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Protein

Poly [ADP-ribose] polymerase

Gene

Parp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. Plays a fundamental role in organizing chromatin on a global scale; isoform e autoregulates Parp transcription by influencing the chromatin structure of its heterochromatic environment.1 Publication

Catalytic activityi

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi1 – 367Add BLAST367
Zinc fingeri7 – 89PARP-type 1PROSITE-ProRule annotationAdd BLAST83
Zinc fingeri111 – 200PARP-type 2PROSITE-ProRule annotationAdd BLAST90

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • DNA ligase (ATP) activity Source: GO_Central
  • histone binding Source: FlyBase
  • NAD+ ADP-ribosyltransferase activity Source: FlyBase
  • NAD binding Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • Cajal body organization Source: FlyBase
  • chromatin modification Source: UniProtKB-KW
  • chromosome organization Source: FlyBase
  • DNA ligation involved in DNA repair Source: GO_Central
  • dorsal/ventral axis specification, ovarian follicular epithelium Source: FlyBase
  • heat shock-mediated polytene chromosome puffing Source: FlyBase
  • innate immune response Source: FlyBase
  • lagging strand elongation Source: GO_Central
  • maintenance of protein location in nucleus Source: FlyBase
  • metamorphosis Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • nucleolus organization Source: FlyBase
  • polytene chromosome puffing Source: FlyBase
  • positive regulation of antibacterial peptide biosynthetic process Source: FlyBase
  • positive regulation of protein localization to nucleus Source: CACAO
  • protein ADP-ribosylation Source: FlyBase
  • regulation of RNA splicing Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • rRNA transcription Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Glycosyltransferase, Transferase

Keywords - Ligandi

DNA-binding, Metal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDAi2.4.2.30. 1994.
ReactomeiR-DME-110362. POLB-Dependent Long Patch Base Excision Repair.
R-DME-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-DME-3108214. SUMOylation of DNA damage response and repair proteins.
R-DME-5696394. DNA Damage Recognition in GG-NER.
R-DME-5696395. Formation of Incision Complex in GG-NER.
R-DME-5696400. Dual Incision in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase (EC:2.4.2.30)
Short name:
PARP
Alternative name(s):
NAD(+) ADP-ribosyltransferase
Short name:
ADPRT
Poly[ADP-ribose] synthase
Gene namesi
Name:Parp
ORF Names:CG40411
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010247. Parp.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication
  • Nucleusnucleolus 1 Publication

  • Note: Highly enriched in nucleoli, heterochromatic chromosomal regions, and diverse euchromatic sites in the cells of most embryonic and adult tissues.

GO - Cellular componenti

  • Cajal body Source: FlyBase
  • chromosome Source: FlyBase
  • cytoplasm Source: GO_Central
  • histone locus body Source: FlyBase
  • nuclear euchromatin Source: FlyBase
  • nucleolus Source: FlyBase
  • polytene chromosome Source: FlyBase
  • polytene chromosome puff Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002113251 – 994Poly [ADP-ribose] polymeraseAdd BLAST994

Keywords - PTMi

ADP-ribosylation

Proteomic databases

PaxDbiP35875.
PRIDEiP35875.

Expressioni

Tissue specificityi

Expressed in adult female oocytes, anal plates of stage 12 embryos and in cells around the central nervous system in later embryos.1 Publication

Developmental stagei

Expressed both maternally and zygotically in embryos, pupae and adults. Expression is highest in embryos.2 Publications

Gene expression databases

BgeeiFBgn0010247.

Interactioni

GO - Molecular functioni

  • histone binding Source: FlyBase

Protein-protein interaction databases

BioGridi78234. 35 interactors.
DIPiDIP-23413N.
IntActiP35875. 1 interactor.
MINTiMINT-836001.
STRINGi7227.FBpp0112608.

