Skip Header

Contribute Send feedback
Read comments (?) or add your own

P31669 (PARP1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length998 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subcellular location

Nucleus.

Tissue specificity

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

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.

Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
NAD
Zinc
   Molecular functionGlycosyltransferase
Transferase
   PTMADP-ribosylation
Gene Ontology (GO)
   Biological processprotein ADP-ribosylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD binding

Inferred from electronic annotation. Source: InterPro

NAD+ ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 998›998Poly [ADP-ribose] polymerase 1
PRO_0000211324

Regions

Domain369 – 46092BRCT
Domain645 – 762118PARP alpha-helical
Domain771 – 997227PARP catalytic
DNA binding‹1 – 356›356
Zinc finger‹1 – 78›78PARP-type 1
Zinc finger99 – 18991PARP-type 2
Region357 – 507151Automodification domain
Motif193 – 1953Nuclear localization signal
Motif207 – 2126Nuclear localization signal

Amino acid modifications

Modified residue3911PolyADP-ribosyl glutamic acid Potential
Modified residue3971PolyADP-ribosyl glutamic acid Potential
Modified residue4191PolyADP-ribosyl glutamic acid Potential
Modified residue4281PolyADP-ribosyl glutamic acid Potential
Modified residue4291PolyADP-ribosyl glutamic acid Potential
Modified residue4451PolyADP-ribosyl glutamic acid Potential
Modified residue4471PolyADP-ribosyl glutamic acid Potential
Modified residue4541PolyADP-ribosyl glutamic acid Potential
Modified residue4671PolyADP-ribosyl glutamic acid Potential
Modified residue4711PolyADP-ribosyl glutamic acid Potential
Modified residue4771PolyADP-ribosyl glutamic acid Potential
Modified residue4951PolyADP-ribosyl glutamic acid Potential
Modified residue4961PolyADP-ribosyl glutamic acid Potential
Modified residue5031PolyADP-ribosyl glutamic acid Potential

Experimental info

Sequence conflict7461Q → E Ref.2
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P31669 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: F5A25E4A3366BAE7

FASTA998111,126
        10         20         30         40         50         60 
AKSGRASCKK CGDNIAKESL GLAIMVQSPM FDGKVPHWHH YSCFWKRARV LSQGDIYGYT 

        70         80         90        100        110        120 
ELRWEDQEMI KKAIETGGAA AGAGGDSKGG KGEMTLNDFA AEYAKSNRSA CKGCEQKIEK 

       130        140        150        160        170        180 
GQIRISKKSV DVERPQLGMI DRWYHPDCFV SSREELDFLP SYSASQLKGF TILSAEDKDS 

       190        200        210        220        230        240 
LKKKLPAVKN EGKRKADEVD GHSAATKKKI KKEKEKESKL EKLLKEQTEL IWHIKDELKK 

       250        260        270        280        290        300 
VCSTNDLKEL LIANKQQVPS GETNIVDRVS DGMAFGALLP CEECSGQFVF KGDAYYCTGD 

       310        320        330        340        350        360 
LSAWTKCVAK TQTPNRKDWV TPKEFHEIPY LKKFKFKRHD RAFPPCAAPT PISPPAAPEP 

       370        380        390        400        410        420 
KPTVEETFPE GKPLTNTKVL LIGKLSKNKD EVKTLIEGLG GKVAGSAHKA NLCISTNKEV 

       430        440        450        460        470        480 
KKMSKKMEEV KAANVRVVSD DFLKEVESGK SVQELLSQFG ISSWGAEIKQ EAVQPTEKQP 

       490        500        510        520        530        540 
SSGPVAGKSS GKVKEEKGSN KSEKKMKLTV KGGAAIDPDS ELEDSCHVLE TGGKIFSATL 

       550        560        570        580        590        600 
GLVDITRGTN SYYKLQLIEH DRDSRYWVFR SWGRVGTVIG SKKLEEMSSK EDAIEHFLNL 

       610        620        630        640        650        660 
YQDKTGNAWH SPNFTKYPKK FYPLEIDYGQ EEDVVKKLSV GAGTKSKLAK PVQELIKLIF 

       670        680        690        700        710        720 
DVESMKKAMV EFEIDLQKMP LGKLSKRQIQ SAYSILSQVQ QAVSESLSEA RLLDLSNQFY 

       730        740        750        760        770        780 
TLIPHDFGMK KPPLLNNLEY IQAKVQMLDN LLDIEVAYSL LRGGADDGEK DPIDVKYEKI 

       790        800        810        820        830        840 
KTDIKVVAKD SEESRIICDY VKNTHADTHN AYDLEVLEIF KIDREGEYQR YKPFKQLHNR 

       850        860        870        880        890        900 
QLLWHGSRTT NFAGILSQGL RIAPPEAPVT GYMFGKGIYF ADMVSKSANY CHAMPGSPIG 

       910        920        930        940        950        960 
LILLGEVALG NMHELKAASQ ITKLPKGKHS VKGLGRTAPD PSATVQLDGV DVPLGKGTSA 

       970        980        990 
NISDTSLLYN EYIVYDIAQV NLKYLLKLKF NYKGGMMW

« Hide

References

[1]Saulier-Le Drean B.M.
Thesis (1992), University of Rennes, France
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"Isolation of cDNAs encoding the catalytic domain of poly(ADP-ribose) polymerase from Xenopus laevis and cherry salmon using heterologous oligonucleotide consensus sequences."
Ozawa Y., Uchida K., Uchida M., Ami Y., Kushida S., Okada N., Miwa M.
Biochem. Biophys. Res. Commun. 193:119-125(1993) [PubMed: 8503897] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 742-876.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z12139 mRNA. Translation: CAA78126.1.
D13810 mRNA. Translation: BAA02966.1.
PIRS31735.
UniGeneXl.1271.

3D structure databases

ProteinModelPortalP31669.
SMRP31669. Positions 1-81, 91-209, 211-345, 372-469, 503-626, 645-993.
ModBaseSearch...

Proteomic databases

PRIDEP31669.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-974938. parp1.

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_XENLA
AccessionPrimary (citable) accession number: P31669
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 31, 2011
This is version 88 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents