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Protein

Poly(ADP-ribose) polymerase pme-2

Gene

pme-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation, a post-translational modification synthesized after DNA damage that appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks and programmed cell death.

Catalytic activityi

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

GO - Molecular functioni

  • DNA ligase (ATP) activity Source: GO_Central
  • NAD+ ADP-ribosyltransferase activity Source: WormBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(ADP-ribose) polymerase pme-2 (EC:2.4.2.30)
Alternative name(s):
Poly ADP-ribose metabolism enzyme 2
Gene namesi
Name:pme-2
ORF Names:E02H1.4
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiE02H1.4; CE01539; WBGene00004050; pme-2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Poly(ADP-ribose) polymerase pme-2PRO_0000211336Add
BLAST

Proteomic databases

EPDiQ09525.
PaxDbiQ09525.

Expressioni

Developmental stagei

Predominantly expressed at early embryonic stages and later in L4 and adult stages.

Gene expression databases

BgeeiWBGene00004050.

Interactioni

Protein-protein interaction databases

IntActiQ09525. 1 interaction.
MINTiMINT-3386456.
STRINGi6239.E02H1.4.1.

Structurei

3D structure databases

ProteinModelPortaliQ09525.
SMRiQ09525. Positions 27-99, 150-531.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 285138PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini309 – 535227PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000016215.
InParanoidiQ09525.
KOiK10798.
OMAiACSGDLN.
OrthoDBiEOG091G0AWB.
PhylomeDBiQ09525.

Family and domain databases

Gene3Di1.20.142.10. 2 hits.
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]

Sequencei

Sequence statusi: Complete.

Q09525-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIINDENGR GYKVHLCKTN IAQNNNKFYD MELLDEGGDF IVKLINGRIG
60 70 80 90 100
YRGVTQLKDF DDLDRAKKFF ESKFYEKTHL HWEERDDEPV PNKYAVVELA
110 120 130 140 150
TNARQTEKEV KKEEPEPEPK VDEKNTRGRK KRGIVKEKKE IKKEEEPVEE
160 170 180 190 200
VNEKLKELMK CICDEDVHLG LLKQLKFNEA FGRPIDCLSL AQLTTGYEIL
210 220 230 240 250
SKIEESIGGK SARRSTRGRP RVADRVLAVK SDGPSLHDIN KYYSLIPHSF
260 270 280 290 300
GFCVPPKIDS HAKIQAEREL LDALKGSIEA SLELKDLKKT ASSKDIYQRL
310 320 330 340 350
YERLPCHLEP VSEEIAGKIG DCLAMRGPTH CYKLSLIDAF ELKDPNEIPT
360 370 380 390 400
EAPVEVQEVP KKRGRKSTKT AAPTVPPPTT KRLLWHGTRV TNVFSILMNG
410 420 430 440 450
LQFPVGDRCG LMFGNGVYFA NVPTKSANYC CPEASKRVFM LLCEVETANP
460 470 480 490 500
LVLYESEIDA DEKMEKAKKT SVYAAGKHTP RDTVEINGIP AFKSNLETIE
510 520 530
EETRLLYDEY VMFNKEHFKI KYVVEVKVDR LTAKEMMA
Length:538
Mass (Da):61,268
Last modified:February 1, 1996 - v1
Checksum:i3144E25465FC7341
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF500111 mRNA. Translation: AAM27196.1.
Z47075 Genomic DNA. Translation: CAA87379.1.
PIRiT20414.
RefSeqiNP_001022057.1. NM_001026886.3.
UniGeneiCel.18275.

Genome annotation databases

EnsemblMetazoaiE02H1.4; E02H1.4; WBGene00004050.
GeneIDi3565967.
KEGGicel:CELE_E02H1.4.
UCSCiE02H1.4. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF500111 mRNA. Translation: AAM27196.1.
Z47075 Genomic DNA. Translation: CAA87379.1.
PIRiT20414.
RefSeqiNP_001022057.1. NM_001026886.3.
UniGeneiCel.18275.

3D structure databases

ProteinModelPortaliQ09525.
SMRiQ09525. Positions 27-99, 150-531.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ09525. 1 interaction.
MINTiMINT-3386456.
STRINGi6239.E02H1.4.1.

Proteomic databases

EPDiQ09525.
PaxDbiQ09525.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiE02H1.4; E02H1.4; WBGene00004050.
GeneIDi3565967.
KEGGicel:CELE_E02H1.4.
UCSCiE02H1.4. c. elegans.

Organism-specific databases

CTDi3565967.
WormBaseiE02H1.4; CE01539; WBGene00004050; pme-2.

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000016215.
InParanoidiQ09525.
KOiK10798.
OMAiACSGDLN.
OrthoDBiEOG091G0AWB.
PhylomeDBiQ09525.

Miscellaneous databases

PROiQ09525.

Gene expression databases

BgeeiWBGene00004050.

Family and domain databases

Gene3Di1.20.142.10. 2 hits.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiPME2_CAEEL
AccessioniPrimary (citable) accession number: Q09525
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 7, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.