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P26446

- PARP1_CHICK

UniProt

P26446 - PARP1_CHICK

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
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    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

    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

    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 – 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.
    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.
    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

    Experimental Info

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

    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: October 1, 2014
    This is version 120 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