CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021237
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytosolic 5'-nucleotidase 3A 
Protein Synonyms/Alias
 Cytosolic 5'-nucleotidase 3; Cytosolic 5'-nucleotidase III; cN-III; Pyrimidine 5'-nucleotidase 1; P5'N-1; P5N-1; PN-I; Uridine 5'-monophosphate hydrolase 1; p36 
Gene Name
 NT5C3A 
Gene Synonyms/Alias
 NT5C3; P5N1; UMPH1; HSPC233 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
47RKTGRKTKIIEMMPEubiquitination[1]
57EMMPEFQKSSVRIKNubiquitination[1]
77EIICGLIKGGAAKLQubiquitination[1]
128RKKLLQLKEKYYAIEubiquitination[1]
182AESDVMLKEGYENFFubiquitination[2]
225GVYHPNVKVVSNFMDubiquitination[2]
240FDETGVLKGFKGELIubiquitination[3]
243TGVLKGFKGELIHVFubiquitination[4, 5]
267TEYFNQLKDNSNIILubiquitination[1, 2, 3]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Can act both as nucleotidase and as phosphotransferase. 
Sequence Annotation
 REGION 203 204 Substrate binding.
 ACT_SITE 88 88 Nucleophile.
 ACT_SITE 90 90 Proton donor.
 METAL 88 88 Magnesium.
 METAL 90 90 Magnesium; via carbonyl oxygen.
 METAL 277 277 Magnesium.
 BINDING 252 252 Substrate.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 336 AA 
Protein Sequence
MRAPSMDRAA VARVGAVASA SVCALVAGVV LAQYIFTLKR KTGRKTKIIE MMPEFQKSSV 60
RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG KRCPTCHNII DNCKLVTDEC 120
RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV EWYTKSHGLL VQQALPKAKL KEIVAESDVM 180
LKEGYENFFD KLQQHSIPVF IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF MDFDETGVLK 240
GFKGELIHVF NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN VEHILKIGYL 300
NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL 336 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0008665; F:2'-phosphotransferase activity; NAS:UniProtKB.
 GO:0008253; F:5'-nucleotidase activity; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
 GO:0006206; P:pyrimidine nucleobase metabolic process; TAS:Reactome.
 GO:0046135; P:pyrimidine nucleoside catabolic process; TAS:Reactome. 
Interpro
 IPR023214; HAD-like_dom.
 IPR006434; Pyrimidine_nucleotidase_eu. 
Pfam
 PF05822; UMPH-1 
SMART
  
PROSITE
  
PRINTS