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)

Q9UGN5

- PARP2_HUMAN

UniProt

Q9UGN5 - PARP2_HUMAN

Protein

Poly [ADP-ribose] polymerase 2

Gene

PARP2

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 139 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks.

    Catalytic activityi

    NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi1 – 8888Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. NAD+ ADP-ribosyltransferase activity Source: UniProtKB-EC
    3. protein binding Source: IntAct

    GO - Biological processi

    1. base-excision repair Source: Ensembl
    2. DNA repair Source: ProtInc
    3. extrinsic apoptotic signaling pathway Source: Ensembl
    4. protein ADP-ribosylation Source: ProtInc

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    DNA-binding, NAD

    Enzyme and pathway databases

    BRENDAi2.4.2.30. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly [ADP-ribose] polymerase 2 (EC:2.4.2.30)
    Short name:
    PARP-2
    Short name:
    hPARP-2
    Alternative name(s):
    ADP-ribosyltransferase diphtheria toxin-like 2
    Short name:
    ARTD2
    NAD(+) ADP-ribosyltransferase 2
    Short name:
    ADPRT-2
    Poly[ADP-ribose] synthase 2
    Short name:
    pADPRT-2
    Gene namesi
    Name:PARP2
    Synonyms:ADPRT2, ADPRTL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:272. PARP2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleolus Source: HPA
    2. nucleoplasm Source: MGI
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24592.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 583583Poly [ADP-ribose] polymerase 2PRO_0000211327Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371N6-acetyllysineBy similarity
    Modified residuei38 – 381N6-acetyllysineBy similarity
    Modified residuei226 – 2261Phosphoserine1 Publication
    Modified residuei232 – 2321Phosphoserine1 Publication

    Post-translational modificationi

    Poly-ADP-ribosylated by PARP1.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UGN5.
    PaxDbiQ9UGN5.
    PRIDEiQ9UGN5.

    PTM databases

    PhosphoSiteiQ9UGN5.

    Expressioni

    Tissue specificityi

    Widely expressed, mainly in actively dividing tissues. The highest levels are in the brain, heart, pancreas, skeletal muscle and testis; also detected in kidney, liver, lung, placenta, ovary and spleen; levels are low in leukocytes, colon, small intestine, prostate and thymus.

    Gene expression databases

    ArrayExpressiQ9UGN5.
    BgeeiQ9UGN5.
    CleanExiHS_PARP2.
    GenevestigatoriQ9UGN5.

    Organism-specific databases

    HPAiHPA052003.

    Interactioni

    Subunit structurei

    Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LRIG3. Homo- and heterodimer with PARP1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FKBP3Q006882EBI-2795348,EBI-1044081
    STACQ994692EBI-2795348,EBI-2652799

    Protein-protein interaction databases

    BioGridi115350. 13 interactions.
    DIPiDIP-48934N.
    IntActiQ9UGN5. 53 interactions.
    MINTiMINT-7914677.
    STRINGi9606.ENSP00000250416.

    Structurei

    Secondary structure

    1
    583
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi236 – 24510
    Helixi248 – 25710
    Turni262 – 2643
    Helixi267 – 2693
    Helixi272 – 29019
    Helixi296 – 30813
    Helixi324 – 34724
    Helixi357 – 3648
    Beta strandi367 – 3715
    Helixi377 – 38812
    Beta strandi398 – 40912
    Helixi412 – 4154
    Beta strandi423 – 4297
    Helixi432 – 4343
    Helixi435 – 4417
    Helixi452 – 4543
    Beta strandi459 – 4668
    Helixi467 – 4726
    Beta strandi478 – 4803
    Beta strandi482 – 49110
    Beta strandi494 – 5007
    Helixi505 – 5084
    Beta strandi514 – 5174
    Beta strandi519 – 5235
    Helixi525 – 5273
    Beta strandi529 – 5313
    Beta strandi534 – 5363
    Beta strandi541 – 5433
    Beta strandi549 – 5513
    Beta strandi554 – 5563
    Beta strandi558 – 5636
    Helixi564 – 5663
    Beta strandi567 – 57812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KCZX-ray2.00A/B235-579[»]
    3KJDX-ray1.95A/B235-579[»]
    ProteinModelPortaliQ9UGN5.
    SMRiQ9UGN5. Positions 92-579.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UGN5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini231 – 348118PARP alpha-helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini356 – 583228PARP catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi4 – 74Nuclear localization signalSequence Analysis
    Motifi35 – 406Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
    Contains 1 PARP catalytic domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG243963.
    HOGENOMiHOG000173055.
    HOVERGENiHBG053514.
    InParanoidiQ9UGN5.
    KOiK10798.
    OMAiFTTIPHV.
    OrthoDBiEOG7KM5S0.
    PhylomeDBiQ9UGN5.
    TreeFamiTF315407.

