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Q96T60

- PNKP_HUMAN

UniProt

Q96T60 - PNKP_HUMAN

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Protein
Bifunctional polynucleotide phosphatase/kinase
Gene
PNKP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

A 3'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.
ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi372 – 3798ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity Source: UniProtKB
  3. damaged DNA binding Source: UniProtKB
  4. double-stranded DNA binding Source: UniProtKB
  5. endonuclease activity Source: UniProtKB
  6. nucleotide kinase activity Source: UniProtKB
  7. polynucleotide 3'-phosphatase activity Source: UniProtKB
  8. protein binding Source: IntAct
  9. purine nucleotide binding Source: UniProtKB

GO - Biological processi

  1. DNA damage response, detection of DNA damage Source: UniProtKB
  2. DNA repair Source: UniProtKB
  3. DNA-dependent DNA replication Source: UniProtKB
  4. dephosphorylation Source: UniProtKB
  5. nucleic acid phosphodiester bond hydrolysis Source: GOC
  6. nucleotide phosphorylation Source: UniProtKB
  7. nucleotide-excision repair, DNA damage removal Source: UniProtKB
  8. polynucleotide 3' dephosphorylation Source: GOC
  9. response to oxidative stress Source: UniProtKB
  10. response to radiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional polynucleotide phosphatase/kinase
Alternative name(s):
DNA 5'-kinase/3'-phosphatase
Polynucleotide kinase-3'-phosphatase
Including the following 2 domains:
Polynucleotide 3'-phosphatase (EC:3.1.3.32)
Alternative name(s):
2'(3')-polynucleotidase
Polynucleotide 5'-hydroxyl-kinase (EC:2.7.1.78)
Gene namesi
Name:PNKP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9154. PNKP.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleolus Source: HPA
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Epileptic encephalopathy, early infantile, 10 (EIEE10) [MIM:613402]: A disease characterized by infantile-onset seizures, microcephaly, severe intellectual disability and delayed motor milestones with absent speech or only achieving a few words. Most patients also have behavioral problems with hyperactivity. Microcephaly is progressive and without neuronal migration or structural abnormalities, consistent with primary microcephaly.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761L → F in EIEE10. 1 Publication
VAR_063835
Natural varianti326 – 3261E → K in EIEE10. 1 Publication
VAR_063836

Keywords - Diseasei

Disease mutation, Mental retardation, Primary microcephaly

Organism-specific databases

MIMi613402. phenotype.
Orphaneti228418. Microcephaly - seizures - developmental delay.
PharmGKBiPA33477.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Bifunctional polynucleotide phosphatase/kinase
PRO_0000058478Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei114 – 1141Phosphoserine1 Publication
Modified residuei118 – 1181Phosphothreonine4 Publications
Modified residuei122 – 1221Phosphothreonine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96T60.
PaxDbiQ96T60.
PRIDEiQ96T60.

PTM databases

PhosphoSiteiQ96T60.

Expressioni

Tissue specificityi

Expressed in many tissues with highest expression in spleen and testis, and lowest expression in small intestine (1 Publication). Expressed in higher amount in pancreas, heart and kidney and at lower levels in brain, lung and liver (1 Publication).2 Publications

Gene expression databases

ArrayExpressiQ96T60.
BgeeiQ96T60.
CleanExiHS_PNKP.
GenevestigatoriQ96T60.

Organism-specific databases

HPAiHPA006782.

Interactioni

Subunit structurei

Monomer By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
XRCC1P188875EBI-1045072,EBI-947466
XRCC4Q134263EBI-1045072,EBI-717592

Protein-protein interaction databases

BioGridi116440. 52 interactions.
IntActiQ96T60. 12 interactions.
MINTiMINT-1199136.
STRINGi9606.ENSP00000323511.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135
Beta strandi31 – 333
Turni37 – 404
Beta strandi51 – 566
Turni57 – 604
Beta strandi61 – 666
Beta strandi68 – 703
Beta strandi84 – 885
Beta strandi92 – 965
Beta strandi99 – 1079

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BRFX-ray1.40A1-110[»]
2W3OX-ray1.85A/B1-110[»]
ProteinModelPortaliQ96T60.
SMRiQ96T60. Positions 8-108, 146-521.

Miscellaneous databases

EvolutionaryTraceiQ96T60.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 110105FHA
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni146 – 337192Phosphatase By similarity
Add
BLAST
Regioni341 – 516176Kinase By similarity
Add
BLAST

Domaini

The FHA domain binds threonine-phosphorylated peptides from XRCC1/4, and is responsible for the recruitment of PNKP to the sites of DNA repair. The affinity is ten times greater if peptides are also phosphorylated on the serine preceeding the phosphothreonine.1 Publication

Sequence similaritiesi

In the N-terminal section; belongs to the DNA 3' phosphatase family.
Contains 1 FHA domain.

