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O88700 (BLM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bloom syndrome protein homolog

Short name=mBLM
EC=3.6.4.12
Alternative name(s):
RecQ helicase homolog
Gene names
Name:Blm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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 By similarity.

Subcellular location

Nucleus By similarity. 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 By similarity.

Tissue specificity

Highly expressed in testis 12-14 days after birth (corresponding to the pachytene phase) and at much lower levels in brain, heart, liver, lung, thymus, kidney and spleen. Ref.2

Post-translational modification

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

Sequence similarities

Belongs to the helicase family. RecQ subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 HRDC domain.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA double-strand break processing

Inferred from sequence or structural similarity. Source: UniProtKB

DNA duplex unwinding

Inferred from direct assay Ref.1. Source: GOC

DNA recombination

Inferred from electronic annotation. Source: InterPro

DNA repair

Inferred from direct assay PubMed 15364958. Source: MGI

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

alpha-beta T cell differentiation

Inferred from mutant phenotype PubMed 17210642. Source: MGI

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to camptothecin

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hydroxyurea

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to ionizing radiation

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome organization

Inferred from mutant phenotype PubMed 15450411PubMed 9808625. Source: MGI

negative regulation of mitotic recombination

Inferred from mutant phenotype PubMed 11101838PubMed 16914751PubMed 17210642PubMed 9808625. Source: MGI

negative regulation of thymocyte apoptotic process

Inferred from mutant phenotype PubMed 11046052. Source: MGI

positive regulation of alpha-beta T cell proliferation

Inferred from mutant phenotype PubMed 17210642. Source: MGI

regulation of binding

Inferred from direct assay PubMed 15364958. Source: MGI

telomere maintenance

Inferred from genetic interaction PubMed 15367665. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17982445. Source: MGI

male germ cell nucleus

Inferred from direct assay PubMed 17696610. Source: MGI

nuclear chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

pronucleus

Inferred from direct assay PubMed 17982445. Source: MGI

replication fork

Inferred from direct assay PubMed 15364958. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent 3'-5' DNA helicase activity

Inferred from direct assay Ref.1. Source: MGI

ATP-dependent DNA helicase activity

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 15364958. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14161416Bloom syndrome protein homolog
PRO_0000205040

Regions

Domain684 – 859176Helicase ATP-binding
Domain885 – 1032148Helicase C-terminal
Domain1217 – 129781HRDC
Nucleotide binding697 – 7048ATP By similarity
Motif803 – 8064DEAH box
Motif1333 – 134816Nuclear localization signal Potential
Compositional bias219 – 23113Poly-Glu
Compositional bias564 – 57411Poly-Asp
Compositional bias1312 – 13176Poly-Glu

Amino acid modifications

Modified residue281Phosphoserine By similarity
Modified residue471Phosphoserine By similarity
Modified residue561Phosphothreonine By similarity
Modified residue1141Phosphothreonine By similarity
Modified residue3631Phosphoserine By similarity
Modified residue4311Phosphoserine By similarity
Modified residue5041Phosphoserine By similarity
Modified residue5131Phosphothreonine By similarity
Modified residue8711N6-acetyllysine By similarity
Modified residue13011Phosphoserine By similarity

Experimental info

Mutagenesis6801Q → P: Reduced ATPase and helicase activities.
Mutagenesis7031K → A: Reduced ATPase and helicase activities.
Mutagenesis8491I → T: Reduced ATPase and helicase activities.
Mutagenesis10631C → S: Reduced ATPase and helicase activities.
Sequence conflict1311L → P in BAA32001. Ref.2
Sequence conflict2291E → EE in BAA32001. Ref.2
Sequence conflict5351V → M in BAA32001. Ref.2
Sequence conflict546 – 5472WN → RT in BAA32001. Ref.2
Sequence conflict5741Missing in BAA32001. Ref.2
Sequence conflict5911T → A in BAA32001. Ref.2
Sequence conflict6211T → N in BAA32001. Ref.2
Sequence conflict12951V → L in BAA32001. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88700 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 447C8110A775DD42

FASTA1,416158,366
        10         20         30         40         50         60 
MAAVPLNNLQ EQLQRHSARK LNNQPSLSKP KSLGFTFKKK TSEGDVSVTS VSVVKTPALS 

        70         80         90        100        110        120 
DKDVNVSEAF SFTESPLHKP KQQAKIEGFF KHFPGRQQSK GTCSEPSLPA TVQTAQDTLC 

       130        140        150        160        170        180 
TTPKTPTAKK LPVAVFKKLE FSSSADSLSD WADMDDFDMS ASDAFASLAK NPATRVSTAQ 

       190        200        210        220        230        240 
KMKKTKRNFF KPPPRKANAV KTDLTPPSPE CLQVDLTKES EEEEEEEEEA EGADCLSRDV 

       250        260        270        280        290        300 
ICIDNDSASE ELTEKDTQES QSLKAHLGAE RGDSEKKSHE DEAVFHSVQN TEYFEHNDND 

       310        320        330        340        350        360 
YDIDFVPPSP EEIISTASSS LKCSSMLKDL DDSDKEKGIL STSEELLSKP EEMTTHKSDA 

       370        380        390        400        410        420 
GTSKDCDAQQ IRIQQQLIHV MEHICKLVDT VPTDELEALN CGTELLQQRN IRRKLLAEAG 

       430        440        450        460        470        480 
FNGNDVRLLG SLWRHRPDSL DNTVQGDSCP VGHPNKELNS PYLLSHSPST EECLPTTTPG 

       490        500        510        520        530        540 
KTGFSATPKN LFERPLLNSH LQKSFVSSNW AETPRMENRN ESTDFPGSVL TSTTVKAQSK 

       550        560        570        580        590        600 
QAASGWNVER HGQASYDIDN FNIDDFDDDD DDDDWENIMH NFPASKSSTA TYPPIKEGGP 

       610        620        630        640        650        660 
VKSLSERISS AKAKFLPVVS TAQNTNLSES IQNCSDKLAQ NLSSKNPKHE HFQSLNFPHT 

       670        680        690        700        710        720 
KEMMKIFHKK FGLHNFRTNQ LEAINAALLG EDCFILMPTG GGKSLCYQLP ACVSPGVTIV 

       730        740        750        760        770        780 
ISPLRSLIVD QVQKLTSFDI PATYLTGDKT DSEAANIYLQ LSKKDPIIKL LYVTPEKVCA 

       790        800        810        820        830        840 
SNRLISTLEN LYERKLLARF VIDEAHCVSQ WGHDFRQDYK RMNMLRQKFP SVPVMALTAT 

       850        860        870        880        890        900 
ANPRVQKDIL TQLKILRPQV FSMSFNRHNL KYYVLPKKPK KVAFDCLEWI RKHHPYDSGI 

       910        920        930        940        950        960 
IYCLSRRECD TMADTLQREG LAALAYHAGL SDSARDEVQH KWINQDNCQV ICATIAFGMG 

       970        980        990       1000       1010       1020 
IDKPDVRFVI HASLPKSMEG YYQESGRAGR DGEISHCVLF YTYHDVTRLK RLIMMEKDGN 

      1030       1040       1050       1060       1070       1080 
YHTKETHVNN LYSMVHYCEN ITECRRIQLL AYFGEKGFNP DFCKKYPDVS CDNCCKTKDY 

      1090       1100       1110       1120       1130       1140 
KTKDVTDDVK NIIRFVQEHS SSPGTRNIGP AGRFTLNMLV DIFLGSKSAK VKSGIFGKGT 

      1150       1160       1170       1180       1190       1200 
TYSRHNAERL FKKLILDKIL DEDLYINAND QPIAYVMLGT KAHSVLSGHL KVDFMETENS 

      1210       1220       1230       1240       1250       1260 
SSIKKQKALV AKVSQREEVV KKCLGELTEV CKLLGKVFGV HYFNIFNTAT LKKLAESLSS 

      1270       1280       1290       1300       1310       1320 
DPEVLLQIDG VTEDKLEKYG AEVIPVLQKY SEWTVPAEDG SPGARGAPED TEEEEEEAPV 

      1330       1340       1350       1360       1370       1380 
SSHYFANQTR NERKRKKMSA THKPKRRRTS YGGFRAKGGS TTCRKTTSKS KFYGVTGSRS 

      1390       1400       1410 
ASCASQATSS ASRKLGIMAP PKPVNRTFLR PSYAFS 

« Hide

References

[1]"Point mutations causing Bloom's syndrome abolish ATPase and DNA helicase activities of the BLM protein."
Bahr A., de Graeve F., Kedinger C., Chatton B.
Oncogene 17:2565-2571(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS.
[2]"cDNA cloning of mouse BLM gene, the homologue to human Bloom's syndrome gene, which is highly expressed in the testis at the mRNA level."
Seki T., Wang W.-S., Okumura N., Seki M., Katada T., Enomoto T.
Biochim. Biophys. Acta 1398:377-381(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Brain, Spermatocyte and Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z98263 mRNA. Translation: CAB10933.1.
AB008674 mRNA. Translation: BAA32001.1.
CCDSCCDS40000.1.
RefSeqNP_001035992.1. NM_001042527.2.
NP_031576.4. NM_007550.4.
UniGeneMm.12932.

3D structure databases

ProteinModelPortalO88700.
SMRO88700. Positions 648-1299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-27643N.

PTM databases

PhosphoSiteO88700.

Proteomic databases

PaxDbO88700.
PRIDEO88700.

Protocols and materials databases

DNASU12144.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081314; ENSMUSP00000080062; ENSMUSG00000030528.
GeneID12144.
KEGGmmu:12144.
UCSCuc009iax.2. mouse.

Organism-specific databases

CTD641.
MGIMGI:1328362. Blm.

Phylogenomic databases

eggNOGCOG0514.
GeneTreeENSGT00550000074520.
HOGENOMHOG000095239.
HOVERGENHBG004850.
InParanoidO88700.
KOK10901.
PhylomeDBO88700.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressO88700.
BgeeO88700.
CleanExMM_BLM.
GenevestigatorO88700.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.150.80. 1 hit.
3.40.50.300. 2 hits.
InterProIPR012532. 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]
PfamPF08072. BDHCT. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
[Graphical view]
SUPFAMSSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsTIGR00614. recQ_fam. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBLM. mouse.
NextBio280473.
PROO88700.
SOURCESearch...

Entry information

Entry nameBLM_MOUSE
AccessionPrimary (citable) accession number: O88700
Secondary accession number(s): O88198
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot