CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019665
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bifunctional polynucleotide phosphatase/kinase 
Protein Synonyms/Alias
 DNA 5'-kinase/3'-phosphatase; Polynucleotide kinase-3'-phosphatase; Polynucleotide 3'-phosphatase; 2'(3')-polynucleotidase; Polynucleotide 5'-hydroxyl-kinase 
Gene Name
 PNKP 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
162VFTAAGVKPQGKVAGubiquitination[1]
183LITTRSGKVFPTGPSubiquitination[1]
226QMSIGRGKLPAEEFKubiquitination[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
 Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. 
Sequence Annotation
 DOMAIN 6 110 FHA.
 NP_BIND 372 379 ATP (Potential).
 REGION 146 337 Phosphatase (By similarity).
 REGION 341 516 Kinase (By similarity).
 MOD_RES 114 114 Phosphoserine.
 MOD_RES 118 118 Phosphothreonine.
 MOD_RES 122 122 Phosphothreonine.  
Keyword
 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; Hydrolase; Kinase; Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Primary microcephaly; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 521 AA 
Protein Sequence
MGEVEAPGRL WLESPPGGAP PIFLPSDGQA LVLGRGPLTQ VTDRKCSRTQ VELVADPETR 60
TVAVKQLGVN PSTTGTQELK PGLEGSLGVG DTLYLVNGLH PLTLRWEETR TPESQPDTPP 120
GTPLVSQDEK RDAELPKKRM RKSNPGWENL EKLLVFTAAG VKPQGKVAGF DLDGTLITTR 180
SGKVFPTGPS DWRILYPEIP RKLRELEAEG YKLVIFTNQM SIGRGKLPAE EFKAKVEAVV 240
EKLGVPFQVL VATHAGLYRK PVTGMWDHLQ EQANDGTPIS IGDSIFVGDA AGRPANWAPG 300
RKKKDFSCAD RLFALNLGLP FATPEEFFLK WPAAGFELPA FDPRTVSRSG PLCLPESRAL 360
LSASPEVVVA VGFPGAGKST FLKKHLVSAG YVHVNRDTLG SWQRCVTTCE TALKQGKRVA 420
IDNTNPDAAS RARYVQCARA AGVPCRCFLF TATLEQARHN NRFREMTDSS HIPVSDMVMY 480
GYRKQFEAPT LAEGFSAILE IPFRLWVEPR LGRLYCQFSE G 521 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0046404; F:ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IDA:UniProtKB.
 GO:0003684; F:damaged DNA binding; NAS:UniProtKB.
 GO:0003690; F:double-stranded DNA binding; TAS:UniProtKB.
 GO:0004519; F:endonuclease activity; NAS:UniProtKB.
 GO:0019201; F:nucleotide kinase activity; IDA:UniProtKB.
 GO:0046403; F:polynucleotide 3'-phosphatase activity; IDA:UniProtKB.
 GO:0042769; P:DNA damage response, detection of DNA damage; IDA:UniProtKB.
 GO:0006261; P:DNA-dependent DNA replication; NAS:UniProtKB.
 GO:0000718; P:nucleotide-excision repair, DNA damage removal; NAS:UniProtKB.
 GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
 GO:0009314; P:response to radiation; NAS:UniProtKB. 
Interpro
 IPR000253; FHA_dom.
 IPR023214; HAD-like_dom.
 IPR006549; HAD-SF_hydro_IIIA.
 IPR027417; P-loop_NTPase.
 IPR013954; PNK3P.
 IPR015636; PNK_3Pase_euk.
 IPR006550; PNK_3Pase_met.
 IPR006551; Polynucleotide_phosphatase.
 IPR008984; SMAD_FHA_domain. 
Pfam
 PF08645; PNK3P 
SMART
  
PROSITE
 PS50006; FHA_DOMAIN 
PRINTS