PARP1_BOVIN
ID PARP1_BOVIN Reviewed; 1016 AA.
AC P18493; Q9TS00;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Poly [ADP-ribose] polymerase 1;
DE Short=PARP-1;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1;
DE Short=ARTD1;
DE AltName: Full=DNA ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 1;
DE Short=ADPRT 1;
DE AltName: Full=Poly[ADP-ribose] synthase 1;
DE AltName: Full=Protein poly-ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=PARP1; Synonyms=ADPRT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2119324; DOI=10.1016/0378-1119(90)90187-v;
RA Saito I., Hatakeyama K., Kido T., Ohkubo H., Nakanishi S., Ueda K.;
RT "Cloning of a full-length cDNA encoding bovine thymus poly(ADP-ribose)
RT synthetase: evolutionarily conserved segments and their potential
RT functions.";
RL Gene 90:249-254(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 648-715 AND 839-904.
RX PubMed=2450019; DOI=10.1111/j.1432-1033.1988.tb13826.x;
RA Taniguchi T., Yamauchi K., Yamamoto T., Toyoshima K., Harada N., Tanaka H.,
RA Takahashi S., Yamamoto H., Fujimoto S.;
RT "Depression in gene expression for poly(ADP-ribose) synthetase during the
RT interferon-gamma-induced activation process of murine macrophage tumor
RT cells.";
RL Eur. J. Biochem. 171:571-575(1988).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair. Mediates
CC glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins:
CC the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor
CC carboxyl group of target residues and further ADP-ribosyl groups are
CC transferred to the 2'-position of the terminal adenosine moiety,
CC building up a polymer with an average chain length of 20-30 units.
CC Serine ADP-ribosylation of proteins constitutes the primary form of
CC ADP-ribosylation of proteins in response to DNA damage. Mainly mediates
CC glutamate and aspartate ADP-ribosylation of target proteins in absence
CC of HPF1. Following interaction with HPF1, catalyzes serine ADP-
CC ribosylation of target proteins; HPF1 conferring serine specificity by
CC completing the PARP1 active site. Also catalyzes tyrosine ADP-
CC ribosylation of target proteins following interaction with HPF1. PARP1
CC initiates the repair of DNA breaks: recognizes and binds DNA breaks
CC within chromatin and recruits HPF1, licensing serine ADP-ribosylation
CC of target proteins, such as histones, thereby promoting decompaction of
CC chromatin and the recruitment of repair factors leading to the
CC reparation of DNA strand breaks. In addition to base excision repair
CC (BER) pathway, also involved in double-strand breaks (DSBs) repair:
CC together with TIMELESS, accumulates at DNA damage sites and promotes
CC homologous recombination repair by mediating poly-ADP-ribosylation.
CC Mediates the poly(ADP-ribosyl)ation of a number of proteins, including
CC itself, APLF and CHFR. In addition to proteins, also able to ADP-
CC ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini
CC containing terminal phosphates and a 2'-OH group in single- and double-
CC stranded DNA, respectively. Required for PARP9 and DTX3L recruitment to
CC DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination
CC promotes the rapid and specific recruitment of 53BP1/TP53BP1,
CC UIMC1/RAP80, and BRCA1 to DNA damage sites. Acts as a regulator of
CC transcription: positively regulates the transcription of MTUS1 and
CC negatively regulates the transcription of MTUS2/TIP150. Plays a role in
CC the positive regulation of IFNG transcription in T-helper 1 cells as
CC part of an IFNG promoter-binding complex with TXK and EEF1A1. Involved
CC in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and
CC NUDT5. Nuclear ATP generation is required for extensive chromatin
CC remodeling events that are energy-consuming.
CC {ECO:0000250|UniProtKB:P09874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142556; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142557; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- SUBUNIT: Homo- and heterodimer with PARP2. Interacts with APTX (By
CC similarity). Component of a base excision repair (BER) complex,
CC containing at least XRCC1, PARP1, PARP2, POLB and LRIG3 (By
CC similarity). Interacts with SRY (By similarity). The SWAP complex
CC consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 (By
CC similarity). Interacts with PARP3; leading to activate PARP1 in absence
CC of DNA (By similarity). Interacts (when poly-ADP-ribosylated) with
CC CHD1L (via macro domain). Interacts with the DNA polymerase alpha
CC catalytic subunit POLA1; this interaction functions as part of the
CC control of replication fork progression. Interacts with EEF1A1 and TXK.
CC Interacts with RNF4. Interacts with RNF146. Interacts with ZNF423.
CC Interacts with APLF. Interacts with SNAI1 (via zinc fingers); the
CC interaction requires SNAI1 to be poly-ADP-ribosylated and non-
CC phosphorylated (active) by GSK3B. Interacts (when poly-ADP-ribosylated)
CC with PARP9 (By similarity). Interacts with NR4A3; activates PARP1 by
CC improving acetylation of PARP1 and suppressing the interaction between
CC PARP1 and SIRT1 (By similarity). Interacts (via catalytic domain) with
CC PUM3; the interaction inhibits the poly-ADP-ribosylation activity of
CC PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress.
CC Interacts (via the PARP catalytic domain) with HPF1. Interacts with
CC ZNF365. Interacts with RRP1B. Interacts with TIMELESS; the interaction
CC is direct. Interacts with CGAS; leading to impede the formation of the
CC PARP1-TIMELESS complex (By similarity). Interacts with KHDC3, the
CC interaction is increased following the formation of DNA double-strand
CC breaks (By similarity). {ECO:0000250|UniProtKB:P09874,
CC ECO:0000250|UniProtKB:P11103, ECO:0000250|UniProtKB:P27008}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09874}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P09874}. Chromosome
CC {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage.
CC {ECO:0000250|UniProtKB:P09874}.
CC -!- DOMAIN: The N-terminal disordered region does not act as a key DNA-
CC binding domain. The WGR and PARP catalytic domains function together to
CC recruit PARP1 to sites of DNA breaks. The N-terminal disordered region
CC is only required for activation on specific types of DNA damage.
CC {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- DOMAIN: The WGR domain bridges two nucleosomes, with the broken DNA
CC aligned in a position suitable for ligation. The bridging induces
CC structural changes in PARP1 that signal the recognition of a DNA break
CC to the catalytic domain of PARP1, promoting HPF1 recruitment and
CC subsequent activation of PARP1, licensing serine ADP-ribosylation of
CC target proteins. {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- PTM: Poly-ADP-ribosylated on glutamate and aspartate residues by
CC autocatalysis. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation
CC mediates the recruitment of CHD1L to DNA damage sites. ADP-ribosylated
CC on serine by autocatalysis; serine ADP-ribosylation takes place
CC following interaction with HPF1 (By similarity). Auto poly-ADP-
CC ribosylated on serine residues, leading to dissociation of the PARP1-
CC HPF1 complex from chromatin (By similarity). Mono-ADP-ribosylated at
CC Lys-523 by SIRT6 in response to oxidative stress, promoting recruitment
CC to double-strand breaks (DSBs) sites (By similarity).
CC {ECO:0000250|UniProtKB:P09874, ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- PTM: S-nitrosylated, leading to inhibit transcription regulation
CC activity. {ECO:0000250|UniProtKB:P11103}.
CC -!- PTM: Phosphorylated by PRKDC and TXK. {ECO:0000250|UniProtKB:P09874}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; D90073; BAA14114.1; -; mRNA.
DR EMBL; X06986; CAA30046.1; -; mRNA.
DR EMBL; X06987; CAA30047.1; -; mRNA.
DR PIR; JS0428; JS0428.
DR RefSeq; NP_777176.1; NM_174751.2.
DR AlphaFoldDB; P18493; -.
DR SMR; P18493; -.
DR STRING; 9913.ENSBTAP00000001113; -.
DR BindingDB; P18493; -.
DR ChEMBL; CHEMBL5691; -.
DR PaxDb; P18493; -.
DR PeptideAtlas; P18493; -.
DR PRIDE; P18493; -.
DR GeneID; 286764; -.
DR KEGG; bta:286764; -.
DR CTD; 142; -.
DR eggNOG; KOG1037; Eukaryota.
DR InParanoid; P18493; -.
DR OrthoDB; 909382at2759; -.
DR PRO; PR:P18493; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005635; C:nuclear envelope; ISS:AgBase.
DR GO; GO:0005730; C:nucleolus; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0018424; P:peptidyl-glutamic acid poly-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; ISS:UniProtKB.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
DR InterPro; IPR038650; PADR1_dom_sf.
DR InterPro; IPR008288; PARP.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08063; PADR1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 2.
DR PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS00347; PARP_ZN_FINGER_1; 2.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
DR PROSITE; PS51977; WGR; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ADP-ribosylation; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Glycosyltransferase; Isopeptide bond; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CHAIN 2..1016
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000211318"
FT DOMAIN 387..478
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 544..640
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 664..781
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 790..1016
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 9..93
FT /note="PARP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT ZN_FING 116..206
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 360..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..526
FT /note="Automodification domain"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT REGION 494..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 210..212
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOTIF 224..229
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT COMPBIAS 509..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 990
FT /note="For poly [ADP-ribose] polymerase activity"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT BINDING 864..866
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 873
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 880
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 906
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 134
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 389
FT /note="PolyADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 409
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 415
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 437
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 446
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 447
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 450
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 458
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 473
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 486
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 490
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 493
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 501
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 506
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 509
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 515
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 516
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 521
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 522
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 523
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 602
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 623
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 206
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 206
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 530
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
SQ 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
