Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96T60

- PNKP_HUMAN

UniProt

Q96T60 - PNKP_HUMAN

Protein

Bifunctional polynucleotide phosphatase/kinase

Gene

PNKP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

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

    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. membrane Source: UniProtKB
    2. nucleolus Source: HPA
    3. nucleus Source: UniProtKB

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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/kinasePRO_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 (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

    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

    1
    521
    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.
    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.
    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.

    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. 1 PublicationCurated

    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. 1 PublicationVSP_055500Add
    BLAST

    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. [Q96T60-1]
    ENST00000596014; ENSP00000472300; ENSG00000039650. [Q96T60-1]
    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 . [Q96T60-1 ]
    ENST00000596014 ; ENSP00000472300 ; ENSG00000039650 . [Q96T60-1 ]
    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

    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: October 1, 2014
    This is version 128 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