SNP23_MOUSE - dbPTM
SNP23_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNP23_MOUSE
UniProt AC O09044
Protein Name Synaptosomal-associated protein 23
Gene Name Snap23
Organism Mus musculus (Mouse).
Sequence Length 210
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 MDNLSPEEVQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCICPCNRTKNFESGKNYKATWGDGGDNSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS
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-------MDNLSPEE
-------CCCCCHHH
7.51-
5Phosphorylation---MDNLSPEEVQLR
---CCCCCHHHHHHH
36.2026643407
17PhosphorylationQLRAHQVTDESLEST
HHHHHHCCHHHHHHH
27.7225619855
20PhosphorylationAHQVTDESLESTRRI
HHHCCHHHHHHHHHH
40.0026824392
23PhosphorylationVTDESLESTRRILGL
CCHHHHHHHHHHHHH
32.2920469934
24PhosphorylationTDESLESTRRILGLA
CHHHHHHHHHHHHHH
18.0025619855
34PhosphorylationILGLAIESQDAGIKT
HHHHHHHCCCCCCEE
27.5219144319
40UbiquitinationESQDAGIKTITMLDE
HCCCCCCEEEEEEHH
32.72-
64UbiquitinationEGMDQINKDMREAEK
HHHHHHHHHHHHHHH
55.31-
71UbiquitinationKDMREAEKTLTELNK
HHHHHHHHHHHHHHH
56.75-
72PhosphorylationDMREAEKTLTELNKC
HHHHHHHHHHHHHHH
30.3428066266
74PhosphorylationREAEKTLTELNKCCG
HHHHHHHHHHHHHCC
43.5928066266
79S-palmitoylationTLTELNKCCGLCICP
HHHHHHHHCCEEEEE
1.8510085154
80S-palmitoylationLTELNKCCGLCICPC
HHHHHHHCCEEEEEC
5.0710085154
83S-palmitoylationLNKCCGLCICPCNRT
HHHHCCEEEEECCCC
1.5010085154
85S-palmitoylationKCCGLCICPCNRTKN
HHCCEEEEECCCCCC
2.8310085154
87S-palmitoylationCGLCICPCNRTKNFE
CCEEEEECCCCCCCC
4.70-
91UbiquitinationICPCNRTKNFESGKN
EEECCCCCCCCCCCC
57.30-
95PhosphorylationNRTKNFESGKNYKAT
CCCCCCCCCCCCCCC
51.4327742792
99PhosphorylationNFESGKNYKATWGDG
CCCCCCCCCCCCCCC
12.8926643407
100UbiquitinationFESGKNYKATWGDGG
CCCCCCCCCCCCCCC
49.05-
102PhosphorylationSGKNYKATWGDGGDN
CCCCCCCCCCCCCCC
26.3124925903
110PhosphorylationWGDGGDNSPSNVVSK
CCCCCCCCCCCCCCC
34.1524925903
112PhosphorylationDGGDNSPSNVVSKQP
CCCCCCCCCCCCCCC
41.9225521595
116PhosphorylationNSPSNVVSKQPSRIT
CCCCCCCCCCCCCCC
22.6925521595
117UbiquitinationSPSNVVSKQPSRITN
CCCCCCCCCCCCCCC
55.40-
120PhosphorylationNVVSKQPSRITNGQP
CCCCCCCCCCCCCCC
33.5423684622
121PhosphorylationVVSKQPSRITNGQPQ
CCCCCCCCCCCCCCC
46.5724719451
123PhosphorylationSKQPSRITNGQPQQT
CCCCCCCCCCCCCCC
31.9924704852
127PhosphorylationSRITNGQPQQTTGAA
CCCCCCCCCCCCCCC
29.6424719451
130PhosphorylationTNGQPQQTTGAASGG
CCCCCCCCCCCCCCC
23.1928285833
135PhosphorylationQQTTGAASGGYIKRI
CCCCCCCCCCCEEEC
32.0125159016
138PhosphorylationTGAASGGYIKRITND
CCCCCCCCEEECCCC
13.5425159016
143PhosphorylationGGYIKRITNDAREDE
CCCEEECCCCCCHHH
30.9525338131
156PhosphorylationDEMEENLTQVGSILG
HHHHHHHHHHHHHHH
32.5625159016
160PhosphorylationENLTQVGSILGNLKN
HHHHHHHHHHHHHHH
18.7821082442
185UbiquitinationAQNQQIQKITEKADT
HHHHHHHHHHHHHCC
53.90-

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
95SPhosphorylationKinaseIKBKBO14920
GPS
95SPhosphorylationKinaseIKKBO88351
PSP
120SPhosphorylationKinaseIKBKBO14920
GPS
120SPhosphorylationKinaseIKKBO88351
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNP23_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STX1A_HUMANSTX1Aphysical
9168999
STX2_HUMANSTX2physical
9168999
STX3_HUMANSTX3physical
9168999
STX4_HUMANSTX4physical
9168999
IKKA_MOUSEChukphysical
23960234
IKKB_MOUSEIkbkbphysical
23960234
IKKB_HUMANIKBKBphysical
18692471
STX1A_MOUSEStx1aphysical
24705552
VAMP2_MOUSEVamp2physical
24705552

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNP23_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-34 AND SER-110,AND MASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY.

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