SNP25_MOUSE - dbPTM
SNP25_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNP25_MOUSE
UniProt AC P60879
Protein Name Synaptosomal-associated protein 25
Gene Name Snap25
Organism Mus musculus (Mouse).
Sequence Length 206
Subcellular Localization Cytoplasm, perinuclear region . Cell membrane
Lipid-anchor . Cell junction, synapse, synaptosome . Colocalizes with KCNB1 at the cell membrane (By similarity). Membrane association requires palmitoylation (PubMed:9349529). Expressed throughout cyto
Protein Description t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. [PubMed: 16672379 Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells (By similarity]
Protein Sequence MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
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
9UbiquitinationAEDADMRNELEEMQR
CCCHHHHHHHHHHHH		52.1227667366
13UbiquitinationDMRNELEEMQRRADQ
HHHHHHHHHHHHHHH		53.9227667366
25PhosphorylationADQLADESLESTRRM
HHHHHHHHHHHHHHH		37.6725521595
28PhosphorylationLADESLESTRRMLQL
HHHHHHHHHHHHHHH		32.2921454597
29PhosphorylationADESLESTRRMLQLV
HHHHHHHHHHHHHHH		16.9621454597
33UbiquitinationLESTRRMLQLVEESK
HHHHHHHHHHHHHHH		3.1927667366
39PhosphorylationMLQLVEESKDAGIRT
HHHHHHHHHHCCCEE		23.4822324799
39UbiquitinationMLQLVEESKDAGIRT
HHHHHHHHHHCCCEE		23.4827667366
40UbiquitinationLQLVEESKDAGIRTL
HHHHHHHHHCCCEEE		55.6822790023
69UbiquitinationEGMDQINKDMKEAEK
HHHHHHHHHHHHHHH		61.9122790023
72UbiquitinationDQINKDMKEAEKNLT
HHHHHHHHHHHHHHH		65.0022790023
76UbiquitinationKDMKEAEKNLTDLGK
HHHHHHHHHHHHHHH		65.3927667366
85S-palmitoylationLTDLGKFCGLCVCPC
HHHHHHHCCEEEECC		4.669349529
88S-palmitoylationLGKFCGLCVCPCNKL
HHHHCCEEEECCCCC		1.479349529
90S-palmitoylationKFCGLCVCPCNKLKS
HHCCEEEECCCCCCC		2.879349529
92S-palmitoylationCGLCVCPCNKLKSSD
CCEEEECCCCCCCCH		6.249349529
96UbiquitinationVCPCNKLKSSDAYKK
EECCCCCCCCHHHHH		49.9127667366
102UbiquitinationLKSSDAYKKAWGNNQ
CCCCHHHHHHHCCCC		37.4227667366
103UbiquitinationKSSDAYKKAWGNNQD
CCCHHHHHHHCCCCC		36.3722790023
115PhosphorylationNQDGVVASQPARVVD
CCCCCCCCCCCEECC		25.7022324799
121UbiquitinationASQPARVVDEREQMA
CCCCCEECCHHHHHH		5.4327667366
126UbiquitinationRVVDEREQMAISGGF
EECCHHHHHHHHCCH		32.5927667366
130PhosphorylationEREQMAISGGFIRRV
HHHHHHHHCCHHHHH		24.2722324799
138PhosphorylationGGFIRRVTNDARENE
CCHHHHHCCCHHHHH		26.1022324799
154PhosphorylationDENLEQVSGIIGNLR
CCCHHHHHHHHHHHH		24.7822817900
184UbiquitinationQIDRIMEKADSNKTR
HHHHHHHHHHHCCCH		39.8627667366
187PhosphorylationRIMEKADSNKTRIDE
HHHHHHHHCCCHHHH		45.1221949876
189UbiquitinationMEKADSNKTRIDEAN
HHHHHHCCCHHHHHH		43.0327667366
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
138TPhosphorylationKinasePRKACAP05132
GPS
138TPhosphorylationKinaseROCK2O75116
PSP
138TPhosphorylationKinaseROCK2Q62868
PSP
138TPhosphorylationKinasePKC-Uniprot
138TPhosphorylationKinasePKA-Uniprot
187SPhosphorylationKinasePKCAP17252
PSP
187SPhosphorylationKinasePRKCAP20444
GPS
187SPhosphorylationKinasePKC-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
85CPalmitoylation

9349529
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 SNP25_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNJC5_MOUSEDnajc5physical
21151134
VAMP2_MOUSEVamp2physical
21151134
STX1A_MOUSEStx1aphysical
21151134
HSP7C_MOUSEHspa8physical
21151134
SGTA_MOUSESgtaphysical
21151134
SYUA_MOUSESncaphysical
21151134
STX1A_RATStx1aphysical
7768895
STX3_RATStx3physical
7768895
STX4_RATStx4physical
7768895
STX2_RATStx2physical
7768895
STX1A_MOUSEStx1aphysical
20798282
VAMP2_MOUSEVamp2physical
20798282
DNJC5_MOUSEDnajc5physical
20798282
SYUA_MOUSESncaphysical
20798282
HGS_MOUSEHgsphysical
16615908
VAMP2_MOUSEVamp2physical
20114047
STX1A_MOUSEStx1aphysical
20114047
TBB5_MOUSETubb5physical
20114047
VA0D1_MOUSEAtp6v0d1physical
20114047
TBB2A_MOUSETubb2aphysical
20114047
SYPH_MOUSESypphysical
20114047
G3P_MOUSEGapdhphysical
20114047
PGBM_MOUSEHspg2physical
20114047
TBA4A_MOUSETuba4aphysical
20114047
TBA1A_MOUSETuba1aphysical
20114047
MAP6_MOUSEMap6physical
20114047
AP2B1_MOUSEAp2b1physical
20114047
PACS1_MOUSEPacs1physical
20114047
AP2A1_MOUSEAp2a1physical
20114047
KINH_MOUSEKif5bphysical
20114047
KIF5C_MOUSEKif5cphysical
20114047
AT1A1_MOUSEAtp1a1physical
20114047
NCKP1_MOUSENckap1physical
20114047
STX1A_MOUSEStx1aphysical
24705552
VAMP2_MOUSEVamp2physical
24705552
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNP25_MOUSE

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Characterization of the palmitoylation domain of SNAP-25.";
Lane S.R., Liu Y.;
J. Neurochem. 69:1864-1869(1997).
Cited for: PALMITOYLATION AT CYS-85; CYS-88; CYS-90 AND CYS-92, AND MUTAGENESISOF CYS-85; CYS-88; CYS-90 AND CYS-92.
Phosphorylation
ReferencePubMed
"Differential phosphorylation of SNAP-25 in vivo by protein kinase Cand protein kinase A.";
Hepp R., Cabaniols J.-P., Roche P.A.;
FEBS Lett. 532:52-56(2002).
Cited for: PHOSPHORYLATION AT THR-138 AND SER-187.

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