CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004446
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2',3'-cyclic-nucleotide 3'-phosphodiesterase 
Protein Synonyms/Alias
 CNP; CNPase 
Gene Name
 Cnp 
Gene Synonyms/Alias
 Cnp1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
15KSHTFLPKLFFRKMSubiquitination[1]
27KMSSSGAKEKPELQFubiquitination[1]
29SSSGAKEKPELQFPFubiquitination[1]
63RGLPGSGKSTLARLIubiquitination[1]
73LARLILEKYHDGTKMubiquitination[1]
79EKYHDGTKMVSADAYacetylation[2]
79EKYHDGTKMVSADAYubiquitination[1]
87MVSADAYKIIPGSRAubiquitination[1]
101ADFSEAYKRLDEDLAubiquitination[1]
161RLDCAQLKEKNQWQLubiquitination[1]
163DCAQLKEKNQWQLSAubiquitination[1]
174QLSADDLKKLKPGLEubiquitination[1]
175LSADDLKKLKPGLEKubiquitination[1]
177ADDLKKLKPGLEKDFacetylation[3, 4]
203KSSETLRKAGQVFLEubiquitination[1]
216LEELGNHKAFKKELRubiquitination[1]
232FISGDEPKEKLELVSubiquitination[1]
234SGDEPKEKLELVSYFubiquitination[1]
254GVLHCTTKFCDYGKAubiquitination[1]
260TKFCDYGKAAGAEEYubiquitination[1]
274YAQQEVVKRSYGKAFubiquitination[1]
315LWPSDLDKPSASEGLubiquitination[1]
370VGELPRGKLYSLGKGubiquitination[1]
376GKLYSLGKGRWMLSLubiquitination[1]
385RWMLSLTKKMEVKAIubiquitination[1]
401TGYYGKGKPVPIHGSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [3] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 
Functional Description
 May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin. 
Sequence Annotation
 ACT_SITE 250 250 Proton acceptor.
 ACT_SITE 329 329 Proton donor.
 BINDING 252 252 Substrate.
 BINDING 331 331 Substrate.
 MOD_RES 110 110 Phosphotyrosine.
 MOD_RES 372 372 Phosphotyrosine.
 MOD_RES 417 417 Cysteine methyl ester (Probable).
 LIPID 417 417 S-farnesyl cysteine (Probable).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Direct protein sequencing; Hydrolase; Lipoprotein; Membrane; Methylation; Phosphoprotein; Prenylation; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 420 AA 
Protein Sequence
MNTSFTRKSH TFLPKLFFRK MSSSGAKEKP ELQFPFLQDE DTVATLHECK TLFILRGLPG 60
SGKSTLARLI LEKYHDGTKM VSADAYKIIP GSRADFSEAY KRLDEDLAGY CRRDIRVLVL 120
DDTNHERERL DQLFEMADQY QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL 180
EKDFLPLYFG WFLTKKSSET LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLELVSY 240
FGKRPPGVLH CTTKFCDYGK AAGAEEYAQQ EVVKRSYGKA FKLSISALFV TPKTAGAQVV 300
LTDQELQLWP SDLDKPSASE GLPPGSRAHV TLGCAADVQP VQTGLDLLDI LQQVKGGSQG 360
EAVGELPRGK LYSLGKGRWM LSLTKKMEVK AIFTGYYGKG KPVPIHGSRK GGAMQICTII 420 
Gene Ontology
 GO:0005615; C:extracellular space; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IDA:MGI.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005902; C:microvillus; IEA:Compara.
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005741; C:mitochondrial outer membrane; IEA:Compara.
 GO:0035748; C:myelin sheath abaxonal region; IEA:Compara.
 GO:0035749; C:myelin sheath adaxonal region; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0031143; C:pseudopodium; IEA:Compara.
 GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IDA:MGI.
 GO:0030551; F:cyclic nucleotide binding; IEA:Compara.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008344; P:adult locomotory behavior; IMP:MGI.
 GO:0007568; P:aging; IEA:Compara.
 GO:0007409; P:axonogenesis; IMP:MGI.
 GO:0009214; P:cyclic nucleotide catabolic process; IEA:InterPro.
 GO:0030900; P:forebrain development; IEA:Compara.
 GO:0000226; P:microtubule cytoskeleton organization; IEA:Compara.
 GO:0046902; P:regulation of mitochondrial membrane permeability; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0009636; P:response to toxic substance; IDA:MGI.
 GO:0016070; P:RNA metabolic process; IEA:InterPro. 
Interpro
 IPR008431; CNPase.
 IPR027417; P-loop_NTPase.
 IPR009097; RNA_ligase/cNuc_Pdiesterase. 
Pfam
 PF05881; CNPase 
SMART
  
PROSITE
  
PRINTS