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P18493 (PARP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Poly [ADP-ribose] polymerase 1
Short name=PARP-1
EC=2.4.2.30
Alternative name(s):
NAD(+) ADP-ribosyltransferase 1
Short name=ADPRT 1
Poly[ADP-ribose] synthase 1
Gene names
Name:PARP1
Synonyms:ADPRT
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length1016 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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 By similarity.

Subcellular location

Nucleus.

Post-translational modification

Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites By similarity.

Phosphorylated by PRKDC and TXK By similarity.

S-nitrosylated, leading to inhibit transcription regulation activity 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.

Sequence similarities

Contains 1 BRCT domain.

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 2 PARP-type zinc fingers.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10161015Poly [ADP-ribose] polymerase 1
PRO_0000211318

Regions

Domain387 – 47892BRCT
Domain664 – 781118PARP alpha-helical
Domain790 – 1016227PARP catalytic
DNA binding2 – 375374
Zinc finger9 – 9385PARP-type 1
Zinc finger116 – 20691PARP-type 2
Region376 – 526151Automodification domain
Motif210 – 2123Nuclear localization signal
Motif224 – 2296Nuclear localization signal

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue411Phosphoserine By similarity
Modified residue1001N6-acetyllysine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue1341N6-acetyllysine By similarity
Modified residue4091PolyADP-ribosyl glutamic acid Potential
Modified residue4151PolyADP-ribosyl glutamic acid Potential
Modified residue4371PolyADP-ribosyl glutamic acid Potential
Modified residue4461PolyADP-ribosyl glutamic acid Potential
Modified residue4471PolyADP-ribosyl glutamic acid Potential
Modified residue4501PolyADP-ribosyl glutamic acid Potential
Modified residue4581PolyADP-ribosyl glutamic acid Potential
Modified residue4731PolyADP-ribosyl glutamic acid Potential
Modified residue4861PolyADP-ribosyl glutamic acid Potential
Modified residue4901PolyADP-ribosyl glutamic acid Potential
Modified residue4931PolyADP-ribosyl glutamic acid Potential
Modified residue5151PolyADP-ribosyl glutamic acid Potential
Modified residue5161PolyADP-ribosyl glutamic acid Potential
Modified residue5221PolyADP-ribosyl glutamic acid Potential
Modified residue6021N6-acetyllysine By similarity
Modified residue6231N6-acetyllysine By similarity
Modified residue7841Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P18493 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 11630D94F04F5B02

FASTA1,016113,486
        10         20         30         40         50         60 
MAESSDKLYR VEYAKSGRAS CKKCKESIPK DSIRMAFMVE SPMFDGKIPH WYHLSCFWKV 

        70         80         90        100        110        120 
GFSIWHPDVE VEGFSELRWD DQQTIKKMAE TGGRTDVSGK GQDGVGSKTE KTLIDFGAGY 

       130        140        150        160        170        180 
AKSNRSTCKS CMEKIDKGQV RLSKKVVYPD KPQLGMVDCW YHPKCFVQKR EELGFRPEFS 

       190        200        210        220        230        240 
ATHLMGFSVL TAEDQETLKK QLPAIKGERK RKGDEVDGID EVTKKKSKKE KDKEIKLEKA 

       250        260        270        280        290        300 
LKAQNDLIWN VKDELKKACS TNDLKELLIF NKQEVPSGES AILDRVADGM VFGALLPCEE 

       310        320        330        340        350        360 
CSGQLVFKGD AYYCTGDVTA WTKCMVKTQT PNRKEWVTPK EFREISYFKK LKIKKQDRIF 

       370        380        390        400        410        420 
PPESSTPVGA AAPPSAASAP AAVHSGPPDK PLSNMKILTL GKLSQNKDEV KATIEKLGGK 

       430        440        450        460        470        480 
LTGTANKASL CISTKKEVDK LNKKMEEVKE ANIRVVSEDF LQDISASTKS LQELLSTHLL 

       490        500        510        520        530        540 
SPWGAEVKVE PVEAVGPKGK SGAAPSKKSK GPVKEEGTNK SEKRMKLTLK GGAAVDPDSG 

       550        560        570        580        590        600 
LEHNAHVLEK GGKVFSATLG LVDIVKGTNS YYKLQLLEDD KESRYWIFRS WGRVGTVIGS 

       610        620        630        640        650        660 
NKLEQMPSKE DAIEHFMKLY EEKTGNAWHS KNFTKHPKKF YPLEIDYGQD EEAVKKLTVN 

       670        680        690        700        710        720 
PGTKSKLPKP VQNLIKMIFD VESMKKAMVE YEIDLQKMPL GKLSKRQIQA AYSILSEVQQ 

       730        740        750        760        770        780 
ALSQGSSDSH ILDLSNRFYT LIPHDFGMKK PPLLNNANSV QAKVEMLDNL LDIEVAYSLL 

       790        800        810        820        830        840 
RGGSDDSSKD PIDVNYEKLK TDIKVVDKDS EEAEIIRKYV KNTHATTHNA YDLEVVDIFK 

       850        860        870        880        890        900 
IEREGESQRY KPFKQLHNRR LLWHGSRTTN FAGILSQGLR IAPPEAPVTG YMFGKGIYFA 

       910        920        930        940        950        960 
DMVSKSANYC HTSQGDPIGL ILLGEAALGN MYELKHARHI SKLPKGKHSV KGLGKTTPDP 

       970        980        990       1000       1010 
SASITVDGVE VPLGTGISSG VNDTCLLYNE YIVYDIAQVH LKYLLKLKFN FKTSLW

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References

[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: 2119324] [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: 2450019] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 648-715 AND 839-904.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D90073 mRNA. Translation: BAA14114.1.
X06986 mRNA. Translation: CAA30046.1.
X06987 mRNA. Translation: CAA30047.1.
IPIIPI00697783.
PIRJS0428.
RefSeqNP_777176.1. NM_174751.2.
UniGeneBt.4803.

3D structure databases

ProteinModelPortalP18493.
SMRP18493. Positions 1-99, 108-362, 389-491, 522-645, 664-1013.
ModBaseSearch...

Protein-protein interaction databases

STRINGP18493.

Proteomic databases

PRIDEP18493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID286764.
KEGGbta:286764.

Organism-specific databases

CTD142.

Phylogenomic databases

eggNOGmaNOG04741.
HOVERGENHBG053513.
InParanoidP18493.
OrthoDBEOG4PG609.

Family and domain databases

InterProIPR001357. BRCT.
IPR008288. NAD_ADPRT.
IPR012982. PADR1.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
Gene3DG3DSA:2.20.140.10. G3DSA:2.20.140.10. 1 hit.
G3DSA:1.20.142.10. PARP_reg. 1 hit.
G3DSA:3.30.1740.10. Znf_PARP. 2 hits.
KOK10798.
PfamPF00533. 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]
PIRSFPIRSF000489. NAD_ADPRT. 1 hit.
SMARTSM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view]
SUPFAMSSF52113. BRCT. 1 hit.
SSF47587. PARP_reg. 1 hit.
SSF142921. SSF142921. 1 hit.
PROSITEPS50172. 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]
ProtoNetSearch...

Entry information

Entry namePARP1_BOVIN
AccessionPrimary (citable) accession number: P18493
Secondary accession number(s): Q9TS00
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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