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Q9R152 (PARP1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. 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
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length1013 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, SWAP70 and SRY. Interacts with TIAM2 and ZNF423. Interacts (when poly-ADP-ribosylated) with CHD1L By similarity. Interacts with EEF1A1, RNF4 and TXK By similarity.

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated by PRKDC and TXK. Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.

Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites 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 – 10131012Poly [ADP-ribose] polymerase 1
PRO_0000211319

Regions

Domain385 – 47692BRCT
Domain661 – 778118PARP alpha-helical
Domain787 – 1013227PARP catalytic
DNA binding2 – 372371 By similarity
Zinc finger9 – 9385PARP-type 1
Zinc finger113 – 20391PARP-type 2
Region373 – 523151Automodification domain By similarity
Motif207 – 2093Nuclear localization signal Potential
Motif221 – 2266Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue411Phosphoserine By similarity
Modified residue971N6-acetyllysine By similarity
Modified residue1051N6-acetyllysine By similarity
Modified residue1311N6-acetyllysine By similarity
Modified residue1791Phosphoserine By similarity
Modified residue4071PolyADP-ribosyl glutamic acid Potential
Modified residue4131PolyADP-ribosyl glutamic acid Potential
Modified residue4351PolyADP-ribosyl glutamic acid Potential
Modified residue4371PolyADP-ribosyl glutamic acid Potential
Modified residue4441PolyADP-ribosyl glutamic acid Potential
Modified residue4451PolyADP-ribosyl glutamic acid Potential
Modified residue4561PolyADP-ribosyl glutamic acid Potential
Modified residue4711PolyADP-ribosyl glutamic acid Potential
Modified residue4841PolyADP-ribosyl glutamic acid Potential
Modified residue4881PolyADP-ribosyl glutamic acid Potential
Modified residue4911PolyADP-ribosyl glutamic acid Potential
Modified residue5121PolyADP-ribosyl glutamic acid Potential
Modified residue5131PolyADP-ribosyl glutamic acid Potential
Modified residue5191PolyADP-ribosyl glutamic acid Potential
Modified residue5991N6-acetyllysine By similarity
Modified residue6201N6-acetyllysine By similarity
Modified residue7811Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9R152 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 90617C4DB91C9DEC

FASTA1,013112,532
        10         20         30         40         50         60 
MAEASERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV 

        70         80         90        100        110        120 
GHSIRQPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD GSGGKSEKTL GDFAAEYAKS 

       130        140        150        160        170        180 
NRSTCKGCME KIEKGQVRLS KKMLDPEKPQ LGMIDRWYHP TCFVKNREEL GFRPEYSASQ 

       190        200        210        220        230        240 
LKGFSLLSAE DKEVLKKQLP GVKSEGKRKG DEVDGADEVA KKKSKKGKDK DSKLEKALKA 

       250        260        270        280        290        300 
QNDLIWNIKD ELKKACSTSD LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG 

       310        320        330        340        350        360 
QLVFKSDAYY CTGDVTAWTK CMVKTQTPSR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE 

       370        380        390        400        410        420 
TSAPAPPHLP PSVTSAPTAV NSSCPADKPL SNMKILTLGK LSQSKDEAKA TIEKLGGKLT 

       430        440        450        460        470        480 
GSANNASLCI STKKEVEKMG KKMEEVQAAN VRVVCEDFLQ DVAASTKSLQ ELLSAHSLSS 

       490        500        510        520        530        540 
WGAEVKVEPV EVAAPKGKSA APSKKSKGLY KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH 

       550        560        570        580        590        600 
SAHVLEKGGK VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR VGTVIGSNKL 

       610        620        630        640        650        660 
EQMPSKEDAV EHFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA VKKLTVKPGT 

       670        680        690        700        710        720 
KSKLPKAVQE LVGMIFDVES MKKALVEYEI DLQKMPLGKL SKRQIQAAYS ILSEVQQAVS 

       730        740        750        760        770        780 
QGSSDSQILD LSNRFYTLIP HDFGMKKPPL LNNADSVQAK VEMLDNLLDI EVAYSLLRGG 

       790        800        810        820        830        840 
SDDSSKDPID VNYEKLKTDI KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVMDIFKIER 

       850        860        870        880        890        900 
EGESQRYKPF KQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV 

       910        920        930        940        950        960 
SKSANYCHTS QGDPIGLILL GEVALGNMYE LKHASHISKL PKGKHSVKGL GKTTPDPSAS 

       970        980        990       1000       1010 
ITLEGVEVPL GTGIPSGVND TCLLYNEYIV YDIAQVNLKY LLKLKFNFKT SLW

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References

[1]"Suppression of the radiation-sensitive phenotype of hamster irs1 and irs2 strains selected for resistance to 3-aminobenzamide."
Ganesh A., Phillips E., Thacker J., Meuth M.
Int. J. Radiat. Biol. 77:609-616(2001) [PubMed: 11382339] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF168781 mRNA. Translation: AAD45817.1.
RefSeqNP_001233650.1. NM_001246721.1.

3D structure databases

ProteinModelPortalQ9R152.
SMRQ9R152. Positions 1-93, 105-359, 381-489, 519-642, 661-1010.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689463.

Phylogenomic databases

HOVERGENHBG053513.

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.
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_CRIGR
AccessionPrimary (citable) accession number: Q9R152
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 91 of the entry and version 3 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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