CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020419
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Uridine-cytidine kinase 2 
Protein Synonyms/Alias
 UCK 2; Cytidine monophosphokinase 2; Testis-specific protein TSA903; Uridine monophosphokinase 2 
Gene Name
 UCK2 
Gene Synonyms/Alias
 UMPK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33SGGTASGKSSVCAKIubiquitination[1]
39GKSSVCAKIVQLLGQubiquitination[1, 2]
54NEVDYRQKQVVILSQubiquitination[1, 2, 3]
73RVLTSEQKAKALKGQubiquitination[2, 4, 5]
75LTSEQKAKALKGQFNubiquitination[1, 4, 6, 7]
78EQKAKALKGQFNFDHubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
96FDNELILKTLKEITEubiquitination[1, 4]
99ELILKTLKEITEGKTubiquitination[1, 2, 4]
105LKEITEGKTVQIPVYubiquitination[1, 4]
202EFCLPTKKYADVIIPubiquitination[1, 3, 6, 7, 10]
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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [3] 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]
 [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]
 [6] 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]
 [7] 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]
 [8] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine. 
Sequence Annotation
 NP_BIND 27 35 ATP.
 BINDING 84 84 Substrate.
 BINDING 112 112 Substrate.
 BINDING 117 117 Substrate.
 BINDING 166 166 Substrate.
 BINDING 176 176 Substrate.
 BINDING 184 184 Substrate.
 BINDING 213 213 ATP.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 254 254 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 261 AA 
Protein Sequence
MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YRQKQVVILS 60
QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELILKTLKE ITEGKTVQIP VYDFVSHSRK 120
EETVTVYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ 180
ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGPSKRQTNG 240
CLNGYTPSRK RQASESSSRP H 261 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0043231; C:intracellular membrane-bounded organelle; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0019206; F:nucleoside kinase activity; EXP:Reactome.
 GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
 GO:0004849; F:uridine kinase activity; IEA:EC.
 GO:0071453; P:cellular response to oxygen levels; IEA:Compara.
 GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
 GO:0007631; P:feeding behavior; IEA:Compara.
 GO:0006206; P:pyrimidine nucleobase metabolic process; TAS:Reactome.
 GO:0043097; P:pyrimidine nucleoside salvage; TAS:Reactome.
 GO:0048678; P:response to axon injury; IEA:Compara.
 GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR006083; PRK/URK.
 IPR000764; Uridine_kinase. 
Pfam
 PF00485; PRK 
SMART
  
PROSITE
  
PRINTS
 PR00988; URIDINKINASE.