STXB5_HUMAN - dbPTM
STXB5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STXB5_HUMAN
UniProt AC Q5T5C0
Protein Name Syntaxin-binding protein 5
Gene Name STXBP5
Organism Homo sapiens (Human).
Sequence Length 1151
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein. Cytoplasmic vesicle membrane
Peripheral membrane protein. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Cell junction, synapse. Cytoplasmic, and associated with vesicular membranes a
Protein Description Plays a regulatory role in calcium-dependent exocytosis and neurotransmitter release. Inhibits membrane fusion between transport vesicles and the plasma membrane. May modulate the assembly of trans-SNARE complexes between transport vesicles and the plasma membrane. Inhibits translocation of GLUT4 from intracellular vesicles to the plasma membrane. Competes with STXBP1 for STX1 binding (By similarity)..
Protein Sequence MRKFNIRKVLDGLTAGSSSASQQQQQQHPPGNREPEIQETLQSEHFQLCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPAILHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSGYVIMWNKAIELSSKSHPGPVVHISDNPMDEGKLLIGFESGTVVLWDLKSKKADYRYTYDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPAKPVQTITPHGKQLKDGKKPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETPYPNDFQEPYAVVVLLEKDLVLIDLAQNGYPIFENPYPLSIHESPVTCCEYFADCPVDLIPALYSVGARQKRQGYSKKEWPINGGNWGLGAQSYPEIIITGHADGSVKFWDASAITLQVLYKLKTSKVFEKSRNKDDRPNTDIVDEDPYAIQIISWCPESRMLCIAGVSAHVIIYRFSKQEVITEVIPMLEVRLLYEINDVETPEGEQPPPLPTPVGGSNPQPIPPQSHPSTSSSSSDGLRDNVPCLKVKNSPLKQSPGYQTELVIQLVWVGGEPPQQITSLAVNSSYGLVVFGNCNGIAMVDYLQKAVLLNLGTIELYGSNDPYRREPRSPRKSRQPSGAGLCDISEGTVVPEDRCKSPTSGSSSPHNSDDEQKMNNFIEKVKTKSRKFSKMVANDIAKMSRKLSLPTDLKPDLDVKDNSFSRSRSSSVTSIDKESREAISALHFCETFTRKTDSSPSPCLWVGTTLGTVLVIALNLPPGGEQRLLQPVIVSPSGTILRLKGAILRMAFLDTTGCLIPPAYEPWREHNVPEEKDEKEKLKKRRPVSVSPSSSQEISENQYAVICSEKQAKVISLPTQNCAYKQNITETSFVLRGDIVALSNSICLACFCANGHIMTFSLPSLRPLLDVYYLPLTNMRIARTFCFTNNGQALYLVSPTEIQRLTYSQETCENLQEMLGELFTPVETPEAPNRGFFKGLFGGGAQSLDREELFGESSSGKASRSLAQHIPGPGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYKDKKWYQF
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
76PhosphorylationQKILAVGTQTGALRL
HHHHEECCCCCCHHH		19.16-
158PhosphorylationPFQSKWLYVGTERGN
CCCCEEEEEEECCCC		8.84-
193PhosphorylationAIELSSKSHPGPVVH
EEHHHCCCCCCCEEE		36.5425849741
202PhosphorylationPGPVVHISDNPMDEG
CCCEEEECCCCCCCC		19.2318452278
217PhosphorylationKLLIGFESGTVVLWD
CEEEEECCCEEEEEE		37.1920068231
232PhosphorylationLKSKKADYRYTYDEA
CCCCCCCEEEEHHHH		15.4620068231
234PhosphorylationSKKADYRYTYDEAIH
CCCCCEEEEHHHHHH		11.9220068231
235PhosphorylationKKADYRYTYDEAIHS
CCCCEEEEHHHHHHH		18.5920068231
236PhosphorylationKADYRYTYDEAIHSV
CCCEEEEHHHHHHHH		11.6720068231
