CN37_MOUSE - dbPTM
CN37_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CN37_MOUSE
UniProt AC P16330
Protein Name 2',3'-cyclic-nucleotide 3'-phosphodiesterase
Gene Name Cnp
Organism Mus musculus (Mouse).
Sequence Length 420
Subcellular Localization Membrane
Lipid-anchor . Melanosome. Firmly bound to membrane structures of brain white matter.
Protein Description May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin..
Protein Sequence MNTSFTRKSHTFLPKLFFRKMSSSGAKEKPELQFPFLQDEDTVATLHECKTLFILRGLPGSGKSTLARLILEKYHDGTKMVSADAYKIIPGSRADFSEAYKRLDEDLAGYCRRDIRVLVLDDTNHERERLDQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRHFISGDEPKEKLELVSYFGKRPPGVLHCTTKFCDYGKAAGAEEYAQQEVVKRSYGKAFKLSISALFVTPKTAGAQVVLTDQELQLWPSDLDKPSASEGLPPGSRAHVTLGCAADVQPVQTGLDLLDILQQVKGGSQGEAVGELPRGKLYSLGKGRWMLSLTKKMEVKAIFTGYYGKGKPVPIHGSRKGGAMQICTII
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
3Phosphorylation-----MNTSFTRKSH
-----CCCCCCCCCC		24.7426643407
4Phosphorylation----MNTSFTRKSHT
----CCCCCCCCCCC		21.4425266776
6Phosphorylation--MNTSFTRKSHTFL
--CCCCCCCCCCCHH		36.6325266776
7 (in isoform 2)Ubiquitination-36.15-
9 (in isoform 2)Ubiquitination-25.19-
9PhosphorylationNTSFTRKSHTFLPKL
CCCCCCCCCCHHHHH		25.1925521595
11PhosphorylationSFTRKSHTFLPKLFF
CCCCCCCCHHHHHHH		33.6822324799
15UbiquitinationKSHTFLPKLFFRKMS
CCCCHHHHHHHHHCC		61.1422790023
22PhosphorylationKLFFRKMSSSGAKEK
HHHHHHCCCCCCCCC		25.1222817900
23PhosphorylationLFFRKMSSSGAKEKP
HHHHHCCCCCCCCCC		29.3220415495
24PhosphorylationFFRKMSSSGAKEKPE
HHHHCCCCCCCCCCC		35.1520415495
27UbiquitinationKMSSSGAKEKPELQF
HCCCCCCCCCCCCCC		70.5622790023
27 (in isoform 2)Ubiquitination-70.5622790023
29UbiquitinationSSSGAKEKPELQFPF
CCCCCCCCCCCCCCC		42.9822790023
29 (in isoform 2)Ubiquitination-42.9822790023
49S-palmitoylationTVATLHECKTLFILR
CEEHHHHCCEEEEEC		2.5828680068
49S-nitrosylationTVATLHECKTLFILR
CEEHHHHCCEEEEEC		2.5824895380
51PhosphorylationATLHECKTLFILRGL
EHHHHCCEEEEECCC		38.2629899451
63UbiquitinationRGLPGSGKSTLARLI
CCCCCCCHHHHHHHH		41.8022790023
65PhosphorylationLPGSGKSTLARLILE
CCCCCHHHHHHHHHH		28.1129899451
73UbiquitinationLARLILEKYHDGTKM
HHHHHHHHHCCCCEE		44.4322790023
79UbiquitinationEKYHDGTKMVSADAY
HHHCCCCEEEECCCH		42.7222790023
79AcetylationEKYHDGTKMVSADAY
HHHCCCCEEEECCCH		42.7222902405
87UbiquitinationMVSADAYKIIPGSRA
EEECCCHHCCCCCCC		35.5622790023
92PhosphorylationAYKIIPGSRADFSEA
CHHCCCCCCCCHHHH		20.9529899451
97PhosphorylationPGSRADFSEAYKRLD
CCCCCCHHHHHHHHC		23.1229899451
101UbiquitinationADFSEAYKRLDEDLA
CCHHHHHHHHCHHHH		54.2422790023
101AcetylationADFSEAYKRLDEDLA
CCHHHHHHHHCHHHH		54.24155355
110PhosphorylationLDEDLAGYCRRDIRV
HCHHHHHHHCCCEEE		4.1629899451
111S-nitrosylationDEDLAGYCRRDIRVL
CHHHHHHHCCCEEEE		2.5524895380
157S-nitrosylationKTAWRLDCAQLKEKN
CCEEEECHHHHHHHC		2.8424895380
161UbiquitinationRLDCAQLKEKNQWQL
EECHHHHHHHCCEEC		55.3422790023
163UbiquitinationDCAQLKEKNQWQLSA
CHHHHHHHCCEECCH		53.5022790023
169PhosphorylationEKNQWQLSADDLKKL
HHCCEECCHHHHHHH		17.9825521595
174AcetylationQLSADDLKKLKPGLE
ECCHHHHHHHCCCCC		64.1570137
174UbiquitinationQLSADDLKKLKPGLE
ECCHHHHHHHCCCCC		64.1522790023
175UbiquitinationLSADDLKKLKPGLEK
CCHHHHHHHCCCCCC		69.8722790023
177AcetylationADDLKKLKPGLEKDF
HHHHHHHCCCCCCCC		46.0121728379
195AcetylationYFGWFLTKKSSETLR
HHHHHHCCCCHHHHH		53.4519859057
203UbiquitinationKSSETLRKAGQVFLE
CCHHHHHHHHHHHHH		61.0422790023
216UbiquitinationLEELGNHKAFKKELR
HHHHCCCHHHHHHHH		60.5622790023
219UbiquitinationLGNHKAFKKELRHFI
HCCCHHHHHHHHHHH		50.64-
227PhosphorylationKELRHFISGDEPKEK
HHHHHHHCCCCCHHH		38.9725521595
232UbiquitinationFISGDEPKEKLELVS
HHCCCCCHHHHHHHH		66.4922790023
234UbiquitinationSGDEPKEKLELVSYF
CCCCCHHHHHHHHHH		54.0822790023
239PhosphorylationKEKLELVSYFGKRPP
HHHHHHHHHHCCCCC		27.6325521595
240PhosphorylationEKLELVSYFGKRPPG
HHHHHHHHHCCCCCC		14.6325521595
254UbiquitinationGVLHCTTKFCDYGKA
CEEEEECCCCCHHHH		26.3322790023
260UbiquitinationTKFCDYGKAAGAEEY
CCCCCHHHHCCHHHH		28.9122790023
267PhosphorylationKAAGAEEYAQQEVVK
HHCCHHHHHHHHHHH		10.9522817900
274AcetylationYAQQEVVKRSYGKAF
HHHHHHHHHHHHHHH		40.5816209469
274UbiquitinationYAQQEVVKRSYGKAF
HHHHHHHHHHHHHHH		40.5822790023
276PhosphorylationQQEVVKRSYGKAFKL
HHHHHHHHHHHHHEE		32.3029899451
284PhosphorylationYGKAFKLSISALFVT
HHHHHEEEEEEEEEC		18.3222817900
286PhosphorylationKAFKLSISALFVTPK
HHHEEEEEEEEECCC		18.6222324799
315UbiquitinationLWPSDLDKPSASEGL
CCCCCCCCCCHHCCC		48.4422790023
326PhosphorylationSEGLPPGSRAHVTLG
HCCCCCCCCEEEEEC		31.8726643407
334S-nitrosylationRAHVTLGCAADVQPV
CEEEEECCCCCCCCC		2.9524895380
355UbiquitinationLDILQQVKGGSQGEA
HHHHHHHHCCCCCEE		53.90-
358PhosphorylationLQQVKGGSQGEAVGE
HHHHHCCCCCEECCC		43.6229899451
370UbiquitinationVGELPRGKLYSLGKG
CCCCCCCCEEEECCC		45.6022790023
372PhosphorylationELPRGKLYSLGKGRW
CCCCCCEEEECCCCE		12.8222324799
373PhosphorylationLPRGKLYSLGKGRWM
CCCCCEEEECCCCEE		40.8721183079
376UbiquitinationGKLYSLGKGRWMLSL
CCEEEECCCCEEEEE		51.0722790023
376AcetylationGKLYSLGKGRWMLSL
CCEEEECCCCEEEEE		51.078394851
382PhosphorylationGKGRWMLSLTKKMEV
CCCCEEEEECCCEEE		20.2125521595
385UbiquitinationRWMLSLTKKMEVKAI
CEEEEECCCEEEEEE		56.2522790023
399AcetylationIFTGYYGKGKPVPIH
EEEECCCCCCEECCC		47.8719843273
401UbiquitinationTGYYGKGKPVPIHGS
EECCCCCCEECCCCC		46.4522790023
408PhosphorylationKPVPIHGSRKGGAMQ
CEECCCCCCCCCCEE		19.3625521595
417FarnesylationKGGAMQICTII----
CCCCEEEEEEC----		0.9518076147
417FarnesylationKGGAMQICTII----
CCCCEEEEEEC----		0.9518076147
417MethylationKGGAMQICTII----
CCCCEEEEEEC----		0.95-
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

Oops, there are no upstream regulatory protein records of CN37_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CN37_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 CN37_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CN37_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CN37_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-110 AND TYR-372, ANDMASS SPECTROMETRY.

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