CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001617
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NAD kinase 
Protein Synonyms/Alias
 Poly(P)/ATP NAD kinase 
Gene Name
 NADK 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
57SPALGSTKEFRRTRSubiquitination[1, 2]
102SQRLTWNKSPKSVLVubiquitination[3]
140NMIVYVEKKVLEDPAubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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
  
Sequence Annotation
 MOD_RES 46 46 Phosphoserine.
 MOD_RES 48 48 Phosphoserine.
 MOD_RES 50 50 Phosphoserine.
 MOD_RES 64 64 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Kinase; Metal-binding; NAD; NADP; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 446 AA 
Protein Sequence
MEMEQEKMTM NKELSPDAAA YCCSACHGDE TWSYNHPIRG RAKSRSLSAS PALGSTKEFR 60
RTRSLHGPCP VTTFGPKACV LQNPQTIMHI QDPASQRLTW NKSPKSVLVI KKMRDASLLQ 120
PFKELCTHLM EENMIVYVEK KVLEDPAIAS DESFGAVKKK FCTFREDYDD ISNQIDFIIC 180
LGGDGTLLYA SSLFQGSVPP VMAFHLGSLG FLTPFSFENF QSQVTQVIEG NAAVVLRSRL 240
KVRVVKELRG KKTAVHNGLG ENGSQAAGLD MDVGKQAMQY QVLNEVVIDR GPSSYLSNVD 300
VYLDGHLITT VQGDGVIVST PTGSTAYAAA AGASMIHPNV PAIMITPICP HSLSFRPIVV 360
PAGVELKIML SPEARNTAWV SFDGRKRQEI RHGDSISITT SCYPLPSICV RDPVSDWFES 420
LAQCLHWNVR KKQAHFEEEE EEEEEG 446 
Gene Ontology
 GO:0005829; C:cytosol; TAS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003951; F:NAD+ kinase activity; IDA:UniProtKB.
 GO:0046034; P:ATP metabolic process; NAS:UniProtKB.
 GO:0019674; P:NAD metabolic process; TAS:Reactome.
 GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
 GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. 
Interpro
 IPR017438; ATP-NAD_kinase_dom_1.
 IPR016064; ATP-NAD_kinase_PpnK-typ.
 IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
 IPR002504; PolyP/ATP_NADK_prd. 
Pfam
 PF01513; NAD_kinase 
SMART
  
PROSITE
  
PRINTS