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 24-JAN-2024, entry version 205. 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, RC Pancreas, 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, ECO:0000255|PROSITE- CC ProRule:PRU00995}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q02880, ECO:0000255|PROSITE- CC ProRule:PRU00995}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000250|UniProtKB:Q02880, ECO:0000255|PROSITE- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyGen; Q64511; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q64511; -. DR PhosphoSitePlus; Q64511; -. DR EPD; Q64511; -. DR jPOST; Q64511; -. DR MaxQB; Q64511; -. DR PaxDb; 10090-ENSMUSP00000017629; -. DR PeptideAtlas; Q64511; -. DR ProteomicsDB; 259155; -. DR Pumba; Q64511; -. DR Antibodypedia; 3893; 331 antibodies from 36 providers. DR DNASU; 21974; -. DR Ensembl; ENSMUST00000017629.12; ENSMUSP00000017629.5; ENSMUSG00000017485.12. DR GeneID; 21974; -. DR KEGG; mmu:21974; -. DR UCSC; uc007shc.1; mouse. DR AGR; MGI:98791; -. 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; 1944951at2759; -. DR PhylomeDB; Q64511; -. DR TreeFam; TF105282; -. DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins. DR BioGRID-ORCS; 21974; 5 hits in 80 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 266 other cell types or tissues. DR ExpressionAtlas; Q64511; baseline and differential. DR Genevisible; Q64511; MM. DR GO; GO:0005829; C:cytosol; 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; IMP:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl. DR GO; GO:0007409; P:axonogenesis; IMP:MGI. DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB. DR GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl. 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:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl. 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; cd16930; HATPase_TopII-like; 1. DR CDD; cd00187; TOP4c; 1. DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1. DR CDD; cd03365; TOPRIM_TopoIIA; 1. DR Gene3D; 3.30.1360.40; -; 1. DR Gene3D; 3.30.1490.30; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1. DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1. DR InterPro; IPR012542; DTHCT. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_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; IPR001154; TopoII_euk. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR031660; TOPRIM_C. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034157; TOPRIM_TopoII. DR PANTHER; PTHR10169:SF36; DNA TOPOISOMERASE 2-BETA; 1. DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 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 PRINTS; PR01158; TOPISMRASEII. DR PRINTS; PR00418; TPI2FAMILY. DR SMART; SM00433; TOP2c; 1. DR SMART; SM00434; TOP4c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1. DR PROSITE; PS52040; TOPO_IIA; 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 DOMAIN 724..1177 FT /note="Topo IIA-type catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384" 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:0000255|PROSITE-ProRule:PRU01384" 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 //