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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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

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 – 370Add BLAST370
Zinc fingeri9 – 91PARP-type 1PROSITE-ProRule annotationAdd BLAST83
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

DNA-binding, Metal-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
Synonyms:ADPRT
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002113221 – 1011Poly [ADP-ribose] polymerase 1Add BLAST1011

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei403PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei404PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei410PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei411PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei432PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei434PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei441PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei442PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei453PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei454PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei468PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei481PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei485PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei488PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei509PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei510PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei517PolyADP-ribosyl glutamic acidSequence analysis1

Keywords - PTMi

ADP-ribosylation

Proteomic databases

PaxDbiP26446.
PRIDEiP26446.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038037.

Structurei

Secondary structure

11011
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi664 – 673Combined sources10
Helixi676 – 685Combined sources10
Turni690 – 692Combined sources3
Helixi695 – 697Combined sources3
Helixi700 – 718Combined sources19
Helixi723 – 736Combined sources14
Helixi752 – 776Combined sources25
Beta strandi782 – 784Combined sources3
Helixi786 – 793Combined sources8
Beta strandi796 – 800Combined sources5
Helixi806 – 817Combined sources12
Helixi821 – 823Combined sources3
Beta strandi825 – 838Combined sources14
Helixi841 – 845Combined sources5
Helixi846 – 850Combined sources5
Beta strandi854 – 861Combined sources8
Helixi863 – 865Combined sources3
Helixi866 – 872Combined sources7
Helixi883 – 885Combined sources3
Beta strandi889 – 897Combined sources9
Helixi898 – 902Combined sources5
Helixi903 – 905Combined sources3
Beta strandi909 – 911Combined sources3
Beta strandi913 – 922Combined sources10
Beta strandi925 – 931Combined sources7
Beta strandi944 – 947Combined sources4
Beta strandi950 – 953Combined sources4
Helixi955 – 957Combined sources3
Beta strandi959 – 961Combined sources3
Beta strandi964 – 966Combined sources3
Beta strandi971 – 973Combined sources3
Beta strandi978 – 980Combined sources3
Beta strandi985 – 989Combined sources5
Helixi991 – 993Combined sources3
Beta strandi994 – 1006Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A26X-ray2.25A652-1011[»]
1EFYX-ray2.20A659-1008[»]
1PAXX-ray2.40A652-1011[»]
2PAWX-ray2.30A652-1011[»]
2PAXX-ray2.40A652-1011[»]
3PAXX-ray2.40A652-1011[»]
4PAXX-ray2.80A652-1011[»]
ProteinModelPortaliP26446.
SMRiP26446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26446.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini382 – 473BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini659 – 776PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini785 – 1011PARP catalyticPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni371 – 522Automodification domainAdd BLAST152

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi207 – 209Nuclear localization signal3
Motifi220 – 225Nuclear 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 fingeri9 – 91PARP-type 1PROSITE-ProRule annotationAdd BLAST83
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP26446.
PhylomeDBiP26446.

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. 2 hits.
PS50064. PARP_ZN_FINGER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26446-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETGDKPYR AEYAKSGRAS CKKCGESIAK DSLRLALMVQ SPMFDGKVPH
60 70 80 90 100
WHHYSCFWKR ARIVSHTDID GFPELRWEDQ EKIKKAIETG ALQEEKGGTR
110 120 130 140 150
KEVGKAEKSL TDFAAEYAKS NRSTCKGCEQ KIEKGQIRIS KKMVHPEKPQ
160 170 180 190 200
LGMIDNWYHP DCFVSRRAEL GFLPAYGATQ LLGFSILKAE DKETLKKQLP
210 220 230 240 250
ATKTEGKRKG EEVDGNVVAK KKSRKEKEKE SKQEKQLKEQ TELIWGIKDE
260 270 280 290 300
LRKVCSTNDL KELLIANKQE VPSGENAILD RVADGMAFGA LLPCEECKGQ
310 320 330 340 350
FVFKSDAYYC SGDITAWTKC VAKTQTPNRK DWVIPKEFRE IPYLKKFKCK
360 370 380 390 400
KQDRIFPPEA ATVNSAPPPP ASAPLTETVT APQDKPLTNM KILTLGKLSK
410 420 430 440 450
NKEEVKNIVE ELGGKMTTTA NKATLCISTQ KEVEKMSKKM EEVKDAKVRV
460 470 480 490 500
VSEEFLKDVK SSNKGFQELL SLHAISPWGA EVKTEHQEVA VDGKCSKPAN
510 520 530 540 550
MKSAGKVKEE QGPSKSEKKM KLTVKGGAAV DPDSGLEDSA HVFEKGGKIF
560 570 580 590 600
SATLGLVDIV KGTNSYYKLQ LLEDDRESRY WVFRSWGRVG TVIGSNKLEQ
610 620 630 640 650
MPSKEDAVEH FLNLYEEKTG NSWHSKNFTK YPKKFYPLEI DYGQDEEAVR
660 670 680 690 700
KLTVSAGTKS KLAKPIQDLI KMIFDVESMK KAMVEFEIDL QKMPLGKLSK
710 720 730 740 750
RQIQSAYSIL NEVQQAVSDG GSESQILDLS NRFYTLIPHD FGMKKPPLLS
760 770 780 790 800
NLEYIQAKVQ MLDNLLDIEV AYSLLRGGNE DGDKDPIDIN YEKLRTDIKV
810 820 830 840 850
VDKDSEEAKI IKQYVKNTHA ATHNAYDLKV VEIFRIEREG ESQRYKPFKQ
860 870 880 890 900
LHNRQLLWHG SRTTNFAGIL SQGLRIAPPE APVTGYMFGK GIYFADMVSK
910 920 930 940 950
SANYCHTSQA DPIGLILLGE VALGNMYELK NASHITKLPK GKHSVKGLGK
960 970 980 990 1000
TAPDPTATTT LDGVEVPLGN GISTGINDTC LLYNEYIVYD VAQVNLKYLL
1010
KLKFNYKTSL W
Length:1,011
Mass (Da):113,520
Last modified:July 15, 1998 - v2
Checksum:i261AED9383139144
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti895A → R in CAA36917 (PubMed:1840535).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52690 mRNA. Translation: CAA36917.1.
PIRiJH0581.
UniGeneiGga.5209.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52690 mRNA. Translation: CAA36917.1.
PIRiJH0581.
UniGeneiGga.5209.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A26X-ray2.25A652-1011[»]
1EFYX-ray2.20A659-1008[»]
1PAXX-ray2.40A652-1011[»]
2PAWX-ray2.30A652-1011[»]
2PAXX-ray2.40A652-1011[»]
3PAXX-ray2.40A652-1011[»]
4PAXX-ray2.80A652-1011[»]
ProteinModelPortaliP26446.
SMRiP26446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038037.

Proteomic databases

PaxDbiP26446.
PRIDEiP26446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP26446.
PhylomeDBiP26446.

Miscellaneous databases

EvolutionaryTraceiP26446.

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. 2 hits.
PS50064. PARP_ZN_FINGER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPARP1_CHICK
AccessioniPrimary (citable) accession number: P26446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 15, 1998
Last modified: November 30, 2016
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

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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.