dbPTM

SYT1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYT1_RAT
UniProt AC	P21707
Protein Name	Synaptotagmin-1
Gene Name	Syt1
Organism	Rattus norvegicus (Rat).
Sequence Length	421
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 Single-p
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..
Protein Sequence	MVSASHPEALAAPVTTVATLVPHNATEPASPGEGKEDAFSKLKQKFMNELHKIPLPPWALIAIAIVAVLLVVTCCFCVCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	N-linked_Glycosylation	VATLVPHNATEPASP EEEECCCCCCCCCCC	42.35	-
74	S-palmitoylation	AVLLVVTCCFCVCKK HHHHHHHHHHHHHHH	0.83	15355980
75	S-palmitoylation	VLLVVTCCFCVCKKC HHHHHHHHHHHHHHH	1.85	15355980
77	S-palmitoylation	LVVTCCFCVCKKCLF HHHHHHHHHHHHHHH	1.88	15355980
79	S-palmitoylation	VTCCFCVCKKCLFKK HHHHHHHHHHHHHHH	3.52	15355980
82	S-palmitoylation	CFCVCKKCLFKKKNK HHHHHHHHHHHHCCC	3.10	15355980
98	Ubiquitination	KGKEKGGKNAINMKD CCCCCCCCCCCCHHH	52.45	-
98	Acetylation	KGKEKGGKNAINMKD CCCCCCCCCCCCHHH	52.45	22902405
104	Ubiquitination	GKNAINMKDVKDLGK CCCCCCHHHHHHHHH	55.68	-
112	Phosphorylation	DVKDLGKTMKDQALK HHHHHHHHHHHHHHC	27.88	10461881
119	Ubiquitination	TMKDQALKDDDAETG HHHHHHHCCCCCCCC	63.23	-
125	Phosphorylation	LKDDDAETGLTDGEE HCCCCCCCCCCCCCC	38.93	-
128	Phosphorylation	DDAETGLTDGEEKEE CCCCCCCCCCCCCCC	43.21	30411139
151	Nitration	KLQYSLDYDFQNNQL CCEEEEECCCCCCEE	24.77	-
190	Ubiquitination	VFLLPDKKKKFETKV EEECCCCCCCCCCHH	69.45	-
196	Ubiquitination	KKKKFETKVHRKTLN CCCCCCCHHCHHCCC	28.93	-
200	Ubiquitination	FETKVHRKTLNPVFN CCCHHCHHCCCHHHC	42.35	-
213	Acetylation	FNEQFTFKVPYSELG HCCCEEEECCHHHHC	38.96	22902405
216	Nitration	QFTFKVPYSELGGKT CEEEECCHHHHCCEE	20.12	-
229	Nitration	KTLVMAVYDFDRFSK EEEEEEEEECCCCCC	11.01	-
229	Phosphorylation	KTLVMAVYDFDRFSK EEEEEEEEECCCCCC	11.01	-
236	Ubiquitination	YDFDRFSKHDIIGEF EECCCCCCCCEEEEE	42.45	-
264	Phosphorylation	EEWRDLQSAEKEEQE HHHHHHHHHHHHHHH	45.77	-
267	Ubiquitination	RDLQSAEKEEQEKLG HHHHHHHHHHHHHHH	67.29	-
267	Acetylation	RDLQSAEKEEQEKLG HHHHHHHHHHHHHHH	67.29	22902405
285	Phosphorylation	FSLRYVPTAGKLTVV HHEEECCCCCEEEEE	37.69	27115346
297	Ubiquitination	TVVILEAKNLKKMDV EEEEEEECCCCCCCC	54.13	-
311	Phosphorylation	VGGLSDPYVKIHLMQ CCCCCCCHHHHEEHH	21.26	-
311	Nitration	VGGLSDPYVKIHLMQ CCCCCCCHHHHEEHH	21.26	-
321	Acetylation	IHLMQNGKRLKKKKT HEEHHCCCCCCCCCC	63.21	22902405
342	Phosphorylation	LNPYYNESFSFEVPF CCCCCCCCCEEECCH	23.66	22673903
344	Phosphorylation	PYYNESFSFEVPFEQ CCCCCCCEEECCHHH	29.76	25705886
364	Phosphorylation	VVVTVLDYDKIGKND EEEEECCHHHCCCCC	18.25	-
364	Nitration	VVVTVLDYDKIGKND EEEEECCHHHCCCCC	18.25	-
369	Ubiquitination	LDYDKIGKNDAIGKV CCHHHCCCCCCCCEE	55.94	-
375	Ubiquitination	GKNDAIGKVFVGYNS CCCCCCCEEEEECCC	26.79	-
380	Phosphorylation	IGKVFVGYNSTGAEL CCEEEEECCCCCHHH	10.71	-
380	Nitration	IGKVFVGYNSTGAEL CCEEEEECCCCCHHH	10.71	-

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
112	T	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
112	T	Phosphorylation	Kinase	CAMK2A	P11275	PSP
112	T	Phosphorylation	Kinase	PRKCA	P05696	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SYT1_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SYT1_RAT !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SYT1_RAT

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Palmitoylation sites and processing of synaptotagmin I, the putativecalcium sensor for neurosecretion."; Heindel U., Schmidt M.F., Veit M.; FEBS Lett. 544:57-62(2003). Cited for: PALMITOYLATION AT CYS-74; CYS-75; CYS-77; CYS-79 AND CYS-82.	12782290 [Abstract]