Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Poly [ADP-ribose] polymerase 1 (PARP-1) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 1) (ARTD1) (NAD( ) ADP-ribosyltransferase 1) (ADPRT 1) (Poly[ADP-ribose] synthase 1)

 PARP1_RAT               Reviewed;        1014 AA.
P27008; O35937;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
18-JUL-2018, entry version 182.
RecName: Full=Poly [ADP-ribose] polymerase 1;
Short=PARP-1;
EC=2.4.2.30;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1;
Short=ARTD1;
AltName: Full=NAD(+) ADP-ribosyltransferase 1;
Short=ADPRT 1;
AltName: Full=Poly[ADP-ribose] synthase 1;
Name=Parp1; Synonyms=Adprt;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Monocyte;
PubMed=9385436;
Beneke S., Meyer R., Buerkle A.;
"Isolation of cDNA encoding full-length rat (Rattus norvegicus) poly
(ADP-ribose) polymerase.";
Biochem. Mol. Biol. Int. 43:755-761(1997).
[2]
SEQUENCE REVISION TO 812.
Beneke S., Meyer R., Buerkle A.;
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
STRAIN=Sprague-Dawley; TISSUE=Prostate;
PubMed=1601134; DOI=10.1016/0014-5793(92)80457-R;
Potvin F., Thibodeau J., Kirkland J.B., Dandenault B., Duchaine C.,
Poirier G.G.;
"Structural analysis of the putative regulatory region of the rat gene
encoding poly(ADP-ribose) polymerase.";
FEBS Lett. 302:269-273(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 515-1014.
STRAIN=Sprague-Dawley; TISSUE=Prostate;
PubMed=2508731;
Thibodeau J., Gradwohl G., Dumas C., Clairoux-Moreau S., Brunet G.;
"Cloning of rodent cDNA coding the poly(ADP-ribose) polymerase
catalytic domain and analysis of mRNA levels during the cell cycle.";
Biochem. Cell Biol. 67:653-660(1989).
[6]
INTERACTION WITH NR4A3.
PubMed=25625556; DOI=10.1111/bph.13091;
Feng X.J., Gao H., Gao S., Li Z., Li H., Lu J., Wang J.J., Huang X.Y.,
Liu M., Zou J., Ye J.T., Liu P.Q.;
"The orphan receptor NOR1 participates in isoprenaline-induced cardiac
hypertrophy by regulating PARP-1.";
Br. J. Pharmacol. 172:2852-2863(2015).
-!- FUNCTION: Involved in the base excision repair (BER) pathway, by
catalyzing the poly(ADP-ribosyl)ation of a limited number of
acceptor proteins involved in chromatin architecture and in DNA
metabolism. This modification follows DNA damages and appears as
an obligatory step in a detection/signaling pathway leading to the
reparation of DNA strand breaks. Mediates the poly(ADP-
ribosyl)ation of APLF and CHFR. Positively regulates the
transcription of MTUS1 and negatively regulates the transcription
of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as
a T-helper 1 (Th1) cell-specific transcription factor and binds
the promoter of IFN-gamma to directly regulate its transcription,
and is thus involved importantly in Th1 cytokine production.
Required for PARP9 and DTX3L recruitment to DNA damage sites.
PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the
rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and
BRCA1 to DNA damage sites. Mediates serine ADP-ribosylation of
target proteins following interaction with HPF1; HPF1 conferring
serine specificity. Mediates the poly(ADP-ribosyl)ation of
histones in a HPF1-dependent manner. Involved in the synthesis of
ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear
ATP generation is required for extensive chromatin remodeling
events that are energy-consuming. {ECO:0000250|UniProtKB:P09874}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000250|UniProtKB:P09874, ECO:0000255|PROSITE-
ProRule:PRU00397}.
-!- SUBUNIT: Component of a base excision repair (BER) complex,
containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and
heterodimer with PARP2. Interacts with PARP3 and APTX. The SWAP
complex consists of NPM1, NCL, PARP1, SWAP70 and SRY. Interacts
with TIAM2 and ZNF423. Interacts (when poly-ADP-ribosylated) with
CHD1L. Interacts with the DNA polymerase alpha catalytic subunit
POLA1; this interaction functions as part of the control of
replication fork progression. Interacts with EEF1A1, RNF4 and TXK.
