SYTL1_HUMAN - dbPTM
SYTL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYTL1_HUMAN
UniProt AC Q8IYJ3
Protein Name Synaptotagmin-like protein 1
Gene Name SYTL1
Organism Homo sapiens (Human).
Sequence Length 562
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . Peripheral membrane protein tightly bound to the cytoplasmic side of cellular membranes.
Protein Description May play a role in vesicle trafficking (By similarity). Binds phosphatidylinositol 3,4,5-trisphosphate. Acts as a RAB27A effector protein and may play a role in cytotoxic granule exocytosis in lymphocytes (By similarity)..
Protein Sequence MPQRGHPSQEGLWALPSLPMAHGPKPETEGLLDLSFLTEEEQEAIAGVLQRDARLRQLEEGRVSKLRASVADPGQLKILTGDWFQEARSQRHHNAHFGSDLVRASMRRKKSTRGDQAPGHDREAEAAVKEKEEGPEPRLTIDEAPQERLRETEGPDFPSPSVPLKASDPEEASQAQEDPGQGDQQVCAEEADPELEPASGGEQEPRPQQAQTKAASQILENGEEAPGPDPSLDRMLSSSSSVSSLNSSTLSGSQMSLSGDAEAVQVRGSVHFALHYEPGAAELRVHVIQCQGLAAARRRRSDPYVKSYLLPDKQSKRKTAVKKRNLNPVFNETLRYSVPQAELQGRVLSLSVWHRESLGRNIFLGEVEVPLDTWDWGSEPTWLPLQPRVPPSPDDLPSRGLLALSLKYVPAGSEGAGLPPSGELHFWVKEARDLLPLRAGSLDTYVQCFVLPDDSQASRQRTRVVRRSLSPVFNHTMVYDGFGPADLRQACAELSLWDHGALANRQLGGTRLSLGTGSSYGLQVPWMDSTPEEKQLWQALLEQPCEWVDGLLPLRTNLAPRT
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
8PhosphorylationMPQRGHPSQEGLWAL
CCCCCCCCCCCCCCC		34.8815998322
69PhosphorylationRVSKLRASVADPGQL
CHHHHHHHCCCCCCE		16.0515998322
111PhosphorylationASMRRKKSTRGDQAP
HHHHHCCCCCCCCCC		26.7728985074
112PhosphorylationSMRRKKSTRGDQAPG
HHHHCCCCCCCCCCC		47.7725056879
140PhosphorylationEGPEPRLTIDEAPQE
CCCCCCCCCCCCCHH		27.8823532336
152 (in isoform 2)Phosphorylation-39.5528348404
155 (in isoform 2)Phosphorylation-33.5628348404
159PhosphorylationTEGPDFPSPSVPLKA
CCCCCCCCCCCCCCC		29.7827050516
161 (in isoform 2)Phosphorylation-40.4828348404
161PhosphorylationGPDFPSPSVPLKASD
CCCCCCCCCCCCCCC		40.4823898821
199PhosphorylationDPELEPASGGEQEPR
CCCCCCCCCCCCCCC		59.0328961369
216PhosphorylationQAQTKAASQILENGE
HHHHHHHHHHHHCCC		23.7123401153
231PhosphorylationEAPGPDPSLDRMLSS
CCCCCCCCHHHHHHC		50.7325404012
237PhosphorylationPSLDRMLSSSSSVSS
CCHHHHHHCCCCCHH		20.87-
238PhosphorylationSLDRMLSSSSSVSSL
CHHHHHHCCCCCHHC		30.2227251275
239PhosphorylationLDRMLSSSSSVSSLN
HHHHHHCCCCCHHCC		24.2127251275
240PhosphorylationDRMLSSSSSVSSLNS
HHHHHCCCCCHHCCC		36.3928348404
241PhosphorylationRMLSSSSSVSSLNSS
HHHHCCCCCHHCCCC		28.1527251275
243PhosphorylationLSSSSSVSSLNSSTL
HHCCCCCHHCCCCCC		30.9328348404
244PhosphorylationSSSSSVSSLNSSTLS
HCCCCCHHCCCCCCC		29.4328348404
248PhosphorylationSVSSLNSSTLSGSQM
CCHHCCCCCCCCCEE		32.0928348404
249PhosphorylationVSSLNSSTLSGSQMS
CHHCCCCCCCCCEEE		25.4328348404
251PhosphorylationSLNSSTLSGSQMSLS
HCCCCCCCCCEEEEC		36.1728348404
253PhosphorylationNSSTLSGSQMSLSGD
CCCCCCCCEEEECCC		21.2328348404
301PhosphorylationAAARRRRSDPYVKSY
HHHHHHCCCCCHHHH		40.9228152594
304PhosphorylationRRRRSDPYVKSYLLP
HHHCCCCCHHHHCCC		26.0428152594
307PhosphorylationRSDPYVKSYLLPDKQ
CCCCCHHHHCCCCCH		15.8028152594
308PhosphorylationSDPYVKSYLLPDKQS
CCCCHHHHCCCCCHH		13.4128152594
392PhosphorylationLQPRVPPSPDDLPSR
CCCCCCCCCCCCCCC		34.5923401153
398PhosphorylationPSPDDLPSRGLLALS
CCCCCCCCCCEEEEE		46.4029691806
405PhosphorylationSRGLLALSLKYVPAG
CCCEEEEEEEEECCC		19.7424719451
468PhosphorylationRTRVVRRSLSPVFNH
HHHHHHHHHCCCCCC		23.7225106551
470PhosphorylationRVVRRSLSPVFNHTM
HHHHHHHCCCCCCCE		21.9222617229
476PhosphorylationLSPVFNHTMVYDGFG
HCCCCCCCEEECCCC		14.9425106551
479PhosphorylationVFNHTMVYDGFGPAD
CCCCCEEECCCCHHH		10.2629978859
522UbiquitinationGTGSSYGLQVPWMDS
CCCCCCCCCCCCCCC		3.3530230243
534UbiquitinationMDSTPEEKQLWQALL
CCCCHHHHHHHHHHH		49.3730230243
562PhosphorylationRTNLAPRT-------
CCCCCCCC-------		41.7327251275
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
241SPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYTL1_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 SYTL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCF2_HUMANNCF2physical
11278853
NCF1_HUMANNCF1physical
11278853
RB27A_HUMANRAB27Aphysical
11980908
RB27A_HUMANRAB27Aphysical
11773082
RAB8A_HUMANRAB8Aphysical
23140275
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 SYTL1_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-392, AND MASSSPECTROMETRY.

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