ID BLM_MOUSE Reviewed; 1416 AA. AC O88700; O88198; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 196. DE RecName: Full=RecQ-like DNA helicase BLM; DE EC=5.6.2.4 {ECO:0000269|PubMed:9655940}; DE AltName: Full=Bloom syndrome protein homolog; DE Short=mBLM; DE AltName: Full=DNA 3'-5' helicase BLM {ECO:0000305}; DE AltName: Full=RecQ helicase homolog; GN Name=Blm; 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], FUNCTION, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF GLN-680; LYS-703; ILE-849 AND CYS-1063. RX PubMed=9840919; DOI=10.1038/sj.onc.1202389; RA Bahr A., de Graeve F., Kedinger C., Chatton B.; RT "Point mutations causing Bloom's syndrome abolish ATPase and DNA helicase RT activities of the BLM protein."; RL Oncogene 17:2565-2571(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=BALB/cJ; TISSUE=Brain, Spermatocyte, and Testis; RX PubMed=9655940; DOI=10.1016/s0167-4781(98)00066-9; RA Seki T., Wang W.-S., Okumura N., Seki M., Katada T., Enomoto T.; RT "cDNA cloning of mouse BLM gene, the homologue to human Bloom's syndrome RT gene, which is highly expressed in the testis at the mRNA level."; RL Biochim. Biophys. Acta 1398:377-381(1998). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-249 AND THR-1311, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [4] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=27010503; DOI=10.1371/journal.pone.0152278; RA Braun J., Meixner A., Brachner A., Foisner R.; RT "The GIY-YIG type endonuclease ankyrin repeat and LEM domain-containing RT protein 1 (ANKLE1) is dispensable for mouse hematopoiesis."; RL PLoS ONE 11:E0152278-E0152278(2016). RN [5] RP FUNCTION, INTERACTION WITH KHDC3; OOEP AND TRIM25, SUBCELLULAR LOCATION, RP UBIQUITINATION AT LYS-264, AND MUTAGENESIS OF LYS-264. RX PubMed=29125140; DOI=10.1038/cr.2017.139; RA Zhao B., Zhang W., Cun Y., Li J., Liu Y., Gao J., Zhu H., Zhou H., RA Zhang R., Zheng P.; RT "Mouse embryonic stem cells have increased capacity for replication fork RT restart driven by the specific Filia-Floped protein complex."; RL Cell Res. 28:69-89(2018). CC -!- FUNCTION: ATP-dependent DNA helicase that unwinds single- and double- CC stranded DNA in a 3'-5' direction (PubMed:9840919). Participates in DNA CC replication and repair (By similarity). Involved in 5'-end resection of CC DNA during double-strand break (DSB) repair: unwinds DNA and recruits CC DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:9840919). CC Negatively regulates sister chromatid exchange (SCE) (PubMed:9840919, CC PubMed:27010503). Stimulates DNA 4-way junction branch migration and CC DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), CC forked duplex DNA and DNA Holliday junction (By similarity). Recruited CC by the KHDC3-OOEP scaffold to DNA replication forks where it is CC retained by TRIM25 ubiquitination, it thereby promotes the restart of CC stalled replication forks. {ECO:0000250|UniProtKB:P54132, CC ECO:0000269|PubMed:27010503, ECO:0000269|PubMed:29125140, CC ECO:0000269|PubMed:9840919}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by CC translocating in the 3'-5' direction.; EC=5.6.2.4; CC Evidence={ECO:0000269|PubMed:9655940}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:9655940}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P54132}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P54132}; CC -!- SUBUNIT: Monomer. Homodimer (via N-terminus). Homotetramer (via N- CC terminus); dimer of dimers. Homohexamer (via N-terminus). Self- CC association negatively regulates DNA unwinding amplitude and rate. CC Oligomer complexes dissociate into monomer in presence of ATP. Part of CC the BRCA1-associated genome surveillance complex (BASC), which contains CC BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 CC protein complex. This association could be a dynamic process changing CC throughout the cell cycle and within subnuclear domains. Interacts with CC RMI complex. Interacts directly with RMI1 (via N-terminal region) CC component of RMI complex. Found in a complex, at least composed of BLM, CC RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts CC with the KHDC3/FILIA-OOEP/FLOPED scaffold complex and TRIM25 at DNA CC replication forks (PubMed:29125140). Interacts with ubiquitinated CC FANCD2 (By similarity). Interacts with SUPV3L1 (By similarity). CC Interacts with TOP3A (via N-terminal region). Interacts with SPIDR (via CC C-terminal region); the interaction is direct and required to target CC BLM to sites of DNA damage. {ECO:0000250|UniProtKB:P54132, CC ECO:0000269|PubMed:29125140}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29125140}. CC Note=Localized to DNA replication forks, especially after DNA damage. CC {ECO:0000269|PubMed:29125140}. CC -!