CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015002
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2',5'-phosphodiesterase 12 
Protein Synonyms/Alias
 2'-PDE; 2-PDE 
Gene Name
 PDE12 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61ALADGSHKNMQRDQSubiquitination[1, 2]
84RIATNALKGHAKAAAubiquitination[3]
97AAAKKSRKSRPNASGubiquitination[3, 4]
202FRWYKEAKPGAAEPEubiquitination[3, 5]
247ADIGLRLKLHCTPGDubiquitination[3]
377LEGVFRIKQHEGLATubiquitination[3]
417LHKELLEKLVLYPSAubiquitination[5]
427LYPSAQEKVLQRSSVubiquitination[1, 2, 3, 4, 5]
462THLYWHPKGGYIRLIubiquitination[3, 6]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the The 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme induces reduction of viral replication in Hela cells, thus counteracting the antiviral pathway probably by inhibiting the 2-5A system. 
Sequence Annotation
 MOD_RES 217 217 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 609 AA 
Protein Sequence
MWRLPGARAA LRVIRTAVEK LSRAEAGSQT AAGAMERAVV RCVPSEPKLS LSFALADGSH 60
KNMQRDQSEP LGRVLSRIAT NALKGHAKAA AAKKSRKSRP NASGGAACSG PGPEPAVFCE 120
PVVKLYYREE AVAEDVLNVD AWQDGAVLQI GDVKYKVERN PPAFTELQLP RYIMAGFPVC 180
PKLSLEFGDP ASSLFRWYKE AKPGAAEPEV GVPSSLSPSS PSSSWTETDV EERVYTPSNA 240
DIGLRLKLHC TPGDGQRFGH SRELESVCVV EAGPGTCTFD HRHLYTKKVT EDALIRTVSY 300
NILADTYAQT EFSRTVLYPY CAPYALELDY RQNLIQKELT GYNADVICLQ EVDRAVFSDS 360
LVPALEAFGL EGVFRIKQHE GLATFYRKSK FSLLSQHDIS FYEALESDPL HKELLEKLVL 420
YPSAQEKVLQ RSSVLQVSVL QSTKDSSKRI CVANTHLYWH PKGGYIRLIQ MAVALAHIRH 480
VSCDLYPGIP VIFCGDFNST PSTGMYHFVI NGSIPEDHED WASNGEEERC NMSLTHFFKL 540
KSACGEPAYT NYVGGFHGCL DYIFIDLNAL EVEQVIPLPS HEEVTTHQAL PSVSHPSDHI 600
ALVCDLKWK 609 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 
Interpro
 IPR005135; Endo/exonuclease/phosphatase. 
Pfam
 PF03372; Exo_endo_phos 
SMART
  
PROSITE
  
PRINTS