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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production (By similarity). Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (By similarity).By similarity

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 bindingi2 – 375374Add
BLAST
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri116 – 20691PARP-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5691.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10161015Poly [ADP-ribose] polymerase 1PRO_0000211318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei41 – 411PhosphoserineBy similarity
Modified residuei100 – 1001N6-acetyllysineBy similarity
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei134 – 1341N6-acetyllysineBy similarity
Cross-linki206 – 206Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei409 – 4091PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei415 – 4151PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei437 – 4371PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei446 – 4461PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei447 – 4471PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei450 – 4501PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei458 – 4581PolyADP-ribosyl glutamic acidSequence analysis
Cross-linki469 – 469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei473 – 4731PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei486 – 4861PolyADP-ribosyl glutamic acidSequence analysis
Cross-linki488 – 488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei490 – 4901PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei493 – 4931PolyADP-ribosyl glutamic acidSequence analysis
Cross-linki514 – 514Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei515 – 5151PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei516 – 5161PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei522 – 5221PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei602 – 6021N6-acetyllysineBy similarity
Modified residuei623 – 6231N6-acetyllysineBy similarity
Cross-linki750 – 750Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei784 – 7841PhosphoserineBy similarity

Post-translational modificationi

Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (By similarity).By similarity
Phosphorylated by PRKDC and TXK.By similarity
S-nitrosylated, leading to inhibit transcription regulation activity.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP18493.
PRIDEiP18493.

Interactioni

Subunit structurei

Component of a base excision repair (BER) complex, containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and heterodimer with PARP2. Interacts with PARP3 and APTX. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 and SRY. Interacts with TIAM2 and ZNF423, Interacts (when poly-ADP-ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression. Interacts with EEF1A1, RNF4 and TXK. Interacts with RNF146. Interacts with SNAI1 (via zinc fingers); the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (when poly-ADP-ribosylated) with PARP9. Interacts with NR4A3; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1. Interacts (via catalytic domain) with PUM3; the interaction inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001113.

Chemistry

BindingDBiP18493.

Structurei

3D structure databases

ProteinModelPortaliP18493.
SMRiP18493. Positions 1-99, 108-362, 389-491, 522-645, 664-1013.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini387 – 47892BRCTPROSITE-ProRule annotationAdd
BLAST
Domaini664 – 781118PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini790 – 1016227PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni376 – 526151Automodification domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi210 – 2123Nuclear localization signal
Motifi224 – 2296Nuclear localization signal

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri116 – 20691PARP-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP18493.
KOiK10798.

Family and domain databases

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18493-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESSDKLYR VEYAKSGRAS CKKCKESIPK DSIRMAFMVE SPMFDGKIPH
60 70 80 90 100
WYHLSCFWKV GFSIWHPDVE VEGFSELRWD DQQTIKKMAE TGGRTDVSGK
110 120 130 140 150
GQDGVGSKTE KTLIDFGAGY AKSNRSTCKS CMEKIDKGQV RLSKKVVYPD
160 170 180 190 200
KPQLGMVDCW YHPKCFVQKR EELGFRPEFS ATHLMGFSVL TAEDQETLKK
210 220 230 240 250
QLPAIKGERK RKGDEVDGID EVTKKKSKKE KDKEIKLEKA LKAQNDLIWN
260 270 280 290 300
VKDELKKACS TNDLKELLIF NKQEVPSGES AILDRVADGM VFGALLPCEE
310 320 330 340 350
CSGQLVFKGD AYYCTGDVTA WTKCMVKTQT PNRKEWVTPK EFREISYFKK
360 370 380 390 400
LKIKKQDRIF PPESSTPVGA AAPPSAASAP AAVHSGPPDK PLSNMKILTL
410 420 430 440 450
GKLSQNKDEV KATIEKLGGK LTGTANKASL CISTKKEVDK LNKKMEEVKE
460 470 480 490 500
ANIRVVSEDF LQDISASTKS LQELLSTHLL SPWGAEVKVE PVEAVGPKGK
510 520 530 540 550
SGAAPSKKSK GPVKEEGTNK SEKRMKLTLK GGAAVDPDSG LEHNAHVLEK
560 570 580 590 600
GGKVFSATLG LVDIVKGTNS YYKLQLLEDD KESRYWIFRS WGRVGTVIGS
610 620 630 640 650
NKLEQMPSKE DAIEHFMKLY EEKTGNAWHS KNFTKHPKKF YPLEIDYGQD
660 670 680 690 700
EEAVKKLTVN PGTKSKLPKP VQNLIKMIFD VESMKKAMVE YEIDLQKMPL
710 720 730 740 750
GKLSKRQIQA AYSILSEVQQ ALSQGSSDSH ILDLSNRFYT LIPHDFGMKK
760 770 780 790 800
PPLLNNANSV QAKVEMLDNL LDIEVAYSLL RGGSDDSSKD PIDVNYEKLK
810 820 830 840 850
TDIKVVDKDS EEAEIIRKYV KNTHATTHNA YDLEVVDIFK IEREGESQRY
860 870 880 890 900
KPFKQLHNRR LLWHGSRTTN FAGILSQGLR IAPPEAPVTG YMFGKGIYFA
910 920 930 940 950
DMVSKSANYC HTSQGDPIGL ILLGEAALGN MYELKHARHI SKLPKGKHSV
960 970 980 990 1000
KGLGKTTPDP SASITVDGVE VPLGTGISSG VNDTCLLYNE YIVYDIAQVH
1010
LKYLLKLKFN FKTSLW
Length:1,016
Mass (Da):113,486
Last modified:January 23, 2007 - v2
Checksum:i11630D94F04F5B02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90073 mRNA. Translation: BAA14114.1.
X06986 mRNA. Translation: CAA30046.1.
X06987 mRNA. Translation: CAA30047.1.
PIRiJS0428.
RefSeqiNP_777176.1. NM_174751.2.
UniGeneiBt.4803.

Genome annotation databases

GeneIDi286764.
KEGGibta:286764.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90073 mRNA. Translation: BAA14114.1.
X06986 mRNA. Translation: CAA30046.1.
X06987 mRNA. Translation: CAA30047.1.
PIRiJS0428.
RefSeqiNP_777176.1. NM_174751.2.
UniGeneiBt.4803.

3D structure databases

ProteinModelPortaliP18493.
SMRiP18493. Positions 1-99, 108-362, 389-491, 522-645, 664-1013.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001113.

Chemistry

BindingDBiP18493.
ChEMBLiCHEMBL5691.

Proteomic databases

PaxDbiP18493.
PRIDEiP18493.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi286764.
KEGGibta:286764.

Organism-specific databases

CTDi142.

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP18493.
KOiK10798.

Miscellaneous databases

PROiP18493.

Family and domain databases

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...

Publicationsi

  1. "Cloning of a full-length cDNA encoding bovine thymus poly(ADP-ribose) synthetase: evolutionarily conserved segments and their potential functions."
    Saito I., Hatakeyama K., Kido T., Ohkubo H., Nakanishi S., Ueda K.
    Gene 90:249-254(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Depression in gene expression for poly(ADP-ribose) synthetase during the interferon-gamma-induced activation process of murine macrophage tumor cells."
    Taniguchi T., Yamauchi K., Yamamoto T., Toyoshima K., Harada N., Tanaka H., Takahashi S., Yamamoto H., Fujimoto S.
    Eur. J. Biochem. 171:571-575(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 648-715 AND 839-904.

Entry informationi

Entry nameiPARP1_BOVIN
AccessioniPrimary (citable) accession number: P18493
Secondary accession number(s): Q9TS00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 147 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

Complete proteome, Reference proteome

Documents

  1. 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.