SYT1_HUMAN - dbPTM
SYT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYT1_HUMAN
UniProt AC P21579
Protein Name Synaptotagmin-1
Gene Name SYT1
Organism Homo sapiens (Human).
Sequence Length 422
Subcellular Localization Cytoplasmic vesicle, secretory vesicle membrane
Single-pass membrane protein . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
Single-pass membrane protein . Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane
Singl
Protein Description May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes. [PubMed: 23999003]
Protein Sequence MVSESHHEALAAPPVTTVATVLPSNATEPASPGEGKEDAFSKLKEKFMNELHKIPLPPWALIAIAIVAVLLVLTCCFCICKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK
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
24PhosphorylationTVATVLPSNATEPAS
EEEEECCCCCCCCCC		34.63-
25N-linked_GlycosylationVATVLPSNATEPASP
EEEECCCCCCCCCCC		49.28UniProtKB CARBOHYD
27O-linked_GlycosylationTVLPSNATEPASPGE
EECCCCCCCCCCCCC		46.91OGP
75S-palmitoylationAVLLVLTCCFCICKK
HHHHHHHHHHHHHHH		1.14-
76S-palmitoylationVLLVLTCCFCICKKC
HHHHHHHHHHHHHHH		2.34-
78S-palmitoylationLVLTCCFCICKKCLF
HHHHHHHHHHHHHHH		1.92-
80S-palmitoylationLTCCFCICKKCLFKK
HHHHHHHHHHHHHHH		3.47-
83S-palmitoylationCFCICKKCLFKKKNK
HHHHHHHHHHHHCCC		3.10-
105UbiquitinationGKNAINMKDVKDLGK
CCCCCCHHHHHHHHH		55.68-
120UbiquitinationTMKDQALKDDDAETG
HHHHHHHCCCCCCCC		63.2321906983
126PhosphorylationLKDDDAETGLTDGEE
HCCCCCCCCCCCCCC		38.9318510355
129PhosphorylationDDAETGLTDGEEKEE
CCCCCCCCCCCCCCC		43.2122617229
134UbiquitinationGLTDGEEKEEPKEEE
CCCCCCCCCCCHHHH		64.1821906983
181PhosphorylationMGGTSDPYVKVFLLP
CCCCCCCCEEEEECC		20.2125884760
202PhosphorylationETKVHRKTLNPVFNE
CCHHCHHCCCHHHCC		31.5519664994
212PhosphorylationPVFNEQFTFKVPYSE
HHHCCCEEEECCHHH		23.4219664994
217PhosphorylationQFTFKVPYSELGGKT
CEEEECCHHHHCCEE		20.1225884760
230PhosphorylationKTLVMAVYDFDRFSK
EEEEEEEEECCCCCC		11.0119060867
237AcetylationYDFDRFSKHDIIGEF
EECCCCCCCCEEEEE		42.4519608861
265PhosphorylationEEWRDLQSAEKEEQE
HHHHHHHHHHHHHHH		45.7724076635
268UbiquitinationRDLQSAEKEEQEKLG
HHHHHHHHHHHHHHH		67.29-
302AcetylationLEAKNLKKMDVGGLS
EEECCCCCCCCCCCC		43.4230592777
312PhosphorylationVGGLSDPYVKIHLMQ
CCCCCCCHHHHEEHH		21.2625884760
329PhosphorylationKRLKKKKTTIKKNTL
CCCCCCCCCCCCCCC		42.5022817900
330PhosphorylationRLKKKKTTIKKNTLN
CCCCCCCCCCCCCCC		39.4122817900
333UbiquitinationKKKTTIKKNTLNPYY
CCCCCCCCCCCCCCC		51.8421906983
343PhosphorylationLNPYYNESFSFEVPF
CCCCCCCCCEEECCH		23.66-
345PhosphorylationPYYNESFSFEVPFEQ
CCCCCCCEEECCHHH		29.76-
365PhosphorylationVVVTVLDYDKIGKND
EEEEECCHHHCCCCC		18.2521082442
381PhosphorylationIGKVFVGYNSTGAEL
CCEEEEECCCCCHHH		10.7128152594
383PhosphorylationKVFVGYNSTGAELRH
EEEEECCCCCHHHHH		21.5328152594
384PhosphorylationVFVGYNSTGAELRHW
EEEECCCCCHHHHHH		36.4528152594
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 SYT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYT1_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 SYT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SV2B_HUMANSV2Bphysical
15466855
CF015_HUMANC6orf15physical
15466855
SV2C_HUMANSV2Cphysical
15466855
STX1A_HUMANSTX1Aphysical
9010211
HNRPQ_HUMANSYNCRIPphysical
10734137
SNP25_HUMANSNAP25physical
10692432
CAC1A_HUMANCACNA1Aphysical
9303303
SNP25_HUMANSNAP25physical
12062043
STX1A_HUMANSTX1Aphysical
10397765
FGF1_HUMANFGF1physical
11432880
RBM14_HUMANRBM14physical
15919756
SIN3A_HUMANSIN3Aphysical
15467731
SYT2_HUMANSYT2physical
28514442
VLDLR_HUMANVLDLRphysical
28514442
CWC22_HUMANCWC22physical
28514442
EI2BG_HUMANEIF2B3physical
28514442
EI2BE_HUMANEIF2B5physical
28514442
EI2BD_HUMANEIF2B4physical
28514442
PGK2_HUMANPGK2physical
28514442
EI2BB_HUMANEIF2B2physical
28514442
LRP2_HUMANLRP2physical
28514442
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 SYT1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237, AND MASS SPECTROMETRY.

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