SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P26446

- PARP1_CHICK

UniProt

P26446 - PARP1_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Poly [ADP-ribose] polymerase 1
Gene
PARP1, ADPRT
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi1 – 370370
Add
BLAST
Zinc fingeri9 – 9183PARP-type 1
Add
BLAST
Zinc fingeri113 – 20391PARP-type 2
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. NAD binding Source: InterPro
  3. NAD+ ADP-ribosyltransferase activity Source: UniProtKB-EC
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein poly-ADP-ribosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10111011Poly [ADP-ribose] polymerase 1
PRO_0000211322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei403 – 4031PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei404 – 4041PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei410 – 4101PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei411 – 4111PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei432 – 4321PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei434 – 4341PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei441 – 4411PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei442 – 4421PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei453 – 4531PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei454 – 4541PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei468 – 4681PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei481 – 4811PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei485 – 4851PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei488 – 4881PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei509 – 5091PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei510 – 5101PolyADP-ribosyl glutamic acid Reviewed prediction
Modified residuei517 – 5171PolyADP-ribosyl glutamic acid Reviewed prediction

Keywords - PTMi

ADP-ribosylation

Proteomic databases

PaxDbiP26446.
PRIDEiP26446.

Interactioni

Subunit structurei

Homodimer Reviewed prediction.

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038037.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi664 – 67310
Helixi676 – 68510
Turni690 – 6923
Helixi695 – 6973
Helixi700 – 71819
Helixi723 – 73614
Helixi752 – 77625
Beta strandi782 – 7843
Helixi786 – 7938
Beta strandi796 – 8005
Helixi806 – 81712
Helixi821 – 8233
Beta strandi825 – 83814
Helixi841 – 8455
Helixi846 – 8505
Beta strandi854 – 8618
Helixi863 – 8653
Helixi866 – 8727
Helixi883 – 8853
Beta strandi889 – 8979
Helixi898 – 9025
Helixi903 – 9053
Beta strandi909 – 9113
Beta strandi913 – 92210
Beta strandi925 – 9317
Beta strandi944 – 9474
Beta strandi950 – 9534
Helixi955 – 9573
Beta strandi959 – 9613
Beta strandi964 – 9663
Beta strandi971 – 9733
Beta strandi978 – 9803
Beta strandi985 – 9895
Helixi991 – 9933
Beta strandi994 – 100613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP26446.
SMRiP26446. Positions 1-91, 105-358, 384-484, 517-640, 659-1009.

Miscellaneous databases

EvolutionaryTraceiP26446.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini382 – 47392BRCT
Add
BLAST
Domaini659 – 776118PARP alpha-helical
Add
BLAST
Domaini785 – 1011227PARP catalytic
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni371 – 522152Automodification domain
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2093Nuclear localization signal
Motifi220 – 2256Nuclear localization signal

Sequence similaritiesi

Contains 1 BRCT domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG243963.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
KOiK10798.
PhylomeDBiP26446.

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.
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]
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.
SM00773. WGR. 1 hit.
[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.

