LOCUS       NP_067524                522 aa            linear   ROD 06-OCT-2024
DEFINITION  bifunctional polynucleotide phosphatase/kinase isoform a [Mus
            musculus].
ACCESSION   NP_067524
VERSION     NP_067524.2
DBSOURCE    REFSEQ: accession NM_021549.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Chakraborty,A., Sreenivasmurthy,S.G., Miller,W., Huai,W.,
            Biswas,T., Mandal,S.M., Bosca,L., Krishnan,B., Ghosh,G. and
            Hazra,T.
  TITLE     Fructose-2,6-bisphosphate restores DNA repair activity of PNKP and
            ameliorates neurodegenerative symptoms in Huntington's disease
  JOURNAL   Proc Natl Acad Sci U S A 121 (39), e2406308121 (2024)
   PUBMED   39298485
  REMARK    GeneRIF: Fructose-2,6-bisphosphate restores DNA repair activity of
            PNKP and ameliorates neurodegenerative symptoms in Huntington's
            disease.
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Shin,W., Alpaugh,W., Hallihan,L.J., Sinha,S., Crowther,E.,
            Martin,G.R., Scheidl-Yee,T., Yang,X., Yoon,G., Goldsmith,T.,
            Berger,N.D., de Almeida,L.G., Dufour,A., Dobrinski,I., Weinfeld,M.,
            Jirik,F.R. and Biernaskie,J.
  TITLE     PNKP is required for maintaining the integrity of progenitor cell
            populations in adult mice
  JOURNAL   Life Sci Alliance 4 (9), e202000790 (2021)
   PUBMED   34226276
  REMARK    GeneRIF: PNKP is required for maintaining the integrity of
            progenitor cell populations in adult mice.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Horton,J.K., Stefanick,D.F., Zhao,M.L., Janoshazi,A.K.,
            Gassman,N.R., Seddon,H.J. and Wilson,S.H.
  TITLE     XRCC1-mediated repair of strand breaks independent of PNKP binding
  JOURNAL   DNA Repair (Amst) 60, 52-63 (2017)
   PUBMED   29100039
  REMARK    GeneRIF: Repair independent of the well documented XRCC1-PNKP
            interaction was studied. XRCC1 can mediate repair of strand breaks
            without PNKP binding.
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Havali-Shahriari,Z., Weinfeld,M. and Glover,J.N.
  TITLE     Characterization of DNA Substrate Binding to the Phosphatase Domain
            of the DNA Repair Enzyme Polynucleotide Kinase/Phosphatase
  JOURNAL   Biochemistry 56 (12), 1737-1745 (2017)
   PUBMED   28276686
  REMARK    GeneRIF: The work indicates that the phosphatase domain of Pnkp
            binds 3'-phosphorylated single-stranded DNAs in a manner that is
            highly dependent on the presence of the 3'-phosphate.
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Coquelle,N., Havali-Shahriari,Z., Bernstein,N., Green,R. and
            Glover,J.N.
  TITLE     Structural basis for the phosphatase activity of polynucleotide
            kinase/phosphatase on single- and double-stranded DNA substrates
  JOURNAL   Proc Natl Acad Sci U S A 108 (52), 21022-21027 (2011)
   PUBMED   22171004
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Garces,F., Pearl,L.H. and Oliver,A.W.
  TITLE     The structural basis for substrate recognition by mammalian
            polynucleotide kinase 3' phosphatase
  JOURNAL   Mol Cell 44 (3), 385-396 (2011)
   PUBMED   22055185
  REMARK    GeneRIF: Structure of dsDNA bound to PNK 5'-kinase domain reveals
            DNA bending facilitating recognition of DNA ends in the context of
            single-strand/double-strand breaks, suggesting close functional
            cooperation in between the kinase/phosphatase active sites.
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Bernstein,N.K., Hammel,M., Mani,R.S., Weinfeld,M., Pelikan,M.,
            Tainer,J.A. and Glover,J.N.
  TITLE     Mechanism of DNA substrate recognition by the mammalian DNA repair
            enzyme, Polynucleotide Kinase
  JOURNAL   Nucleic Acids Res 37 (18), 6161-6173 (2009)
   PUBMED   19671525
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Bernstein,N.K., Williams,R.S., Rakovszky,M.L., Cui,D., Green,R.,
            Karimi-Busheri,F., Mani,R.S., Galicia,S., Koch,C.A., Cass,C.E.,
            Durocher,D., Weinfeld,M. and Glover,J.N.
  TITLE     The molecular architecture of the mammalian DNA repair enzyme,
            polynucleotide kinase
  JOURNAL   Mol Cell 17 (5), 657-670 (2005)
   PUBMED   15749016
  REMARK    GeneRIF: analysis of the molecular architecture of polynucleotide
            kinase
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY118349.1, CX223963.1, AK049992.1, AC158231.2 and BY579541.1.
            
            On Dec 2, 2006 this sequence version replaced NP_067524.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Variants 1 and 2
            both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057659.1, AK049992.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 28.94 cM"
     Protein         1..522
                     /product="bifunctional polynucleotide phosphatase/kinase
                     isoform a"
                     /EC_number="2.7.1.78"
                     /EC_number="3.1.3.32"
                     /note="bifunctional polynucleotide phosphatase/kinase; DNA
                     5'-kinase/3'-phosphatase"
                     /calculated_mol_wt=57083
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q96T60; propagated from
                     UniProtKB/Swiss-Prot (Q9JLV6.2)"
     Region          3..522
                     /region_name="PNK-3'Pase"
                     /note="polynucleotide 5'-kinase 3'-phosphatase; TIGR01663"
                     /db_xref="CDD:130724"
     Region          110..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLV6.2)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96T60; propagated from
                     UniProtKB/Swiss-Prot (Q9JLV6.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9JLV6.2)"
     Region          145..336
                     /region_name="Phosphatase.
                     /evidence=ECO:0000303|PubMed:15749016"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLV6.2)"
     Region          340..517
                     /region_name="Kinase.
                     /evidence=ECO:0000303|PubMed:15749016"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9JLV6.2)"
     CDS             1..522
                     /gene="Pnkp"
                     /gene_synonym="1810009G08Rik; PNK"
                     /coded_by="NM_021549.3:259..1827"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS39945.1"
                     /db_xref="GeneID:59047"
                     /db_xref="MGI:MGI:1891698"
ORIGIN      
        1 msqlgsrgrl wlqsptggpp piflpsdgqa lvlgrgpltq vtdrkcsrnq veliadpesr
       61 tvavkqlgvn pstvgvqelk pglsgslslg dvlylvngly pltlrweels tsgsqpdapp
      121 dtpgdpeege dtepqkkrvr ksslgweslk kllvftasgv kpqgkvaafd ldgtlittrs
      181 gkvfptspsd wrilypeipk klqelaaegy klviftnqmg igrgklpaev fkgkveavle
      241 klgvpfqvlv athaglnrkp vsgmwdhlqe qanegipisv edsvfvgdaa grlanwapgr
      301 kkkdfscadr lfalnvglpf atpeefflkw paarfelpaf dprtissagp lylpesssll
      361 spnpevvvav gfpgagkstf iqehlvsagy vhvnrdtlgs wqrcvsscqa alrqgkrvvi
      421 dntnpdvpsr aryiqcakda gvpcrcfnfc atieqarhnn rfremtdpsh apvsdmvmfs
      481 yrkqfepptl aegfleilei pfrlqehldp alqrlyrqfs eg
//
