCHHHHCC-		47.79-
590 (in isoform 2)Phosphorylation-63.5629899451
591 (in isoform 2)Phosphorylation-51.4822807455
593PhosphorylationNKTDEEISS------
CCCHHHHCC------		33.0225521595
594PhosphorylationKTDEEISS-------
CCHHHHCC-------		50.3225521595
594 (in isoform 2)Phosphorylation-50.3225521595
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
241SPhosphorylationKinaseMAPK1P63085
GPS
241SPhosphorylationKinaseMAPK3Q63844
GPS
306SPhosphorylationKinasePKC-FAMILY-GPS
306SPhosphorylationKinasePKC_GROUP-PhosphoELM
313SPhosphorylationKinasePKC-FAMILY-GPS
313SPhosphorylationKinasePKC_GROUP-PhosphoELM
473YPhosphorylationKinaseSRCP12931
PSP
473YPhosphorylationKinaseSRCP05480
PSP
479TPhosphorylationKinaseDYRK1AQ61214
PSP
574TPhosphorylationKinaseCDK5P49615
PhosphoELM
574TPhosphorylationKinaseMAPK1P63085
GPS
574TPhosphorylationKinaseMAPK3Q63844
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STXB1_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 STXB1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of STXB1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STXB1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-507, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, AND MASSSPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107; SER-142; TYR-145;SER-146; SER-345 AND THR-346, AND MASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473, AND MASSSPECTROMETRY.

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