SYT7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SYT7_HUMAN
• UniProt AC: O43581
• Protein Name: Synaptotagmin-7 {ECO:0000305}
• Gene Name: SYT7 {ECO:0000312|HGNC:HGNC:11514}
• Organism: Homo sapiens (Human).
• Sequence Length: 403
• Subcellular Localization: Cell membrane ; Single-pass membrane protein . Cell junction, synapse, presynaptic cell membrane ; Single-pass membrane protein . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane ; Single-pass membrane protein . Lysosome membrane ; Single
• Protein Description: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory and synaptic vesicles through Ca(2+) and phospholipid binding to the C2 domain (By similarity). Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity). SYT7 binds Ca(2+) with high affinity and slow kinetics compared to other synaptotagmins (By similarity). Involved in Ca(2+)-triggered lysosomal exocytosis, a major component of the plasma membrane repair. [PubMed: 11342594 Ca(2+)-regulated delivery of lysosomal membranes to the cell surface is also involved in the phagocytic uptake of particles by macrophages (By similarity Ca(2+)-triggered lysosomal exocytosis also plays a role in bone remodeling by regulating secretory pathways in osteoclasts and osteoblasts (By similarity In case of infection, involved in participates cell invasion by Trypanosoma cruzi via Ca(2+)-triggered lysosomal exocytosis]
• Protein Sequence: MYRDPEAASPGAPSRDVLLVSAIITVSLSVTVVLCGLCHWCQRKLGKRYKNSLETVGTPDSGRGRSEKKAIKLPAGGKAVNTAPVPGQTPHDESDRRTEPRSSVSDLVNSLTSEMLMLSPGSEEDEAHEGCSRENLGRIQFSVGYNFQESTLTVKIMKAQELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEGFPYEKVVQRILYLQVLDYDRFSRNDPIGEVSIPLNKVDLTQMQTFWKDLKPCSDGSGSRGELLLSLCYNPSANSIIVNIIKARNLKAMDIGGTSDPYVKVWLMYKDKRVEKKKTVTMKRNLNPIFNESFAFDIPTEKLRETTIIITVMDKDKLSRNDVIGKIYLSWKSGPGEVKHWKDMIARPRQPVAQWHQLKA

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
2	Phosphorylation	------MYRDPEAAS ------CCCCHHHCC	24.59	23663014
9	Phosphorylation	YRDPEAASPGAPSRD CCCHHHCCCCCCCHH	30.80	23663014
49	Phosphorylation	QRKLGKRYKNSLETV HHHHHHHHHCHHHCC	20.29	27732954
50	Ubiquitination	RKLGKRYKNSLETVG HHHHHHHHCHHHCCC	44.06	32142685
52	Phosphorylation	LGKRYKNSLETVGTP HHHHHHCHHHCCCCC	24.35	22617229
55	Phosphorylation	RYKNSLETVGTPDSG HHHCHHHCCCCCCCC	29.54	25849741
58	Phosphorylation	NSLETVGTPDSGRGR CHHHCCCCCCCCCCC	21.42	30278072
58 (in isoform 6)	Phosphorylation	-	21.42	25849741
58 (in isoform 5)	Phosphorylation	-	21.42	25849741
58 (in isoform 4)	Phosphorylation	-	21.42	25849741
58 (in isoform 3)	Phosphorylation	-	21.42	25849741
61 (in isoform 6)	Phosphorylation	-	31.43	25849741
61 (in isoform 5)	Phosphorylation	-	31.43	25849741
61 (in isoform 4)	Phosphorylation	-	31.43	25849741
61 (in isoform 3)	Phosphorylation	-	31.43	25849741
61	Phosphorylation	ETVGTPDSGRGRSEK HCCCCCCCCCCCCCC	31.43	25849741
82	Phosphorylation	AGGKAVNTAPVPGQT CCCEEEECCCCCCCC	26.24	23312004
89	Phosphorylation	TAPVPGQTPHDESDR CCCCCCCCCCCCCCC	28.62	28348404
94	Phosphorylation	GQTPHDESDRRTEPR CCCCCCCCCCCCCCC	42.34	28348404
98	Phosphorylation	HDESDRRTEPRSSVS CCCCCCCCCCCCHHH	51.76	28348404
102	Phosphorylation	DRRTEPRSSVSDLVN CCCCCCCCHHHHHHH	45.89	26657352
103	Phosphorylation	RRTEPRSSVSDLVNS CCCCCCCHHHHHHHH	27.24	28348404
105	Phosphorylation	TEPRSSVSDLVNSLT CCCCCHHHHHHHHHH	27.46	28348404
112 (in isoform 2)	Phosphorylation	-	23.59	28102081
118 (in isoform 2)	Phosphorylation	-	5.00	28102081
119	Phosphorylation	TSEMLMLSPGSEEDE HHHHHCCCCCCHHHH	17.16	27251275
122	Phosphorylation	MLMLSPGSEEDEAHE HHCCCCCCHHHHHHC	40.99	28348404
122 (in isoform 2)	Phosphorylation	-	40.99	28102081
142	Phosphorylation	NLGRIQFSVGYNFQE HCCCEEEEEECCCCC	9.77	28270605
145	Phosphorylation	RIQFSVGYNFQESTL CEEEEEECCCCCCEE	15.62	28270605
145 (in isoform 4)	Phosphorylation	-	15.62	28842319
150	Phosphorylation	VGYNFQESTLTVKIM EECCCCCCEEEEEEE	20.24	28270605
151 (in isoform 4)	Phosphorylation	-	26.20	27135362
151	Phosphorylation	GYNFQESTLTVKIMK ECCCCCCEEEEEEEE	26.20	28270605
153	Phosphorylation	NFQESTLTVKIMKAQ CCCCCEEEEEEEECC	21.60	28270605
156 (in isoform 3)	Phosphorylation	-	2.73	28102081
156 (in isoform 5)	Phosphorylation	-	2.73	28102081
157 (in isoform 4)	Phosphorylation	-	2.14	28842319
158	Acetylation	TLTVKIMKAQELPAK EEEEEEEECCCCCCC	50.84	7409969
162 (in isoform 5)	Phosphorylation	-	3.12	28102081
162 (in isoform 3)	Phosphorylation	-	3.12	28102081
166 (in isoform 3)	Phosphorylation	-	45.08	28102081
166 (in isoform 5)	Phosphorylation	-	45.08	28102081
176	Acetylation	GTSDPFVKIYLLPDK CCCCCCEEEEECCCC	26.47	7409979
197	Phosphorylation	KVKRKNLNPHWNETF HCCCCCCCCCCCCCC	35.47	27251275
220 (in isoform 3)	Phosphorylation	-	7.85	28842319
226 (in isoform 3)	Phosphorylation	-	12.59	27135362
232 (in isoform 3)	Phosphorylation	-	59.20	28842319
301	Phosphorylation	KAMDIGGTSDPYVKV CCEECCCCCCHHHEE	25.41	28102081
302	Phosphorylation	AMDIGGTSDPYVKVW CEECCCCCCHHHEEE	39.60	28102081
305	Phosphorylation	IGGTSDPYVKVWLMY CCCCCCHHHEEEEEE	20.21	28102081
312	Phosphorylation	YVKVWLMYKDKRVEK HHEEEEEECCCCCCC	17.54	-
322	Phosphorylation	KRVEKKKTVTMKRNL CCCCCCCEEEECCCC	30.04	22817900
362	Phosphorylation	VMDKDKLSRNDVIGK EECHHHCCCCCCCEE	34.48	28102081
382	Ubiquitination	KSGPGEVKHWKDMIA CCCCCCCHHHHHHHC	39.17	-

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

Oops, there are no upstream regulatory protein records of SYT7_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SYT7_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SYT7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HNRPQ_HUMAN	SYNCRIP	physical	10734137

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-322, AND MASSSPECTROMETRY.
PubMed: 18187866