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Database: UniProt
Entry: O88700
LinkDB: O88700
Original site: O88700 
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   11-DEC-2019, entry version 175.
DE   RecName: Full=Bloom syndrome protein homolog;
DE            Short=mBLM;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:P54132};
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, AND MUTAGENESIS.
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).
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).
CC       {ECO:0000250|UniProtKB:P54132, ECO:0000269|PubMed:27010503,
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       ubiquitinated FANCD2. Interacts with RMI complex. Interacts directly
CC       with RMI1 (via N-terminal region) component of RMI complex. Interacts
CC       with SUPV3L1. Found in a complex, at least composed of BLM, RAD51 and
CC       SPIDR; the complex formation is mediated by SPIDR. Interacts with TOP3A
CC       (via N-terminal region). Interacts with SPIDR (via C-terminal region);
CC       the interaction is direct and required to target BLM to sites of DNA
CC       damage. {ECO:0000250|UniProtKB:P54132}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Together with SPIDR,
CC       is redistributed in discrete nuclear DNA damage-induced foci following
CC       hydroxyurea (HU) or camptothecin (CPT) treatment. Accumulated at sites
CC       of DNA damage in a RMI complex- and SPIDR-dependent manner (By
CC       similarity). {ECO:0000250}.
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: 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}.
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   SMR; O88700; -.
DR   BioGrid; 198357; 1.
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   MaxQB; O88700; -.
DR   PaxDb; O88700; -.
DR   PeptideAtlas; O88700; -.
DR   PRIDE; O88700; -.
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   eggNOG; KOG0351; Eukaryota.
DR   eggNOG; COG0514; LUCA.
DR   GeneTree; ENSGT00940000156800; -.
DR   HOGENOM; HOG000095239; -.
DR   InParanoid; O88700; -.
DR   KO; K10901; -.
DR   OMA; TRNIKHV; -.
DR   OrthoDB; 445763at2759; -.
DR   PhylomeDB; O88700; -.
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-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
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   ChiTaRS; Blm; mouse.
DR   PRO; PR:O88700; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O88700; protein.
DR   Bgee; ENSMUSG00000030528; Expressed in 176 organ(s), highest expression level in embryonic stem cell.
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; ISO:MGI.
DR   GO; GO:0016605; C:PML body; ISO:MGI.
DR   GO; GO:0045120; C:pronucleus; IDA: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:0036310; F:annealing helicase activity; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATPase activity; 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:0008094; F:DNA-dependent ATPase 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: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:0072757; P:cellular response to camptothecin; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0035690; P:cellular response to drug; IGI:MGI.
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:0051276; P:chromosome organization; 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; IBA:GO_Central.
DR   GO; GO:0044806; P:G-quadruplex DNA unwinding; IMP:BHF-UCL.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; ISO: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: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-dependent DNA replication; ISS:UniProtKB.
DR   GO; GO:0031297; P:replication fork processing; ISO:MGI.
DR   GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP: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   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; 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="Bloom syndrome protein homolog"
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   NP_BIND         676..680
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P54132"
FT   NP_BIND         700..704
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P54132"
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   MOTIF           803..806
FT                   /note="DEAH box"
FT   MOTIF           1333..1348
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        219..231
FT                   /note="Poly-Glu"
FT   COMPBIAS        564..574
FT                   /note="Poly-Asp"
FT   COMPBIAS        1312..1317
FT                   /note="Poly-Glu"
FT   METAL           1044
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P54132"
FT   METAL           1063
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P54132"
FT   METAL           1071
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P54132"
FT   METAL           1074
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:P54132"
FT   BINDING         990
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:P54132"
FT   BINDING         1247
FT                   /note="ATP"
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:0000244|PubMed:21183079"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|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        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         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
//
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