242PhosphorylationTYDEAIHSVAWHHEG
EHHHHHHHHEEEECC		13.8620068231
305PhosphorylationVEFKTTRSGEPFIIL
EEEEECCCCCCEEEE		45.4720873877
313PhosphorylationGEPFIILSGGLSYDT
CCCEEEEECCCCCCC		22.0220873877
317PhosphorylationIILSGGLSYDTVGRR
EEEECCCCCCCCCCC		25.0020873877
318PhosphorylationILSGGLSYDTVGRRP
EEECCCCCCCCCCCC		22.2220873877
320PhosphorylationSGGLSYDTVGRRPCL
ECCCCCCCCCCCCEE		19.3420873877
459PhosphorylationITGHADGSVKFWDAS
EECCCCCCEEECCHH		23.76-
502PhosphorylationDIVDEDPYAIQIISW
CCCCCCCCHHHEEEE		28.76-
542UbiquitinationVITEVIPMLEVRLLY
HHHCHHHHHEEEEEE		3.2424816145
556PhosphorylationYEINDVETPEGEQPP
EEECCCCCCCCCCCC		26.8720058876
657PhosphorylationNGIAMVDYLQKAVLL
CCEECHHHHHHHHHH		10.3020068231
668PhosphorylationAVLLNLGTIELYGSN
HHHHCCCCEEECCCC		17.9120068231
672PhosphorylationNLGTIELYGSNDPYR
CCCCEEECCCCCCCC		13.0120068231
674PhosphorylationGTIELYGSNDPYRRE
CCEEECCCCCCCCCC		25.2220068231
678PhosphorylationLYGSNDPYRREPRSP
ECCCCCCCCCCCCCC		25.7620068231
683UbiquitinationDPYRREPRSPRKSRQ
CCCCCCCCCCCCCCC		55.3224816145
684PhosphorylationPYRREPRSPRKSRQP
CCCCCCCCCCCCCCC		39.5124719451
688PhosphorylationEPRSPRKSRQPSGAG
CCCCCCCCCCCCCCC		37.1123401153
692PhosphorylationPRKSRQPSGAGLCDI
CCCCCCCCCCCCCCC		32.7023401153
700PhosphorylationGAGLCDISEGTVVPE
CCCCCCCCCCEECCC		19.4030108239
703 (in isoform 2)Phosphorylation-17.8028111955
703PhosphorylationLCDISEGTVVPEDRC
CCCCCCCEECCCCCC		17.8023882029
712 (in isoform 2)Phosphorylation-36.7226657352
712PhosphorylationVPEDRCKSPTSGSSS
CCCCCCCCCCCCCCC		36.7228060719
714PhosphorylationEDRCKSPTSGSSSPH
CCCCCCCCCCCCCCC		53.4625850435
714 (in isoform 2)Phosphorylation-53.4628111955
715PhosphorylationDRCKSPTSGSSSPHN
CCCCCCCCCCCCCCC		39.8125850435
715 (in isoform 2)Phosphorylation-39.8128111955
717PhosphorylationCKSPTSGSSSPHNSD
CCCCCCCCCCCCCCC		27.6625850435
718PhosphorylationKSPTSGSSSPHNSDD
CCCCCCCCCCCCCCH		51.9525850435
719PhosphorylationSPTSGSSSPHNSDDE
CCCCCCCCCCCCCHH		31.6925850435
723PhosphorylationGSSSPHNSDDEQKMN
CCCCCCCCCHHHHHH		43.3218707149
723 (in isoform 2)Phosphorylation-43.3225849741
726 (in isoform 2)Phosphorylation-58.0329507054
729 (in isoform 3)Phosphorylation-5.0422210691
731 (in isoform 3)Phosphorylation-35.4622210691
732 (in isoform 3)Phosphorylation-6.9222210691
744PhosphorylationKTKSRKFSKMVANDI
HHHHHHHHHHHHHHH		23.9118669648
749PhosphorylationKFSKMVANDIAKMSR
HHHHHHHHHHHHHHH		29.7933259812
755PhosphorylationANDIAKMSRKLSLPT
HHHHHHHHHHCCCCC		26.0926074081
759PhosphorylationAKMSRKLSLPTDLKP
HHHHHHCCCCCCCCC		35.0229255136
762PhosphorylationSRKLSLPTDLKPDLD
HHHCCCCCCCCCCCC		60.2930278072
774PhosphorylationDLDVKDNSFSRSRSS
CCCCCCCCCCCCCCC		34.4323927012
776PhosphorylationDVKDNSFSRSRSSSV
