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Q9UGN5

- PARP2_HUMAN

UniProt

Q9UGN5 - PARP2_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UGN5.
CleanExiHS_PARP2.
ExpressionAtlasiQ9UGN5. baseline and differential.
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. 20 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 – 24510Combined sources
Helixi248 – 25710Combined sources
Turni262 – 2643Combined sources
Helixi267 – 2693Combined sources
Helixi272 – 29019Combined sources
Helixi296 – 30813Combined sources
Helixi324 – 34724Combined sources
Helixi357 – 3648Combined sources
Beta strandi367 – 3715Combined sources
Helixi377 – 38812Combined sources
Beta strandi398 – 40912Combined sources
Helixi412 – 4154Combined sources
Beta strandi423 – 4297Combined sources
Helixi432 – 4343Combined sources
Helixi435 – 4417Combined sources
Helixi452 – 4543Combined sources
Beta strandi459 – 4668Combined sources
Helixi467 – 4726Combined sources
Beta strandi478 – 4803Combined sources
Beta strandi482 – 49110Combined sources
Beta strandi494 – 5007Combined sources
Helixi505 – 5084Combined sources
Beta strandi514 – 5174Combined sources
Beta strandi519 – 5235Combined sources
Helixi525 – 5273Combined sources
Beta strandi529 – 5313Combined sources
Beta strandi534 – 5363Combined sources
Beta strandi541 – 5433Combined sources
Beta strandi549 – 5513Combined sources
Beta strandi554 – 5563Combined sources
Beta strandi558 – 5636Combined sources
Helixi564 – 5663Combined sources
Beta strandi567 – 57812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KCZX-ray2.00A/B235-579[»]
3KJDX-ray1.95A/B235-579[»]
4PJVX-ray2.50A/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.
GeneTreeiENSGT00390000017341.
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

        10         20         30         40         50
MAARRRRSTG GGRARALNES KRVNNGNTAP EDSSPAKKTR RCQRQESKKM
60 70 80 90 100
PVAGGKANKD RTEDKQDGMP GRSWASKRVS ESVKALLLKG KAPVDPECTA
110 120 130 140 150
KVGKAHVYCE GNDVYDVMLN QTNLQFNNNK YYLIQLLEDD AQRNFSVWMR
160 170 180 190 200
WGRVGKMGQH SLVACSGNLN KAKEIFQKKF LDKTKNNWED REKFEKVPGK
210 220 230 240 250
YDMLQMDYAT NTQDEEETKK EESLKSPLKP ESQLDLRVQE LIKLICNVQA
260 270 280 290 300
MEEMMMEMKY NTKKAPLGKL TVAQIKAGYQ SLKKIEDCIR AGQHGRALME
310 320 330 340 350
ACNEFYTRIP HDFGLRTPPL IRTQKELSEK IQLLEALGDI EIAIKLVKTE
360 370 380 390 400
LQSPEHPLDQ HYRNLHCALR PLDHESYEFK VISQYLQSTH APTHSDYTMT
410 420 430 440 450
LLDLFEVEKD GEKEAFREDL HNRMLLWHGS RMSNWVGILS HGLRIAPPEA
460 470 480 490 500
PITGYMFGKG IYFADMSSKS ANYCFASRLK NTGLLLLSEV ALGQCNELLE
510 520 530 540 550
ANPKAEGLLQ GKHSTKGLGK MAPSSAHFVT LNGSTVPLGP ASDTGILNPD
560 570 580
GYTLNYNEYI VYNPNQVRMR YLLKVQFNFL QLW
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. Curated
The sequence AAL77437.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB41505.2 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4PJV X-ray 2.50 A/B 235-579 [» ]
ProteinModelPortali Q9UGN5.
SMRi Q9UGN5. Positions 92-579.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115350. 20 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.
GeneTreei ENSGT00390000017341.
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

Bgeei Q9UGN5.
CleanExi HS_PARP2.
ExpressionAtlasi Q9UGN5. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 141 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