- TISSUE SPECIFICITY: Highly expressed in testis 12-14 days after birth CC (corresponding to the pachytene phase) and at much lower levels in CC brain, heart, liver, lung, thymus, kidney and spleen (PubMed:9840919, CC PubMed:27010503). Expressed in bone marrow (PubMed:27010503). CC {ECO:0000269|PubMed:27010503, ECO:0000269|PubMed:9655940}. CC -!- DOMAIN: The N-terminal region mediates dimerization and CC homooligomerization. Both the helicase ATP-binding domain and the CC helicase C-terminal domain form intramolecular interactions with the CC HRDC domain in a ATP-dependent manner. The HRDC domain is required for CC single-stranded DNA (ssDNA) and DNA Holliday junction binding. CC {ECO:0000250|UniProtKB:P54132}. CC -!- PTM: Poly-ubiquitinated by TRIM25 at Lys-264. Deubiquitinated by USP37; CC leading to stabilization in order to sustain the DNA damage response CC (By similarity). {ECO:0000250|UniProtKB:P54132, CC ECO:0000269|PubMed:29125140}. CC -!- PTM: Phosphorylated in response to DNA damage. Phosphorylation requires CC the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the CC presence of RMI1 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily. CC {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; Z98263; CAB10933.1; -; mRNA. DR EMBL; AB008674; BAA32001.1; -; mRNA. DR CCDS; CCDS40000.1; -. DR RefSeq; NP_001035992.1; NM_001042527.2. DR RefSeq; NP_031576.4; NM_007550.4. DR AlphaFoldDB; O88700; -. DR SMR; O88700; -. DR BioGRID; 198357; 8. DR ComplexPortal; CPX-3303; BTR double Holliday Junction dissolution complex. DR CORUM; O88700; -. DR DIP; DIP-27643N; -. DR STRING; 10090.ENSMUSP00000127995; -. DR iPTMnet; O88700; -. DR PhosphoSitePlus; O88700; -. DR EPD; O88700; -. DR jPOST; O88700; -. DR MaxQB; O88700; -. DR PaxDb; 10090-ENSMUSP00000127995; -. DR PeptideAtlas; O88700; -. DR ProteomicsDB; 281695; -. DR Pumba; O88700; -. DR Antibodypedia; 704; 556 antibodies from 37 providers. DR DNASU; 12144; -. DR Ensembl; ENSMUST00000081314.11; ENSMUSP00000080062.5; ENSMUSG00000030528.13. DR GeneID; 12144; -. DR KEGG; mmu:12144; -. DR UCSC; uc009iax.2; mouse. DR AGR; MGI:1328362; -. DR CTD; 641; -. DR MGI; MGI:1328362; Blm. DR VEuPathDB; HostDB:ENSMUSG00000030528; -. DR eggNOG; KOG0351; Eukaryota. DR GeneTree; ENSGT00940000156800; -. DR HOGENOM; CLU_001103_1_1_1; -. DR InParanoid; O88700; -. DR OMA; FHVMEDI; -. DR OrthoDB; 5474026at2759; -. DR PhylomeDB; O88700; -. DR Reactome; R-MMU-174414; Processive synthesis on the C-strand of the telomere. DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates. DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange. DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends. DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange. DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint. DR BioGRID-ORCS; 12144; 8 hits in 116 CRISPR screens. DR ChiTaRS; Blm; mouse. DR PRO; PR:O88700; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; O88700; Protein. DR Bgee; ENSMUSG00000030528; Expressed in embryonic post-anal tail and 166 other cell types or tissues. DR ExpressionAtlas; O88700; baseline and differential. DR GO; GO:0005694; C:chromosome; IBA:GO_Central. DR GO; GO:0000781; C:chromosome, telomeric region; IMP:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0000800; C:lateral element; ISO:MGI. DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI. DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; ISO:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; ISO:MGI. DR GO; GO:0045120; C:pronucleus; IDA:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; ISO:MGI. DR GO; GO:0005657; C:replication fork; IDA:MGI. DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:MGI. DR GO; GO:1905773; F:8-hydroxy-2'-deoxyguanosine DNA binding; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI. DR GO; GO:0000405; F:bubble DNA binding; ISO:MGI. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB. DR GO; GO:1990814; F:DNA/DNA annealing activity; ISO:MGI. DR GO; GO:0061749; F:forked DNA-dependent helicase activity; ISS:UniProtKB. DR GO; GO:0000400; F:four-way junction DNA binding; ISS:UniProtKB. DR GO; GO:0009378; F:four-way junction helicase activity; ISS:UniProtKB. DR GO; GO:0051880; F:G-quadruplex DNA binding; ISO:MGI. DR GO; GO:0004386; F:helicase activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0140677; F:molecular function activator activity; ISO:MGI. DR GO; GO:0002039; F:p53 binding; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB. DR GO; GO:0061821; F:telomeric D-loop binding; ISO:MGI. DR GO; GO:0061849; F:telomeric G-quadruplex DNA binding; ISO:MGI. DR GO; GO:0000403; F:Y-form DNA binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI. DR GO; GO:0046633; P:alpha-beta T cell proliferation; IMP:MGI. DR GO; GO:0072757; P:cellular response to camptothecin; ISS:UniProtKB. DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB. DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IGI:MGI. DR GO; GO:0051276; P:chromosome organization; IMP:MGI. DR GO; GO:1904157; P:DN4 thymocyte differentiation; IMP:MGI. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0000729; P:DNA double-strand break processing; ISS:UniProtKB. DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI. DR GO; GO:0006281; P:DNA repair; IDA:MGI. DR GO; GO:0006260; P:DNA replication; IMP:BHF-UCL. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI. DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IMP:BHF-UCL. DR GO; GO:0033080; P:immature T cell proliferation in thymus; IMP:MGI. DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:MGI. DR GO; GO:0006312; P:mitotic recombination; IMP:MGI. DR GO; GO:0051782; P:negative regulation of cell division; ISO:MGI. DR GO; GO:0045910; P:negative regulation of DNA recombination; ISO:MGI. DR GO; GO:0045950; P:negative regulation of mitotic recombination; IMP:UniProtKB. DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IMP:MGI. DR GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IMP:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IGI:MGI. DR GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IMP:MGI. DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB. DR GO; GO:0090329; P:regulation of DNA-templated DNA replication; ISS:UniProtKB. DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB. DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:MGI. DR GO; GO:0071139; P:resolution of DNA recombination intermediates; ISO:MGI. DR GO; GO:0010165; P:response to X-ray; ISO:MGI. DR GO; GO:0000723; P:telomere maintenance; IGI:MGI. DR GO; GO:0061820; P:telomeric D-loop disassembly; ISO:MGI. DR CDD; cd18016; DEXHc_RecQ2_BLM; 1. DR CDD; cd18794; SF2_C_RecQ; 1. DR Gene3D; 1.10.150.80; HRDC domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR012532; BDHCT. DR InterPro; IPR032439; BDHCT_assoc. DR InterPro; IPR032437; BLM_N. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS. DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR010997; HRDC-like_sf. DR InterPro; IPR002121; HRDC_dom. DR InterPro; IPR044876; HRDC_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR032284; RecQ_Zn-bd. DR InterPro; IPR018982; RQC_domain. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR NCBIfam; TIGR00614; recQ_fam; 1. DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1. DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1. DR Pfam; PF08072; BDHCT; 1. DR Pfam; PF16204; BDHCT_assoc; 1. DR Pfam; PF16202; BLM_N; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF00570; HRDC; 1. DR Pfam; PF16124; RecQ_Zn_bind; 1. DR Pfam; PF09382; RQC; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00341; HRDC; 1. DR SMART; SM00956; RQC; 1. DR SUPFAM; SSF47819; HRDC-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50967; HRDC; 1. DR Genevisible; O88700; MM. PE 1: Evidence at protein level; KW Acetylation; ATP-binding; DNA damage; DNA repair; DNA replication; KW DNA-binding; Helicase; Hydrolase; Isomerase; Isopeptide bond; KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Ubl conjugation; Zinc. FT CHAIN 1..1416 FT /note="RecQ-like DNA helicase BLM" FT /id="PRO_0000205040" FT DOMAIN 684..859 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000250|UniProtKB:P54132, FT ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 885..1032 FT /note="Helicase C-terminal" FT /evidence="ECO:0000250|UniProtKB:P54132, FT ECO:0000255|PROSITE-ProRule:PRU00542" FT DOMAIN 1217..1297 FT /note="HRDC" FT /evidence="ECO:0000250|UniProtKB:P54132, FT ECO:0000255|PROSITE-ProRule:PRU00328" FT REGION 13..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 170..237 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 249..281 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 367..419 FT /note="Necessary for dimerization and homooligomerization" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 878..881 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 905..907 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 1008..1011 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 1102..1144 FT /note="DNA Holliday junction binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 1115..1117 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 1126..1130 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 1165..1171 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 1232..1249 FT /note="Necessary for ssDNA and DNA Holliday junction FT binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT REGION 1295..1405 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 803..806 FT /note="DEAH box" FT MOTIF 1333..1348 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 13..31 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 217..233 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1335..1352 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1360..1393 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 676..680 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P54132" FT BINDING 700..704 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P54132" FT BINDING 990 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P54132" FT BINDING 1044 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P54132" FT BINDING 1063 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P54132" FT BINDING 1071 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P54132" FT BINDING 1074 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P54132" FT BINDING 1247 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P54132" FT SITE 725 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT SITE 816 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT SITE 928 FT /note="3' overhang DNA-binding; via amide nitrogen" FT /evidence="ECO:0000250|UniProtKB:P54132" FT SITE 954 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT SITE 976 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT SITE 1115 FT /note="3' overhang DNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 28 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 56 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 114 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 249 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 343 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 363 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 431 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 469 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 504 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 513 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 871 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 1202 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 1301 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MOD_RES 1311 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 31 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 38 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 55 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 62 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 91 