dbPTM

SNAPN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SNAPN_HUMAN
UniProt AC	O95295
Protein Name	SNARE-associated protein Snapin
Gene Name	SNAPIN
Organism	Homo sapiens (Human).
Sequence Length	136
Subcellular Localization	Membrane Peripheral membrane protein Cytoplasmic side . Cytoplasm, cytosol . Cytoplasm, perinuclear region . Golgi apparatus membrane . Lysosome membrane . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane . Colocalizes with NANOS
Protein Description	Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells. [PubMed: 17182842]
Protein Sequence	MAGAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDPYVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGIYPPGSPGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGAGSAAV ------CCCCCCCCC	19.28	22814378
6	Phosphorylation	--MAGAGSAAVSGAG --CCCCCCCCCCCCC	16.72	28464451
10	Phosphorylation	GAGSAAVSGAGTPVA CCCCCCCCCCCCCCC	20.42	29255136
14	Phosphorylation	AAVSGAGTPVAGPTG CCCCCCCCCCCCCCH	17.66	29255136
20	Phosphorylation	GTPVAGPTGRDLFAE CCCCCCCCHHHHHHH	43.88	29255136
50	O-linked_Glycosylation	HVHAVRESQVELREQ HHHHHHHHHHHHHHH	29.03	11283605
50	Phosphorylation	HVHAVRESQVELREQ HHHHHHHHHHHHHHH	29.03	15269257
73	Ubiquitination	CRINEDQKVALDLDP HCCCCCCCEECCCHH	41.62	29967540
83	Ubiquitination	LDLDPYVKKLLNARR CCCHHHHHHHHHHHH	31.68	32015554
83	Acetylation	LDLDPYVKKLLNARR CCCHHHHHHHHHHHH	31.68	25953088
112	Phosphorylation	RLRRLNHSVAKETAR HHHHHHHHHHHHHHH	23.77	22067460
117	Phosphorylation	NHSVAKETARRRAML HHHHHHHHHHHHHHH	25.43	26074081
126	Phosphorylation	RRRAMLDSGIYPPGS HHHHHHHCCCCCCCC	24.11	23401153
129	Phosphorylation	AMLDSGIYPPGSPGK HHHHCCCCCCCCCCC	13.60	27461979
133	Phosphorylation	SGIYPPGSPGK---- CCCCCCCCCCC----	35.93	19664994
136	Ubiquitination	YPPGSPGK------- CCCCCCCC-------	61.62	24816145

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
50	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
50	S	Phosphorylation	Kinase	PKA	-	Uniprot
117	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
133	S	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF13	O43567	PMID:22890573

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BL1S1_HUMAN	BLOC1S1	physical	15102850
BL1S2_HUMAN	BLOC1S2	physical	15102850
DTBP1_HUMAN	DTNBP1	physical	15102850
SNP23_HUMAN	SNAP23	physical	12877659
RGS7_HUMAN	RGS7	physical	12659861
LAMC1_HUMAN	LAMC1	physical	16169070
GASP1_HUMAN	GPRASP1	physical	16169070
KIF5C_HUMAN	KIF5C	physical	16169070
SPAG5_HUMAN	SPAG5	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
HAP1_HUMAN	HAP1	physical	16169070
KAT5_HUMAN	KAT5	physical	16169070
MIC60_HUMAN	IMMT	physical	16169070
KAT7_HUMAN	KAT7	physical	16169070
ELP1_HUMAN	IKBKAP	physical	16169070
SNP25_HUMAN	SNAP25	physical	10195194
RNF13_HUMAN	RNF13	physical	22890573
SNP25_HUMAN	SNAP25	physical	22890573
BL1S2_HUMAN	BLOC1S2	physical	26344197

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 SNAPN_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-14 AND SER-133, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND SER-133, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-14 AND SER-133, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.	17287340 [Abstract]