    Family and domain databases

    Gene3Di1.20.142.10. 1 hit.
    2.20.140.10. 1 hit.
    3.90.228.10. 1 hit.
    InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR004102. Poly(ADP-ribose)pol_reg_dom.
    IPR008893. WGR_domain.
    [Graphical view]
    PfamiPF00644. PARP. 1 hit.
    PF02877. PARP_reg. 1 hit.
    PF05406. WGR. 1 hit.
    [Graphical view]
    SMARTiSM00773. WGR. 1 hit.
    [Graphical view]
    SUPFAMiSSF142921. SSF142921. 1 hit.
    SSF47587. SSF47587. 1 hit.
    PROSITEiPS51060. PARP_ALPHA_HD. 1 hit.
    PS51059. PARP_CATALYTIC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UGN5-1) [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

    MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM    50
    PVAGGKANKD RTEDKQDGMP GRSWASKRVS ESVKALLLKG KAPVDPECTA 100
    KVGKAHVYCE GNDVYDVMLN QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR 150
    WGRVGKMGQH SLVACSGNLN KAKEIFQKKF LDKTKNNWED REKFEKVPGK 200
    YDMLQMDYAT NTQDEEETKK EESLKSPLKP ESQLDLRVQE LIKLICNVQA 250
    MEEMMMEMKY NTKKAPLGKL TVAQIKAGYQ SLKKIEDCIR AGQHGRALME 300
    ACNEFYTRIP HDFGLRTPPL IRTQKELSEK IQLLEALGDI EIAIKLVKTE 350
    LQSPEHPLDQ HYRNLHCALR PLDHESYEFK VISQYLQSTH APTHSDYTMT 400
    LLDLFEVEKD GEKEAFREDL HNRMLLWHGS RMSNWVGILS HGLRIAPPEA 450
    PITGYMFGKG IYFADMSSKS ANYCFASRLK NTGLLLLSEV ALGQCNELLE 500
    ANPKAEGLLQ GKHSTKGLGK MAPSSAHFVT LNGSTVPLGP ASDTGILNPD 550
    GYTLNYNEYI VYNPNQVRMR YLLKVQFNFL QLW 583
    Length:583
    Mass (Da):66,206
    Last modified:September 26, 2001 - v2
    Checksum:i5B7AE8AE531836AF
    GO
    Isoform 2 (identifier: Q9UGN5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         68-80: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:570
    Mass (Da):64,805
    Checksum:i335A5B64E758FDFF
    GO

    Sequence cautioni

    The sequence AAD29857.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAB41505.2 differs from that shown. Reason: Erroneous initiation.
    The sequence AAL77437.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti447 – 4471P → H in AAD29857. (PubMed:10329013)Curated
    Sequence conflicti481 – 4811N → H in BAA92017. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti161 – 1611S → N.1 Publication
    Corresponds to variant rs3093905 [ dbSNP | Ensembl ].
    VAR_019174
    Natural varianti168 – 1681N → S.1 Publication
    Corresponds to variant rs3093906 [ dbSNP | Ensembl ].
    VAR_019175
    Natural varianti235 – 2351D → G.1 Publication
    Corresponds to variant rs3093921 [ dbSNP | Ensembl ].
    VAR_019176
    Natural varianti285 – 2851I → V.1 Publication
    Corresponds to variant rs3093925 [ dbSNP | Ensembl ].
    VAR_019177
    Natural varianti296 – 2961R → Q.1 Publication
    Corresponds to variant rs3093926 [ dbSNP | Ensembl ].
    VAR_019178
    Natural varianti331 – 3311I → T.
    Corresponds to variant rs2275010 [ dbSNP | Ensembl ].
    VAR_050462

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei68 – 8013Missing in isoform 2. 1 PublicationVSP_004537Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ236912 mRNA. Translation: CAB65088.1.
    AF085734 mRNA. Translation: AAD29857.1. Different initiation.
    AJ236876 mRNA. Translation: CAB41505.2. Different initiation.
    AK001980 mRNA. Translation: BAA92017.1. Different termination.
    AF479321 Genomic DNA. Translation: AAL77437.1. Sequence problems.
    CCDSiCCDS41910.1. [Q9UGN5-1]
    CCDS45077.1. [Q9UGN5-2]
    RefSeqiNP_001036083.1. NM_001042618.1. [Q9UGN5-2]
    NP_005475.2. NM_005484.3. [Q9UGN5-1]
    UniGeneiHs.409412.

    Genome annotation databases

    EnsembliENST00000250416; ENSP00000250416; ENSG00000129484. [Q9UGN5-1]
    ENST00000429687; ENSP00000392972; ENSG00000129484. [Q9UGN5-2]
    GeneIDi10038.
    KEGGihsa:10038.
    UCSCiuc001vxb.1. human. [Q9UGN5-1]
    uc001vxd.3. human. [Q9UGN5-2]

    Polymorphism databases

    DMDMi17380230.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ236912 mRNA. Translation: CAB65088.1 .
    AF085734 mRNA. Translation: AAD29857.1 . Different initiation.
    AJ236876 mRNA. Translation: CAB41505.2 . Different initiation.
    AK001980 mRNA. Translation: BAA92017.1 . Different termination.
    AF479321 Genomic DNA. Translation: AAL77437.1 . Sequence problems.
    CCDSi CCDS41910.1. [Q9UGN5-1 ]
    CCDS45077.1. [Q9UGN5-2 ]
    RefSeqi NP_001036083.1. NM_001042618.1. [Q9UGN5-2 ]
    NP_005475.2. NM_005484.3. [Q9UGN5-1 ]
    UniGenei Hs.409412.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KCZ X-ray 2.00 A/B 235-579 [» ]
    3KJD X-ray 1.95 A/B 235-579 [» ]
    ProteinModelPortali Q9UGN5.
    SMRi Q9UGN5. Positions 92-579.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115350. 13 interactions.
    DIPi DIP-48934N.
    IntActi Q9UGN5. 53 interactions.
    MINTi MINT-7914677.
    STRINGi 9606.ENSP00000250416.

    Chemistry

    BindingDBi Q9UGN5.
    ChEMBLi CHEMBL5366.
    GuidetoPHARMACOLOGYi 2772.

    PTM databases

    PhosphoSitei Q9UGN5.

    Polymorphism databases

    DMDMi 17380230.

    Proteomic databases

    MaxQBi Q9UGN5.
    PaxDbi Q9UGN5.
    PRIDEi Q9UGN5.

    Protocols and materials databases

    DNASUi 10038.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250416 ; ENSP00000250416 ; ENSG00000129484 . [Q9UGN5-1 ]
    ENST00000429687 ; ENSP00000392972 ; ENSG00000129484 . [Q9UGN5-2 ]
    GeneIDi 10038.
    KEGGi hsa:10038.
    UCSCi uc001vxb.1. human. [Q9UGN5-1 ]
    uc001vxd.3. human. [Q9UGN5-2 ]

    Organism-specific databases

    CTDi 10038.
    GeneCardsi GC14P020811.
    HGNCi HGNC:272. PARP2.
    HPAi HPA052003.
    MIMi 607725. gene.
    neXtProti NX_Q9UGN5.
    PharmGKBi PA24592.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG243963.
    HOGENOMi HOG000173055.
    HOVERGENi HBG053514.
    InParanoidi Q9UGN5.
    KOi K10798.
    OMAi FTTIPHV.
    OrthoDBi EOG7KM5S0.
    PhylomeDBi Q9UGN5.
    TreeFami TF315407.

    Enzyme and pathway databases

    BRENDAi 2.4.2.30. 2681.

    Miscellaneous databases

    ChiTaRSi PARP2. human.
    EvolutionaryTracei Q9UGN5.
    GeneWikii PARP2.
    GenomeRNAii 10038.
    NextBioi 37907.
    PROi Q9UGN5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UGN5.
    Bgeei Q9UGN5.
    CleanExi HS_PARP2.
    Genevestigatori Q9UGN5.

    Family and domain databases

    Gene3Di 1.20.142.10. 1 hit.
    2.20.140.10. 1 hit.
    3.90.228.10. 1 hit.
    InterProi IPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR004102. Poly(ADP-ribose)pol_reg_dom.
    IPR008893. WGR_domain.
    [Graphical view ]
    Pfami PF00644. PARP. 1 hit.
    PF02877. PARP_reg. 1 hit.
    PF05406. WGR. 1 hit.
    [Graphical view ]
    SMARTi SM00773. WGR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF142921. SSF142921. 1 hit.
    SSF47587. SSF47587. 1 hit.
    PROSITEi PS51060. PARP_ALPHA_HD. 1 hit.
    PS51059. PARP_CATALYTIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fetal brain.
    2. "A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues."
      Johansson M.
      Genomics 57:442-445(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-583 (ISOFORM 1).
      Tissue: Fetal brain.
    3. "pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans."
      Berghammer H., Ebner M., Marksteiner R., Auer B.
      FEBS Lett. 449:259-263(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-583 (ISOFORM 1).
      Tissue: Fibroblast.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Placenta.
    5. NIEHS SNPs program
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-161; SER-168; GLY-235; VAL-285 AND GLN-296.
    6. "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1."
      Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V., Menissier-de Murcia J., de Murcia G.M.
      J. Biol. Chem. 277:23028-23036(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARP1; XRCC1; POLB AND LRIG3.
    7. "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
      Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
      Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-226 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structure of the catalytic domain of human PARP2 in complex with PARP inhibitor ABT-888."
      Karlberg T., Hammarstrom M., Schutz P., Svensson L., Schuler H.
      Biochemistry 49:1056-1058(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 235-579 IN COMPLEX WITH PARP INHIBITORS, SUBUNIT.

    Entry informationi

    Entry nameiPARP2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UGN5
    Secondary accession number(s): Q8TEU4
    , Q9NUV2, Q9UMR4, Q9Y6C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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