SYT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SYT1_MOUSE
• UniProt AC: P46096
• Protein Name: Synaptotagmin-1
• Gene Name: Syt1
• Organism: Mus musculus (Mouse).
• Sequence Length: 421
• Subcellular Localization: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Single-pass membrane protein . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Single-pass membrane protein . Cytoplasmic vesicle, secretory vesicle, chromaffin granul
• Protein Description: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. [PubMed: 7961887 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 (By similarity]
• Protein Sequence: MVSASRPEALAAPVTTVATLVPHNATEPASPGEGKEDAFSKLKQKFMNELHKIPLPPWALIAIAIVAVLLVVTCCFCVCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK

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
15	O-linked_Glycosylation	EALAAPVTTVATLVP HHHHCCCEEEEEECC	17.94	12048209
16	O-linked_Glycosylation	ALAAPVTTVATLVPH HHHCCCEEEEEECCC	14.37	12048209
24	N-linked_Glycosylation	VATLVPHNATEPASP EEEECCCCCCCCCCC	42.35	-
74	S-palmitoylation	AVLLVVTCCFCVCKK HHHHHHHHHHHHHHH	0.83	-
75	S-palmitoylation	VLLVVTCCFCVCKKC HHHHHHHHHHHHHHH	1.85	-
77	S-palmitoylation	LVVTCCFCVCKKCLF HHHHHHHHHHHHHHH	1.88	-
79	S-palmitoylation	VTCCFCVCKKCLFKK HHHHHHHHHHHHHHH	3.52	-
82	S-palmitoylation	CFCVCKKCLFKKKNK HHHHHHHHHHHHCCC	3.10	-
104	Ubiquitination	GKNAINMKDVKDLGK CCCCCCHHHHHHHHH	55.68	22790023
112	Phosphorylation	DVKDLGKTMKDQALK HHHHHHHHHHHHHHC	27.88	29899451
114	Ubiquitination	KDLGKTMKDQALKDD HHHHHHHHHHHHCCC	52.50	-
119	Ubiquitination	TMKDQALKDDDAETG HHHHHHHCCCCCCCC	63.23	22790023
125	Phosphorylation	LKDDDAETGLTDGEE HCCCCCCCCCCCCCC	38.93	25521595
128	Phosphorylation	DDAETGLTDGEEKEE CCCCCCCCCCCCCCC	43.21	25521595
133	Ubiquitination	GLTDGEEKEEPKEEE CCCCCCCCCCCHHHH	64.18	22790023
189	Ubiquitination	KVFLLPDKKKKFETK EEEECCCCCCCCCCH	65.63	22790023
200	Ubiquitination	FETKVHRKTLNPVFN CCCHHCHHCCCHHHC	42.35	22790023
201	Phosphorylation	ETKVHRKTLNPVFNE CCHHCHHCCCHHHCC	31.55	25521595
213	Ubiquitination	FNEQFTFKVPYSELG HCCCEEEECCHHHHC	38.96	22790023
223	Phosphorylation	YSELGGKTLVMAVYD HHHHCCEEEEEEEEE	28.05	25177544
229	Phosphorylation	KTLVMAVYDFDRFSK EEEEEEEEECCCCCC	11.01	22817900
235	Phosphorylation	VYDFDRFSKHDIIGE EEECCCCCCCCEEEE	29.94	29899451
236	Ubiquitination	YDFDRFSKHDIIGEF EECCCCCCCCEEEEE	42.45	22790023
264	Phosphorylation	EEWRDLQSAEKEEQE HHHHHHHHHHHHHHH	45.77	22817900
267	Ubiquitination	RDLQSAEKEEQEKLG HHHHHHHHHHHHHHH	67.29	22790023
272	Ubiquitination	AEKEEQEKLGDICFS HHHHHHHHHHHHHHH	58.42	22790023
277	S-nitrosylation	QEKLGDICFSLRYVP HHHHHHHHHHEEECC	1.95	24895380
285	Phosphorylation	FSLRYVPTAGKLTVV HHEEECCCCCEEEEE	37.69	25521595
297	Ubiquitination	TVVILEAKNLKKMDV EEEEEEECCCCCCCC	54.13	22790023
301	Ubiquitination	LEAKNLKKMDVGGLS EEECCCCCCCCCCCC	43.42	22790023
308	Phosphorylation	KMDVGGLSDPYVKIH CCCCCCCCCCHHHHE	39.55	20415495
311	Phosphorylation	VGGLSDPYVKIHLMQ CCCCCCCHHHHEEHH	21.26	22817900
313	Ubiquitination	GLSDPYVKIHLMQNG CCCCCHHHHEEHHCC	20.68	22790023
321	Ubiquitination	IHLMQNGKRLKKKKT HEEHHCCCCCCCCCC	63.21	22790023
332	Ubiquitination	KKKTTIKKNTLNPYY CCCCCCCCCCCCCCC	51.84	22790023
339	Phosphorylation	KNTLNPYYNESFSFE CCCCCCCCCCCCEEE	17.45	29899451
342	Phosphorylation	LNPYYNESFSFEVPF CCCCCCCCCEEECCH	23.66	29899451
344	Phosphorylation	PYYNESFSFEVPFEQ CCCCCCCEEECCHHH	29.76	22817900
364	Phosphorylation	VVVTVLDYDKIGKND EEEEECCHHHCCCCC	18.25	-
369	Ubiquitination	LDYDKIGKNDAIGKV CCHHHCCCCCCCCEE	55.94	22790023
375	Ubiquitination	GKNDAIGKVFVGYNS CCCCCCCEEEEECCC	26.79	22790023
380	Phosphorylation	IGKVFVGYNSTGAEL CCEEEEECCCCCHHH	10.71	22817900
382	Phosphorylation	KVFVGYNSTGAELRH EEEEECCCCCHHHHH	21.53	29899451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SYT1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SYT1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SYT1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SYT1_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128, AND MASSSPECTROMETRY.
PubMed: 17114649

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-229 AND TYR-380, ANDMASS SPECTROMETRY.
PubMed: 18034455