CCCCCCCCCCCCCCC		29.2124260401
778PhosphorylationKDNSFSRSRSSSVTS
CCCCCCCCCCCCCEE		35.0025159151
780PhosphorylationNSFSRSRSSSVTSID
CCCCCCCCCCCEECC		28.3623927012
781PhosphorylationSFSRSRSSSVTSIDK
CCCCCCCCCCEECCH		27.9325463755
782PhosphorylationFSRSRSSSVTSIDKE
CCCCCCCCCEECCHH		30.5729255136
784PhosphorylationRSRSSSVTSIDKESR
CCCCCCCEECCHHHH		23.1623927012
785PhosphorylationSRSSSVTSIDKESRE
CCCCCCEECCHHHHH		27.0023927012
790PhosphorylationVTSIDKESREAISAL
CEECCHHHHHHHHHH		40.9623403867
851UbiquitinationIVSPSGTILRLKGAI
EECCCCHHHHHHHHH		2.1024816145
855MalonylationSGTILRLKGAILRMA
CCHHHHHHHHHHHHH		39.6026320211
871UbiquitinationLDTTGCLIPPAYEPW
ECCCCCCCCCCCCCH		4.4624816145
887UbiquitinationEHNVPEEKDEKEKLK
HCCCCCCHHHHHHHH		70.3124816145
900PhosphorylationLKKRRPVSVSPSSSQ
HHHCCCCCCCCCCCC		21.4021712546
902PhosphorylationKRRPVSVSPSSSQEI
HCCCCCCCCCCCCCC		16.1423401153
904PhosphorylationRPVSVSPSSSQEISE
CCCCCCCCCCCCCCC		34.8128450419
905PhosphorylationPVSVSPSSSQEISEN
CCCCCCCCCCCCCCC		39.1530576142
906PhosphorylationVSVSPSSSQEISENQ
CCCCCCCCCCCCCCC		35.8521712546
910PhosphorylationPSSSQEISENQYAVI
CCCCCCCCCCCEEEE		29.7328450419
914PhosphorylationQEISENQYAVICSEK
CCCCCCCEEEECCHH		17.8928450419
919PhosphorylationNQYAVICSEKQAKVI
CCEEEECCHHHCEEE		36.3828450419
924MalonylationICSEKQAKVISLPTQ
ECCHHHCEEEECCCC		37.2926320211
975PhosphorylationIMTFSLPSLRPLLDV
EEEEECCCCHHHEEE		42.1624719451
1039PhosphorylationELFTPVETPEAPNRG
HHCCCCCCCCCCCCC		27.0226657352
1058PhosphorylationLFGGGAQSLDREELF
CCCCCCCCCCHHHHH		31.5330624053
1076PhosphorylationSSGKASRSLAQHIPG
CCCHHHHHHHHCCCC		26.0927535140
1127PhosphorylationERTAAMLSSAESFSK
HHHHHHHHCHHHHHH		17.8925072903
1128PhosphorylationRTAAMLSSAESFSKH
HHHHHHHCHHHHHHH		31.9023401153
1131PhosphorylationAMLSSAESFSKHAHE
HHHHCHHHHHHHHHH		34.2423401153
1133PhosphorylationLSSAESFSKHAHEIM
HHCHHHHHHHHHHHH		32.5828857561
1142MethylationHAHEIMLKYKDKKWY
HHHHHHHHCCCCCCC		32.64-
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
723SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STXB5_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 STXB5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of STXB5_HUMAN !!
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 STXB5_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-785, AND MASSSPECTROMETRY.
"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-759; SER-782 ANDSER-785, 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 THR-784 AND SER-785, ANDMASS SPECTROMETRY.
"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-759, 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 THR-762, AND MASSSPECTROMETRY.

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