Interacts with RNF146. Interacts with SNAI1 (via zinc fingers);
the interaction requires SNAI1 to be poly-ADP-ribosylated and non-
phosphorylated (active) by GSK3B (By similarity). Interacts (when
poly-ADP-ribosylated) with PARP9 (By similarity). Interacts with
NR4A3; activates PARP1 by improving acetylation of PARP1 and
suppressing the interaction between PARP1 and SIRT1
(PubMed:25625556). Interacts (via catalytic domain) with PUM3; the
interaction inhibits the poly(ADP-ribosyl)ation activity of PARP1
and the degradation of PARP1 by CASP3 following genotoxic stress.
Interacts (via the PARP catalytic domain) with HPF1 (By
similarity). Interacts with RRP1B (By similarity).
{ECO:0000250|UniProtKB:P09874, ECO:0000269|PubMed:25625556}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09874}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:P09874}. Note=Localizes
at sites of DNA damage. {ECO:0000250|UniProtKB:P09874}.
-!- PTM: Phosphorylated by PRKDC and TXK.
{ECO:0000250|UniProtKB:P09874}.
-!- PTM: Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates
the recruitment of CHD1L to DNA damage sites. ADP-ribosylated on
serine by autocatalysis; serine ADP-ribosylation takes place
following interaction with HPF1. {ECO:0000250|UniProtKB:P09874}.
-!- PTM: S-nitrosylated, leading to inhibit transcription regulation
activity. {ECO:0000250|UniProtKB:P11103}.
-!- 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 CAUTION:
Sequence=CAA46478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U94340; AAC53544.1; -; mRNA.
EMBL; BC085765; AAH85765.1; -; mRNA.
EMBL; X65496; CAA46477.1; -; Genomic_DNA.
EMBL; X65497; CAA46478.1; ALT_INIT; Genomic_DNA.
PIR; S21163; S21163.
PIR; S26057; S26057.
RefSeq; NP_037195.1; NM_013063.2.
UniGene; Rn.11327; -.
PDB; 2LE0; NMR; -; A=389-487.
PDBsum; 2LE0; -.
ProteinModelPortal; P27008; -.
SMR; P27008; -.
BioGrid; 247621; 16.
STRING; 10116.ENSRNOP00000004232; -.
BindingDB; P27008; -.
ChEMBL; CHEMBL4664; -.
CarbonylDB; P27008; -.
iPTMnet; P27008; -.
PhosphoSitePlus; P27008; -.
PaxDb; P27008; -.
PRIDE; P27008; -.
Ensembl; ENSRNOT00000004232; ENSRNOP00000004232; ENSRNOG00000003084.
GeneID; 25591; -.
KEGG; rno:25591; -.
UCSC; RGD:2053; rat.
CTD; 142; -.
RGD; 2053; Parp1.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
GeneTree; ENSGT00390000017341; -.
HOGENOM; HOG000030402; -.
HOVERGEN; HBG053513; -.
InParanoid; P27008; -.
KO; K10798; -.
OMA; WNHASCI; -.
OrthoDB; EOG091G13H1; -.
PhylomeDB; P27008; -.
TreeFam; TF316616; -.
Reactome; R-RNO-110362; POLB-Dependent Long Patch Base Excision Repair.
Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-RNO-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-RNO-5696400; Dual Incision in GG-NER.
PRO; PR:P27008; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000003084; -.
Genevisible; P27008; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0030331; F:estrogen receptor binding; IPI:RGD.
GO; GO:0042826; F:histone deacetylase binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0051287; F:NAD binding; IDA:RGD.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:RGD.
GO; GO:1990404; F:protein ADP-ribosylase activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0046332; F:SMAD binding; IPI:RGD.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0016763; F:transferase activity, transferring pentosyl groups; NAS:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
GO; GO:1904646; P:cellular response to amyloid-beta; IMP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:RGD.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:0071294; P:cellular response to zinc ion; IEP:RGD.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; IDA:RGD.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
GO; GO:0043504; P:mitochondrial DNA repair; IEA:Ensembl.
GO; GO:2001170; P:negative regulation of ATP biosynthetic process; IEA:Ensembl.
GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:RGD.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:RGD.
GO; GO:1904762; P:positive regulation of myofibroblast differentiation; IMP:RGD.
GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:RGD.
GO; GO:1903518; P:positive regulation of single strand break repair; IEA:Ensembl.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:BHF-UCL.
GO; GO:0006471; P:protein ADP-ribosylation; IDA:RGD.
GO; GO:0016540; P:protein autoprocessing; IDA:RGD.
GO; GO:0070212; P:protein poly-ADP-ribosylation; IMP:BHF-UCL.
GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
GO; GO:0044030; P:regulation of DNA methylation; IMP:RGD.
GO; GO:1903376; P:regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IMP:RGD.
GO; GO:0010990; P:regulation of SMAD protein complex assembly; IMP:RGD.
GO; GO:1904044; P:response to aldosterone; IEP:RGD.
GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
CDD; cd00027; BRCT; 1.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 2.20.140.10; -; 1.
Gene3D; 2.20.25.630; -; 1.
Gene3D; 3.30.1740.10; -; 2.
Gene3D; 3.40.50.10190; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR012982; PADR1.
InterPro; IPR038650; PADR1_dom_sf.
InterPro; IPR008288; PARP.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
InterPro; IPR036930; WGR_dom_sf.
InterPro; IPR008893; WGR_domain.
InterPro; IPR001510; Znf_PARP.
InterPro; IPR036957; Znf_PARP_sf.
Pfam; PF00533; BRCT; 1.
Pfam; PF08063; PADR1; 1.
Pfam; PF00644; PARP; 1.
Pfam; PF02877; PARP_reg; 1.
Pfam; PF05406; WGR; 1.
Pfam; PF00645; zf-PARP; 2.
PIRSF; PIRSF000489; NAD_ADPRT; 1.
SMART; SM00292; BRCT; 1.
SMART; SM01335; PADR1; 1.
SMART; SM00773; WGR; 1.
SMART; SM01336; zf-PARP; 2.
SUPFAM; SSF142921; SSF142921; 1.
SUPFAM; SSF47587; SSF47587; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS00347; PARP_ZN_FINGER_1; 2.
PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Complete proteome;
DNA damage; DNA repair; DNA-binding; Glycosyltransferase;
Isopeptide bond; Metal-binding; NAD; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P09874}.
CHAIN 2 1014 Poly [ADP-ribose] polymerase 1.
/FTId=PRO_0000211321.
DOMAIN 386 477 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 662 779 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 788 1014 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
DNA_BIND 2 373
ZN_FING 9 93 PARP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
ZN_FING 113 203 PARP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
REGION 374 524 Automodification domain.
MOTIF 207 209 Nuclear localization signal.
MOTIF 221 226 Nuclear localization signal.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 97 97 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 131 131 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 408 408 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 414 414 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 436 436 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 438 438 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 445 445 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 446 446 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 457 457 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 485 485 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 489 489 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 492 492 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 500 500 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 507 507 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 513 513 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 514 514 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 519 519 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 520 520 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 600 600 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 621 621 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 782 782 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 192 192 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 203 203 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 250 250 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 468 468 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 487 487 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 487 487 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 528 528 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 748 748 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 748 748 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CONFLICT 639 639 Y -> H (in Ref. 5; CAA46478).
{ECO:0000305}.
CONFLICT 642 642 E -> A (in Ref. 5; CAA46478).
{ECO:0000305}.
CONFLICT 753 753 N -> D (in Ref. 5; CAA46478).
{ECO:0000305}.
STRAND 394 398 {ECO:0000244|PDB:2LE0}.
HELIX 406 416 {ECO:0000244|PDB:2LE0}.
STRAND 422 424 {ECO:0000244|PDB:2LE0}.
STRAND 427 431 {ECO:0000244|PDB:2LE0}.
HELIX 434 439 {ECO:0000244|PDB:2LE0}.
HELIX 442 449 {ECO:0000244|PDB:2LE0}.
STRAND 453 455 {ECO:0000244|PDB:2LE0}.
HELIX 458 465 {ECO:0000244|PDB:2LE0}.
HELIX 470 476 {ECO:0000244|PDB:2LE0}.
SEQUENCE 1014 AA; 112660 MW; BE1B6F2B29B887ED CRC64;
MAEATERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV
GHSIRQPDTE VDGFSELRWD DQQKVKKTAE AGGVAGKGQH GGGGKAEKTL GDFAAEYAKS
NRSTCKGCME KIEKGQMRLS KKMLDPEKPQ LGMIDRWYHP TCFVKNRDEL GFRPEYSASQ
LKGFSLLSAE DKEALKKQLP AVKSEGKRKC DEVDGIDEVA KKKSKKGKDK ESSKLEKALK
AQNELVWNIK DELKKACSTN DLKELLIFNQ QQVPSGESAI LDRVADGMAF GALLPCKECS
GQLVFKSDAY YCTGDVTAWT KCMVKTQNPS RKEWVTPKEF REISYLKKLK IKKQDRLFPP
ESSAPAPPAP PVSITSAPTA VNSSAPADKP LSNMKILTLG KLSQNKDEAK AMIEKLGGKL
TGSANKASLC ISTKKEVEKM SKKMEEVKAA NVRVVCEDFL QDVSASAKSL QELLSAHSLS
SWGAEVKVEP GEVVVPKGKS AAPSKKSKGA VKEEGVNKSE KRMKLTLKGG AAVDPDSGLE
HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLESDKE SRYWIFRSWG RVGTVIGSNK
LEQMPSKEDA VEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLAVKPG
TKSKLPKPVQ ELVGMIFDVE SMKKALVEYE IDLQKMPLGK LSRRQIQAAY SILSEVQQAV
SQGSSESQIL DLSNRFYTLI PHDFGMKKPP LLNNTDSVQA KVEMLDNLLD IEVAYSLLRG
GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEVIRKYVKN THATTHNAYD LEVIDIFKIE
REGESQRYKP FRQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTAPDPSA
SITLDGVEVP LGTGIPSGVN DTCLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW


Related products :

Catalog number Product name Quantity
E0947h ELISA ADPRT,ADPRT 1,Homo sapiens,Human,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,PPOL 96T
U0947h CLIA ADPRT,ADPRT 1,Homo sapiens,Human,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,PPOL 96T
E0947h ELISA kit ADPRT,ADPRT 1,Homo sapiens,Human,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,PPOL 96T
E0947m ELISA kit Adprp,Adprt,ADPRT 1,Adprt1,Mouse,msPARP,Mus musculus,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
U0947m CLIA Adprp,Adprt,ADPRT 1,Adprt1,Mouse,msPARP,Mus musculus,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947m ELISA Adprp,Adprt,ADPRT 1,Adprt1,Mouse,msPARP,Mus musculus,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
U0947b CLIA ADPRT,ADPRT 1,Bos taurus,Bovine,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947r ELISA Adprt,ADPRT 1,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,Rat,Rattus norvegicus 96T
E0947r ELISA kit Adprt,ADPRT 1,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,Rat,Rattus norvegicus 96T
U0947r CLIA Adprt,ADPRT 1,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,Rat,Rattus norvegicus 96T
E0947b ELISA kit ADPRT,ADPRT 1,Bos taurus,Bovine,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947b ELISA ADPRT,ADPRT 1,Bos taurus,Bovine,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
EIAAB29923 Adprt2,ADPRT-2,Adprtl2,Aspartl2,Mouse,mPARP-2,Mus musculus,NAD(+) ADP-ribosyltransferase 2,pADPRT-2,Parp2,PARP-2,Poly [ADP-ribose] polymerase 2,Poly[ADP-ribose] synthase 2
EIAAB29924 ADPRT2,ADPRT-2,ADPRTL2,Homo sapiens,hPARP-2,Human,NAD(+) ADP-ribosyltransferase 2,pADPRT-2,PARP2,PARP-2,Poly [ADP-ribose] polymerase 2,Poly[ADP-ribose] synthase 2
EIAAB29925 ADPRT3,ADPRT-3,ADPRTL3,Homo sapiens,hPARP-3,Human,IRT1,NAD(+) ADP-ribosyltransferase 3,pADPRT-3,PARP3,PARP-3,Poly [ADP-ribose] polymerase 3,Poly[ADP-ribose] synthase 3
E0947c ELISA kit ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
U0947c CLIA ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947c ELISA ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
18-003-42429 Poly [ADP-ribose] polymerase 1 - EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.1 mg Protein A
18-003-42430 Poly [ADP-ribose] polymerase 2 - EC 2.4.2.30; PARP-2; NAD(+) ADP-ribosyltransferase 2; Poly[ADP-ribose] synthetase 2; pADPRT-2; hPARP-2 Polyclonal 0.05 mg Aff Pur
20-272-190972 cleaved PARP - Mouse monoclonal [194C1439] to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Monoclonal 0.05 mg
17-001-30065 Poly [ADP- - EC 2.4.2.30; PARP-2; NAD(+) ADP-ribosyltransferase 2; Poly[ADP-ribose] synthetase 2; pADPRT-2; hPARP-2 Serum 0.1 mg
18-272-197066 cleaved PARP - Rabbit polyclonal to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.05 mg
18-272-197065 cleaved PARP - Rabbit polyclonal to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.05 mg
18-272-197067 cleaved PARP - Rabbit polyclonal to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur