NSF_MOUSE - dbPTM
NSF_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSF_MOUSE
UniProt AC P46460
Protein Name Vesicle-fusing ATPase
Gene Name Nsf
Organism Mus musculus (Mouse).
Sequence Length 744
Subcellular Localization Cytoplasm.
Protein Description Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack GRIA2 leads to influence GRIA2 membrane cycling (By similarity)..
Protein Sequence MAGRTMQAARCPTDELSLSNCAVVNEKDFQSGQHVMVRTSPNHKYIFTLRTHPSVVPGCIAFSLPQRKWAGLSIGQDIEVALYSFDKAKQCIGTMTIEIDFLQKKNIDSNPYDTDKMAAEFIQQFNNQAFSVGQQLVFSFNDKLFGLLVKDIEAMDPSILKGEPASGKRQKIEVGLVVGNSQVAFEKAENSSLNLIGKAKTKENRQSIINPDWNFEKMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGLVRAAQSTAMNRHIKASTKVEVDMEKAESLQVTRGDFLASLENDIKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALMREEGASPLDFD
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
11S-nitrosylationRTMQAARCPTDELSL
CCCCCCCCCCCCCCC
3.5022588120
21S-nitrosylationDELSLSNCAVVNEKD
CCCCCCCCEEECHHH
2.4622588120
31PhosphorylationVNEKDFQSGQHVMVR
ECHHHCCCCCEEEEE
40.1829899451
59S-palmitoylationHPSVVPGCIAFSLPQ
CCCCCCCEEEECCCC
1.3328680068
94PhosphorylationKAKQCIGTMTIEIDF
HHHHHEEEEEEEEEE
7.39-
105AcetylationEIDFLQKKNIDSNPY
EEEEHHHCCCCCCCC
46.2923806337
105MalonylationEIDFLQKKNIDSNPY
EEEEHHHCCCCCCCC
46.2926320211
105UbiquitinationEIDFLQKKNIDSNPY
EEEEHHHCCCCCCCC
46.2927667366
109PhosphorylationLQKKNIDSNPYDTDK
HHHCCCCCCCCCHHH
35.5925521595
161UbiquitinationAMDPSILKGEPASGK
HCCHHHHCCCCCCCC
60.6022790023
192PhosphorylationFEKAENSSLNLIGKA
HHHHCCCCCCCCEEC
32.6219854140
198UbiquitinationSSLNLIGKAKTKENR
CCCCCCEECCCHHHH
39.4522790023
207PhosphorylationKTKENRQSIINPDWN
CCHHHHHCCCCCCCC
23.3825521595
217UbiquitinationNPDWNFEKMGIGGLD
CCCCCHHHCCCCCCC
37.9922790023
228PhosphorylationGGLDKEFSDIFRRAF
CCCCHHHHHHHHHHH
30.7822817900
250S-nitrosocysteineEIVEQMGCKHVKGIL
HHHHHHCCCEEEEEE
2.01-
250S-nitrosylationEIVEQMGCKHVKGIL
HHHHHHCCCEEEEEE
2.0116418269
259PhosphorylationHVKGILLYGPPGCGK
EEEEEEEECCCCCCH
24.9222817900
264S-nitrosylationLLYGPPGCGKTLLAR
EEECCCCCCHHHHHH
6.6116418269
264S-nitrosocysteineLLYGPPGCGKTLLAR
EEECCCCCCHHHHHH
6.61-
266UbiquitinationYGPPGCGKTLLARQI
ECCCCCCHHHHHHHH
39.8222790023
293UbiquitinationNGPEILNKYVGESEA
CCHHHHHHHCCCCHH
37.5622790023
294PhosphorylationGPEILNKYVGESEAN
CHHHHHHHCCCCHHH
16.7729899451
304UbiquitinationESEANIRKLFADAEE
CCHHHHHHHHCCHHH
44.1322790023
339PhosphorylationAICKQRGSMAGSTGV
HHHHHCCCCCCCCCC
13.9820415495
343PhosphorylationQRGSMAGSTGVHDTV
HCCCCCCCCCCHHHH
16.6722817900
344PhosphorylationRGSMAGSTGVHDTVV
CCCCCCCCCCHHHHH
42.1629899451
349PhosphorylationGSTGVHDTVVNQLLS
CCCCCHHHHHHHHHH
16.1020415495
356PhosphorylationTVVNQLLSKIDGVEQ
HHHHHHHHCCCCHHH
35.8420415495
401UbiquitinationEIGLPDEKGRLQILH
EECCCCCCCCEEEEE
57.6322790023
411PhosphorylationLQILHIHTARMRGHQ
EEEEEEECCHHCCCE
18.5023970565
421PhosphorylationMRGHQLLSADVDIKE
HCCCEEECCCCCHHH
30.8922817900
434UbiquitinationKELAVETKNFSGAEL
HHHHHCCCCCCHHHH
42.3522790023
437PhosphorylationAVETKNFSGAELEGL
HHCCCCCCHHHHHHH
46.6222817900
450PhosphorylationGLVRAAQSTAMNRHI
HHHHHHHHHHHHHHH
17.2622817900
460PhosphorylationMNRHIKASTKVEVDM
HHHHHCCCCEEEECH
24.6122817900
461PhosphorylationNRHIKASTKVEVDME
HHHHCCCCEEEECHH
43.9222817900
462UbiquitinationRHIKASTKVEVDMEK
HHHCCCCEEEECHHH
33.6222790023
469UbiquitinationKVEVDMEKAESLQVT
EEEECHHHHHHCCCC
51.3122790023
472PhosphorylationVDMEKAESLQVTRGD
ECHHHHHHCCCCCHH
29.0329176673
531PhosphorylationLVQQTKNSDRTPLVS
EEEECCCCCCCCEEE
29.9920531401
534PhosphorylationQTKNSDRTPLVSVLL
ECCCCCCCCEEEEEE
26.4320531401
538PhosphorylationSDRTPLVSVLLEGPP
CCCCCEEEEEECCCC
18.0920531401
547PhosphorylationLLEGPPHSGKTALAA
EECCCCCCCHHHHHH
48.0020531401
550PhosphorylationGPPHSGKTALAAKIA
CCCCCCHHHHHHHHH
30.3520531401
555UbiquitinationGKTALAAKIAEESNF
CHHHHHHHHHHHCCC
36.5222790023
569PhosphorylationFPFIKICSPDKMIGF
CCEEEECCCCCCCCC
39.3422817900
577PhosphorylationPDKMIGFSETAKCQA
CCCCCCCCHHHHHHH
28.9125521595
599S-nitrosylationAYKSQLSCVVVDDIE
HHHHCCCEEEECCHH
3.5122588120
699UbiquitinationTTIAQQVKGKKVWIG
CCHHHHHCCCEEEEH
61.7522790023
702UbiquitinationAQQVKGKKVWIGIKK
HHHHCCCEEEEHHHH
52.0122790023
708MethylationKKVWIGIKKLLMLIE
CEEEEHHHHHHHHHH
31.96-
709MethylationKVWIGIKKLLMLIEM
EEEEHHHHHHHHHHH
44.95-
739PhosphorylationLMREEGASPLDFD--
HHHHCCCCCCCCC--
36.5325521595

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
460SPhosphorylationKinasePRKCEP16054
GPS
569SPhosphorylationKinaseCDK16Q00536
PSP
569SPhosphorylationKinaseCDK16Q04735
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
569SPhosphorylation

16461345

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 NSF_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NSF_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-259, AND MASSSPECTROMETRY.

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