TOP2B_MOUSE
ID TOP2B_MOUSE Reviewed; 1612 AA.
AC Q64511; Q7TQG4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=DNA topoisomerase 2-beta;
DE EC=5.6.2.2 {ECO:0000250|UniProtKB:Q02880, ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II, beta isozyme;
GN Name=Top2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Miyaike M., Adachi N., Kikuchi A.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1509; SER-1511;
RP SER-1513; SER-1537 AND SER-1539, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1509 AND SER-1511,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1324; TYR-1358; SER-1363;
RP SER-1376; SER-1387; THR-1390; SER-1400; TYR-1408; SER-1453; SER-1460;
RP SER-1509; SER-1511; SER-1513; SER-1537; SER-1539 AND SER-1568, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-3, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP INTERACTION WITH KIAA1210.
RX PubMed=28203736; DOI=10.1095/biolreprod.116.145458;
RA Iwamori T., Iwamori N., Matsumoto M., Ono E., Matzuk M.M.;
RT "Identification of KIAA1210 as a novel X-chromosome-linked protein that
RT localizes to the acrosome and associates with the ectoplasmic
RT specialization in testes.";
RL Biol. Reprod. 96:469-477(2017).
RN [10]
RP DISRUPTION PHENOTYPE, FUNCTION, AND MUTAGENESIS OF GLU-581.
RX PubMed=31409799; DOI=10.1038/s41467-019-11570-6;
RA Broderick L., Yost S., Li D., McGeough M.D., Booshehri L.M., Guaderrama M.,
RA Brydges S.D., Kucharova K., Patel N.C., Harr M., Hakonarson H., Zackai E.,
RA Cowell I.G., Austin C.A., Huegle B., Gebauer C., Zhang J., Xu X., Wang J.,
RA Croker B.A., Frazer K.A., Putnam C.D., Hoffman H.M.;
RT "Mutations in topoisomerase IIbeta result in a B cell immunodeficiency.";
RL Nat. Commun. 10:3644-3644(2019).
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. Plays a role in B-cell
CC differentiation. {ECO:0000269|PubMed:31409799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000250|UniProtKB:Q02880,
CC ECO:0000255|PROSITE-ProRule:PRU00995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q02880,
CC ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q02880,
CC ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q02880,
CC 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:0000250|UniProtKB:Q02880,
CC ECO:0000255|PROSITE-ProRule:PRU00995};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with KIAA1210
CC (PubMed:28203736). Interacts with PLSCR1 (By similarity).
CC {ECO:0000250|UniProtKB:Q02880, ECO:0000269|PubMed:28203736}.
CC -!- INTERACTION:
CC Q64511; Q9WVE0: Aicda; NbExp=3; IntAct=EBI-2325586, EBI-3835567;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q02880}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q02880}. Nucleus {ECO:0000250|UniProtKB:Q02880}.
CC -!- DISRUPTION PHENOTYPE: Knockout animals have B-cell developmental
CC defects affecting multiple stages of development likely due to
CC transcriptional defects. These mutant mice have altered splenic
CC follicle structure with reduce marginal zone and follicular B-cell
CC zones; immunophenotyping show decreased B- cells at all stages of
CC development. Mutant mice fail to mount an antibody response to
CC vaccination and B-cells fail to proliferate in response to stimulation,
CC indicating deficits in B-cell function. {ECO:0000269|PubMed:31409799}.
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; D38046; BAA07236.1; -; mRNA.
DR EMBL; BC041106; AAH41106.1; -; mRNA.
DR EMBL; BC054541; AAH54541.1; -; mRNA.
DR CCDS; CCDS26833.1; -.
DR RefSeq; NP_033435.2; NM_009409.2.
DR AlphaFoldDB; Q64511; -.
DR SMR; Q64511; -.
DR BioGRID; 204277; 16.
DR IntAct; Q64511; 8.
DR MINT; Q64511; -.
DR STRING; 10090.ENSMUSP00000017629; -.
DR ChEMBL; CHEMBL5564; -.
DR iPTMnet; Q64511; -.
DR PhosphoSitePlus; Q64511; -.
DR EPD; Q64511; -.
DR jPOST; Q64511; -.
DR MaxQB; Q64511; -.
DR PaxDb; Q64511; -.
DR PeptideAtlas; Q64511; -.
DR PRIDE; Q64511; -.
DR ProteomicsDB; 259155; -.
DR Antibodypedia; 3893; 301 antibodies from 36 providers.
DR DNASU; 21974; -.
DR Ensembl; ENSMUST00000017629; ENSMUSP00000017629; ENSMUSG00000017485.
DR GeneID; 21974; -.
DR KEGG; mmu:21974; -.
DR UCSC; uc007shc.1; mouse.
DR CTD; 7155; -.
DR MGI; MGI:98791; Top2b.
DR VEuPathDB; HostDB:ENSMUSG00000017485; -.
DR eggNOG; KOG0355; Eukaryota.
DR GeneTree; ENSGT00940000157921; -.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; Q64511; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 117851at2759; -.
DR PhylomeDB; Q64511; -.
DR TreeFam; TF105282; -.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR BioGRID-ORCS; 21974; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Top2b; mouse.
DR PRO; PR:Q64511; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q64511; protein.
DR Bgee; ENSMUSG00000017485; Expressed in cortical plate and 263 other tissues.
DR ExpressionAtlas; Q64511; baseline and differential.
DR Genevisible; Q64511; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003916; F:DNA topoisomerase activity; ISS:UniProtKB.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0045870; P:positive regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISO:MGI.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
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; IPR028467; Top2b.
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 PANTHER; PTHR10169:SF36; PTHR10169:SF36; 1.
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; DNA-binding; Isomerase; Isopeptide bond;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Topoisomerase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..1612
FT /note="DNA topoisomerase 2-beta"
FT /id="PRO_0000145370"
FT DOMAIN 464..581
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 351..353
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 999..1008
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 1098..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1499
FT /note="Interaction with PLSCR1"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT COMPBIAS 1098..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 814
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 157..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 385..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 470
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 550
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 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 552
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 498
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 501
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 670
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 671
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 732
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 766
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 813
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 865
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 940
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1280
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1358
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1390
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1408
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1562
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1596
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 355
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 427
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 434
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 588
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 593
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 631
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 634
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 700
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1080
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1427
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT CROSSLNK 1477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02880"
FT MUTAGEN 581
FT /note="Missing: Impairs B-cell development."
FT /evidence="ECO:0000269|PubMed:31409799"
FT CONFLICT 16
FT /note="V -> A (in Ref. 1; BAA07236)"
FT /evidence="ECO:0000305"
FT CONFLICT 1434
FT /note="L -> P (in Ref. 1; BAA07236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1612 AA; 181909 MW; 974D9D5DAD0DB96A CRC64;
MAKSSLAGSD GALTWVNNAT KKEELETANK NDSTKKLSVE RVYQKKTQLE HILLRPDTYI
GSVEPLTQLM WVYDEDVGMN CREVTFVPGL YKIFDEILVN AADNKQRDKN MTCIKVSIDP
ESNIISIWNN GKGIPVVEHK VEKVYVPALI FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN
IFSTKFTVET ACKEYKHSFK QTWMNNMMKT SEAKIKHFDG EDYTCITFQP DLSKFKMEKL
DKDIVALMTR RAYDLAGSCK GVKVMFNGKK LPVNGFRSYV DLYVKDKLDE TGVALKVIHE
LANERWDVCL TLSEKGFQQI SFVNSIATTK GGRHVDYVVD QVVSKLIEVV KKKNKAGVSV
KPFQVKNHIW VFINCLIENP TFDSQTKENM TLQPKSFGSK CQLSEKFFKA ASNCGIVESI
LNWVKFKAQT QLNKKCSSVK YSKIKGIPKL DDANDAGGKH SLECTLILTE GDSAKSLAVS
GLGVIGRDRY GVFPLRGKIL NVREASHKQI MENAEINNII KIVGLQYKKS YDDAESLKTL
RYGKIMIMTD QDQDGSHIKG LLINFIHHNW PSLLKHGFLE EFITPIVKAS KNKQELSFYS
IPEFDEWKKH IENQKAWKIK YYKGLGTSTA KEAKEYFADM ERHRILFRYA GPEDDAAITL
AFSKKKIDDR KEWLTNFMED RRQRRLHGLP EQFLYGTATK HLTYNDFINK ELILFSNSDN
ERSIPSLVDG FKPGQRKVLF TCFKRNDKRE VKVAQLAGSV AEMSAYHHGE QALMMTIVNL
AQNFVGSNNI NLLQPIGQFG TRLHGGKDAA SPRYIFTMLS SLARLLFPAV DDNLLKFLYD
DNQRVEPEWY IPIIPMVLIN GAEGIGTGWA CKLPNYDARE IVNNVRRMLE GLDPHPMLPN
YKNFKGTIQE LGQNQYAVSG EIFVVDRNTV EITELPVRTW TQVYKEQVLE PMLNGTDKTP
ALISDYKEYH TDTTVKFVVK MTEEKLAQAE AAGLHKVFKL QTTLTCNSMV LFDHMGCLKK
YETVQDILKE FFDLRLSYYG LRKEWLVGML GAESTKLNNQ ARFILEKIQG KITIENRSKK
DLIQMLVQRG YESDPVKAWK EAQEKAAEEE DSQNQHDDSS SDSGTPSGPD FNYILNMSLW
SLTKEKVEEL IKQRDTKGRE VNDLKRKSPS DLWKEDLAAF VEELDKVEAQ EREDILAGMS
GKAIKGKVGK PKVKKLQLEE TMPSPYGRRI VPEITAMKAD ASRKLLKKKK GDPDTTVVKV
EFDEEFSGTP AEGTGEETLT PSAPVNKGPK PKREKKEPGT RVRKTPTSTG KTNAKKVKKR
NPWSDDESKS ESDLEEAEPV VIPRDSLLRR AAAERPKYTF DFSEEEDDDA AAADDSNDLE
ELKVKASPIT NDGEDEFVPS DGLDKDEYAF SSGKSKATPE KSSNDKKSQD FGNLFSFPSY
SQKSEDDSAK FDSNEEDTAS VFAPSFGLKQ TDKLPSKTVA AKKGKPPSDT APKAKRAPKQ
KKIVETINSD SDSEFGIPKK TTTPKGKGRG AKKRKASGSE NEGDYNPGRK PSKTASKKPK
KTSFDQDSDV DIFPSDFTSE PPALPRTGRA RKEVKYFAES DEEEDVDFAM FN
