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P54132

- BLM_HUMAN

UniProt

P54132 - BLM_HUMAN

Protein

Bloom syndrome protein

Gene

BLM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE).4 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi689 – 6968ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. annealing helicase activity Source: UniProtKB
    2. ATPase activity Source: UniProtKB
    3. ATP binding Source: UniProtKB
    4. ATP-dependent 3'-5' DNA helicase activity Source: Ensembl
    5. ATP-dependent DNA helicase activity Source: UniProtKB
    6. ATP-dependent helicase activity Source: UniProtKB
    7. bubble DNA binding Source: UniProtKB
    8. four-way junction helicase activity Source: UniProtKB
    9. G-quadruplex DNA binding Source: UniProtKB
    10. helicase activity Source: UniProtKB
    11. p53 binding Source: UniProtKB
    12. protein binding Source: UniProtKB
    13. single-stranded DNA binding Source: UniProtKB

    GO - Biological processi

    1. alpha-beta T cell differentiation Source: Ensembl
    2. ATP catabolic process Source: GOC
    3. cellular response to camptothecin Source: UniProtKB
    4. cellular response to DNA damage stimulus Source: UniProtKB
    5. cellular response to hydroxyurea Source: UniProtKB
    6. cellular response to ionizing radiation Source: UniProtKB
    7. DNA double-strand break processing Source: UniProtKB
    8. DNA duplex unwinding Source: GOC
    9. DNA recombination Source: UniProtKB
    10. DNA repair Source: UniProtKB
    11. DNA strand renaturation Source: GOC
    12. double-strand break repair via homologous recombination Source: UniProtKB
    13. G2 DNA damage checkpoint Source: UniProtKB
    14. mitotic G2 phase Source: UniProtKB
    15. negative regulation of cell division Source: UniProtKB
    16. negative regulation of DNA recombination Source: UniProtKB
    17. negative regulation of mitotic recombination Source: Ensembl
    18. negative regulation of thymocyte apoptotic process Source: Ensembl
    19. positive regulation of alpha-beta T cell proliferation Source: Ensembl
    20. positive regulation of transcription, DNA-templated Source: UniProtKB
    21. protein oligomerization Source: UniProtKB
    22. regulation of binding Source: Ensembl
    23. regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    24. replication fork processing Source: UniProtKB
    25. replication fork protection Source: UniProtKB
    26. response to X-ray Source: UniProtKB
    27. telomere maintenance Source: Ensembl

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_27271. Meiotic recombination.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bloom syndrome protein (EC:3.6.4.12)
    Alternative name(s):
    DNA helicase, RecQ-like type 2
    Short name:
    RecQ2
    RecQ protein-like 3
    Gene namesi
    Name:BLM
    Synonyms:RECQ2, RECQL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:1058. BLM.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Together with SPIDR, is redistributed in discrete nuclear DNA damage-induced foci following hydroxyurea (HU) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a RMI complex- and SPIDR-dependent manner.

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. lateral element Source: UniProtKB
    3. male germ cell nucleus Source: Ensembl
    4. nuclear chromosome Source: UniProtKB
    5. nuclear matrix Source: UniProtKB
    6. nucleolus Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. PML body Source: UniProtKB
    9. pronucleus Source: Ensembl
    10. replication fork Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Bloom syndrome (BLM) [MIM:210900]: An autosomal recessive disorder. It is characterized by proportionate pre- and postnatal growth deficiency, sun-sensitive telangiectatic hypo- and hyperpigmented skin, predisposition to malignancy, and chromosomal instability.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti672 – 6721Q → R in BLM. 1 Publication
    VAR_006901
    Natural varianti841 – 8411I → T in BLM.
    VAR_016032
    Natural varianti843 – 8431T → I in BLM. 1 Publication
    VAR_006902
    Natural varianti878 – 8781C → R in BLM. 1 Publication
    VAR_016033
    Natural varianti891 – 8911G → E in BLM.
    VAR_009138
    Natural varianti901 – 9011C → Y in BLM.
    VAR_009139
    Natural varianti1036 – 10361C → F in BLM. 1 Publication
    VAR_009140
    Natural varianti1055 – 10551C → S in BLM. 1 Publication
    VAR_006903

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi210900. phenotype.
    Orphaneti125. Bloom syndrome.
    PharmGKBiPA25369.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14171417Bloom syndrome proteinPRO_0000205039Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281Phosphoserine1 Publication
    Modified residuei48 – 481Phosphoserine1 Publication
    Modified residuei57 – 571Phosphothreonine1 Publication
    Modified residuei114 – 1141Phosphothreonine1 Publication
    Modified residuei168 – 1681Phosphoserine1 Publication
    Modified residuei171 – 1711Phosphothreonine1 Publication
    Modified residuei358 – 3581Phosphoserine1 Publication
    Modified residuei419 – 4191Phosphoserine2 Publications
    Modified residuei422 – 4221Phosphoserine2 Publications
    Modified residuei426 – 4261Phosphoserine1 Publication
    Modified residuei499 – 4991Phosphoserine2 Publications
    Modified residuei508 – 5081Phosphothreonine1 Publication
    Modified residuei863 – 8631N6-acetyllysine1 Publication
    Modified residuei1295 – 12951Phosphoserine1 Publication
    Modified residuei1296 – 12961Phosphoserine1 Publication
    Modified residuei1310 – 13101Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP54132.
    PaxDbiP54132.
    PRIDEiP54132.

    PTM databases

    PhosphoSiteiP54132.

    Miscellaneous databases

    PMAP-CutDBP54132.

    Expressioni

    Gene expression databases

    ArrayExpressiP54132.
    BgeeiP54132.
    CleanExiHS_BLM.
    GenevestigatoriP54132.

    Organism-specific databases

    HPAiHPA005689.

    Interactioni

    Subunit structurei

    Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with ubiquitinated FANCD2. Interacts with RMI complex. Interacts directly with RMI1 (via N-terminal region) component of RMI complex. Interacts with SUPV3L1. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with TOP3A (via N-terminal region). Interacts with SPIDR (via C-terminal region); the interaction is direct and required to target BLM to sites of DNA damage.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRIP1Q9BX6316EBI-621372,EBI-3509650
    FEN1P397484EBI-621372,EBI-707816
    RAD51DO757714EBI-621372,EBI-1055693
    RMI1Q9H9A710EBI-621372,EBI-621339
    RPA1P276943EBI-621372,EBI-621389
    TERF1P542743EBI-621372,EBI-710997
    TERF2Q155548EBI-621372,EBI-706637
    UIMC1Q96RL12EBI-621372,EBI-725300
    WRNQ141919EBI-621372,EBI-368417

    Protein-protein interaction databases

    BioGridi107110. 72 interactions.
    DIPiDIP-33322N.
    IntActiP54132. 22 interactions.
    MINTiMINT-131918.
    STRINGi9606.ENSP00000347232.

    Structurei

    Secondary structure

    1
    1417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi643 – 6453
    Helixi652 – 66110
    Helixi672 – 6809
    Beta strandi685 – 6884
    Helixi697 – 7059
    Beta strandi706 – 7138
    Helixi717 – 72913
    Beta strandi734 – 7418
    Helixi743 – 75311
    Beta strandi755 – 7573
    Beta strandi762 – 7654
    Helixi769 – 7724
    Helixi774 – 78512
    Beta strandi789 – 7957
    Helixi797 – 8004
    Helixi811 – 82010
    Beta strandi826 – 8305
    Helixi835 – 84511
    Beta strandi851 – 8533
    Beta strandi862 – 8687
    Helixi871 – 8733
    Helixi874 – 88512
    Beta strandi891 – 8944
    Helixi898 – 91013
    Beta strandi915 – 9195
    Helixi924 – 93512
    Beta strandi941 – 9455
    Helixi947 – 9504
    Beta strandi960 – 9656
    Helixi970 – 9778
    Turni979 – 9835
    Beta strandi987 – 9937
    Helixi995 – 100511
    Helixi1015 – 103117
    Helixi1037 – 10448
    Helixi1054 – 10574
    Helixi1059 – 10613
    Helixi1064 – 10674
    Turni1069 – 10713
    Beta strandi1074 – 10763
    Helixi1078 – 109013
    Beta strandi1096 – 10994
    Helixi1111 – 11199
    Turni1129 – 11368
    Helixi1139 – 115113
    Beta strandi1154 – 11618
    Beta strandi1163 – 11664
    Beta strandi1167 – 11737
    Helixi1177 – 11815
    Beta strandi1188 – 11903
    Helixi1195 – 11973
    Beta strandi1207 – 12093
    Helixi1210 – 123324
    Helixi1237 – 12393
    Helixi1243 – 125210
    Helixi1257 – 12604
    Beta strandi1263 – 12653
    Helixi1268 – 128316
    Turni1284 – 12885

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KV2NMR-A1210-1294[»]
    2RRDNMR-A1200-1295[»]
    3WE2X-ray2.70A/B1068-1209[»]
    3WE3X-ray2.90A/B1068-1209[»]
    4CDGX-ray2.79A/B636-1298[»]
    4CGZX-ray3.20A636-1298[»]
    4O3MX-ray2.30A640-1298[»]
    ProteinModelPortaliP54132.
    SMRiP54132. Positions 639-1295.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54132.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini676 – 851176Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini877 – 1024148Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini1212 – 129281HRDCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni301 – 600300Necessary for interaction with SPIDRAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi795 – 7984DEAH box
    Motifi1334 – 134916Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi292 – 2998Poly-Asp
    Compositional biasi310 – 3167Poly-Ser
    Compositional biasi557 – 56610Poly-Asp

    Sequence similaritiesi

    Belongs to the helicase family. RecQ subfamily.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 HRDC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0514.
    HOGENOMiHOG000095239.
    HOVERGENiHBG004850.
    InParanoidiP54132.
    KOiK10901.
    OMAiCLEWIRK.
    OrthoDBiEOG72NRPB.
    PhylomeDBiP54132.
    TreeFamiTF317801.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.150.80. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR012532. BDHCT.
    IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR004589. DNA_helicase_ATP-dep_RecQ.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR010997. HRDC-like.
    IPR002121. HRDC_dom.
    IPR027417. P-loop_NTPase.
    IPR018982. RQC_domain.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF08072. BDHCT. 1 hit.
    PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00570. HRDC. 1 hit.
    PF09382. RQC. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00341. HRDC. 1 hit.
    SM00956. RQC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47819. SSF47819. 1 hit.
    SSF52540. SSF52540. 3 hits.
    TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
    PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS50967. HRDC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54132-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVPQNNLQ EQLERHSART LNNKLSLSKP KFSGFTFKKK TSSDNNVSVT     50
    NVSVAKTPVL RNKDVNVTED FSFSEPLPNT TNQQRVKDFF KNAPAGQETQ 100
    RGGSKSLLPD FLQTPKEVVC TTQNTPTVKK SRDTALKKLE FSSSPDSLST 150
    INDWDDMDDF DTSETSKSFV TPPQSHFVRV STAQKSKKGK RNFFKAQLYT 200
    TNTVKTDLPP PSSESEQIDL TEEQKDDSEW LSSDVICIDD GPIAEVHINE 250
    DAQESDSLKT HLEDERDNSE KKKNLEEAEL HSTEKVPCIE FDDDDYDTDF 300
    VPPSPEEIIS ASSSSSKCLS TLKDLDTSDR KEDVLSTSKD LLSKPEKMSM 350
    QELNPETSTD CDARQISLQQ QLIHVMEHIC KLIDTIPDDK LKLLDCGNEL 400
    LQQRNIRRKL LTEVDFNKSD ASLLGSLWRY RPDSLDGPME GDSCPTGNSM 450
    KELNFSHLPS NSVSPGDCLL TTTLGKTGFS ATRKNLFERP LFNTHLQKSF 500
    VSSNWAETPR LGKKNESSYF PGNVLTSTAV KDQNKHTASI NDLERETQPS 550
    YDIDNFDIDD FDDDDDWEDI MHNLAASKSS TAAYQPIKEG RPIKSVSERL 600
    SSAKTDCLPV SSTAQNINFS ESIQNYTDKS AQNLASRNLK HERFQSLSFP 650
    HTKEMMKIFH KKFGLHNFRT NQLEAINAAL LGEDCFILMP TGGGKSLCYQ 700
    LPACVSPGVT VVISPLRSLI VDQVQKLTSL DIPATYLTGD KTDSEATNIY 750
    LQLSKKDPII KLLYVTPEKI CASNRLISTL ENLYERKLLA RFVIDEAHCV 800
    SQWGHDFRQD YKRMNMLRQK FPSVPVMALT ATANPRVQKD ILTQLKILRP 850
    QVFSMSFNRH NLKYYVLPKK PKKVAFDCLE WIRKHHPYDS GIIYCLSRRE 900
    CDTMADTLQR DGLAALAYHA GLSDSARDEV QQKWINQDGC QVICATIAFG 950
    MGIDKPDVRF VIHASLPKSV EGYYQESGRA GRDGEISHCL LFYTYHDVTR 1000
    LKRLIMMEKD GNHHTRETHF NNLYSMVHYC ENITECRRIQ LLAYFGENGF 1050
    NPDFCKKHPD VSCDNCCKTK DYKTRDVTDD VKSIVRFVQE HSSSQGMRNI 1100
    KHVGPSGRFT MNMLVDIFLG SKSAKIQSGI FGKGSAYSRH NAERLFKKLI 1150
    LDKILDEDLY INANDQAIAY VMLGNKAQTV LNGNLKVDFM ETENSSSVKK 1200
    QKALVAKVSQ REEMVKKCLG ELTEVCKSLG KVFGVHYFNI FNTVTLKKLA 1250
    ESLSSDPEVL LQIDGVTEDK LEKYGAEVIS VLQKYSEWTS PAEDSSPGIS 1300
    LSSSRGPGRS AAEELDEEIP VSSHYFASKT RNERKRKKMP ASQRSKRRKT 1350
    ASSGSKAKGG SATCRKISSK TKSSSIIGSS SASHTSQATS GANSKLGIMA 1400
    PPKPINRPFL KPSYAFS 1417
    Length:1,417
    Mass (Da):159,000
    Last modified:October 1, 1996 - v1
    Checksum:i423DF5F381194E11
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371K → R.1 Publication
    Corresponds to variant rs28384988 [ dbSNP | Ensembl ].
    VAR_022295
    Natural varianti298 – 2981T → M.1 Publication
    Corresponds to variant rs28384991 [ dbSNP | Ensembl ].
    VAR_022296
    Natural varianti591 – 5911R → Q.1 Publication
    Corresponds to variant rs28385012 [ dbSNP | Ensembl ].
    VAR_022297
    Natural varianti672 – 6721Q → R in BLM. 1 Publication
    VAR_006901
    Natural varianti841 – 8411I → T in BLM.
    VAR_016032
    Natural varianti843 – 8431T → I in BLM. 1 Publication
    VAR_006902
    Natural varianti868 – 8681P → L.1 Publication
    Corresponds to variant rs11852361 [ dbSNP | Ensembl ].
    VAR_022298
    Natural varianti878 – 8781C → R in BLM. 1 Publication
    VAR_016033
    Natural varianti891 – 8911G → E in BLM.
    VAR_009138
    Natural varianti901 – 9011C → Y in BLM.
    VAR_009139
    Natural varianti1036 – 10361C → F in BLM. 1 Publication
    VAR_009140
    Natural varianti1043 – 10431A → D.
    Corresponds to variant rs2229035 [ dbSNP | Ensembl ].
    VAR_051731
    Natural varianti1055 – 10551C → S in BLM. 1 Publication
    VAR_006903
    Natural varianti1205 – 12051V → I.
    Corresponds to variant rs28385141 [ dbSNP | Ensembl ].
    VAR_022299
    Natural varianti1209 – 12091S → T.
    Corresponds to variant rs1801256 [ dbSNP | Ensembl ].
    VAR_014912
    Natural varianti1213 – 12131E → K.1 Publication
    Corresponds to variant rs28385142 [ dbSNP | Ensembl ].
    VAR_022300
    Natural varianti1321 – 13211V → I.1 Publication
    Corresponds to variant rs7167216 [ dbSNP | Ensembl ].
    VAR_022301

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39817 mRNA. Translation: AAA87850.1.
    AY886902 Genomic DNA. Translation: AAW62255.1.
    BC093622 mRNA. Translation: AAH93622.1.
    BC101567 mRNA. Translation: AAI01568.1.
    BC115030 mRNA. Translation: AAI15031.1.
    BC115032 mRNA. Translation: AAI15033.1.
    CCDSiCCDS10363.1.
    PIRiA57570.
    RefSeqiNP_000048.1. NM_000057.3.
    NP_001274175.1. NM_001287246.1.
    NP_001274176.1. NM_001287247.1.
    NP_001274177.1. NM_001287248.1.
    UniGeneiHs.725208.

    Genome annotation databases

    EnsembliENST00000355112; ENSP00000347232; ENSG00000197299.
    GeneIDi641.
    KEGGihsa:641.
    UCSCiuc002bpr.3. human.

    Polymorphism databases

    DMDMi1705486.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    BLMbase

    BLM mutation db

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39817 mRNA. Translation: AAA87850.1 .
    AY886902 Genomic DNA. Translation: AAW62255.1 .
    BC093622 mRNA. Translation: AAH93622.1 .
    BC101567 mRNA. Translation: AAI01568.1 .
    BC115030 mRNA. Translation: AAI15031.1 .
    BC115032 mRNA. Translation: AAI15033.1 .
    CCDSi CCDS10363.1.
    PIRi A57570.
    RefSeqi NP_000048.1. NM_000057.3.
    NP_001274175.1. NM_001287246.1.
    NP_001274176.1. NM_001287247.1.
    NP_001274177.1. NM_001287248.1.
    UniGenei Hs.725208.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KV2 NMR - A 1210-1294 [» ]
    2RRD NMR - A 1200-1295 [» ]
    3WE2 X-ray 2.70 A/B 1068-1209 [» ]
    3WE3 X-ray 2.90 A/B 1068-1209 [» ]
    4CDG X-ray 2.79 A/B 636-1298 [» ]
    4CGZ X-ray 3.20 A 636-1298 [» ]
    4O3M X-ray 2.30 A 640-1298 [» ]
    ProteinModelPortali P54132.
    SMRi P54132. Positions 639-1295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107110. 72 interactions.
    DIPi DIP-33322N.
    IntActi P54132. 22 interactions.
    MINTi MINT-131918.
    STRINGi 9606.ENSP00000347232.

    Chemistry

    ChEMBLi CHEMBL1293237.

    PTM databases

    PhosphoSitei P54132.

    Polymorphism databases

    DMDMi 1705486.

    Proteomic databases

    MaxQBi P54132.
    PaxDbi P54132.
    PRIDEi P54132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355112 ; ENSP00000347232 ; ENSG00000197299 .
    GeneIDi 641.
    KEGGi hsa:641.
    UCSCi uc002bpr.3. human.

    Organism-specific databases

    CTDi 641.
    GeneCardsi GC15P091260.
    GeneReviewsi BLM.
    HGNCi HGNC:1058. BLM.
    HPAi HPA005689.
    MIMi 210900. phenotype.
    604610. gene.
    neXtProti NX_P54132.
    Orphaneti 125. Bloom syndrome.
    PharmGKBi PA25369.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0514.
    HOGENOMi HOG000095239.
    HOVERGENi HBG004850.
    InParanoidi P54132.
    KOi K10901.
    OMAi CLEWIRK.
    OrthoDBi EOG72NRPB.
    PhylomeDBi P54132.
    TreeFami TF317801.

    Enzyme and pathway databases

    Reactomei REACT_27271. Meiotic recombination.

    Miscellaneous databases

    EvolutionaryTracei P54132.
    GeneWikii Bloom_syndrome_protein.
    GenomeRNAii 641.
    NextBioi 2600.
    PMAP-CutDB P54132.
    PROi P54132.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54132.
    Bgeei P54132.
    CleanExi HS_BLM.
    Genevestigatori P54132.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.150.80. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR012532. BDHCT.
    IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR004589. DNA_helicase_ATP-dep_RecQ.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR010997. HRDC-like.
    IPR002121. HRDC_dom.
    IPR027417. P-loop_NTPase.
    IPR018982. RQC_domain.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF08072. BDHCT. 1 hit.
    PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00570. HRDC. 1 hit.
    PF09382. RQC. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    SM00341. HRDC. 1 hit.
    SM00956. RQC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47819. SSF47819. 1 hit.
    SSF52540. SSF52540. 3 hits.
    TIGRFAMsi TIGR00614. recQ_fam. 1 hit.
    PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS50967. HRDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Bloom's syndrome gene product is homologous to RecQ helicases."
      Ellis N.A., Groden J., Ye T.-Z., Straughen J., Lennon D.J., Ciocci S., Proytcheva M., German J.
      Cell 83:655-666(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS BLM ARG-672; ILE-843 AND SER-1055.
    2. "The Bloom's syndrome gene product is a 3'-5' DNA helicase."
      Karow J.K., Chakraverty R.K., Hickson I.D.
      J. Biol. Chem. 272:30611-30614(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: B-cell.
    3. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-137; MET-298; GLN-591; LEU-868; ILE-1205 LYS-1213 AND ILE-1321.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "BLM (the causative gene of Bloom syndrome) protein translocation into the nucleus by a nuclear localization signal."
      Kaneko H., Orii K.O., Matsui E., Shimozawa N., Fukao T., Matsumoto T., Shimamoto A., Furuichi Y., Hayakawa S., Kasahara K., Kondo N.
      Biochem. Biophys. Res. Commun. 240:348-353(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL.
    6. "BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures."
      Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.
      Genes Dev. 14:927-939(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF BLM AS MEMBER OF BASC.
    7. "BLM and the FANC proteins collaborate in a common pathway in response to stalled replication forks."
      Pichierri P., Franchitto A., Rosselli F.
      EMBO J. 23:3154-3163(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FANCD2, PHOSPHORYLATION.
    8. "The BLM helicase is necessary for normal DNA double-strand break repair."
      Langland G., Elliott J., Li Y., Creaney J., Dixon K., Groden J.
      Cancer Res. 62:2766-2770(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPAIR.
    9. "BLAP75, an essential component of Bloom's syndrome protein complexes that maintain genome integrity."
      Yin J., Sobeck A., Xu C., Meetei A.R., Hoatlin M., Li L., Wang W.
      EMBO J. 24:1465-1476(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RMI1, PHOSPHORYLATION.
    10. "A double Holliday junction dissolvasome comprising BLM, topoisomerase III alpha, and BLAP75."
      Raynard S., Bussen W., Sung P.
      J. Biol. Chem. 281:13861-13864(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RMI1.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND THR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Interaction of human SUV3 RNA/DNA helicase with BLM helicase; loss of the SUV3 gene results in mouse embryonic lethality."
      Pereira M., Mason P., Szczesny R.J., Maddukuri L., Dziwura S., Jedrzejczak R., Paul E., Wojcik A., Dybczynska L., Tudek B., Bartnik E., Klysik J., Bohr V.A., Stepien P.P.
      Mech. Ageing Dev. 128:609-617(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUPV3L1.
    13. "RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability."
      Xu D., Guo R., Sobeck A., Bachrati C.Z., Yang J., Enomoto T., Brown G.W., Hoatlin M.E., Hickson I.D., Wang W.
      Genes Dev. 22:2843-2855(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RMI1.
    14. "BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome."
      Singh T.R., Ali A.M., Busygina V., Raynard S., Fan Q., Du C.-H., Andreassen P.R., Sung P., Meetei A.R.
      Genes Dev. 22:2856-2868(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RMI1.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-57; THR-114; SER-358; SER-419; SER-422; SER-1295; SER-1296 AND SER-1310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-168; THR-171; SER-419; SER-422 AND SER-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair."
      Nimonkar A.V., Genschel J., Kinoshita E., Polaczek P., Campbell J.L., Wyman C., Modrich P., Kowalczykowski S.C.
      Genes Dev. 25:350-362(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DNA2.
    21. "Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."
      Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.
      Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SPIDR AND RAD51, INTERACTION WITH RMI1; SPIDR AND TOP3A, SUBCELLULAR LOCATION.
    22. "Characterization of a new BLM mutation associated with a topoisomerase II alpha defect in a patient with Bloom's syndrome."
      Foucault F., Vaury C., Barakat A., Thibout D., Planchon P., Jaulin C., Praz F., Amor-Gueret M.
      Hum. Mol. Genet. 6:1427-1434(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BLM PHE-1036.
    23. "Identification of a novel BLM missense mutation (2706T>C) in a Moroccan patient with Bloom's syndrome."
      Barakat A., Ababou M., Onclercq R., Dutertre S., Chadli E., Hda N., Benslimane A., Amor-Gueret M.
      Hum. Mutat. 15:584-585(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BLM ARG-878.

    Entry informationi

    Entry nameiBLM_HUMAN
    AccessioniPrimary (citable) accession number: P54132
    Secondary accession number(s): Q52M96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3