CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020115
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cancer-related nucleoside-triphosphatase 
Protein Synonyms/Alias
 NTPase; Nucleoside triphosphate phosphohydrolase 
Gene Name
 NTPCR 
Gene Synonyms/Alias
 C1orf57 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15TGPPGVGKTTLIHKAubiquitination[1]
21GKTTLIHKASEVLKSacetylation[2]
21GKTTLIHKASEVLKSubiquitination[3]
27HKASEVLKSSGVPVDubiquitination[1]
73GLEPPPGKRECRVGQubiquitination[1]
148LGTIPVPKGKPLALVubiquitination[3]
150TIPVPKGKPLALVEEubiquitination[1]
165IRNRKDVKVFNVTKEacetylation[2, 4, 5]
165IRNRKDVKVFNVTKEubiquitination[3]
171VKVFNVTKENRNHLLubiquitination[1, 3, 5]
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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] 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]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] 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
 Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency. 
Sequence Annotation
 NP_BIND 9 16 ATP (Probable).
 NP_BIND 109 116 ATP (Probable).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 165 165 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 190 AA 
Protein Sequence
MARHVFLTGP PGVGKTTLIH KASEVLKSSG VPVDGFYTEE VRQGGRRIGF DVVTLSGTRG 60
PLSRVGLEPP PGKRECRVGQ YVVDLTSFEQ LALPVLRNAD CSSGPGQRVC VIDEIGKMEL 120
FSQLFIQAVR QTLSTPGTII LGTIPVPKGK PLALVEEIRN RKDVKVFNVT KENRNHLLPD 180
IVTCVQSSRK 190 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0017111; F:nucleoside-triphosphatase activity; IEA:EC.
 GO:0019204; F:nucleotide phosphatase activity; IEA:InterPro.
 GO:0016740; F:transferase activity; IEA:InterPro. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR004948; Nuc-triphosphatase_THEP1.
 IPR027417; P-loop_NTPase. 
Pfam
 PF03266; NTPase_1 
SMART
 SM00382; AAA 
PROSITE
  
PRINTS