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P26446 (PARP1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:ADPRT
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length1011 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Subunit structure

Homodimer Potential.

Subcellular location

Nucleus.

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

Chain1 – 10111011Poly [ADP-ribose] polymerase 1
PRO_0000211322

Regions

Domain382 – 47392BRCT
Domain659 – 776118PARP alpha-helical
Domain785 – 1011227PARP catalytic
DNA binding1 – 370370
Zinc finger9 – 9183PARP-type 1
Zinc finger113 – 20391PARP-type 2
Region371 – 522152Automodification domain
Motif207 – 2093Nuclear localization signal
Motif220 – 2256Nuclear localization signal

Amino acid modifications

Modified residue4031PolyADP-ribosyl glutamic acid Potential
Modified residue4041PolyADP-ribosyl glutamic acid Potential
Modified residue4101PolyADP-ribosyl glutamic acid Potential
Modified residue4111PolyADP-ribosyl glutamic acid Potential
Modified residue4321PolyADP-ribosyl glutamic acid Potential
Modified residue4341PolyADP-ribosyl glutamic acid Potential
Modified residue4411PolyADP-ribosyl glutamic acid Potential
Modified residue4421PolyADP-ribosyl glutamic acid Potential
Modified residue4531PolyADP-ribosyl glutamic acid Potential
Modified residue4541PolyADP-ribosyl glutamic acid Potential
Modified residue4681PolyADP-ribosyl glutamic acid Potential
Modified residue4811PolyADP-ribosyl glutamic acid Potential
Modified residue4851PolyADP-ribosyl glutamic acid Potential
Modified residue4881PolyADP-ribosyl glutamic acid Potential
Modified residue5091PolyADP-ribosyl glutamic acid Potential
Modified residue5101PolyADP-ribosyl glutamic acid Potential
Modified residue5171PolyADP-ribosyl glutamic acid Potential

Experimental info

Sequence conflict8951A → R in CAA36917. Ref.1

Secondary structure

1 ................................................................ 1011
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26446 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 261AED9383139144

FASTA1,011113,520
        10         20         30         40         50         60 
MAETGDKPYR AEYAKSGRAS CKKCGESIAK DSLRLALMVQ SPMFDGKVPH WHHYSCFWKR 

        70         80         90        100        110        120 
ARIVSHTDID GFPELRWEDQ EKIKKAIETG ALQEEKGGTR KEVGKAEKSL TDFAAEYAKS 

       130        140        150        160        170        180 
NRSTCKGCEQ KIEKGQIRIS KKMVHPEKPQ LGMIDNWYHP DCFVSRRAEL GFLPAYGATQ 

       190        200        210        220        230        240 
LLGFSILKAE DKETLKKQLP ATKTEGKRKG EEVDGNVVAK KKSRKEKEKE SKQEKQLKEQ 

       250        260        270        280        290        300 
TELIWGIKDE LRKVCSTNDL KELLIANKQE VPSGENAILD RVADGMAFGA LLPCEECKGQ 

       310        320        330        340        350        360 
FVFKSDAYYC SGDITAWTKC VAKTQTPNRK DWVIPKEFRE IPYLKKFKCK KQDRIFPPEA 

       370        380        390        400        410        420 
ATVNSAPPPP ASAPLTETVT APQDKPLTNM KILTLGKLSK NKEEVKNIVE ELGGKMTTTA 

       430        440        450        460        470        480 
NKATLCISTQ KEVEKMSKKM EEVKDAKVRV VSEEFLKDVK SSNKGFQELL SLHAISPWGA 

       490        500        510        520        530        540 
EVKTEHQEVA VDGKCSKPAN MKSAGKVKEE QGPSKSEKKM KLTVKGGAAV DPDSGLEDSA 

       550        560        570        580        590        600 
HVFEKGGKIF SATLGLVDIV KGTNSYYKLQ LLEDDRESRY WVFRSWGRVG TVIGSNKLEQ 

       610        620        630        640        650        660 
MPSKEDAVEH FLNLYEEKTG NSWHSKNFTK YPKKFYPLEI DYGQDEEAVR KLTVSAGTKS 

       670        680        690        700        710        720 
KLAKPIQDLI KMIFDVESMK KAMVEFEIDL QKMPLGKLSK RQIQSAYSIL NEVQQAVSDG 

       730        740        750        760        770        780 
GSESQILDLS NRFYTLIPHD FGMKKPPLLS NLEYIQAKVQ MLDNLLDIEV AYSLLRGGNE 

       790        800        810        820        830        840 
DGDKDPIDIN YEKLRTDIKV VDKDSEEAKI IKQYVKNTHA ATHNAYDLKV VEIFRIEREG 

       850        860        870        880        890        900 
ESQRYKPFKQ LHNRQLLWHG SRTTNFAGIL SQGLRIAPPE APVTGYMFGK GIYFADMVSK 

       910        920        930        940        950        960 
SANYCHTSQA DPIGLILLGE VALGNMYELK NASHITKLPK GKHSVKGLGK TAPDPTATTT 

       970        980        990       1000       1010 
LDGVEVPLGN GISTGINDTC LLYNEYIVYD VAQVNLKYLL KLKFNYKTSL W

« Hide

References

[1]"Chicken poly(ADP-ribose) synthetase: complete deduced amino acid sequence and comparison with mammalian enzyme sequences."
Ittel M.-E., Garnier J.-M., Jeltsch J.-M., Niedergang C.
Gene 102:157-164(1991) [PubMed: 1840535] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Oviduct.
[2]"Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken."
Ruf A., Mennissier-de Murcia J., de Murcia G.M., Schulz G.E.
Proc. Natl. Acad. Sci. U.S.A. 93:7481-7485(1996) [PubMed: 8755499] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 659-1011.
[3]"Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling."
Ruf A., de Murcia G.M., Schulz G.E.
Biochemistry 37:3893-3900(1998) [PubMed: 9521710] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 659-1011, SEQUENCE REVISION TO 895.
[4]"The mechanism of the elongation and branching reaction of poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis."
Ruf A., Rolli V., de Murcia G.M., Schulz G.E.
J. Mol. Biol. 278:57-65(1998) [PubMed: 9571033] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 659-1011.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52690 mRNA. Translation: CAA36917.1.
IPIIPI00823125.
PIRJH0581.
RefSeqNP_990594.1. NM_205263.1.
UniGeneGga.5209.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP26446.
SMRP26446. Positions 1-91, 105-358, 384-484, 517-640, 659-1009.
ModBaseSearch...

Protein-protein interaction databases

STRINGP26446.

Proteomic databases

PRIDEP26446.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396199.
KEGGgga:396199.

Organism-specific databases

CTD142.

Phylogenomic databases

eggNOGveNOG04545.
GeneTreeENSGT00390000017341.
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.
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_CHICK
AccessionPrimary (citable) accession number: P26446
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 15, 1998
Last modified: November 16, 2011
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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