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Protein

Poly [ADP-ribose] polymerase 1

Gene

parp1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -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. Involved in the synthesis of ATP in the nucleus. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.By similarity

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.

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 bindingi‹1 – 356Add BLAST›356
Zinc fingeri‹1 – 78PARP-type 1PROSITE-ProRule annotationAdd BLAST›78
Zinc fingeri99 – 189PARP-type 2PROSITE-ProRule annotationAdd BLAST91

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Glycosyltransferase, Transferase
LigandMetal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 1 (EC:2.4.2.30)
Short name:
PARP-1
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 1
Short name:
ARTD1
NAD(+) ADP-ribosyltransferase 1
Short name:
ADPRT 1
Poly[ADP-ribose] synthase 1
Gene namesi
Name:parp1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000211324‹1 – 998Poly [ADP-ribose] polymerase 1Add BLAST›998

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei391PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei397PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei419PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei428PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei429PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei445PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei447PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei454PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei467PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei471PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei477PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei495PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei496PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei503PolyADP-ribosyl glutamic acidSequence analysis1

Keywords - PTMi

ADP-ribosylation

Proteomic databases

PRIDEiP31669

Expressioni

Tissue specificityi

Predominantly expressed in ovary, oocytes and brain. Low expression in liver.

Interactioni

Protein-protein interaction databases

IntActiP31669, 1 interactor

Structurei

3D structure databases

ProteinModelPortaliP31669
SMRiP31669
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini369 – 460BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini645 – 762PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini771 – 997PARP catalyticPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni357 – 507Automodification domainAdd BLAST151

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi193 – 195Nuclear localization signal3
Motifi207 – 212Nuclear localization signal6

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri‹1 – 78PARP-type 1PROSITE-ProRule annotationAdd BLAST›78
Zinc fingeri99 – 189PARP-type 2PROSITE-ProRule annotationAdd BLAST91

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOVERGENiHBG053513

Family and domain databases

CDDicd00027 BRCT, 1 hit
Gene3Di1.20.142.10, 1 hit
2.20.140.10, 1 hit
2.20.25.630, 1 hit
3.30.1740.10, 2 hits
3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR012982 PADR1
IPR038650 PADR1_dom_sf
IPR008288 PARP
IPR012317 Poly(ADP-ribose)pol_cat_dom
IPR004102 Poly(ADP-ribose)pol_reg_dom
IPR036616 Poly(ADP-ribose)pol_reg_dom_sf
IPR036930 WGR_dom_sf
IPR008893 WGR_domain
IPR001510 Znf_PARP
IPR036957 Znf_PARP_sf
PfamiView protein in Pfam
PF00533 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
PIRSFiPIRSF000489 NAD_ADPRT, 1 hit
SMARTiView protein in SMART
SM00292 BRCT, 1 hit
SM01335 PADR1, 1 hit
SM00773 WGR, 1 hit
SM01336 zf-PARP, 2 hits
SUPFAMiSSF142921 SSF142921, 1 hit
SSF47587 SSF47587, 1 hit
SSF52113 SSF52113, 1 hit
PROSITEiView protein in PROSITE
PS50172 BRCT, 1 hit
PS51060 PARP_ALPHA_HD, 1 hit
PS51059 PARP_CATALYTIC, 1 hit
PS00347 PARP_ZN_FINGER_1, 2 hits
PS50064 PARP_ZN_FINGER_2, 2 hits

Sequencei

Sequence statusi: Fragment.

P31669-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
AKSGRASCKK CGDNIAKESL GLAIMVQSPM FDGKVPHWHH YSCFWKRARV
60 70 80 90 100
LSQGDIYGYT ELRWEDQEMI KKAIETGGAA AGAGGDSKGG KGEMTLNDFA
110 120 130 140 150
AEYAKSNRSA CKGCEQKIEK GQIRISKKSV DVERPQLGMI DRWYHPDCFV
160 170 180 190 200
SSREELDFLP SYSASQLKGF TILSAEDKDS LKKKLPAVKN EGKRKADEVD
210 220 230 240 250
GHSAATKKKI KKEKEKESKL EKLLKEQTEL IWHIKDELKK VCSTNDLKEL
260 270 280 290 300
LIANKQQVPS GETNIVDRVS DGMAFGALLP CEECSGQFVF KGDAYYCTGD
310 320 330 340 350
LSAWTKCVAK TQTPNRKDWV TPKEFHEIPY LKKFKFKRHD RAFPPCAAPT
360 370 380 390 400
PISPPAAPEP KPTVEETFPE GKPLTNTKVL LIGKLSKNKD EVKTLIEGLG
410 420 430 440 450
GKVAGSAHKA NLCISTNKEV KKMSKKMEEV KAANVRVVSD DFLKEVESGK
460 470 480 490 500
SVQELLSQFG ISSWGAEIKQ EAVQPTEKQP SSGPVAGKSS GKVKEEKGSN
510 520 530 540 550
KSEKKMKLTV KGGAAIDPDS ELEDSCHVLE TGGKIFSATL GLVDITRGTN
560 570 580 590 600
SYYKLQLIEH DRDSRYWVFR SWGRVGTVIG SKKLEEMSSK EDAIEHFLNL
610 620 630 640 650
YQDKTGNAWH SPNFTKYPKK FYPLEIDYGQ EEDVVKKLSV GAGTKSKLAK
660 670 680 690 700
PVQELIKLIF DVESMKKAMV EFEIDLQKMP LGKLSKRQIQ SAYSILSQVQ
710 720 730 740 750
QAVSESLSEA RLLDLSNQFY TLIPHDFGMK KPPLLNNLEY IQAKVQMLDN
760 770 780 790 800
LLDIEVAYSL LRGGADDGEK DPIDVKYEKI KTDIKVVAKD SEESRIICDY
810 820 830 840 850
VKNTHADTHN AYDLEVLEIF KIDREGEYQR YKPFKQLHNR QLLWHGSRTT
860 870 880 890 900
NFAGILSQGL RIAPPEAPVT GYMFGKGIYF ADMVSKSANY CHAMPGSPIG
910 920 930 940 950
LILLGEVALG NMHELKAASQ ITKLPKGKHS VKGLGRTAPD PSATVQLDGV
960 970 980 990
DVPLGKGTSA NISDTSLLYN EYIVYDIAQV NLKYLLKLKF NYKGGMMW
Length:998
Mass (Da):111,126
Last modified:July 1, 1993 - v1
Checksum:iF5A25E4A3366BAE7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti746Q → E (PubMed:8503897).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12139 mRNA Translation: CAA78126.1
D13810 mRNA Translation: BAA02966.1
PIRiS31735
UniGeneiXl.1271

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12139 mRNA Translation: CAA78126.1
D13810 mRNA Translation: BAA02966.1
PIRiS31735
UniGeneiXl.1271

3D structure databases

ProteinModelPortaliP31669
SMRiP31669
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP31669, 1 interactor

Proteomic databases

PRIDEiP31669

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG053513

Family and domain databases

CDDicd00027 BRCT, 1 hit
Gene3Di1.20.142.10, 1 hit
2.20.140.10, 1 hit
2.20.25.630, 1 hit
3.30.1740.10, 2 hits
3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR012982 PADR1
IPR038650 PADR1_dom_sf
IPR008288 PARP
IPR012317 Poly(ADP-ribose)pol_cat_dom
IPR004102 Poly(ADP-ribose)pol_reg_dom
IPR036616 Poly(ADP-ribose)pol_reg_dom_sf
IPR036930 WGR_dom_sf
IPR008893 WGR_domain
IPR001510 Znf_PARP
IPR036957 Znf_PARP_sf
PfamiView protein in Pfam
PF00533 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
PIRSFiPIRSF000489 NAD_ADPRT, 1 hit
SMARTiView protein in SMART
SM00292 BRCT, 1 hit
SM01335 PADR1, 1 hit
SM00773 WGR, 1 hit
SM01336 zf-PARP, 2 hits
SUPFAMiSSF142921 SSF142921, 1 hit
SSF47587 SSF47587, 1 hit
SSF52113 SSF52113, 1 hit
PROSITEiView protein in PROSITE
PS50172 BRCT, 1 hit
PS51060 PARP_ALPHA_HD, 1 hit
PS51059 PARP_CATALYTIC, 1 hit
PS00347 PARP_ZN_FINGER_1, 2 hits
PS50064 PARP_ZN_FINGER_2, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiPARP1_XENLA
AccessioniPrimary (citable) accession number: P31669
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 25, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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