CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022446
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Diphosphoinositol polyphosphate phosphohydrolase 2 
Protein Synonyms/Alias
 DIPP-2; Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2; Nucleoside diphosphate-linked moiety X motif 4; Nudix motif 4 
Gene Name
 NUDT4 
Gene Synonyms/Alias
 DIPP2; KIAA0487; HDCMB47P 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MMKFKPNQTRubiquitination[1]
74VYEEAGVKGKLGRLLubiquitination[1]
76EEAGVKGKLGRLLGIubiquitination[1]
134IKVLQCHKPVHAEYLubiquitination[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] 
Functional Description
 Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but not Ap5A. The major reaction products are ADP and p4a from Ap6A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA. 
Sequence Annotation
 DOMAIN 18 144 Nudix hydrolase.
 REGION 18 20 Substrate binding (By similarity).
 REGION 89 91 Substrate binding (By similarity).
 MOTIF 51 72 Nudix box.
 ACT_SITE 69 69 Proton acceptor (By similarity).
 METAL 50 50 Magnesium 1; via carbonyl oxygen (By
 METAL 66 66 Magnesium 2 (By similarity).
 METAL 66 66 Magnesium 3 (By similarity).
 METAL 70 70 Magnesium 1 (By similarity).
 BINDING 10 10 Substrate (By similarity).
 BINDING 41 41 Substrate (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 180 AA 
Protein Sequence
MMKFKPNQTR TYDREGFKKR AACLCFRSEQ EDEVLLVSSS RYPDQWIVPG GGMEPEEEPG 60
GAAVREVYEE AGVKGKLGRL LGIFEQNQDR KHRTYVYVLT VTEILEDWED SVNIGRKREW 120
FKVEDAIKVL QCHKPVHAEY LEKLKLGCSP ANGNSTVPSL PDNNALFVTA AQTSGLPSSV 180
R 181 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IDA:UniProtKB.
 GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; TAS:Reactome.
 GO:0052846; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity; IEA:EC.
 GO:0052847; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity; IEA:EC.
 GO:0052843; F:inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity; IEA:EC.
 GO:0052848; F:inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity; IEA:EC.
 GO:0052844; F:inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity; IEA:EC.
 GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0030515; F:snoRNA binding; ISS:UniProtKB.
 GO:0019722; P:calcium-mediated signaling; TAS:UniProtKB.
 GO:0009187; P:cyclic nucleotide metabolic process; TAS:ProtInc.
 GO:0019935; P:cyclic-nucleotide-mediated signaling; TAS:UniProtKB.
 GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
 GO:0046907; P:intracellular transport; TAS:UniProtKB.
 GO:0046831; P:regulation of RNA export from nucleus; TAS:UniProtKB. 
Interpro
 IPR020084; NUDIX_hydrolase_CS.
 IPR000086; NUDIX_hydrolase_dom.
 IPR015797; NUDIX_hydrolase_dom-like. 
Pfam
 PF00293; NUDIX 
SMART
  
PROSITE
 PS51462; NUDIX
 PS00893; NUDIX_BOX 
PRINTS