TOP2A_RAT
ID TOP2A_RAT Reviewed; 1526 AA.
AC P41516;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
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; Synonyms=Top-2, Top2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8390253; DOI=10.1006/bbrc.1993.1694;
RA Park S.H., Yoon J.H., Kwon Y.D., Park S.D.;
RT "Nucleotide sequence analysis of the cDNA for rat DNA topoisomerase II.";
RL Biochem. Biophys. Res. Commun. 193:787-793(1993).
RN [2]
RP INTERACTION WITH HNRNPU.
RX PubMed=20554522; DOI=10.1074/jbc.m110.112979;
RA Kawano S., Miyaji M., Ichiyasu S., Tsutsui K.M., Tsutsui K.;
RT "Regulation of DNA Topoisomerase IIbeta through RNA-dependent association
RT with heterogeneous nuclear ribonucleoprotein U (hnRNP U).";
RL J. Biol. Chem. 285:26451-26460(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1210; SER-1328;
RP SER-1333; THR-1350; SER-1383 AND SER-1387, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (PubMed:20554522). Interacts with MCM3AP (By similarity). Interacts
CC with ERCC6 (By similarity). Interacts with PLSCR1 (By similarity).
CC Interacts with GCNA; this interaction allows the resolution of
CC topoisomerase II (TOP2A) DNA-protein cross-links (By similarity).
CC {ECO:0000250|UniProtKB:P11388, ECO:0000250|UniProtKB:Q01320,
CC ECO:0000269|PubMed:20554522}.
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.
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; Z46372; CAA86496.1; -; mRNA.
DR EMBL; Z19552; CAA79611.1; -; mRNA.
DR EMBL; Z29676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A48536; A48536.
DR PIR; JN0598; JN0598.
DR RefSeq; NP_071519.2; NM_022183.2.
DR AlphaFoldDB; P41516; -.
DR SMR; P41516; -.
DR BioGRID; 261906; 3.
DR IntAct; P41516; 1.
DR STRING; 10116.ENSRNOP00000040257; -.
DR ChEMBL; CHEMBL3400; -.
DR iPTMnet; P41516; -.
DR PhosphoSitePlus; P41516; -.
DR jPOST; P41516; -.
DR PaxDb; P41516; -.
DR PRIDE; P41516; -.
DR GeneID; 360243; -.
DR KEGG; rno:360243; -.
DR CTD; 7153; -.
DR RGD; 62048; Top2a.
DR eggNOG; KOG0355; Eukaryota.
DR InParanoid; P41516; -.
DR OrthoDB; 117851at2759; -.
DR PhylomeDB; P41516; -.
DR BRENDA; 5.6.2.2; 5301.
DR BRENDA; 5.99.1.3; 5301.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR PRO; PR:P41516; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:RGD.
DR GO; GO:0000793; C:condensed chromosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0003916; F:DNA topoisomerase activity; IDA:RGD.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0030263; P:apoptotic chromosome condensation; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IEP:RGD.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEP:RGD.
DR GO; GO:0030261; P:chromosome condensation; ISO:RGD.
DR GO; GO:0007059; P:chromosome segregation; ISO:RGD.
DR GO; GO:0006266; P:DNA ligation; ISO:RGD.
DR GO; GO:0006265; P:DNA topological change; IDA:RGD.
DR GO; GO:0040016; P:embryonic cleavage; ISO:RGD.
DR GO; GO:0007143; P:female meiotic nuclear division; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:1905463; P:negative regulation of DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0045870; P:positive regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
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:0010212; P:response to ionizing radiation; IEP:RGD.
DR GO; GO:0071107; P:response to parathyroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 1: Evidence at protein 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..1526
FT /note="DNA topoisomerase 2-alpha"
FT /id="PRO_0000145366"
FT DOMAIN 453..570
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 340..342
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 988..997
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1087..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1435
FT /note="Interaction with PLSCR1"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT COMPBIAS 1229..1244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 803
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 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 146..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 374..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 459
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 539
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 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 SITE 487
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 490
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 659
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 721
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 755
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 761
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 802
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 854
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT SITE 929
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:0007744|PubMed:22673903"
FT MOD_RES 280
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1293
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 1298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1323
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1418
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1438
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01320"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT MOD_RES 1521
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 154
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 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 395
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 414
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 423
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 464
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 582
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 612
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 630
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 637
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 653
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 674
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1073
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1359
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 1369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT CROSSLNK 1488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11388"
SQ SEQUENCE 1526 AA; 173221 MW; A1961ABBDB1B050F CRC64;
MELSPLQPVN ENMLLNKKKN EDGKKRLSVE RIYQKKTQLE HILLRPDTYI GSVELVTQQM
WVYDEDVGIN YREVTFVPGL YKIFDEILVN AADNKQRDPK MSCIRVTMMR NNLISIWNNG
KGIPVVEHKV EKMYVPALIF GQLLTSSNYD DDEKKVTGGR NGYGAKLCNI FSTKFTVETA
SREYKKMFKQ TWMDNMGRAG DMELKPFSGE DYTCITFQPD LSKFKMQSLD KDIVALMVRR
AYDIAGSTKD VKVFLNGNRL PVKGFRSYVD MYLKDKVDET GNALKVVHEQ VNPRWEVCLT
MSEKGFQQIS FVNSIATSKG GRHVDYVADQ IVSKLVDVVK KKNKGGVAVK ADQVKNHMWI
FGNAVIENPT FDSQTKENMT LQAKSFGSTC QLSEKFIKAA IGCGIVESIL NWVKFKAQIQ
LNKKCSAVKH NRIKGIPKLD DANDAGSRNS AECTLILTEG DSAKTLAVSG LGVVGRDKYG
VFPLRGKILN VREASHKQIM ENAEINNIIK IVGLQYKKNY EDEDSLKTLR YGKIMIMTDQ
DQDGSHIKGL LINFIHHNWP SLLRHRFLEE FITPIVKVSK NKQEIAFYSL PEFEEWKSTN
PNHKKWKVKY YKGLGTSTSK EAKEYFANMK RHRIQFKYSG PEDDAAISLA FSKKQVDDRK
EWLTNFMEDR RQRKLLGLPE DYLYGQTTMY LTYNDFINKE LILFSNSDNE RSIPSMVDGL
KPGQRKVLFT CFKRNDKREV KVAQLAGSVA EMSSYHHGEM SLMMTIINLA QNFVGSNNLN
LLQPIGQFGT RLHGGKDSAS PRYIFTMLSP LARLLFPSKD DHTLRFLYDD NQRVEPEWYI
PIIPMVLING AEGIGTGWSC KIPNFDVREV VNNIRRLLDG EEPLPMLPSY KNYKGTIEEL
ASNQYVINGE VAILNSTTIE ITELPIRTWT QTYKEQVLEP MLNGTEKTPP LITDYREYHT
DTTVKFVIKM TEEKLAEAER VGLHKVFKLQ TSLTCNSMVL FDHVGCLKKY DTVLDILRDF
FELRLKYYGL RKEWLLGMLG AESSKLNNQA RFILEKIDGK IVIENKPKKE LIKVLIQRGY
DSDPVKAWKE AQQKVPEEEE NEENEESESE STSPAAESGP TFNYLLDMPL WYLTKEKKDE
LCKQRDEKEQ ELNTLKKKTP SDLWKEDLAA FVEELEVVEA KEKQDEQVGL PGKGVKAKGK
KAQISEVLPS PVGKRVIPQV TMEMRAEAEK KIRRKIKSEN VEGTPAEDGA EPGLRQRLEK
RQKREPGTRA KKQTTLPFKP IKKAQKQNPW SDSESDMSSN ESNFDVPPRE KEPRIAATKA
KFTADLDSDD DFSGLDEKDE DEDFFPLDDT PPKTKMPPKN TKKALKPQKS STSVDLESDG
KDSVPASPGA SAADVPAETE PSKPSSKQTV GVKRTITKGQ SLTSTAGTKK RAVPKETKSD
SALNAHVSKK PAPAKAKNSR KRMPSSSDSS DSEFEKAISK GATSKKLKGE ERDFHVDLDD
TVAPRAKSGR ARKPIKYLEE SDDDLF
