CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008228
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytosolic purine 5'-nucleotidase 
Protein Synonyms/Alias
 Cytosolic 5'-nucleotidase II 
Gene Name
 NT5C2 
Gene Synonyms/Alias
 NT5B; NT5CP; PNT5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21DMPANMDKHALKKYRubiquitination[1]
140TREQYPNKFIQRDDTubiquitination[1, 2, 3]
186TSCETGFKDGDLFMSubiquitination[1]
211AVDWVHYKGSLKEKTubiquitination[1, 2, 3, 4, 5]
215VHYKGSLKEKTVENLubiquitination[1]
217YKGSLKEKTVENLEKubiquitination[1]
228NLEKYVVKDGKLPLLubiquitination[1]
231KYVVKDGKLPLLLSRubiquitination[1, 4, 5]
244SRMKEVGKVFLATNSubiquitination[2, 3]
254LATNSDYKYTDKIMTubiquitination[2, 3]
292LILVDARKPLFFGEGubiquitination[1]
344DLLGAKGKDILYIGDubiquitination[1, 4, 5]
359HIFGDILKSKKRQGWubiquitination[1, 4]
515NRTSVDFKDTDYKRHubiquitination[1, 4]
520DFKDTDYKRHQLTRSubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides. 
Sequence Annotation
 REGION 202 210 Substrate binding (Potential).
 ACT_SITE 52 52 Nucleophile.
 ACT_SITE 54 54 Proton donor.
 METAL 52 52 Magnesium.
 METAL 54 54 Magnesium; via carbonyl oxygen.
 METAL 351 351 Magnesium.
 BINDING 127 127 Allosteric activator 1.
 BINDING 154 154 Allosteric activator 2.
 BINDING 354 354 Allosteric activator 2.
 BINDING 436 436 Allosteric activator 1; via carbonyl
 BINDING 453 453 Allosteric activator 2.
 MOD_RES 502 502 Phosphoserine.
 MOD_RES 527 527 Phosphoserine (By similarity).  
Keyword
 3D-structure; Allosteric enzyme; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 561 AA 
Protein Sequence
MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY 60
KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV 120
CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS 180
CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK 240
EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT 300
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS 360
KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ 420
RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA 480
HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA 540
PQEITHCHDE DDDEEEEEEE E 561 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0008253; F:5'-nucleotidase activity; EXP:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050146; F:nucleoside phosphotransferase activity; TAS:Reactome.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0017144; P:drug metabolic process; TAS:Reactome.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome. 
Interpro
 IPR023214; HAD-like_dom.
 IPR008380; HAD-SF_hydro_IG_5-nucl.
 IPR016695; Pur_nucleotidase. 
Pfam
 PF05761; 5_nucleotid 
SMART
  
PROSITE
  
PRINTS