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Protein

Bifunctional polynucleotide phosphatase/kinase

Gene

PNKP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 3798ATPSequence Analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity Source: UniProtKB
  • damaged DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • endonuclease activity Source: UniProtKB
  • nucleotide kinase activity Source: UniProtKB
  • polynucleotide 3'-phosphatase activity Source: UniProtKB
  • purine nucleotide binding Source: UniProtKB

GO - Biological processi

  • base-excision repair Source: Reactome
  • dephosphorylation Source: UniProtKB
  • DNA 3' dephosphorylation involved in DNA repair Source: GO_Central
  • DNA damage response, detection of DNA damage Source: UniProtKB
  • DNA-dependent DNA replication Source: UniProtKB
  • DNA repair Source: UniProtKB
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • nucleotide-excision repair, DNA damage removal Source: UniProtKB
  • nucleotide phosphorylation Source: UniProtKB
  • polynucleotide 3' dephosphorylation Source: GOC
  • response to oxidative stress Source: UniProtKB
  • 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

Enzyme and pathway databases

BRENDAi2.7.1.78. 2681.
3.1.3.32. 2681.
ReactomeiREACT_355367. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.

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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9154. PNKP.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Microcephaly, seizures, and developmental delay (MCSZ)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613402
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761L → F in MCSZ. 1 Publication
VAR_063835
Natural varianti326 – 3261E → K in MCSZ. 1 Publication
VAR_063836
Ataxia-oculomotor apraxia 4 (AOA4)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive disease characterized by cerebellar ataxia, oculomotor apraxia, areflexia and peripheral neuropathy.

See also OMIM:616267
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti375 – 3751G → W in AOA4. 1 Publication
VAR_073369
Natural varianti408 – 4081Missing in AOA4. 1 Publication
VAR_073370

Keywords - Diseasei

Disease mutation, Epilepsy, Mental retardation, Neurodegeneration, Primary microcephaly

Organism-specific databases

MIMi613402. phenotype.
616267. phenotype.
Orphaneti1934. Early infantile epileptic encephalopathy.
PharmGKBiPA33477.

Polymorphism and mutation databases

BioMutaiPNKP.
DMDMi50401132.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Bifunctional polynucleotide phosphatase/kinasePRO_0000058478Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei114 – 1141Phosphoserine1 Publication
Modified residuei118 – 1181Phosphothreonine5 Publications
Modified residuei122 – 1221Phosphothreonine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96T60.
PaxDbiQ96T60.
PRIDEiQ96T60.

PTM databases

DEPODiQ96T60.
PhosphoSiteiQ96T60.

Expressioni

Tissue specificityi

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).2 Publications

Gene expression databases

BgeeiQ96T60.
CleanExiHS_PNKP.
ExpressionAtlasiQ96T60. baseline and differential.
GenevisibleiQ96T60. HS.

Organism-specific databases

HPAiHPA006782.

Interactioni

Subunit structurei

Monomer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
IKZF1Q134223EBI-1045072,EBI-745305
TNIP1Q150253EBI-1045072,EBI-357849
XRCC1P188875EBI-1045072,EBI-947466
XRCC4Q134263EBI-1045072,EBI-717592
ZBTB14O438293EBI-1045072,EBI-10176632
ZNF639Q9UID63EBI-1045072,EBI-947476

Protein-protein interaction databases

BioGridi116440. 57 interactions.
IntActiQ96T60. 16 interactions.
MINTiMINT-1199136.
STRINGi9606.ENSP00000323511.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135Combined sources
Beta strandi31 – 333Combined sources
Turni37 – 404Combined sources
Beta strandi51 – 566Combined sources
Turni57 – 604Combined sources
Beta strandi61 – 666Combined sources
Beta strandi68 – 703Combined sources
Beta strandi84 – 885Combined sources
Beta strandi92 – 965Combined sources
Beta strandi99 – 1079Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ96T60.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni146 – 337192PhosphataseBy similarityAdd
BLAST
Regioni341 – 516176KinaseBy similarityAdd
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.Curated
Contains 1 FHA domain.Curated

Phylogenomic databases

eggNOGiCOG0241.
GeneTreeiENSGT00570000079163.
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. AlignAdd to basket

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

        10         20         30         40         50
MGEVEAPGRL WLESPPGGAP PIFLPSDGQA LVLGRGPLTQ VTDRKCSRTQ
60 70 80 90 100
VELVADPETR TVAVKQLGVN PSTTGTQELK PGLEGSLGVG DTLYLVNGLH
110 120 130 140 150
PLTLRWEETR TPESQPDTPP GTPLVSQDEK RDAELPKKRM RKSNPGWENL
160 170 180 190 200
EKLLVFTAAG VKPQGKVAGF DLDGTLITTR SGKVFPTGPS DWRILYPEIP
210 220 230 240 250
RKLRELEAEG YKLVIFTNQM SIGRGKLPAE EFKAKVEAVV EKLGVPFQVL
260 270 280 290 300
VATHAGLYRK PVTGMWDHLQ EQANDGTPIS IGDSIFVGDA AGRPANWAPG
310 320 330 340 350
RKKKDFSCAD RLFALNLGLP FATPEEFFLK WPAAGFELPA FDPRTVSRSG
360 370 380 390 400
PLCLPESRAL LSASPEVVVA VGFPGAGKST FLKKHLVSAG YVHVNRDTLG
410 420 430 440 450
SWQRCVTTCE TALKQGKRVA IDNTNPDAAS RARYVQCARA AGVPCRCFLF
460 470 480 490 500
TATLEQARHN NRFREMTDSS HIPVSDMVMY GYRKQFEAPT LAEGFSAILE
510 520
IPFRLWVEPR LGRLYCQFSE G
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61A → P in AAD50639 (PubMed:10446193).Curated
Sequence conflicti18 – 181G → E in AAD51135 (PubMed:10446192).Curated
Sequence conflicti458 – 4581R → C in AAD47379 (Ref. 3) Curated

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 MCSZ. 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 MCSZ. 1 Publication
VAR_063836
Natural varianti375 – 3751G → W in AOA4. 1 Publication
VAR_073369
Natural varianti408 – 4081Missing in AOA4. 1 Publication
VAR_073370
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. 1 PublicationVSP_055500Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q96T60-1]
RefSeqiNP_009185.2. NM_007254.3. [Q96T60-1]
UniGeneiHs.78016.

Genome annotation databases

EnsembliENST00000322344; ENSP00000323511; ENSG00000039650. [Q96T60-1]
ENST00000596014; ENSP00000472300; ENSG00000039650. [Q96T60-1]
GeneIDi11284.
KEGGihsa:11284.
UCSCiuc002pqg.3. human. [Q96T60-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q96T60-1]
RefSeqiNP_009185.2. NM_007254.3. [Q96T60-1]
UniGeneiHs.78016.

3D structure databases

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

Protein-protein interaction databases

BioGridi116440. 57 interactions.
IntActiQ96T60. 16 interactions.
MINTiMINT-1199136.
STRINGi9606.ENSP00000323511.

PTM databases

DEPODiQ96T60.
PhosphoSiteiQ96T60.

Polymorphism and mutation databases

BioMutaiPNKP.
DMDMi50401132.

Proteomic databases

MaxQBiQ96T60.
PaxDbiQ96T60.
PRIDEiQ96T60.

Protocols and materials databases

DNASUi11284.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322344; ENSP00000323511; ENSG00000039650. [Q96T60-1]
ENST00000596014; ENSP00000472300; ENSG00000039650. [Q96T60-1]
GeneIDi11284.
KEGGihsa:11284.
UCSCiuc002pqg.3. human. [Q96T60-1]

Organism-specific databases

CTDi11284.
GeneCardsiGC19M050364.
HGNCiHGNC:9154. PNKP.
HPAiHPA006782.
MIMi605610. gene.
613402. phenotype.
616267. phenotype.
neXtProtiNX_Q96T60.
Orphaneti1934. Early infantile epileptic encephalopathy.
PharmGKBiPA33477.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0241.
GeneTreeiENSGT00570000079163.
HOGENOMiHOG000031466.
HOVERGENiHBG053624.
InParanoidiQ96T60.
KOiK08073.
OMAiDIYRKPR.
OrthoDBiEOG7HQN87.
PhylomeDBiQ96T60.
TreeFamiTF313738.

Enzyme and pathway databases

BRENDAi2.7.1.78. 2681.
3.1.3.32. 2681.
ReactomeiREACT_355367. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.

Miscellaneous databases

EvolutionaryTraceiQ96T60.
GeneWikiiPNKP.
GenomeRNAii11284.
NextBioi42959.
PROiQ96T60.
SOURCEiSearch...

Gene expression databases

BgeeiQ96T60.
CleanExiHS_PNKP.
ExpressionAtlasiQ96T60. baseline and differential.
GenevisibleiQ96T60. HS.

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.
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: INVOLVEMENT IN AOA4, VARIANTS AOA4 TRP-375 AND THR-408 DEL.
  18. "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.
  19. Cited for: VARIANTS MCSZ 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: June 24, 2015
This is version 137 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.