SNG2_HUMAN - dbPTM
SNG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNG2_HUMAN
UniProt AC O43760
Protein Name Synaptogyrin-2 {ECO:0000305}
Gene Name SYNGR2 {ECO:0000312|HGNC:HGNC:11499}
Organism Homo sapiens (Human).
Sequence Length 224
Subcellular Localization Cytoplasmic vesicle membrane
Multi-pass membrane protein . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
Multi-pass membrane protein . Localizes to cytoplasmic vesicles associated with the recycling endosomes.
Lipid droplet.
Protein Description May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane.; (Microbial infection) May play a role in the assembly of cytoplasmic inclusion bodies required for SFTS phlebovirus replication..
Protein Sequence MESGAYGAAKAGGSFDLRRFLTQPQVVARAVCLVFALIVFSCIYGEGYSNAHESKQMYCVFNRNEDACRYGSAIGVLAFLASAFFLVVDAYFPQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAVTNPKDVLVGADSVRAAITFSFFSIFSWGVLASLAYQRYKAGVDDFIQNYVDPTPDPNTAYASYPGASVDNYQQPPFTQNAETTEGYQPPPVY
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
1Acetylation-------MESGAYGA
-------CCCCCCCC
9.2622223895
3Phosphorylation-----MESGAYGAAK
-----CCCCCCCCHH
27.6823401153
6Phosphorylation--MESGAYGAAKAGG
--CCCCCCCCHHCCC
15.7227259358
10UbiquitinationSGAYGAAKAGGSFDL
CCCCCCHHCCCCCCH
47.2121890473
14PhosphorylationGAAKAGGSFDLRRFL
CCHHCCCCCCHHHHH
18.0525850435
181PhosphorylationVDDFIQNYVDPTPDP
HHHHHHHCCCCCCCC
7.00-
194PhosphorylationDPNTAYASYPGASVD
CCCCCCCCCCCCCCC
21.13-
203PhosphorylationPGASVDNYQQPPFTQ
CCCCCCCCCCCCCCC
12.2222817900
218PhosphorylationNAETTEGYQPPPVY-
CCCCCCCCCCCCCC-
16.1822817900
224PhosphorylationGYQPPPVY-------
CCCCCCCC-------
20.7120736484

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 SNG2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNG2_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 SNG2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCAR3_HUMANSCARA3physical
25416956

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 SNG2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.

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