PARP1_CRIGR
ID PARP1_CRIGR Reviewed; 1013 AA.
AC Q9R152;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11382339; DOI=10.1080/09553000110036133;
RA Ganesh A., Phillips E., Thacker J., Meuth M.;
RT "Suppression of the radiation-sensitive phenotype of hamster irs1 and irs2
RT strains selected for resistance to 3-aminobenzamide.";
RL Int. J. Radiat. Biol. 77:609-616(2001).
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-520 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; AF168781; AAD45817.1; -; mRNA.
DR RefSeq; NP_001233650.1; NM_001246721.1.
DR AlphaFoldDB; Q9R152; -.
DR SMR; Q9R152; -.
DR STRING; 10029.NP_001233650.1; -.
DR ChEMBL; CHEMBL2321638; -.
DR PRIDE; Q9R152; -.
DR GeneID; 100689463; -.
DR KEGG; cge:100689463; -.
DR CTD; 142; -.
DR eggNOG; KOG1037; Eukaryota.
DR OrthoDB; 909382at2759; -.
DR PRO; PR:Q9R152; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CHAIN 2..1013
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000211319"
FT DOMAIN 385..476
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 541..637
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 661..778
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 787..1013
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 113..203
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 198..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..523
FT /note="Automodification domain"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT REGION 495..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..209
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOTIF 221..226
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT ACT_SITE 987
FT /note="For poly [ADP-ribose] polymerase activity"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT BINDING 861..863
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 870
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 877
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 903
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 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 274
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 387
FT /note="PolyADP-ribosyl aspartic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 407
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 413
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 435
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 444
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 445
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 456
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 471
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 484
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 488
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 491
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 499
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 503
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 512
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 513
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 518
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 519
FT /note="PolyADP-ribosyl glutamic acid"
FT /evidence="ECO:0000255"
FT MOD_RES 520
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 599
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 620
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 511
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 747
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT CROSSLNK 747
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P09874"
SQ SEQUENCE 1013 AA; 112532 MW; 90617C4DB91C9DEC CRC64;
MAEASERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV
GHSIRQPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD GSGGKSEKTL GDFAAEYAKS
NRSTCKGCME KIEKGQVRLS KKMLDPEKPQ LGMIDRWYHP TCFVKNREEL GFRPEYSASQ
LKGFSLLSAE DKEVLKKQLP GVKSEGKRKG DEVDGADEVA KKKSKKGKDK DSKLEKALKA
QNDLIWNIKD ELKKACSTSD LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG
QLVFKSDAYY CTGDVTAWTK CMVKTQTPSR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE
TSAPAPPHLP PSVTSAPTAV NSSCPADKPL SNMKILTLGK LSQSKDEAKA TIEKLGGKLT
GSANNASLCI STKKEVEKMG KKMEEVQAAN VRVVCEDFLQ DVAASTKSLQ ELLSAHSLSS
WGAEVKVEPV EVAAPKGKSA APSKKSKGLY KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH
SAHVLEKGGK VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR VGTVIGSNKL
EQMPSKEDAV EHFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA VKKLTVKPGT
KSKLPKAVQE LVGMIFDVES MKKALVEYEI DLQKMPLGKL SKRQIQAAYS ILSEVQQAVS
QGSSDSQILD LSNRFYTLIP HDFGMKKPPL LNNADSVQAK VEMLDNLLDI EVAYSLLRGG
SDDSSKDPID VNYEKLKTDI KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVMDIFKIER
EGESQRYKPF KQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV
SKSANYCHTS QGDPIGLILL GEVALGNMYE LKHASHISKL PKGKHSVKGL GKTTPDPSAS
ITLEGVEVPL GTGIPSGVND TCLLYNEYIV YDIAQVNLKY LLKLKFNFKT SLW
