SNP25_RAT - dbPTM
SNP25_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNP25_RAT
UniProt AC P60881
Protein Name Synaptosomal-associated protein 25
Gene Name Snap25
Organism Rattus norvegicus (Rat).
Sequence Length 206
Subcellular Localization Cytoplasm, perinuclear region . Cell membrane
Lipid-anchor . Cell junction, synapse, synaptosome . Membrane association requires palmitoylation (By similarity). Expressed throughout cytoplasm, concentrating at the perinuclear region (By similarity)
Protein Description t-SNARE involved in the molecular regulation of neurotransmitter release. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells. [PubMed: 12403834 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.]
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
25PhosphorylationADQLADESLESTRRM
HHHHHHHHHHHHHHH
37.6728432305
28PhosphorylationLADESLESTRRMLQL
HHHHHHHHHHHHHHH
32.2928432305
29PhosphorylationADESLESTRRMLQLV
HHHHHHHHHHHHHHH
16.96-
40UbiquitinationLQLVEESKDAGIRTL
HHHHHHHHHCCCEEE
55.68-
69UbiquitinationEGMDQINKDMKEAEK
HHHHHHHHHHHHHHH
61.91-
72UbiquitinationDQINKDMKEAEKNLT
HHHHHHHHHHHHHHH
65.00-
76UbiquitinationKDMKEAEKNLTDLGK
HHHHHHHHHHHHHHH
65.39-
85S-palmitoylationLTDLGKFCGLCVCPC
HHHHHHHCCEEEECC
4.6612837618
88S-palmitoylationLGKFCGLCVCPCNKL
HHHHCCEEEECCCCC
1.4712837618
90S-palmitoylationKFCGLCVCPCNKLKS
HHCCEEEECCCCCCC
2.8712837618
92S-palmitoylationCGLCVCPCNKLKSSD
CCEEEECCCCCCCCH
6.2412837618
102UbiquitinationLKSSDAYKKAWGNNQ
CCCCHHHHHHHCCCC
37.42-
103UbiquitinationKSSDAYKKAWGNNQD
CCCHHHHHHHCCCCC
36.37-
130PhosphorylationEREQMAISGGFIRRV
HHHHHHHHCCHHHHH
24.2728432305
138PhosphorylationGGFIRRVTNDARENE
CCHHHHHCCCHHHHH
26.1025403869
154PhosphorylationDENLEQVSGIIGNLR
CCCHHHHHHHHHHHH
24.7828551015
184UbiquitinationQIDRIMEKADSNKTR
HHHHHHHHHHHCCCH
39.86-
187PhosphorylationRIMEKADSNKTRIDE
HHHHHHHHCCCHHHH
45.1210965039
189UbiquitinationMEKADSNKTRIDEAN
HHHHHHCCCHHHHHH
43.03-
205PhosphorylationRATKMLGSG------
HHHHHHCCC------
37.0528551015

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
138TPhosphorylationKinasePKACAP00517
PSP
138TPhosphorylationKinasePRKACAP27791
GPS
138TPhosphorylationKinasePRKCAP05696
GPS
138TPhosphorylationKinasePKA-FAMILY-GPS
138TPhosphorylationKinasePKC-FAMILY-GPS
138TPhosphorylationKinasePKC-Uniprot
138TPhosphorylationKinasePKA-Uniprot
187SPhosphorylationKinasePRKCAP17252
GPS
187SPhosphorylationKinasePKCAP05696
PSP
187SPhosphorylationKinasePRKCBP05771
GPS
187SPhosphorylationKinasePKC-FAMILY-GPS
187SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
85CPalmitoylation

-

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_RAT !!

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
HGS_RATHgsphysical
10510169
HGS_RATHgsphysical
10825299
STX1B_RATStx1bphysical
10825299

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNP25_RAT

loading...

Related Literatures of Post-Translational Modification
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.

TOP