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Reviewed, UniProtKB/Swiss-Prot Q9JLV6 (PNKP_MOUSE)

Last modified February 9, 2010. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional polynucleotide phosphatase/kinase
Alternative name(s):
    Polynucleotide kinase-3'-phosphatase
    DNA 5'-kinase/3'-phosphatase
Including the following 2 domains:
    1- Recommended name:
            Polynucleotide 3'-phosphatase
              EC=3.1.3.32
        Alternative name(s):
            2'(3')-polynucleotidase
    2- Recommended name:
            Polynucleotide 5'-hydroxyl-kinase
              EC=2.7.1.78
Gene names
Name: Pnkp
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

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 + H2O = a polynucleotide + phosphate.

ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA.

Subcellular location

Nucleus By similarity.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.3

Sequence similarities

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

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JLV6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9JLV6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     163-191: QGKVAAFDLDGTLITTRSGKVFPTSPSDW → RA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Bifunctional polynucleotide phosphatase/kinase
PRO_0000058479

Regions

Nucleotide binding371 – 3788ATP Potential

Amino acid modifications

Modified residue1141Phosphoserine Ref.3
Modified residue1221Phosphothreonine Ref.3

Natural variations

Alternative sequence163 – 19129QGKVA…SPSDW → RA in isoform 2.
VSP_010771

Experimental info

Sequence conflict771H → Q in AAF36487. Ref.1
Sequence conflict2161Missing in AAF36487. Ref.1

Secondary structure

...................................................................................... 522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: C691C0A6DA9F47FE

FASTA52257,223
        10         20         30         40         50         60 
MSQLGSRGRL WLQSPTGGPP PIFLPSDGQA LVLGRGPLTQ VTDRKCSRNQ VELIADPESR 

        70         80         90        100        110        120 
TVAVKQLGVN PSTVGVHELK PGLSGSLSLG DVLYLVNGLY PLTLRWEELS TSGSQPDAPP 

       130        140        150        160        170        180 
DTPGDPEEGE DTEPQKKRVR KSSLGWESLK KLLVFTASGV KPQGKVAAFD LDGTLITTRS 

       190        200        210        220        230        240 
GKVFPTSPSD WRILYPEIPK KLQELAAEGY KLVIFTNQMG IGRGKLPAEV FKGKVEAVLE 

       250        260        270        280        290        300 
KLGVPFQVLV ATHAGLNRKP VSGMWDHLQE QANEGIPISV EDSVFVGDAA GRLANWAPGR 

       310        320        330        340        350        360 
KKKDFSCADR LFALNVGLPF ATPEEFFLKW PAARFELPAF DPRTISSAGP LYLPESSSLL 

       370        380        390        400        410        420 
SPNPEVVVAV GFPGAGKSTF IQEHLVSAGY VHVNRDTLGS WQRCVSSCQA ALRQGKRVVI 

       430        440        450        460        470        480 
DNTNPDVPSR ARYIQCAKDA GVPCRCFNFC ATIEQARHNN RFREMTDPSH APVSDMVMFS 

       490        500        510        520 
YRKQFEPPTL AEGFLEILEI PFRLQEHLDP ALQRLYRQFS EG 

« Hide

Isoform 2.

Checksum: 6FE381B1531C953C
Show »

FASTA49554,373

References

« Hide 'large scale' references
[1]Beaulieu N., Lasko D.D.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Spleen.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Mammary tumor.
[3]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND THR-122, MASS SPECTROMETRY.
[4]"The forkhead-associated (FHA) domain-like structure from mouse polynucleotide kinase 3'-phosphatase."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-106.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF129451 mRNA. Translation: AAF36487.1.
BC057659 mRNA. Translation: AAH57659.1.
IPIIPI00124762.
IPI00454118.
UniGeneMm.238254

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJXNMR-A1-106[»]
1YJ5X-ray2.80A/B140-522[»]
C1-143[»]
1YJMX-ray2.20A/B/C1-110[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JLV6.

PTM databases

PhosphoSiteQ9JLV6.

Proteomic databases

PRIDEQ9JLV6.

Genome annotation databases

EnsemblENSMUST00000003044; ENSMUSP00000003044; ENSMUSG00000002963; Mus musculus. [Genome view]
ENSMUST00000085410; ENSMUSP00000082531; ENSMUSG00000002963; Mus musculus. [Genome view]
ENSMUST00000107876; ENSMUSP00000103508; ENSMUSG00000002963; Mus musculus. [Genome view]
UCSCuc009grf.1. mouse.

Organism-specific databases

MGIMGI:1891698. Pnkp.

Phylogenomic databases

HOGENOMHBG714111.
HOVERGENQ9JLV6.
InParanoidQ9JLV6.

Enzyme and pathway databases

BRENDA2.7.1.78. 244.
3.1.3.32. 244.

Gene expression databases

ArrayExpressQ9JLV6.
BgeeQ9JLV6.
CleanExMM_PNKP.
GenevestigatorQ9JLV6.
GermOnlineENSMUSG00000002963. Mus musculus.

Family and domain databases

InterProIPR006551. DNA-3-Pase.
IPR006549. HAD-SF_hydro_IIIA.
IPR006550. PNK-3Pase.
IPR015636. PNK_3Pase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERPTHR12083. PNK_3Pase. 1 hit.
TIGRFAMsTIGR01664. DNA-3_-Pase. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01663. PNK-3_Pase. 1 hit.
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry namePNKP_MOUSE
AccessionPrimary (citable) accession number: Q9JLV6
Secondary accession number(s): Q6PFA3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents