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P26446

- PARP1_CHICK

UniProt

P26446 - PARP1_CHICK

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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

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.PROSITE-ProRule annotation

Regions

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. NAD+ ADP-ribosyltransferase activity Source: UniProtKB-EC
  3. NAD binding Source: InterPro
  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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

ADP-ribosylation

Proteomic databases

PaxDbiP26446.
PRIDEiP26446.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038037.

Structurei

Secondary structure

1
1011
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi664 – 67310Combined sources
Helixi676 – 68510Combined sources
Turni690 – 6923Combined sources
Helixi695 – 6973Combined sources
Helixi700 – 71819Combined sources
Helixi723 – 73614Combined sources
Helixi752 – 77625Combined sources
Beta strandi782 – 7843Combined sources
Helixi786 – 7938Combined sources
Beta strandi796 – 8005Combined sources
Helixi806 – 81712Combined sources
Helixi821 – 8233Combined sources
Beta strandi825 – 83814Combined sources
Helixi841 – 8455Combined sources
Helixi846 – 8505Combined sources
Beta strandi854 – 8618Combined sources
Helixi863 – 8653Combined sources
Helixi866 – 8727Combined sources
Helixi883 – 8853Combined sources
Beta strandi889 – 8979Combined sources
Helixi898 – 9025Combined sources
Helixi903 – 9053Combined sources
Beta strandi909 – 9113Combined sources
Beta strandi913 – 92210Combined sources
Beta strandi925 – 9317Combined sources
Beta strandi944 – 9474Combined sources
Beta strandi950 – 9534Combined sources
Helixi955 – 9573Combined sources
Beta strandi959 – 9613Combined sources
Beta strandi964 – 9663Combined sources
Beta strandi971 – 9733Combined sources
Beta strandi978 – 9803Combined sources
Beta strandi985 – 9895Combined sources
Helixi991 – 9933Combined sources
Beta strandi994 – 100613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26446.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini382 – 47392BRCTPROSITE-ProRule annotationAdd
BLAST
Domaini659 – 776118PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini785 – 1011227PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

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

Motif

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

Sequence similaritiesi

Contains 1 BRCT domain.PROSITE-ProRule annotation
Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 2 PARP-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 9183PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 20391PARP-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG243963.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP26446.
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

        10         20         30         40         50
MAETGDKPYR AEYAKSGRAS CKKCGESIAK DSLRLALMVQ SPMFDGKVPH
60 70 80 90 100
WHHYSCFWKR ARIVSHTDID GFPELRWEDQ EKIKKAIETG ALQEEKGGTR
110 120 130 140 150
KEVGKAEKSL TDFAAEYAKS NRSTCKGCEQ KIEKGQIRIS KKMVHPEKPQ
160 170 180 190 200
LGMIDNWYHP DCFVSRRAEL GFLPAYGATQ LLGFSILKAE DKETLKKQLP
210 220 230 240 250
ATKTEGKRKG EEVDGNVVAK KKSRKEKEKE SKQEKQLKEQ TELIWGIKDE
260 270 280 290 300
LRKVCSTNDL KELLIANKQE VPSGENAILD RVADGMAFGA LLPCEECKGQ
310 320 330 340 350
FVFKSDAYYC SGDITAWTKC VAKTQTPNRK DWVIPKEFRE IPYLKKFKCK
360 370 380 390 400
KQDRIFPPEA ATVNSAPPPP ASAPLTETVT APQDKPLTNM KILTLGKLSK
410 420 430 440 450
NKEEVKNIVE ELGGKMTTTA NKATLCISTQ KEVEKMSKKM EEVKDAKVRV
460 470 480 490 500
VSEEFLKDVK SSNKGFQELL SLHAISPWGA EVKTEHQEVA VDGKCSKPAN
510 520 530 540 550
MKSAGKVKEE QGPSKSEKKM KLTVKGGAAV DPDSGLEDSA HVFEKGGKIF
560 570 580 590 600
SATLGLVDIV KGTNSYYKLQ LLEDDRESRY WVFRSWGRVG TVIGSNKLEQ
610 620 630 640 650
MPSKEDAVEH FLNLYEEKTG NSWHSKNFTK YPKKFYPLEI DYGQDEEAVR
660 670 680 690 700
KLTVSAGTKS KLAKPIQDLI KMIFDVESMK KAMVEFEIDL QKMPLGKLSK
710 720 730 740 750
RQIQSAYSIL NEVQQAVSDG GSESQILDLS NRFYTLIPHD FGMKKPPLLS
760 770 780 790 800
NLEYIQAKVQ MLDNLLDIEV AYSLLRGGNE DGDKDPIDIN YEKLRTDIKV
810 820 830 840 850
VDKDSEEAKI IKQYVKNTHA ATHNAYDLKV VEIFRIEREG ESQRYKPFKQ
860 870 880 890 900
LHNRQLLWHG SRTTNFAGIL SQGLRIAPPE APVTGYMFGK GIYFADMVSK
910 920 930 940 950
SANYCHTSQA DPIGLILLGE VALGNMYELK NASHITKLPK GKHSVKGLGK
960 970 980 990 1000
TAPDPTATTT LDGVEVPLGN GISTGINDTC LLYNEYIVYD VAQVNLKYLL
1010
KLKFNYKTSL W
Length:1,011
Mass (Da):113,520
Last modified:July 15, 1998 - v2
Checksum:i261AED9383139144
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti895 – 8951A → R in CAA36917. (PubMed:1840535)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P26446.
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: November 26, 2014
This is version 122 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