CN37_RAT - dbPTM
CN37_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CN37_RAT
UniProt AC P13233
Protein Name 2',3'-cyclic-nucleotide 3'-phosphodiesterase
Gene Name Cnp
Organism Rattus norvegicus (Rat).
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 MSTSFARKSHTFLPKIFFRKMSSSGAKDKPELQFPFLQDEDTVATLHECKTLFILRGLPGSGKSTLARLIVEKYHNGTKMVSADAYKIIPGSRADFSEEYKRLDEDLAGYCRRDIRVLVLDDTNHERERLDQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSLDDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRHFISGDEPKEKLDLVSYFGKRPPGVLHCTTKFCDYGKATGAEEYAQQDVVRRSYGKAFKLSISALFVTPKTAGAQVVLNEQELQLWPSDLDKPSSSESLPPGSRAHVTLGCAADVQPVQTGLDLLEILQQVKGGSQGEEVGELPRGKLYSLGKGRWMLSLAKKMEVKAIFTGYYGKGKPVPVHGSRKGGAMQICTII
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
9PhosphorylationSTSFARKSHTFLPKI
CCHHHHCCCCCHHHH		23.3927097102
11PhosphorylationSFARKSHTFLPKIFF
HHHHCCCCCHHHHHH		33.6827097102
15AcetylationKSHTFLPKIFFRKMS
CCCCCHHHHHHHHCC		55.0522902405
22PhosphorylationKIFFRKMSSSGAKDK
HHHHHHCCCCCCCCC		25.1225403869
23PhosphorylationIFFRKMSSSGAKDKP
HHHHHCCCCCCCCCC		29.3228551015
27"N6,N6-dimethyllysine"KMSSSGAKDKPELQF
HCCCCCCCCCCCCCC		70.57-
27MethylationKMSSSGAKDKPELQF
HCCCCCCCCCCCCCC		70.57-
29"N6,N6-dimethyllysine"SSSGAKDKPELQFPF
CCCCCCCCCCCCCCC		39.42-
29UbiquitinationSSSGAKDKPELQFPF
CCCCCCCCCCCCCCC		39.42-
29MethylationSSSGAKDKPELQFPF
CCCCCCCCCCCCCCC		39.42-
29AcetylationSSSGAKDKPELQFPF
CCCCCCCCCCCCCCC		39.4222902405
73MethylationLARLIVEKYHNGTKM
HHHHHHHHHHCCEEE		40.70-
73UbiquitinationLARLIVEKYHNGTKM
HHHHHHHHHHCCEEE		40.70-
73AcetylationLARLIVEKYHNGTKM
HHHHHHHHHHCCEEE		40.7022902405
79MethylationEKYHNGTKMVSADAY
HHHHCCEEEEECCHH		38.41-
86PhosphorylationKMVSADAYKIIPGSR
EEEECCHHHHCCCCC		11.85-
87AcetylationMVSADAYKIIPGSRA
EEECCHHHHCCCCCC		35.5622902405
87UbiquitinationMVSADAYKIIPGSRA
EEECCHHHHCCCCCC		35.56-
97PhosphorylationPGSRADFSEEYKRLD
CCCCCCCCHHHHHCC		30.0222673903
101AcetylationADFSEEYKRLDEDLA
CCCCHHHHHCCHHHH		50.1722902405
101UbiquitinationADFSEEYKRLDEDLA
CCCCHHHHHCCHHHH		50.17-
110PhosphorylationLDEDLAGYCRRDIRV
CCHHHHHHHCCCEEE		4.16-
161UbiquitinationRLDCAQLKEKNQWQL
EEEHHHHHHHCCEEC		55.34-
161AcetylationRLDCAQLKEKNQWQL
EEEHHHHHHHCCEEC		55.3422902405
163AcetylationDCAQLKEKNQWQLSL
EHHHHHHHCCEECCH		53.5022902405
163UbiquitinationDCAQLKEKNQWQLSL
EHHHHHHHCCEECCH		53.50-
169PhosphorylationEKNQWQLSLDDLKKL
HHCCEECCHHHHHHH		18.0430411139
174UbiquitinationQLSLDDLKKLKPGLE
ECCHHHHHHHCCCCC		64.15-
174AcetylationQLSLDDLKKLKPGLE
ECCHHHHHHHCCCCC		64.1522902405
175AcetylationLSLDDLKKLKPGLEK
CCHHHHHHHCCCCCC		69.8725786129
175UbiquitinationLSLDDLKKLKPGLEK
CCHHHHHHHCCCCCC		69.87-
177AcetylationLDDLKKLKPGLEKDF
HHHHHHHCCCCCCCC		46.0122902405
195AcetylationYFGWFLTKKSSETLR
HHHHHHCCCCHHHHH		53.4522902405
216UbiquitinationLEELGNHKAFKKELR
HHHHCCCHHHHHHHH		60.56-
216AcetylationLEELGNHKAFKKELR
HHHHCCCHHHHHHHH		60.5622902405
220AcetylationGNHKAFKKELRHFIS
CCCHHHHHHHHHHHC		56.3722902405
220UbiquitinationGNHKAFKKELRHFIS
CCCHHHHHHHHHHHC		56.37-
227PhosphorylationKELRHFISGDEPKEK
HHHHHHHCCCCCHHH		38.9725403869
232AcetylationFISGDEPKEKLDLVS
HHCCCCCHHHHCHHH		66.4922902405
232UbiquitinationFISGDEPKEKLDLVS
HHCCCCCHHHHCHHH		66.49-
234UbiquitinationSGDEPKEKLDLVSYF
CCCCCHHHHCHHHHH		54.12-
234AcetylationSGDEPKEKLDLVSYF
CCCCCHHHHCHHHHH		54.1222902405
239PhosphorylationKEKLDLVSYFGKRPP
HHHHCHHHHHCCCCC		23.2622673903
243AcetylationDLVSYFGKRPPGVLH
CHHHHHCCCCCCEEE		52.4022902405
254UbiquitinationGVLHCTTKFCDYGKA
CEEEEECCCCCCCCC		26.33-
254AcetylationGVLHCTTKFCDYGKA
CEEEEECCCCCCCCC		26.3322902405
260UbiquitinationTKFCDYGKATGAEEY
CCCCCCCCCCCCHHH		36.22-
260AcetylationTKFCDYGKATGAEEY
CCCCCCCCCCCCHHH		36.2222902405
262PhosphorylationFCDYGKATGAEEYAQ
CCCCCCCCCCHHHHH		40.1722673903
279AcetylationVVRRSYGKAFKLSIS
HHHHHHHHHHEEEEE		42.2822902405
315AcetylationLWPSDLDKPSSSESL
CCCCCCCCCCCCCCC		54.8422902405
315UbiquitinationLWPSDLDKPSSSESL
CCCCCCCCCCCCCCC		54.84-
355UbiquitinationLEILQQVKGGSQGEE
HHHHHHHHCCCCCCC		53.90-
358PhosphorylationLQQVKGGSQGEEVGE
HHHHHCCCCCCCCCC		43.6222673903
370AcetylationVGELPRGKLYSLGKG
CCCCCCCCEEECCCC		45.6022902405
372PhosphorylationELPRGKLYSLGKGRW
CCCCCCEEECCCCHH		12.82-
373PhosphorylationLPRGKLYSLGKGRWM
CCCCCEEECCCCHHH		40.8722673903
376AcetylationGKLYSLGKGRWMLSL
CCEEECCCCHHHHHH		51.0722902405
376UbiquitinationGKLYSLGKGRWMLSL
CCEEECCCCHHHHHH		51.07-
382PhosphorylationGKGRWMLSLAKKMEV
CCCHHHHHHHHHCCE		15.3522673903
385AcetylationRWMLSLAKKMEVKAI
HHHHHHHHHCCEEEE		58.9322902405
399AcetylationIFTGYYGKGKPVPVH
EEECCCCCCCEECCC		47.8722902405
401UbiquitinationTGYYGKGKPVPVHGS
ECCCCCCCEECCCCC		46.45-
408PhosphorylationKPVPVHGSRKGGAMQ
CEECCCCCCCCCCEE		18.8825403869
417FarnesylationKGGAMQICTII----
CCCCEEEEEEC----		0.957884818
417FarnesylationKGGAMQICTII----
CCCCEEEEEEC----		0.957884818
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_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CN37_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRNL_YEASTTRL1genetic
18094118
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CN37_RAT

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Related Literatures of Post-Translational Modification

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