SYTL4_HUMAN - dbPTM
SYTL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYTL4_HUMAN
UniProt AC Q96C24
Protein Name Synaptotagmin-like protein 4
Gene Name SYTL4
Organism Homo sapiens (Human).
Sequence Length 671
Subcellular Localization Membrane
Peripheral membrane protein. Cell membrane
Peripheral membrane protein. Cytoplasmic vesicle, secretory vesicle membrane
Peripheral membrane protein. Detected close to the plasma membrane and on secretory granules. In pancreas, interacts w
Protein Description Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity)..
Protein Sequence MSELLDLSFLSEEEKDLILSVLQRDEEVRKADEKRIRRLKNELLEIKRKGAKRGSQHYSDRTCARCQESLGRLSPKTNTCRGCNHLVCRDCRIQESNGTWRCKVCAKEIELKKATGDWFYDQKVNRFAYRTGSEIIRMSLRHKPAVSKRETVGQSLLHQTQMGDIWPGRKIIQERQKEPSVLFEVPKLKSGKSALEAESESLDSFTADSDSTSRRDSLDKSGLFPEWKKMSAPKSQVEKETQPGGQNVVFVDEGEMIFKKNTRKILRPSEYTKSVIDLRPEDVVHESGSLGDRSKSVPGLNVDMEEEEEEEDIDHLVKLHRQKLARSSMQSGSSMSTIGSMMSIYSEAGDFGNIFVTGRIAFSLKYEQQTQSLVVHVKECHQLAYADEAKKRSNPYVKTYLLPDKSRQGKRKTSIKRDTINPLYDETLRYEIPESLLAQRTLQFSVWHHGRFGRNTFLGEAEIQMDSWKLDKKLDHCLPLHGKISAESPTGLPSHKGELVVSLKYIPASKTPVGGDRKKSKGGEGGELQVWIKEAKNLTAAKAGGTSDSFVKGYLLPMRNKASKRKTPVMKKTLNPHYNHTFVYNGVRLEDLQHMCLELTVWDREPLASNDFLGGVRLGVGTGISNGEVVDWMDSTGEEVSLWQKMRQYPGSWAEGTLQLRSSMAKQKLGL
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
2Phosphorylation------MSELLDLSF
------CCHHHCHHH		36.6325159151
8PhosphorylationMSELLDLSFLSEEEK
CCHHHCHHHCCHHHH		24.6528348404
11PhosphorylationLLDLSFLSEEEKDLI
HHCHHHCCHHHHHHH		40.7422199227
47UbiquitinationKNELLEIKRKGAKRG
HHHHHHHHHHCCCCC		38.39-
69PhosphorylationTCARCQESLGRLSPK
HHHHHHHHHHCCCCC		15.3928060719
74PhosphorylationQESLGRLSPKTNTCR
HHHHHCCCCCCCCCC		24.0023898821
123UbiquitinationGDWFYDQKVNRFAYR
CCCHHHHHCCEEEHH		38.28-
130MethylationKVNRFAYRTGSEIIR
HCCEEEHHHHHHHHH		29.22115918085
133PhosphorylationRFAYRTGSEIIRMSL
EEEHHHHHHHHHHHH		25.6329970186
137MethylationRTGSEIIRMSLRHKP
HHHHHHHHHHHHCCC		17.82115918089
177UbiquitinationKIIQERQKEPSVLFE
HHHHHHHCCCCEEEE		77.23-
180PhosphorylationQERQKEPSVLFEVPK
HHHHCCCCEEEECCC		32.3228060719
193PhosphorylationPKLKSGKSALEAESE
CCCCCCCCHHHHHHH		41.4325850435
199PhosphorylationKSALEAESESLDSFT
CCHHHHHHHCHHHCC		39.2630631047
201PhosphorylationALEAESESLDSFTAD
HHHHHHHCHHHCCCC		46.9130175587
204PhosphorylationAESESLDSFTADSDS
HHHHCHHHCCCCCCC		29.7730175587
206PhosphorylationSESLDSFTADSDSTS
HHCHHHCCCCCCCCC		33.2430631047
209PhosphorylationLDSFTADSDSTSRRD
HHHCCCCCCCCCCHH		30.8828450419
211PhosphorylationSFTADSDSTSRRDSL
HCCCCCCCCCCHHHC		32.0328450419
212PhosphorylationFTADSDSTSRRDSLD
CCCCCCCCCCHHHCC		31.1028450419
213PhosphorylationTADSDSTSRRDSLDK
CCCCCCCCCHHHCCC		29.3028450419
217PhosphorylationDSTSRRDSLDKSGLF
CCCCCHHHCCCCCCC		36.3323401153
220UbiquitinationSRRDSLDKSGLFPEW
CCHHHCCCCCCCHHH		52.28-
221PhosphorylationRRDSLDKSGLFPEWK
CHHHCCCCCCCHHHH		40.1623927012
231PhosphorylationFPEWKKMSAPKSQVE
CHHHHHCCCCHHHCE		50.75-
269PhosphorylationTRKILRPSEYTKSVI
CCHHCCHHHCCCCHH		36.4823186163
271PhosphorylationKILRPSEYTKSVIDL
HHCCHHHCCCCHHCC		24.6528152594
272PhosphorylationILRPSEYTKSVIDLR
HCCHHHCCCCHHCCC		16.8823186163
274PhosphorylationRPSEYTKSVIDLRPE
CHHHCCCCHHCCCHH		19.2623401153
287PhosphorylationPEDVVHESGSLGDRS
HHHCCCCCCCCCCCC		20.8530266825
289PhosphorylationDVVHESGSLGDRSKS
HCCCCCCCCCCCCCC		38.1623401153
294PhosphorylationSGSLGDRSKSVPGLN
CCCCCCCCCCCCCCC		33.7423401153
296PhosphorylationSLGDRSKSVPGLNVD
CCCCCCCCCCCCCCC		34.4923401153
327 (in isoform 2)Phosphorylation-25.2622210691
327PhosphorylationHRQKLARSSMQSGSS
HHHHHHHHHCCCCCC		25.2628060719
328 (in isoform 2)Phosphorylation-18.4522210691
328PhosphorylationRQKLARSSMQSGSSM
HHHHHHHHCCCCCCH		18.4528060719
331PhosphorylationLARSSMQSGSSMSTI
HHHHHCCCCCCHHHH		31.8128060719
331 (in isoform 2)Phosphorylation-31.8122210691
333PhosphorylationRSSMQSGSSMSTIGS
HHHCCCCCCHHHHHH		28.2828060719
334PhosphorylationSSMQSGSSMSTIGSM
HHCCCCCCHHHHHHH		21.9328060719
336PhosphorylationMQSGSSMSTIGSMMS
CCCCCCHHHHHHHHH		20.8628060719
337PhosphorylationQSGSSMSTIGSMMSI
CCCCCHHHHHHHHHH		22.2528060719
340PhosphorylationSSMSTIGSMMSIYSE
CCHHHHHHHHHHHHC		13.8828060719
343PhosphorylationSTIGSMMSIYSEAGD
HHHHHHHHHHHCCCC		15.1028060719
345PhosphorylationIGSMMSIYSEAGDFG
HHHHHHHHHCCCCCC		7.9828270605
346PhosphorylationGSMMSIYSEAGDFGN
HHHHHHHHCCCCCCC		21.2123403867
357PhosphorylationDFGNIFVTGRIAFSL
CCCCEEEEEEEEEEE		15.2524719451
363PhosphorylationVTGRIAFSLKYEQQT
EEEEEEEEEECHHHC		18.2224719451
366PhosphorylationRIAFSLKYEQQTQSL
EEEEEEECHHHCCEE		25.02-
396PhosphorylationAKKRSNPYVKTYLLP
HHHHCCCCCEEEECC		20.87-
456PhosphorylationHGRFGRNTFLGEAEI
CCCCCCCCEECEEEE		20.9027050516
485PhosphorylationLPLHGKISAESPTGL
EECCCEEECCCCCCC		29.4830266825
488PhosphorylationHGKISAESPTGLPSH
CCEEECCCCCCCCCC		27.7230266825
490PhosphorylationKISAESPTGLPSHKG
EEECCCCCCCCCCCC		61.7130266825
494PhosphorylationESPTGLPSHKGELVV
CCCCCCCCCCCEEEE		42.7628060719
510UbiquitinationLKYIPASKTPVGGDR
EEEEECCCCCCCCCC		59.98-
511PhosphorylationKYIPASKTPVGGDRK
EEEECCCCCCCCCCC		22.2523403867
520PhosphorylationVGGDRKKSKGGEGGE
CCCCCCCCCCCCCCC		39.3027251275
546PhosphorylationTAAKAGGTSDSFVKG
CCHHCCCCCHHHHHH		28.57-
547PhosphorylationAAKAGGTSDSFVKGY
CHHCCCCCHHHHHHH		34.23-
554PhosphorylationSDSFVKGYLLPMRNK
CHHHHHHHCHHCCCC		10.1928102081
563PhosphorylationLPMRNKASKRKTPVM
HHCCCCCCCCCCCCC		34.30-
567PhosphorylationNKASKRKTPVMKKTL
CCCCCCCCCCCHHCC		25.75-
600PhosphorylationQHMCLELTVWDREPL
HHHHEECEECCCCCC		15.3526074081
609PhosphorylationWDREPLASNDFLGGV
CCCCCCCCCCCCCCC		44.6126074081
622PhosphorylationGVRLGVGTGISNGEV
CCEEEECCCCCCCEE		29.0026074081
625PhosphorylationLGVGTGISNGEVVDW
EEECCCCCCCEEEEC		39.8826074081
649PhosphorylationLWQKMRQYPGSWAEG
HHHHHHCCCCCHHHH		10.1321712546
652PhosphorylationKMRQYPGSWAEGTLQ
HHHCCCCCHHHHHHH		20.7121712546
657PhosphorylationPGSWAEGTLQLRSSM
CCCHHHHHHHHHHHH		11.6624719451
662PhosphorylationEGTLQLRSSMAKQKL
HHHHHHHHHHHHHHH		32.8124719451
666AcetylationQLRSSMAKQKLGL--
HHHHHHHHHHHCC--		39.057664603
668AcetylationRSSMAKQKLGL----
HHHHHHHHHCC----		43.767664613
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 SYTL4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYTL4_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 SYTL4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STXB1_HUMANSTXBP1physical
12590134
STX1A_HUMANSTX1Aphysical
12590134
RB27A_HUMANRAB27Aphysical
12590134
RAB3A_HUMANRAB3Aphysical
12590134
RAB8A_HUMANRAB8Aphysical
12590134
RAB8A_HUMANRAB8Aphysical
12176990
RB27A_HUMANRAB27Aphysical
12176990
STX1A_HUMANSTX1Aphysical
12101244
RB27A_HUMANRAB27Aphysical
11773082
RAB8A_HUMANRAB8Aphysical
11773082
RAB3A_HUMANRAB3Aphysical
11773082
RAB8A_HUMANRAB8Aphysical
23140275
STXB1_HUMANSTXBP1physical
15563604
RAB8A_HUMANRAB8Aphysical
24700782
RB27A_HUMANRAB27Aphysical
24700782
STXB1_HUMANSTXBP1physical
24700782
STX3_HUMANSTX3physical
24700782
STX2_HUMANSTX2physical
24700782
STX3_HUMANSTX3physical
26553929
RAB3B_HUMANRAB3Bphysical
26553929
RAB8A_HUMANRAB8Aphysical
26553929
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
DB00030Insulin Regular
Regulatory Network of SYTL4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-201; SER-204; SER-217AND SER-289, AND MASS 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-74; SER-201; SER-204;SER-289 AND SER-488, AND MASS SPECTROMETRY.
"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-289, AND MASSSPECTROMETRY.

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