dbPTM

SNP23_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SNP23_HUMAN
UniProt AC	O00161
Protein Name	Synaptosomal-associated protein 23
Gene Name	SNAP23
Organism	Homo sapiens (Human).
Sequence Length	211
Subcellular Localization	Cell membrane Peripheral membrane protein. Cell membrane Lipid-anchor. Cell junction, synapse, synaptosome. Mainly localized to the plasma membrane.
Protein Description	Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion..
Protein Sequence	MDNLSSEEIQQRAHQITDESLESTRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLDQINKDMRETEKTLTELNKCCGLCVCPCNRTKNFESGKAYKTTWGDGGENSPCNVVSKQPGPVTNGQLQQPTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQNPQIKRITDKADTNRDRIDIANARAKKLIDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDNLSSEE -------CCCCCHHH	7.51	20068231
5	Phosphorylation	---MDNLSSEEIQQR ---CCCCCHHHHHHH	41.79	23401153
5 (in isoform 1)	Phosphorylation	-	41.79	-
6	Phosphorylation	--MDNLSSEEIQQRA --CCCCCHHHHHHHH	42.27	29255136
6 (in isoform 1)	Phosphorylation	-	42.27	-
17	Phosphorylation	QQRAHQITDESLEST HHHHHHCCHHHHHHH	27.43	23898821
20	Phosphorylation	AHQITDESLESTRRI HHHCCHHHHHHHHHH	40.00	23401153
20 (in isoform 1)	Phosphorylation	-	40.00	-
23	Phosphorylation	ITDESLESTRRILGL CCHHHHHHHHHHHHH	32.29	23401153
23 (in isoform 1)	Phosphorylation	-	32.29	-
24	Phosphorylation	TDESLESTRRILGLA CHHHHHHHHHHHHHH	18.00	29255136
24 (in isoform 1)	Phosphorylation	-	18.00	-
34	Phosphorylation	ILGLAIESQDAGIKT HHHHHHHCCCCCCEE	27.52	30266825
34 (in isoform 1)	Phosphorylation	-	27.52	-
40 (in isoform 1)	Ubiquitination	-	32.72	21906983
40 (in isoform 2)	Ubiquitination	-	32.72	21906983
40	Ubiquitination	ESQDAGIKTITMLDE HCCCCCCEEEEEHHH	32.72	21906983
44	Sulfoxidation	AGIKTITMLDEQKEQ CCCEEEEEHHHHHHH	3.82	21406390
49 (in isoform 1)	Ubiquitination	-	45.43	21906983
49	Ubiquitination	ITMLDEQKEQLNRIE EEEHHHHHHHHHHHH	45.43	21906983
49 (in isoform 2)	Ubiquitination	-	45.43	21906983
64 (in isoform 1)	Ubiquitination	-	55.31	21906983
64	Ubiquitination	EGLDQINKDMRETEK HHHHHHHHHHHHHHH	55.31	21906983
64 (in isoform 2)	Ubiquitination	-	55.31	21906983
69	Phosphorylation	INKDMRETEKTLTEL HHHHHHHHHHHHHHH	32.20	23312004
71	Ubiquitination	KDMRETEKTLTELNK HHHHHHHHHHHHHHH	57.14	-
72	Phosphorylation	DMRETEKTLTELNKC HHHHHHHHHHHHHHH	32.45	23312004
74	Phosphorylation	RETEKTLTELNKCCG HHHHHHHHHHHHHCC	43.59	23312004
79	S-palmitoylation	TLTELNKCCGLCVCP HHHHHHHHCCEEEEC	1.85	31142470
80	S-palmitoylation	LTELNKCCGLCVCPC HHHHHHHCCEEEECC	5.07	31142470
83	S-palmitoylation	LNKCCGLCVCPCNRT HHHHCCEEEECCCCC	1.47	31142470
85	S-palmitoylation	KCCGLCVCPCNRTKN HHCCEEEECCCCCCC	2.87	31142470
87	S-palmitoylation	CGLCVCPCNRTKNFE CCEEEECCCCCCCCC	4.56	31142470
91	Ubiquitination	VCPCNRTKNFESGKA EECCCCCCCCCCCCE	57.30	-
95	Phosphorylation	NRTKNFESGKAYKTT CCCCCCCCCCEEECC	41.26	22817900
97	Acetylation	TKNFESGKAYKTTWG CCCCCCCCEEECCCC	58.80	25953088
97	Ubiquitination	TKNFESGKAYKTTWG CCCCCCCCEEECCCC	58.80	-
99	Phosphorylation	NFESGKAYKTTWGDG CCCCCCEEECCCCCC	16.62	28450419
100	Ubiquitination	FESGKAYKTTWGDGG CCCCCEEECCCCCCC	44.32	-
101	Phosphorylation	ESGKAYKTTWGDGGE CCCCEEECCCCCCCC	18.33	22167270
102	Phosphorylation	SGKAYKTTWGDGGEN CCCEEECCCCCCCCC	24.25	22167270
108 (in isoform 1)	Phosphorylation	-	61.13	-
110	Phosphorylation	WGDGGENSPCNVVSK CCCCCCCCCCCEEEC	26.91	19664994
112	S-palmitoylation	DGGENSPCNVVSKQP CCCCCCCCCEEECCC	6.40	21044946
112	S-nitrosylation	DGGENSPCNVVSKQP CCCCCCCCCEEECCC	6.40	2212679
116	Phosphorylation	NSPCNVVSKQPGPVT CCCCCEEECCCCCCC	22.69	23927012
117	Ubiquitination	SPCNVVSKQPGPVTN CCCCEEECCCCCCCC	49.23	-
123	Phosphorylation	SKQPGPVTNGQLQQP ECCCCCCCCCCCCCC	36.44	26074081
131	Phosphorylation	NGQLQQPTTGAASGG CCCCCCCCCCCCCCC	33.26	21945579
132	Phosphorylation	GQLQQPTTGAASGGY CCCCCCCCCCCCCCC	31.35	21945579
132 (in isoform 2)	Ubiquitination	-	31.35	21906983
136	Phosphorylation	QPTTGAASGGYIKRI CCCCCCCCCCCEEEC	32.01	21945579
139	Phosphorylation	TGAASGGYIKRITND CCCCCCCCEEECCCC	13.54	21945579
141 (in isoform 1)	Ubiquitination	-	29.30	21906983
141	Ubiquitination	AASGGYIKRITNDAR CCCCCCEEECCCCCC	29.30	21906983
144	Phosphorylation	GGYIKRITNDAREDE CCCEEECCCCCCHHH	30.95	28270605
157	Phosphorylation	DEMEENLTQVGSILG HHHHHHHHHHHHHHH	32.56	26657352
161	Phosphorylation	ENLTQVGSILGNLKD HHHHHHHHHHHHHHH	18.78	25159151
169	Sulfoxidation	ILGNLKDMALNIGNE HHHHHHHHHHHCCCC	4.34	21406390
185 (in isoform 1)	Ubiquitination	-	32.28	21906983
185	Ubiquitination	DAQNPQIKRITDKAD CCCCCCHHHHCCCCC	32.28	2190698
190	Ubiquitination	QIKRITDKADTNRDR CHHHHCCCCCCCHHH	39.24	-
193	Phosphorylation	RITDKADTNRDRIDI HHCCCCCCCHHHHHH	36.69	27470641
211	Phosphorylation	RAKKLIDS------- HHHHHHCC-------	34.82	26074081

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
23	S	Phosphorylation	Kinase	KPCA	P17252	PhosphoELM
23	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
24	T	Phosphorylation	Kinase	KPCA	P17252	PhosphoELM
24	T	Phosphorylation	Kinase	PRKCA	P05696	GPS
95	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
95	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
95	S	Phosphorylation	Kinase	PKM	P14618	PSP
161	S	Phosphorylation	Kinase	KPCA	P17252	PhosphoELM
161	S	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 SNP23_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 SNP23_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SNAPN_HUMAN	SNAPIN	physical	12877659
ABI2_HUMAN	ABI2	physical	16189514
ABI3_HUMAN	ABI3	physical	16189514
SEGN_HUMAN	SCGN	physical	16189514
FXR2_HUMAN	FXR2	physical	16189514
SNAA_HUMAN	NAPA	physical	16189514
SNTG1_HUMAN	SNTG1	physical	12877659
STXB5_HUMAN	STXBP5	physical	12832401
STX2_HUMAN	STX2	physical	12828989
STX3_HUMAN	STX3	physical	12828989
STX4_HUMAN	STX4	physical	12828989
VAMP2_HUMAN	VAMP2	physical	12828989
VAMP3_HUMAN	VAMP3	physical	12828989
VAMP8_HUMAN	VAMP8	physical	12828989
STX1A_HUMAN	STX1A	physical	9168999
STX2_HUMAN	STX2	physical	9168999
STX3_HUMAN	STX3	physical	9168999
STX4_HUMAN	STX4	physical	9168999
KINH_HUMAN	KIF5B	physical	12475239
STX12_HUMAN	STX12	physical	9507000
VAMP2_HUMAN	VAMP2	physical	10820264
VAMP8_HUMAN	VAMP8	physical	10820264
VAMP3_HUMAN	VAMP3	physical	10820264
STX4_HUMAN	STX4	physical	10820264
STX11_HUMAN	STX11	physical	10036234
SCAM1_HUMAN	SCAMP1	physical	12124380
SCAM2_HUMAN	SCAMP2	physical	12124380
STX4_HUMAN	STX4	physical	10713150
STX6_HUMAN	STX6	physical	11001914
STX4_HUMAN	STX4	physical	12556468
VAMP3_HUMAN	VAMP3	physical	12556468
MATR3_HUMAN	MATR3	physical	21900206
STX11_HUMAN	STX11	physical	21900206
STX4_HUMAN	STX4	physical	22939629
UBQL2_HUMAN	UBQLN2	physical	22939629
YES_HUMAN	YES1	physical	22939629
SNP23_HUMAN	SNAP23	physical	25416956
VAMP5_HUMAN	VAMP5	physical	25416956
SNAB_HUMAN	NAPB	physical	25416956
STX2_HUMAN	STX2	physical	10820264
CHM2A_HUMAN	CHMP2A	physical	28514442

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 SNP23_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-102 AND SER-110, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 1-12, AND ACETYLATION AT MET-1.	12665801 [Abstract]
Palmitoylation
Reference	PubMed
"Site-specific analysis of protein S-acylation by resin-assistedcapture."; Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,Stamler J.S., Casey P.J.; J. Lipid Res. 52:393-398(2011). Cited for: PALMITOYLATION AT CYS-79; CYS-80; CYS-83; CYS-85; CYS-87 AND CYS-112.	21044946 [Abstract]
Phosphorylation
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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-102 AND SER-110, 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-110, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASSSPECTROMETRY.	18691976 [Abstract]
"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 SER-110, AND MASSSPECTROMETRY.	18187866 [Abstract]