O88700 · BLM_MOUSE

  • Protein
    RecQ-like DNA helicase BLM
  • Gene
    Blm
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction (PubMed:9840919).
Participates in DNA replication and repair (By similarity).
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 (PubMed:9840919).
Negatively regulates sister chromatid exchange (SCE) (PubMed:27010503, PubMed:9840919).
Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Unwinds G-quadruplex DNA. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (By similarity).
Recruited by the KHDC3-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site676-680ATP (UniProtKB | ChEBI)
Binding site700-704ATP (UniProtKB | ChEBI)
Site7253' overhang DNA-binding
Site8163' overhang DNA-binding
Site9283' overhang DNA-binding; via amide nitrogen
Site9543' overhang DNA-binding
Site9763' overhang DNA-binding
Binding site990ATP (UniProtKB | ChEBI)
Binding site1044Zn2+ (UniProtKB | ChEBI)
Binding site1063Zn2+ (UniProtKB | ChEBI)
Binding site1071Zn2+ (UniProtKB | ChEBI)
Binding site1074Zn2+ (UniProtKB | ChEBI)
Site11153' overhang DNA-binding
Binding site1247ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromosome
Cellular Componentchromosome, telomeric region
Cellular Componentcytoplasm
Cellular Componentmale germ cell nucleus
Cellular Componentnuclear chromosome
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentpronucleus
Cellular ComponentRecQ family helicase-topoisomerase III complex
Cellular Componentreplication fork
Molecular Function3'-5' DNA helicase activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular FunctionDNA helicase activity
Molecular Functionforked DNA-dependent helicase activity
Molecular Functionfour-way junction DNA binding
Molecular Functionfour-way junction helicase activity
Molecular Functionisomerase activity
Molecular Functionprotein homodimerization activity
Molecular Functionsingle-stranded DNA binding
Molecular Functionzinc ion binding
Biological Processalpha-beta T cell differentiation
Biological Processalpha-beta T cell proliferation
Biological Processcellular response to camptothecin
Biological Processcellular response to hydroxyurea
Biological Processcellular response to ionizing radiation
Biological Processcellular response to xenobiotic stimulus
Biological Processchromosome organization
Biological ProcessDN4 thymocyte differentiation
Biological ProcessDNA damage response
Biological ProcessDNA double-strand break processing
Biological ProcessDNA repair
Biological ProcessDNA replication
Biological ProcessDNA unwinding involved in DNA replication
Biological Processdouble-strand break repair via homologous recombination
Biological ProcessG-quadruplex DNA unwinding
Biological Processimmature T cell proliferation in thymus
Biological Processmitotic recombination
Biological Processnegative regulation of mitotic recombination
Biological Processnegative regulation of thymocyte apoptotic process
Biological Processpositive regulation of alpha-beta T cell proliferation
Biological Processpositive regulation of double-strand break repair via homologous recombination
Biological Processpositive regulation of immature T cell proliferation in thymus
Biological Processprotein complex oligomerization
Biological Processprotein homooligomerization
Biological Processregulation of DNA-templated DNA replication
Biological Processreplication fork processing
Biological Processreplication-born double-strand break repair via sister chromatid exchange
Biological Processresolution of DNA recombination intermediates
Biological Processtelomere maintenance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RecQ-like DNA helicase BLM
  • EC number
  • Alternative names
    • Bloom syndrome protein homolog (mBLM)
    • DNA 3'-5' helicase BLM
    • RecQ helicase homolog

Gene names

    • Name
      Blm

Organism names

  • Taxonomic identifier
  • Strain
    • BALB/cJ
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O88700
  • Secondary accessions
    • O88198

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis264Reduces TRIM25-mediated ubiquitination in response to DNA damage. Reduces recruitment of BLM to replication forks and impairs the restart of stalled replication forks.
Mutagenesis680Reduced ATPase and helicase activities.
Mutagenesis703Reduced ATPase and helicase activities.
Mutagenesis849Reduced ATPase and helicase activities.
Mutagenesis1063Reduced ATPase and helicase activities.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 91 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00002050401-1416RecQ-like DNA helicase BLM
Modified residue28Phosphoserine
Cross-link31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue47Phosphoserine
Cross-link55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue56Phosphothreonine
Cross-link62Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue114Phosphothreonine
Cross-link129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue247Phosphoserine
Modified residue249Phosphoserine
Cross-link264Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue333Phosphoserine
Modified residue343Phosphoserine
Cross-link349Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue363Phosphoserine
Modified residue431Phosphoserine
Cross-link456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue469Phosphoserine
Cross-link481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link489Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue504Phosphoserine
Modified residue513Phosphothreonine
Cross-link536Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link596Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link602Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue871N6-acetyllysine
Cross-link1130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1202Phosphoserine
Cross-link1204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1301Phosphoserine
Modified residue1311Phosphothreonine
Cross-link1371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1394Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Post-translational modification

Poly-ubiquitinated by TRIM25 at Lys-264. Deubiquitinated by USP37; leading to stabilization in order to sustain the DNA damage response (By similarity).
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).

Keywords

Proteomic databases

PTM databases

Expression

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 (PubMed:27010503, PubMed:9840919).
Expressed in bone marrow (PubMed:27010503).

Gene expression databases

Interaction

Subunit

Monomer. Homodimer (via N-terminus). Homotetramer (via N-terminus); dimer of dimers. Homohexamer (via N-terminus). Self-association negatively regulates DNA unwinding amplitude and rate. Oligomer complexes dissociate into monomer in presence of ATP. 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 RMI complex. Interacts directly with RMI1 (via N-terminal region) component of RMI complex. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with the KHDC3/FILIA-OOEP/FLOPED scaffold complex and TRIM25 at DNA replication forks (PubMed:29125140).
Interacts with ubiquitinated FANCD2 (By similarity).
Interacts with SUPV3L1 (By similarity).
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
View interactors in UniProtKB
View CPX-3303 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain, motif.

TypeIDPosition(s)Description
Compositional bias13-31Polar residues
Region13-34Disordered
Region170-237Disordered
Compositional bias217-233Acidic residues
Region249-281Disordered
Region367-419Necessary for dimerization and homooligomerization
Domain684-859Helicase ATP-binding
Motif803-806DEAH box
Region878-8813' overhang DNA-binding
Domain885-1032Helicase C-terminal
Region905-9073' overhang DNA-binding
Region1008-10113' overhang DNA-binding
Region1102-1144DNA Holliday junction binding
Region1115-11173' overhang DNA-binding
Region1126-11303' overhang DNA-binding
Region1165-11713' overhang DNA-binding
Domain1217-1297HRDC
Region1232-1249Necessary for ssDNA and DNA Holliday junction binding
Region1295-1405Disordered
Motif1333-1348Nuclear localization signal
Compositional bias1335-1352Basic residues
Compositional bias1360-1393Polar residues

Domain

The N-terminal region mediates dimerization and homooligomerization. Both the helicase ATP-binding domain and the helicase C-terminal domain form intramolecular interactions with the HRDC domain in a ATP-dependent manner. The HRDC domain is required for single-stranded DNA (ssDNA) and DNA Holliday junction binding.

Sequence similarities

Belongs to the helicase family. RecQ subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,416
  • Mass (Da)
    158,366
  • Last updated
    1998-11-01 v1
  • Checksum
    447C8110A775DD42
MAAVPLNNLQEQLQRHSARKLNNQPSLSKPKSLGFTFKKKTSEGDVSVTSVSVVKTPALSDKDVNVSEAFSFTESPLHKPKQQAKIEGFFKHFPGRQQSKGTCSEPSLPATVQTAQDTLCTTPKTPTAKKLPVAVFKKLEFSSSADSLSDWADMDDFDMSASDAFASLAKNPATRVSTAQKMKKTKRNFFKPPPRKANAVKTDLTPPSPECLQVDLTKESEEEEEEEEEAEGADCLSRDVICIDNDSASEELTEKDTQESQSLKAHLGAERGDSEKKSHEDEAVFHSVQNTEYFEHNDNDYDIDFVPPSPEEIISTASSSLKCSSMLKDLDDSDKEKGILSTSEELLSKPEEMTTHKSDAGTSKDCDAQQIRIQQQLIHVMEHICKLVDTVPTDELEALNCGTELLQQRNIRRKLLAEAGFNGNDVRLLGSLWRHRPDSLDNTVQGDSCPVGHPNKELNSPYLLSHSPSTEECLPTTTPGKTGFSATPKNLFERPLLNSHLQKSFVSSNWAETPRMENRNESTDFPGSVLTSTTVKAQSKQAASGWNVERHGQASYDIDNFNIDDFDDDDDDDDWENIMHNFPASKSSTATYPPIKEGGPVKSLSERISSAKAKFLPVVSTAQNTNLSESIQNCSDKLAQNLSSKNPKHEHFQSLNFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNYHTKETHVNNLYSMVHYCENITECRRIQLLAYFGEKGFNPDFCKKYPDVSCDNCCKTKDYKTKDVTDDVKNIIRFVQEHSSSPGTRNIGPAGRFTLNMLVDIFLGSKSAKVKSGIFGKGTTYSRHNAERLFKKLILDKILDEDLYINANDQPIAYVMLGTKAHSVLSGHLKVDFMETENSSSIKKQKALVAKVSQREEVVKKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVLQKYSEWTVPAEDGSPGARGAPEDTEEEEEEAPVSSHYFANQTRNERKRKKMSATHKPKRRRTSYGGFRAKGGSTTCRKTTSKSKFYGVTGSRSASCASQATSSASRKLGIMAPPKPVNRTFLRPSYAFS

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9PZ97E9PZ97_MOUSEBlm1419
A0A0U1RPP0A0A0U1RPP0_MOUSEBlm155
A0A0U1RPS3A0A0U1RPS3_MOUSEBlm42
A0A0U1RNI0A0A0U1RNI0_MOUSEBlm51

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias13-31Polar residues
Sequence conflict131in Ref. 2; BAA32001
Compositional bias217-233Acidic residues
Sequence conflict229in Ref. 2; BAA32001
Sequence conflict535in Ref. 2; BAA32001
Sequence conflict546-547in Ref. 2; BAA32001
Sequence conflict574in Ref. 2; BAA32001
Sequence conflict591in Ref. 2; BAA32001
Sequence conflict621in Ref. 2; BAA32001
Sequence conflict1295in Ref. 2; BAA32001
Compositional bias1335-1352Basic residues
Compositional bias1360-1393Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z98263
EMBL· GenBank· DDBJ
CAB10933.1
EMBL· GenBank· DDBJ
mRNA
AB008674
EMBL· GenBank· DDBJ
BAA32001.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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