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Protein FULL name: bifunctional polynucleotide phosphatase/kinase [Homo sapiens].
PNKP (Homo sapiens) is product of expression of
PNKP
gene.
PNKP is involved in:
BER in Homo sapiens
Keywords:
FUNCTION: Catalyzes the phosphorylation of DNA at 5'-hydroxyl
termini and can dephosphorylate its 3'-phosphate termini. Plays an
important function in DNA repair following ionizing radiation or
oxidative damage.
CATALYTIC ACTIVITY: A 3'-phosphopolynucleotide + H(2)O = a
polynucleotide + phosphate.
CATALYTIC ACTIVITY: ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA.
INTERACTION:
Q9UHI6:DDX20; NbExp=1; IntAct=EBI-1045072, EBI-347658;
Q86Y56:HEATR2; NbExp=1; IntAct=EBI-1045072, EBI-719966;
Q9Y4W2:LAS1L; NbExp=1; IntAct=EBI-1045072, EBI-1051591;
P49916:LIG3; NbExp=1; IntAct=EBI-1045072, EBI-1753381;
P49917:LIG4; NbExp=1; IntAct=EBI-1045072, EBI-847896;
P25205:MCM3; NbExp=1; IntAct=EBI-1045072, EBI-355153;
O60936:NOL3; NbExp=1; IntAct=EBI-1045072, EBI-740992;
Q8N1F7:NUP93; NbExp=1; IntAct=EBI-1045072, EBI-1042703;
O75746:SLC25A12; NbExp=1; IntAct=EBI-1045072, EBI-1047585;
P18887:XRCC1; NbExp=1; IntAct=EBI-1045072, EBI-947466;
Q13426:XRCC4; NbExp=1; IntAct=EBI-1045072, EBI-717592;
P27348:YWHAQ; NbExp=1; IntAct=EBI-1045072, EBI-359854;
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Expressed in many tissues with highest
expression in spleen and testis, and lowest expression in small
intestine (PubMed:10446192). Expressed in higher amount in
pancreas, heart and kidney and at lower levels in brain, lung and
liver (PubMed:10446193).
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
SIMILARITY: In the N-terminal section; belongs to the DNA 3'
phosphatase family.
SEQUENCE CAUTION:
Sequence=AAD47379.1; Type=Frameshift; Positions=Several;
WEB RESOURCE: Name=NIEHS-SNPs;
[LINK]
Links to other databases:
Protein sequence:
MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQ
VELVADPETRTVAVKQLGVNPSTTGTQELKPGLEGSLGVGDTLYLVNGLH
PLTLRWEETRTPESQPDTPPGTPLVSQDEKRDAELPKKRMRKSNPGWENL
EKLLVFTAAGVKPQGKVAGFDLDGTLITTRSGKVFPTGPSDWRILYPEIP
RKLRELEAEGYKLVIFTNQMSIGRGKLPAEEFKAKVEAVVEKLGVPFQVL
VATHAGLYRKPVTGMWDHLQEQANDGTPISIGDSIFVGDAAGRPANWAPG
RKKKDFSCADRLFALNLGLPFATPEEFFLKWPAAGFELPAFDPRTVSRSG
PLCLPESRALLSASPEVVVAVGFPGAGKSTFLKKHLVSAGYVHVNRDTLG
SWQRCVTTCETALKQGKRVAIDNTNPDAASRARYVQCARAAGVPCRCFLF
TATLEQARHNNRFREMTDSSHIPVSDMVMYGYRKQFEAPTLAEGFSAILE
IPFRLWVEPRLGRLYCQFSEG
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PNKP (Homo sapiens) is able to recognize following damages:
PNKP (Homo sapiens) belongs to following protein families:
References:
Title
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Authors
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Journal
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Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3'-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage.
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Jilani A, Ramotar D, Slack C, Ong C, Yang XM, Scherer SW, Lasko DD
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J Biol Chem
Aug. 20, 1999
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Molecular characterization of a human DNA kinase.
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Karimi-Busheri F, Daly G, Robins P, Canas B, Pappin DJ, Sgouros J, Miller GG, Fakhrai H, Davis EM, Le Beau MM, Weinfeld M
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J Biol Chem
Aug. 20, 1999
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The DNA sequence and biology of human chromosome 19.
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Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM
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Nature
April 1, 2004
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
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Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J
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Genome Res
Oct. 1, 2004
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Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
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Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M
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Cell
Nov. 3, 2006
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ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
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Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ
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Science
May 25, 2007
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A quantitative atlas of mitotic phosphorylation.
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Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP
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Proc Natl Acad Sci U S A
Aug. 5, 2008
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Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
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Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK
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Sci Signal
Jan. 1, 2009
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Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
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Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S
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Anal Chem
June 1, 2009
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Last modification of this entry: Oct. 14, 2010.
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