TOP2A_PIG
ID TOP2A_PIG Reviewed; 1533 AA.
AC O46374;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=DNA topoisomerase 2-alpha;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II, alpha isozyme;
GN Name=TOP2A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Ito Y.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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-1106 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; AB009387; BAA23778.1; -; mRNA.
DR RefSeq; NP_999049.1; NM_213884.1.
DR AlphaFoldDB; O46374; -.
DR SMR; O46374; -.
DR STRING; 9823.ENSSSCP00000018518; -.
DR PaxDb; O46374; -.
DR PeptideAtlas; O46374; -.
DR PRIDE; O46374; -.
DR GeneID; 396917; -.
DR KEGG; ssc:396917; -.
DR CTD; 7153; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; O46374; -.
DR OMA; PMDDNIL; -.
DR OrthoDB; 117851at2759; -.
DR TreeFam; TF105282; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; O46374; SS.
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; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; 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:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
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; Reference proteome; Topoisomerase;
KW Ubl conjugation.
FT CHAIN 1..1533
FT /note="DNA topoisomerase 2-alpha"
FT /id="PRO_0000145365"
FT DOMAIN 455..572
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..344
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 990..999
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1090..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1441
FT /note="Interaction with PLSCR1"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 805
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 148..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 376..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 461
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 541
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 541
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 489
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 492
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 662
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 723
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 757
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 763
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 804
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 856
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 931
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 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1106
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1295
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 1299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1327
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1343
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1424
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1444
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1451
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 1472
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1527
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 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 386
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 397
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 466
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 529
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 599
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 614
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 625
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 632
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 655
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 662
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1075
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1367
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1387
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1461
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1494
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
SQ SEQUENCE 1533 AA; 174307 MW; 529782573BCA6BD2 CRC64;
MEVSPLQPVN ENMQVNKTKK NEEAKKRLSI ERIYQKKTQL EHILLRPDTY IGSVESVTQQ
MWVYDEDIGI NYREVTFVPG LYKIFDEILV NAADNKQRDP KMSCIRVTID PENNLISIWN
NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN YDDEEKKVTG GRNGYGAKLC NIFSTKFTVE
TASREYKKMF KQTWMDNMGR AGEMELKPFN GEDYTCITFH PDLSKFKMQS LDKDIVALMV
RRAYDIAGST KDVKVFLNGN KLPVKGFRSY VDLYLKDKVD ETGNPLKIIH EQVNHRWEVC
LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVAKLVDV VKKKNKGGVA VKAHQVKNHM
WIFVNALIEN PTFDSQTKEN MTLQVKSFGS TCQLSEKFIK AAIGCGIVES ILNWVKFKAQ
VQLNKKCSAV KHNRIKGIPK LDDANDAGGR NSTECTLILT EGDSAKTLAV SGLGVVGRDK
YGVFPLRGKI LNVREASHKQ IMENAEINNI IKIVGLQYKK NYEDEDSLKT LRYGKIMIMT
DQDQDGSHIK GLLINFIHHN WPSLLRHRFL EEFITPIVKV SKNKQEMAFY SLPEFEEWKS
STPNHKKWKV KYYKGLGTST SKEAKEYFAD MKRHRIQFKY SGPEDDAAIS LAFSKKQIDD
RKEWLTHFME DRRQRKLLGL PEDYLYGQTT TYLTYNDFIN KELILFSNSD NERSIPSMVD
GLKPGQRKVL FTCFKRNDKR EVKVAQLAGS VAEMSSYHHG EMSLMMTIIN LAQNFVGSNN
LNLLQPIGQF GTRLHGGKDS ASPRYIFTML SPLARLLFPP KDDHTLKFLY DDNQRVEPEW
YIPIIPMVLI NGAEGIGTGW SCKIPNFDVR EVVNNIRLLM DGEEPLPMLP SYKNFKGTIE
ELAPNQYVIS GEVAILNSTT IEISELPIRT WTQTYKEQVL EPMLNGTEKT PPLITDYREY
HTDTTVKFVV KMTEEKLAEA ERVGLHKVFK LQTSLTCNSM VLFDHVGCLK KYDTVLDILR
DFFELRLKYY GLRKEWLLGM LGAESAKLNN QARFILEKID GKIIIENKPK KELIKVLIQR
GYDSDPVKAW KEAQQKVPDE EENEESDNEK EADKSDSVAD SGPTFNYLLD MPLWYLTKEK
KDELCKLRNE KEQELETLKR KSPSDLWKED LAAFIEELEA VEAKEKQDEQ IGLPGKGGKA
KGKKTQMAEV LPSPCGKRVI PRVTVEMKAE AEKKIKKKIK SENTEGSPQE DGMEVEGLKQ
RLEKKQKREP GTKTKKQTTL PFKPIKKAKK RNPWSDSESD ISSDESNFNV PPREKEPRRA
AAKTKFTVDL DSDEDFSDAD EKTRDEDFVP SDTSPQKAET SPKHTNKEPK PQKSTPSVSD
FDADDAKDNV PPSPSSPVAD FPAVTETIKP VSKKNVTVKK TAAKSQSSTS TTGAKKRAAP
KGAKKDPDLD SDVSKKPNPP KPKGRRKRKP STSDDSDSNF EKMISKAVTS KKPKGESDDF
HLDLDLAVAS RAKSGRTKKP IKYLEESDED DLF