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 129 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 191 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 201 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 264 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:29125140" FT CROSSLNK 349 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 456 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 481 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 489 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 503 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 536 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 540 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 596 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 602 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 612 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 1130 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 1204 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 1212 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 1371 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT CROSSLNK 1394 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P54132" FT MUTAGEN 264 FT /note="K->R: Reduces TRIM25-mediated ubiquitination in FT response to DNA damage. Reduces recruitment of BLM to FT replication forks and impairs the restart of stalled FT replication forks." FT /evidence="ECO:0000269|PubMed:29125140" FT MUTAGEN 680 FT /note="Q->P: Reduced ATPase and helicase activities." FT /evidence="ECO:0000269|PubMed:9840919" FT MUTAGEN 703 FT /note="K->A: Reduced ATPase and helicase activities." FT /evidence="ECO:0000269|PubMed:9840919" FT MUTAGEN 849 FT /note="I->T: Reduced ATPase and helicase activities." FT /evidence="ECO:0000269|PubMed:9840919" FT MUTAGEN 1063 FT /note="C->S: Reduced ATPase and helicase activities." FT /evidence="ECO:0000269|PubMed:9840919" FT CONFLICT 131 FT /note="L -> P (in Ref. 2; BAA32001)" FT /evidence="ECO:0000305" FT CONFLICT 229 FT /note="E -> EE (in Ref. 2; BAA32001)" FT /evidence="ECO:0000305" FT CONFLICT 535 FT /note="V -> M (in Ref. 2; BAA32001)" FT /evidence="ECO:0000305" FT CONFLICT 546..547 FT /note="WN -> RT (in Ref. 2; BAA32001)" FT /evidence="ECO:0000305" FT CONFLICT 574 FT /note="Missing (in Ref. 2; BAA32001)" FT /evidence="ECO:0000305" FT CONFLICT 591 FT /note="T -> A (in Ref. 2; BAA32001)" FT /evidence="ECO:0000305" FT CONFLICT 621 FT /note="T -> N (in Ref. 2; BAA32001)" FT /evidence="ECO:0000305" FT CONFLICT 1295 FT /note="V -> L (in Ref. 2; BAA32001)" FT /evidence="ECO:0000305" SQ SEQUENCE 1416 AA; 158366 MW; 447C8110A775DD42 CRC64; MAAVPLNNLQ EQLQRHSARK LNNQPSLSKP KSLGFTFKKK TSEGDVSVTS VSVVKTPALS DKDVNVSEAF SFTESPLHKP KQQAKIEGFF KHFPGRQQSK GTCSEPSLPA TVQTAQDTLC TTPKTPTAKK LPVAVFKKLE FSSSADSLSD WADMDDFDMS ASDAFASLAK NPATRVSTAQ KMKKTKRNFF KPPPRKANAV KTDLTPPSPE CLQVDLTKES EEEEEEEEEA EGADCLSRDV ICIDNDSASE ELTEKDTQES QSLKAHLGAE RGDSEKKSHE DEAVFHSVQN TEYFEHNDND YDIDFVPPSP EEIISTASSS LKCSSMLKDL DDSDKEKGIL STSEELLSKP EEMTTHKSDA GTSKDCDAQQ IRIQQQLIHV MEHICKLVDT VPTDELEALN CGTELLQQRN IRRKLLAEAG FNGNDVRLLG SLWRHRPDSL DNTVQGDSCP VGHPNKELNS PYLLSHSPST EECLPTTTPG KTGFSATPKN LFERPLLNSH LQKSFVSSNW AETPRMENRN ESTDFPGSVL TSTTVKAQSK QAASGWNVER HGQASYDIDN FNIDDFDDDD DDDDWENIMH NFPASKSSTA TYPPIKEGGP VKSLSERISS AKAKFLPVVS TAQNTNLSES IQNCSDKLAQ NLSSKNPKHE HFQSLNFPHT KEMMKIFHKK FGLHNFRTNQ LEAINAALLG EDCFILMPTG GGKSLCYQLP ACVSPGVTIV ISPLRSLIVD QVQKLTSFDI PATYLTGDKT DSEAANIYLQ LSKKDPIIKL LYVTPEKVCA SNRLISTLEN LYERKLLARF VIDEAHCVSQ WGHDFRQDYK RMNMLRQKFP SVPVMALTAT ANPRVQKDIL TQLKILRPQV FSMSFNRHNL KYYVLPKKPK KVAFDCLEWI RKHHPYDSGI IYCLSRRECD TMADTLQREG LAALAYHAGL SDSARDEVQH KWINQDNCQV ICATIAFGMG IDKPDVRFVI HASLPKSMEG YYQESGRAGR DGEISHCVLF YTYHDVTRLK RLIMMEKDGN YHTKETHVNN LYSMVHYCEN ITECRRIQLL AYFGEKGFNP DFCKKYPDVS CDNCCKTKDY KTKDVTDDVK NIIRFVQEHS SSPGTRNIGP AGRFTLNMLV DIFLGSKSAK VKSGIFGKGT TYSRHNAERL FKKLILDKIL DEDLYINAND QPIAYVMLGT KAHSVLSGHL KVDFMETENS SSIKKQKALV AKVSQREEVV KKCLGELTEV CKLLGKVFGV HYFNIFNTAT LKKLAESLSS DPEVLLQIDG VTEDKLEKYG AEVIPVLQKY SEWTVPAEDG SPGARGAPED TEEEEEEAPV SSHYFANQTR NERKRKKMSA THKPKRRRTS YGGFRAKGGS TTCRKTTSKS KFYGVTGSRS ASCASQATSS ASRKLGIMAP PKPVNRTFLR PSYAFS //