Phylogenomic databases

eggNOGiCOG0241.
HOGENOMiHOG000031466.
HOVERGENiHBG053624.
InParanoidiQ96T60.
KOiK08073.
OMAiDIYRKPR.
OrthoDBiEOG7HQN87.
PhylomeDBiQ96T60.
TreeFamiTF313738.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.40.50.1000. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR000253. FHA_dom.
IPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR027417. P-loop_NTPase.
IPR013954. PNK3P.
IPR006550. PNK_3Pase_met.
IPR006551. Polynucleotide_phosphatase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF08645. PNK3P. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01664. DNA-3'-Pase. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01663. PNK-3'Pase. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96T60-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGEVEAPGRL WLESPPGGAP PIFLPSDGQA LVLGRGPLTQ VTDRKCSRTQ    50
VELVADPETR TVAVKQLGVN PSTTGTQELK PGLEGSLGVG DTLYLVNGLH 100
PLTLRWEETR TPESQPDTPP GTPLVSQDEK RDAELPKKRM RKSNPGWENL 150
EKLLVFTAAG VKPQGKVAGF DLDGTLITTR SGKVFPTGPS DWRILYPEIP 200
RKLRELEAEG YKLVIFTNQM SIGRGKLPAE EFKAKVEAVV EKLGVPFQVL 250
VATHAGLYRK PVTGMWDHLQ EQANDGTPIS IGDSIFVGDA AGRPANWAPG 300
RKKKDFSCAD RLFALNLGLP FATPEEFFLK WPAAGFELPA FDPRTVSRSG 350
PLCLPESRAL LSASPEVVVA VGFPGAGKST FLKKHLVSAG YVHVNRDTLG 400
SWQRCVTTCE TALKQGKRVA IDNTNPDAAS RARYVQCARA AGVPCRCFLF 450
TATLEQARHN NRFREMTDSS HIPVSDMVMY GYRKQFEAPT LAEGFSAILE 500
IPFRLWVEPR LGRLYCQFSE G 521
Length:521
Mass (Da):57,076
Last modified:December 1, 2001 - v1
Checksum:i22B5C94D41E62516
GO
Isoform 2 (identifier: Q96T60-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQ → MQILTPPLQSS

Note: No experimental confirmation available.

Show »
Length:482
Mass (Da):53,004
Checksum:iD079EBCC7DAD8402
GO

Sequence cautioni

The sequence AAD47379.1 differs from that shown. Reason: Frameshift at several positions.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201P → S.1 Publication
Corresponds to variant rs3739168 [ dbSNP | Ensembl ].
VAR_019260
Natural varianti63 – 631A → V.1 Publication
Corresponds to variant rs3739173 [ dbSNP | Ensembl ].
VAR_019261
Natural varianti176 – 1761L → F in EIEE10. 1 Publication
VAR_063835
Natural varianti180 – 1801R → S.1 Publication
Corresponds to variant rs3739185 [ dbSNP | Ensembl ].
VAR_019262
Natural varianti196 – 1961Y → N.1 Publication
Corresponds to variant rs3739186 [ dbSNP | Ensembl ].
VAR_019263
Natural varianti326 – 3261E → K in EIEE10. 1 Publication
VAR_063836
Natural varianti478 – 4781V → G.1 Publication
Corresponds to variant rs3739206 [ dbSNP | Ensembl ].
VAR_019264

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050MGEVE…CSRTQ → MQILTPPLQSS in isoform 2.
VSP_055500Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61A → P in AAD50639. 1 Publication
Sequence conflicti18 – 181G → E in AAD51135. 1 Publication
Sequence conflicti458 – 4581R → C in AAD47379. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF126486 mRNA. Translation: AAD51135.1.
AF125807 mRNA. Translation: AAD50639.1.
AF120499 mRNA. Translation: AAD47379.1. Frameshift.
AF354258 Genomic DNA. Translation: AAK57340.1.
AY133033 Genomic DNA. Translation: AAM82170.1.
AC018766 Genomic DNA. Translation: AAF44716.1.
BC002519 mRNA. Translation: AAH02519.2.
BC033822 mRNA. Translation: AAH33822.1.
CCDSiCCDS12783.1.
RefSeqiNP_009185.2. NM_007254.3.
UniGeneiHs.78016.

Genome annotation databases

EnsembliENST00000322344; ENSP00000323511; ENSG00000039650.
ENST00000596014; ENSP00000472300; ENSG00000039650.
GeneIDi11284.
KEGGihsa:11284.
UCSCiuc002pqg.3. human.

Polymorphism databases

DMDMi50401132.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF126486 mRNA. Translation: AAD51135.1 .
AF125807 mRNA. Translation: AAD50639.1 .
AF120499 mRNA. Translation: AAD47379.1 . Frameshift.
AF354258 Genomic DNA. Translation: AAK57340.1 .
AY133033 Genomic DNA. Translation: AAM82170.1 .
AC018766 Genomic DNA. Translation: AAF44716.1 .
BC002519 mRNA. Translation: AAH02519.2 .
BC033822 mRNA. Translation: AAH33822.1 .
CCDSi CCDS12783.1.
RefSeqi NP_009185.2. NM_007254.3.
UniGenei Hs.78016.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BRF X-ray 1.40 A 1-110 [» ]
2W3O X-ray 1.85 A/B 1-110 [» ]
ProteinModelPortali Q96T60.
SMRi Q96T60. Positions 8-108, 146-521.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116440. 52 interactions.
IntActi Q96T60. 12 interactions.
MINTi MINT-1199136.
STRINGi 9606.ENSP00000323511.

PTM databases

PhosphoSitei Q96T60.

Polymorphism databases

DMDMi 50401132.

Proteomic databases

MaxQBi Q96T60.
PaxDbi Q96T60.
PRIDEi Q96T60.

Protocols and materials databases

DNASUi 11284.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322344 ; ENSP00000323511 ; ENSG00000039650 .
ENST00000596014 ; ENSP00000472300 ; ENSG00000039650 .
GeneIDi 11284.
KEGGi hsa:11284.
UCSCi uc002pqg.3. human.

Organism-specific databases

CTDi 11284.
GeneCardsi GC19M050364.
HGNCi HGNC:9154. PNKP.
HPAi HPA006782.
MIMi 605610. gene.
613402. phenotype.
neXtProti NX_Q96T60.
Orphaneti 228418. Microcephaly - seizures - developmental delay.
PharmGKBi PA33477.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0241.
HOGENOMi HOG000031466.
HOVERGENi HBG053624.
InParanoidi Q96T60.
KOi K08073.
OMAi DIYRKPR.
OrthoDBi EOG7HQN87.
PhylomeDBi Q96T60.
TreeFami TF313738.

Miscellaneous databases

EvolutionaryTracei Q96T60.
GeneWikii PNKP.
GenomeRNAii 11284.
NextBioi 42959.
PROi Q96T60.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96T60.
Bgeei Q96T60.
CleanExi HS_PNKP.
Genevestigatori Q96T60.

Family and domain databases

Gene3Di 2.60.200.20. 1 hit.
3.40.50.1000. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR000253. FHA_dom.
IPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR027417. P-loop_NTPase.
IPR013954. PNK3P.
IPR006550. PNK_3Pase_met.
IPR006551. Polynucleotide_phosphatase.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
Pfami PF08645. PNK3P. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01664. DNA-3'-Pase. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01663. PNK-3'Pase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Jilani A., Ramotar D., Slack C., Ong C., Yang X.M., Scherer S.W., Lasko D.D.
    J. Biol. Chem. 274:24176-24186(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHARACTERIZATION.
  3. "Cloning a cDNA which is differently expressed in malignancies."
    Yang H.W., Piao H.Y., Chen Y.Z., Hayashi Y.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Genomic organization, physical mapping and expression analysis of the human polynucleotide kinase-3'-phosphatase (PNKP) gene."
    Scorilas A., Katsaros N.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. NIEHS SNPs program
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-20; VAL-63; SER-180; ASN-196 AND GLY-478.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., 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.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., 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 S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., 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 T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Blood and Ovary.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND THR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK."
    Ali A.A., Jukes R.M., Pearl L.H., Oliver A.W.
    Nucleic Acids Res. 37:1701-1712(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-110 ALONE AND IN COMPLEX WITH XRCC1 PHOSPHOPEPTIDE, DOMAIN FHA.
  17. Cited for: VARIANTS EIEE10 PHE-176 AND LYS-326.

Entry informationi

Entry nameiPNKP_HUMAN
AccessioniPrimary (citable) accession number: Q96T60
Secondary accession number(s): Q9BUL2
, Q9P1V2, Q9UKU8, Q9UNF8, Q9UNI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 1, 2001
Last modified: September 3, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi