TOP2A_CRIGR
ID TOP2A_CRIGR Reviewed; 1526 AA.
AC P41515;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=DNA topoisomerase 2-alpha;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:8380592};
DE AltName: Full=DNA topoisomerase II, alpha isozyme;
GN Name=TOP2A; Synonyms=TOP-2, TOP2;
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], AND VARIANT GLN-493.
RX PubMed=8380592; DOI=10.1016/s0021-9258(18)53976-4;
RA Chan V.T., Ng S.W., Eder J.P., Schnipper L.E.;
RT "Molecular cloning and identification of a point mutation in the
RT topoisomerase II cDNA from an etoposide-resistant Chinese hamster ovary
RT cell line.";
RL J. Biol. Chem. 268:2160-2165(1993).
CC -!- FUNCTION: Key decatenating enzyme that alters DNA topology by binding
CC to two double-stranded DNA molecules, generating a double-stranded
CC break in one of the strands, passing the intact strand through the
CC broken strand, and religating the broken strand (By similarity). May
CC play a role in regulating the period length of ARNTL/BMAL1
CC transcriptional oscillation (By similarity).
CC {ECO:0000250|UniProtKB:P11388, ECO:0000250|UniProtKB:Q01320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with COPS5 (By
CC similarity). Interacts with RECQL5; this stimulates DNA decatenation
CC (By similarity). Interacts with SETMAR; stimulates the topoisomerase
CC activity (By similarity). Interacts with DHX9; this interaction occurs
CC in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates
CC DHX9-mediated double-stranded DNA and RNA duplex helicase activity and
CC stimulates TOP2A-mediated supercoiled DNA relaxation activity (By
CC similarity). Interacts with HNRNPU (via C-terminus); this interaction
CC protects the topoisomerase TOP2A from degradation and positively
CC regulates the relaxation of supercoiled DNA in a RNA-dependent manner
CC (By similarity). Interacts with MCM3AP (By similarity). Interacts with
CC ERCC6 (By similarity). Interacts with PLSCR1 (By similarity). Interacts
CC with GCNA; this interaction allows the resolution of topoisomerase II
CC (TOP2A) DNA-protein cross-links (By similarity).
CC {ECO:0000250|UniProtKB:P11388, ECO:0000250|UniProtKB:P41516,
CC ECO:0000250|UniProtKB:Q01320}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11388}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus
CC {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P11388}.
CC -!- PTM: Phosphorylation has no effect on catalytic activity (By
CC similarity). However, phosphorylation at Ser-1105 by CSNK1D/CK1
CC promotes DNA cleavable complex formation (By similarity).
CC {ECO:0000250|UniProtKB:P11388}.
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; L04607; AAA37023.1; -; mRNA.
DR PIR; A44406; A44406.
DR RefSeq; NP_001233667.1; NM_001246738.1.
DR AlphaFoldDB; P41515; -.
DR SMR; P41515; -.
DR STRING; 10029.NP_001233667.1; -.
DR Ensembl; ENSCGRT00001026641; ENSCGRP00001022396; ENSCGRG00001020913.
DR GeneID; 100689304; -.
DR KEGG; cge:100689304; -.
DR CTD; 7153; -.
DR eggNOG; KOG0355; Eukaryota.
DR GeneTree; ENSGT00940000157539; -.
DR OMA; PMDDNIL; -.
DR OrthoDB; 117851at2759; -.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0030263; P:apoptotic chromosome condensation; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0006266; P:DNA ligation; IEA:Ensembl.
DR GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
DR GO; GO:0040016; P:embryonic cleavage; IEA:Ensembl.
DR GO; GO:0007143; P:female meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:1905463; P:negative regulation of DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045870; P:positive regulation of single stranded viral RNA replication via double stranded DNA intermediate; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR InterPro; IPR012542; DTHCT.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF08070; DTHCT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Biological rhythms; Cytoplasm; DNA-binding;
KW Isomerase; Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Topoisomerase; Ubl conjugation.
