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Pnkp

Protein FULL name:

bifunctional polynucleotide phosphatase/kinase [Mus musculus].


Pnkp (Mus musculus) is product of expression of Pnkp gene.






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 (By similarity).

CATALYTIC ACTIVITY: A 3'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate.

CATALYTIC ACTIVITY: ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA.

SUBCELLULAR LOCATION: Nucleus (By similarity).

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

SIMILARITY: In the N-terminal section; belongs to the DNA 3' phosphatase family.


NCBI GenPept GI number(s): 118601009
Species: Mus musculus

Links to other databases:

Database ID Link
Uniprot Q9JLV6 Q9JLV6
PFAM: - Q9JLV6 (Link - using uniprot id)
InterPro: - Q9JLV6 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MSQLGSRGRLWLQSPTGGPPPIFLPSDGQALVLGRGPLTQVTDRKCSRNQ
VELIADPESRTVAVKQLGVNPSTVGVQELKPGLSGSLSLGDVLYLVNGLY
PLTLRWEELSTSGSQPDAPPDTPGDPEEGEDTEPQKKRVRKSSLGWESLK
KLLVFTASGVKPQGKVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPK
KLQELAAEGYKLVIFTNQMGIGRGKLPAEVFKGKVEAVLEKLGVPFQVLV
ATHAGLNRKPVSGMWDHLQEQANEGIPISVEDSVFVGDAAGRLANWAPGR
KKKDFSCADRLFALNVGLPFATPEEFFLKWPAARFELPAFDPRTISSAGP
LYLPESSSLLSPNPEVVVAVGFPGAGKSTFIQEHLVSAGYVHVNRDTLGS
WQRCVSSCQAALRQGKRVVIDNTNPDVPSRARYIQCAKDAGVPCRCFNFC
ATIEQARHNNRFREMTDPSHAPVSDMVMFSYRKQFEPPTLAEGFLEILEI
PFRLQEHLDPALQRLYRQFSEG

Pnkp (Mus musculus) is able to recognize following damages:
Pnkp (Mus musculus) belongs to following protein families:
References:

Title Authors Journal
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). 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 Genome Res Oct. 1, 2004
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. 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 Science May 25, 2007


Last modification of this entry: Oct. 6, 2010.

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