BLM_MOUSE
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 03-AUG-2022, entry version 187.
DE RecName: Full=RecQ-like DNA helicase BLM;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P54132};
DE AltName: Full=Bloom syndrome protein homolog;
DE Short=mBLM;
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, TISSUE SPECIFICITY, AND MUTAGENESIS
RP 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=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; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:P54132};
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.
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}.
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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; O88700; -.
DR PeptideAtlas; O88700; -.
DR PRIDE; O88700; -.
DR ProteomicsDB; 281695; -.
DR Antibodypedia; 704; 500 antibodies from 37 providers.
DR DNASU; 12144; -.
DR Ensembl; ENSMUST00000081314; ENSMUSP00000080062; ENSMUSG00000030528.
DR GeneID; 12144; -.
DR KEGG; mmu:12144; -.
DR UCSC; uc009iax.2; mouse.
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; CGRFTMN; -.
DR OrthoDB; 445763at2759; -.
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 111 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 163 other tissues.
DR ExpressionAtlas; O88700; baseline and differential.
DR Genevisible; O88700; MM.
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: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: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:0006974; P:cellular response to DNA damage stimulus; 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:1901655; P:cellular response to ketone; IGI:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IGI:MGI.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; IGI:MGI.
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:0000729; P:DNA double-strand break processing; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
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: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:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0051098; P:regulation of binding; IDA:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
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 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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.80; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00614; recQ_fam; 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.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Isopeptide bond; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW 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