FT CHAIN 1..1526
FT /note="DNA topoisomerase 2-alpha"
FT /id="PRO_0000145362"
FT DOMAIN 454..571
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..343
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 989..998
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1089..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1434
FT /note="Interaction with PLSCR1"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT COMPBIAS 1252..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1342
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 804
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 147..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 375..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 488
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 491
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 660
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 661
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 722
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 756
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 762
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 803
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 855
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 930
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1105
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1242
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1349
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1417
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1437
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 17
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 351
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 598
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 621
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 631
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 675
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1074
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1380
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT VARIANT 493
FT /note="R -> Q (in cells resistant to the antineoplastic
FT agents VP-16 and VM-26)"
FT /evidence="ECO:0000269|PubMed:8380592"
SQ SEQUENCE 1526 AA; 173197 MW; 5FB2D8FBF1C02929 CRC64;
MELSPLQPVN ENMQMNKKKN EDAKKRLSIE RIYQKKTQLE HILLRPDTYI GSVELVTQQM
WVYDEDVGIN YREVTFVPGL YKIFDEILVN AADNKQRDPK MSCIRVTIDP ENNLISIWNN
GKGIPVVEHK VEKMYVPALI FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTRFTVET
ASKEYKKMFK QTWMDNMGRA GDMELKPFNG EDYTCITFQP DLSKFKMQSL DKDIVALMVR
RAYDIAGSTK DVKVFLNGNK LPVKGFRSYV DMYLKDKLDE TGNALKVVHE QVNPRWEVCL
TMSEKGFQQI SFVNSIATSK GGRHVDYVAD QIVSKLVDVV KKKNKGGVAV KAHQVKNHMW
IFVNALIENP TFDSQTKENM TLQAKSFGST CQLSEKFIKA AIGCGIVESI LNWVKFKAQI
QLNKKCSAVK HNRIKGIPKL DDANDAGSRN STECTLILTE GDSAKTLAVS GLGVVGRDKY
GVFPLRGKIL NVREASHKQI MENAEINNII KIVGLQYKKN YEDEDSLKTL RYGKIMIMTD
QDQDGSHIKG LLINFIHHNW PSLLRHRFLE EFITPIVKVS KNKQELAFYS LPEFEEWKSS
TPNHKKWKVK YYKGLGTSTS KEAKEYFADM KRHRIQFKYS GPEDDAAISL AFSKKQVDDR
KEWLTHFMED RRQRKLLGLP EDYLYGQTTT YLTYNDFINK ELILFSNSDN ERSIPSMVDG
LKPGQRKVLF TCFKRNDKRE VKVAQLAGSV AEMSSYHHGE MSLMMTIINL AQNFVGSNNL
NLLQPIGQFG TRLHGGKDSA SPRYIFTMLS PLTRLLFPPK DDHTLKFLYD DNQRVEPEWY
IPIIPMVLIN GAEGIGTGWS CKIPNFDIRE VVNNIRRLLD GEEPLPMLPS YKNFKGTIEE
LASNQYVING EVAILNSTTI EISELPIRTW TQTYKEQVLE PMLNGTEKTP PLITDYREYH
TDTTVKFVIK MTEEKLAEAE RVGLHKVFKL QTSLTCNSMV LFDHVGCLKK YDTVLDILKD
FFELRLKYYG LRKEWLLGML GAESAKLNNQ ARFILEKIDG KIIIENKPKK ELIKVLIQRG
YDSDPVKAWK EAQQKVPDEE ENEESDNENS DSVAESGPTF NYLLDMPLWY LTKEKKDELC
KQRNEKEQEL NTLKNKSPSD LWKEDLAVFI EELEVVEAKE KQDEQVGLPG KGGKAKGKKA
QMSEVLPSPH GKRVIPQVTM EMKAEAEKKI RKKIKSENVE GTPTENGLEL GSLKQRIEKK
QKKEPGAMTK KQTTLAFKPI KKGKKRNPWS DSESDMSSNE SNVDVPPREK DPRRAATKAK
FTMDLDSDED FSGSDGKDED EDFFPLDTTP PKTKIPQKNT KKALKPQKSA MSGDPESDEK
DSVPASPGPP AADLPADTEQ LKPSSKQTVA VKKTATKSQS STSTAGTKKR AVPKGSKSDS
ALNAHGPEKP VPAKAKNSRK RKQSSSDDSD SDFEKVVSKV AASKKSKGEN QDFRVDLDET
MVPRAKSGRA KKPIKYLEES DDDDLF