Structurei

3D structure databases

ProteinModelPortaliP35875.
SMRiP35875.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini380 – 471BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini644 – 761PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini770 – 994PARP catalyticPROSITE-ProRule annotationAdd BLAST225

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni368 – 507Automodification domainAdd BLAST140

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi208 – 210Nuclear localization signal3
Motifi223 – 228Nuclear localization signal6

Sequence similaritiesi

Contains 1 BRCT domain.PROSITE-ProRule annotation
Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 2 PARP-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri7 – 89PARP-type 1PROSITE-ProRule annotationAdd BLAST83
Zinc fingeri111 – 200PARP-type 2PROSITE-ProRule annotationAdd BLAST90

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
InParanoidiP35875.
KOiK10798.
OMAiTHASTHK.
OrthoDBiEOG091G13H1.
PhylomeDBiP35875.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.30.1740.10. 2 hits.
3.40.50.10190. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR012982. PADR1.
IPR008288. PARP.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
PF00645. zf-PARP. 2 hits.
[Graphical view]
PIRSFiPIRSF000489. NAD_ADPRT. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM01335. PADR1. 1 hit.
SM00773. WGR. 1 hit.
SM01336. zf-PARP. 2 hits.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS00347. PARP_ZN_FINGER_1. 1 hit.
PS50064. PARP_ZN_FINGER_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform II (identifier: P35875-1) [UniParc]FASTAAdd to basket
Also known as: B, Long

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
MDIELPYLAE YARTGRATCK GCKSTISKDT LRIAVMVQSA FHDAKVPNWF
60 70 80 90 100
HKTCFFKNQR PSSVGDIQNI GNLRFADQKE LTDLVENIQE VISAQLGKKR
110 120 130 140 150
SKAFNLALKD FGIEYAKSSR STCRGCEQKI NKDLVRLRKT VYDTEVGMKY
160 170 180 190 200
GGQPLWHHLE CFAQLRSELG WFASGEDMPG FQSLADDDQA KVKNAIPPIK
210 220 230 240 250
SEELPDTKRA KMELSDTNEE GEKKQRLKDQ NDAYFRFRDD IKNKMKKKDI
260 270 280 290 300
DILLKFNNQQ PVTGDTEKLF DQTADLLTFG AIESCSECNS CQFIVNKSGY
310 320 330 340 350
ICNGNHSEWT KCNKLLKEPT RSACIVPKEL KALYNFLNTV KEIPSTRIFN
360 370 380 390 400
NFPPNKSTFS RSLLKTNKNN DVLVRPTIPR ISPPLYNLKF SIIGLKNQHK
410 420 430 440 450
ELRKRIENLG GKFEVKISEN TIAIISTELE IQKKSTRMKF AEELGIHIVP
460 470 480 490 500
IEFLDFVEAD TEGAIKYINS TCICSWGTDP KSRIPKETTK SLNSNSIYTK
510 520 530 540 550
SMPVSRTFKV KDGLAVDPDS GLEDIAHVYV DSNNKYSVVL GLTDIQRNKN
560 570 580 590 600
SYYKVQLLKA DKKEKYWIFR SWGRIGTNIG NSKLEEFDTS ESAKRNFKEI
610 620 630 640 650
YADKTGNEYE QRDNFVKRTG RMYPIEIQYD DDQKLVKHES HFFTSKLEIS
660 670 680 690 700
VQNLIKLIFD IDSMNKTLME FHIDMDKMPL GKLSAHQIQS AYRVVKEIYN
710 720 730 740 750
VLECGSNTAK LIDATNRFYT LIPHNFGVQL PTLIETHQQI EDLRQMLDSL
760 770 780 790 800
AEIEVAYSII KSEDVSDACN PLDNHYAQIK TQLVALDKNS EEFSILSQYV
810 820 830 840 850
KNTHASTHKS YDLKIVDVFK VSRQGEARRF KPFKKLHNRK LLWHGSRLTN
860 870 880 890 900
FVGILSHGLR IAPPEAPPTG YMFGKGIYFA DMVSKSANYC CTSQQNSTGL
910 920 930 940 950
MLLSEVALGD MMECTSAKYI NKLSNNKHSC FGRGRTMPDP TKSYIRSDGV
960 970 980 990
EIPYGETITD EHLKSSLLYN EYIVYDVAQV NIQYLFRMEF KYSY
Length:994
Mass (Da):113,792
Last modified:June 1, 1994 - v1
Checksum:iACA85A270DD29E08
GO
Isoform I (identifier: P35875-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     376-565: Missing.

Show »
Length:804
Mass (Da):92,303
Checksum:i52719FF12193871F
GO
Isoform E (identifier: P35875-3) [UniParc]FASTAAdd to basket
Also known as: Embryonic

The sequence of this isoform differs from the canonical sequence as follows:
     607-613: NEYEQRD → MHFSEIH
     614-994: Missing.

Show »
Length:613
Mass (Da):69,956
Checksum:iB82605E1E3804868
GO

Sequence cautioni

The sequence AAM50807 differs from that shown. Reason: Erroneous initiation.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004536376 – 565Missing in isoform I. CuratedAdd BLAST190
Alternative sequenceiVSP_013203607 – 613NEYEQRD → MHFSEIH in isoform E. 1 Publication7
Alternative sequenceiVSP_013204614 – 994Missing in isoform E. 1 PublicationAdd BLAST381

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13806 mRNA. Translation: BAA02964.1.
AF051548
, AF051544, AF051545, AF051546, AF051547 Genomic DNA. Translation: AAC24518.1.
AF533701 mRNA. Translation: AAM93435.1.
AE014297 Genomic DNA. Translation: EDP28045.1.
BT015238 mRNA. Translation: AAT94467.1.
AY118947 mRNA. Translation: AAM50807.1. Different initiation.
PIRiA47474.
RefSeqiNP_001104452.1. NM_001110982.3. [P35875-1]
UniGeneiDm.7847.

Genome annotation databases

EnsemblMetazoaiFBtr0113885; FBpp0112608; FBgn0010247. [P35875-1]
GeneIDi3355109.
KEGGidme:Dmel_CG40411.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13806 mRNA. Translation: BAA02964.1.
AF051548
, AF051544, AF051545, AF051546, AF051547 Genomic DNA. Translation: AAC24518.1.
AF533701 mRNA. Translation: AAM93435.1.
AE014297 Genomic DNA. Translation: EDP28045.1.
BT015238 mRNA. Translation: AAT94467.1.
AY118947 mRNA. Translation: AAM50807.1. Different initiation.
PIRiA47474.
RefSeqiNP_001104452.1. NM_001110982.3. [P35875-1]
UniGeneiDm.7847.

3D structure databases

ProteinModelPortaliP35875.
SMRiP35875.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi78234. 35 interactors.
DIPiDIP-23413N.
IntActiP35875. 1 interactor.
MINTiMINT-836001.
STRINGi7227.FBpp0112608.

Proteomic databases

PaxDbiP35875.
PRIDEiP35875.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0113885; FBpp0112608; FBgn0010247. [P35875-1]
GeneIDi3355109.
KEGGidme:Dmel_CG40411.

Organism-specific databases

CTDi3355109.
FlyBaseiFBgn0010247. Parp.

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
InParanoidiP35875.
KOiK10798.
OMAiTHASTHK.
OrthoDBiEOG091G13H1.
PhylomeDBiP35875.

Enzyme and pathway databases

BRENDAi2.4.2.30. 1994.
ReactomeiR-DME-110362. POLB-Dependent Long Patch Base Excision Repair.
R-DME-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-DME-3108214. SUMOylation of DNA damage response and repair proteins.
R-DME-5696394. DNA Damage Recognition in GG-NER.
R-DME-5696395. Formation of Incision Complex in GG-NER.
R-DME-5696400. Dual Incision in GG-NER.

Miscellaneous databases

GenomeRNAii3355109.
PROiP35875.

Gene expression databases

BgeeiFBgn0010247.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.30.1740.10. 2 hits.
3.40.50.10190. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR012982. PADR1.
IPR008288. PARP.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
PF00645. zf-PARP. 2 hits.
[Graphical view]
PIRSFiPIRSF000489. NAD_ADPRT. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM01335. PADR1. 1 hit.
SM00773. WGR. 1 hit.
SM01336. zf-PARP. 2 hits.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS00347. PARP_ZN_FINGER_1. 1 hit.
PS50064. PARP_ZN_FINGER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPARP_DROME
AccessioniPrimary (citable) accession number: P35875
Secondary accession number(s): A8Y590
, Q7PLT6, Q8MSB5, Q8MU87, Q9W5Q5, Q9W5S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.