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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_BOVIN             Reviewed;        1016 AA.
P18493; Q9TS00;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 163.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2119324; DOI=10.1016/0378-1119(90)90187-V;
Saito I., Hatakeyama K., Kido T., Ohkubo H., Nakanishi S., Ueda K.;
"Cloning of a full-length cDNA encoding bovine thymus poly(ADP-ribose)
synthetase: evolutionarily conserved segments and their potential
functions.";
Gene 90:249-254(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 648-715 AND 839-904.
PubMed=2450019; DOI=10.1111/j.1432-1033.1988.tb13826.x;
Taniguchi T., Yamauchi K., Yamamoto T., Toyoshima K., Harada N.,
Tanaka H., Takahashi S., Yamamoto H., Fujimoto S.;
"Depression in gene expression for poly(ADP-ribose) synthetase during
the interferon-gamma-induced activation process of murine macrophage
tumor cells.";
Eur. J. Biochem. 171:571-575(1988).
-!- 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:
Reaction=NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide +
(ADP-D-ribosyl)(n+1)-acceptor.; EC=2.4.2.30;
Evidence={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 and 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. Interacts (when poly-ADP-
ribosylated) with PARP9. Interacts with NR4A3; activates PARP1 by
improving acetylation of PARP1 and suppressing the interaction
between PARP1 and SIRT1. 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.
Interacts with RRP1B. {ECO:0000250|UniProtKB:P09874,
ECO:0000250|UniProtKB:P27008}.
-!- 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.
-----------------------------------------------------------------------
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EMBL; D90073; BAA14114.1; -; mRNA.
EMBL; X06986; CAA30046.1; -; mRNA.
EMBL; X06987; CAA30047.1; -; mRNA.
PIR; JS0428; JS0428.
RefSeq; NP_777176.1; NM_174751.2.
UniGene; Bt.4803; -.
ProteinModelPortal; P18493; -.
SMR; P18493; -.
STRING; 9913.ENSBTAP00000001113; -.
BindingDB; P18493; -.
ChEMBL; CHEMBL5691; -.
PaxDb; P18493; -.
PeptideAtlas; P18493; -.
PRIDE; P18493; -.
GeneID; 286764; -.
KEGG; bta:286764; -.
CTD; 142; -.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
HOGENOM; HOG000030402; -.
HOVERGEN; HBG053513; -.
InParanoid; P18493; -.
KO; K10798; -.
PRO; PR:P18493; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005635; C:nuclear envelope; ISS:AgBase.
GO; GO:0005730; C:nucleolus; ISS:AgBase.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
GO; GO:1990404; F:protein ADP-ribosylase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; ISS:UniProtKB.
GO; GO:0070212; P:protein poly-ADP-ribosylation; IBA:GO_Central.
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.
2: Evidence at transcript level;
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 1016 Poly [ADP-ribose] polymerase 1.
/FTId=PRO_0000211318.
DOMAIN 387 478 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 664 781 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 790 1016 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
DNA_BIND 2 375
ZN_FING 9 93 PARP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
ZN_FING 116 206 PARP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
REGION 376 526 Automodification domain.
MOTIF 210 212 Nuclear localization signal.
MOTIF 224 229 Nuclear localization signal.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 100 100 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 134 134 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 409 409 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 415 415 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 437 437 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 446 446 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 447 447 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 450 450 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 458 458 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 473 473 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 486 486 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 490 490 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 493 493 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 501 501 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 509 509 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 515 515 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 516 516 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 521 521 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 522 522 PolyADP-ribosyl glutamic acid.
{ECO:0000255}.
MOD_RES 602 602 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 623 623 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 784 784 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
MOD_RES 788 788 Phosphoserine.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 206 206 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 206 206 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 252 252 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 488 488 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 488 488 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 514 514 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 530 530 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P09874}.
CROSSLNK 750 750 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P09874}.
SEQUENCE 1016 AA; 113486 MW; 11630D94F04F5B02 CRC64;
MAESSDKLYR VEYAKSGRAS CKKCKESIPK DSIRMAFMVE SPMFDGKIPH WYHLSCFWKV
GFSIWHPDVE VEGFSELRWD DQQTIKKMAE TGGRTDVSGK GQDGVGSKTE KTLIDFGAGY
AKSNRSTCKS CMEKIDKGQV RLSKKVVYPD KPQLGMVDCW YHPKCFVQKR EELGFRPEFS
ATHLMGFSVL TAEDQETLKK QLPAIKGERK RKGDEVDGID EVTKKKSKKE KDKEIKLEKA
LKAQNDLIWN VKDELKKACS TNDLKELLIF NKQEVPSGES AILDRVADGM VFGALLPCEE
CSGQLVFKGD AYYCTGDVTA WTKCMVKTQT PNRKEWVTPK EFREISYFKK LKIKKQDRIF
PPESSTPVGA AAPPSAASAP AAVHSGPPDK PLSNMKILTL GKLSQNKDEV KATIEKLGGK
LTGTANKASL CISTKKEVDK LNKKMEEVKE ANIRVVSEDF LQDISASTKS LQELLSTHLL
SPWGAEVKVE PVEAVGPKGK SGAAPSKKSK GPVKEEGTNK SEKRMKLTLK GGAAVDPDSG
LEHNAHVLEK GGKVFSATLG LVDIVKGTNS YYKLQLLEDD KESRYWIFRS WGRVGTVIGS
NKLEQMPSKE DAIEHFMKLY EEKTGNAWHS KNFTKHPKKF YPLEIDYGQD EEAVKKLTVN
PGTKSKLPKP VQNLIKMIFD VESMKKAMVE YEIDLQKMPL GKLSKRQIQA AYSILSEVQQ
ALSQGSSDSH ILDLSNRFYT LIPHDFGMKK PPLLNNANSV QAKVEMLDNL LDIEVAYSLL
RGGSDDSSKD PIDVNYEKLK TDIKVVDKDS EEAEIIRKYV KNTHATTHNA YDLEVVDIFK
IEREGESQRY KPFKQLHNRR LLWHGSRTTN FAGILSQGLR IAPPEAPVTG YMFGKGIYFA
DMVSKSANYC HTSQGDPIGL ILLGEAALGN MYELKHARHI SKLPKGKHSV KGLGKTTPDP
SASITVDGVE VPLGTGISSG VNDTCLLYNE YIVYDIAQVH LKYLLKLKFN FKTSLW


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