P26446-1 [UniParc]FASTAAdd to Basket

« Hide

MAETGDKPYR AEYAKSGRAS CKKCGESIAK DSLRLALMVQ SPMFDGKVPH     50
WHHYSCFWKR ARIVSHTDID GFPELRWEDQ EKIKKAIETG ALQEEKGGTR 100
KEVGKAEKSL TDFAAEYAKS NRSTCKGCEQ KIEKGQIRIS KKMVHPEKPQ 150
LGMIDNWYHP DCFVSRRAEL GFLPAYGATQ LLGFSILKAE DKETLKKQLP 200
ATKTEGKRKG EEVDGNVVAK KKSRKEKEKE SKQEKQLKEQ TELIWGIKDE 250
LRKVCSTNDL KELLIANKQE VPSGENAILD RVADGMAFGA LLPCEECKGQ 300
FVFKSDAYYC SGDITAWTKC VAKTQTPNRK DWVIPKEFRE IPYLKKFKCK 350
KQDRIFPPEA ATVNSAPPPP ASAPLTETVT APQDKPLTNM KILTLGKLSK 400
NKEEVKNIVE ELGGKMTTTA NKATLCISTQ KEVEKMSKKM EEVKDAKVRV 450
VSEEFLKDVK SSNKGFQELL SLHAISPWGA EVKTEHQEVA VDGKCSKPAN 500
MKSAGKVKEE QGPSKSEKKM KLTVKGGAAV DPDSGLEDSA HVFEKGGKIF 550
SATLGLVDIV KGTNSYYKLQ LLEDDRESRY WVFRSWGRVG TVIGSNKLEQ 600
MPSKEDAVEH FLNLYEEKTG NSWHSKNFTK YPKKFYPLEI DYGQDEEAVR 650
KLTVSAGTKS KLAKPIQDLI KMIFDVESMK KAMVEFEIDL QKMPLGKLSK 700
RQIQSAYSIL NEVQQAVSDG GSESQILDLS NRFYTLIPHD FGMKKPPLLS 750
NLEYIQAKVQ MLDNLLDIEV AYSLLRGGNE DGDKDPIDIN YEKLRTDIKV 800
VDKDSEEAKI IKQYVKNTHA ATHNAYDLKV VEIFRIEREG ESQRYKPFKQ 850
LHNRQLLWHG SRTTNFAGIL SQGLRIAPPE APVTGYMFGK GIYFADMVSK 900
SANYCHTSQA DPIGLILLGE VALGNMYELK NASHITKLPK GKHSVKGLGK 950
TAPDPTATTT LDGVEVPLGN GISTGINDTC LLYNEYIVYD VAQVNLKYLL 1000
KLKFNYKTSL W 1011
Length:1,011
Mass (Da):113,520
Last modified:July 15, 1998 - v2
Checksum:i261AED9383139144
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti895 – 8951A → R in CAA36917. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52690 mRNA. Translation: CAA36917.1.
PIRiJH0581.
RefSeqiNP_990594.1. NM_205263.1.
UniGeneiGga.5209.

Genome annotation databases

GeneIDi396199.
KEGGigga:396199.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52690 mRNA. Translation: CAA36917.1 .
PIRi JH0581.
RefSeqi NP_990594.1. NM_205263.1.
UniGenei Gga.5209.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A26 X-ray 2.25 A 652-1011 [» ]
1EFY X-ray 2.20 A 659-1008 [» ]
1PAX X-ray 2.40 A 652-1011 [» ]
2PAW X-ray 2.30 A 652-1011 [» ]
2PAX X-ray 2.40 A 652-1011 [» ]
3PAX X-ray 2.40 A 652-1011 [» ]
4PAX X-ray 2.80 A 652-1011 [» ]
ProteinModelPortali P26446.
SMRi P26446. Positions 1-91, 105-358, 384-484, 517-640, 659-1009.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000038037.

Proteomic databases

PaxDbi P26446.
PRIDEi P26446.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396199.
KEGGi gga:396199.

Organism-specific databases

CTDi 142.

Phylogenomic databases

eggNOGi NOG243963.
HOGENOMi HOG000030402.
HOVERGENi HBG053513.
KOi K10798.
PhylomeDBi P26446.

Miscellaneous databases

EvolutionaryTracei P26446.
NextBioi 20816251.
PROi P26446.

Family and domain databases

Gene3Di 1.20.142.10. 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.
InterProi IPR001357. BRCT_dom.
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 ]
Pfami PF00533. 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 ]
PIRSFi PIRSF000489. NAD_ADPRT. 1 hit.
SMARTi SM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view ]
SUPFAMi SSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. 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 ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 659-1011.

Entry informationi

Entry nameiPARP1_CHICK
AccessioniPrimary (citable) accession number: P26446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 119 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi