O88700 · BLM_MOUSE
- ProteinRecQ-like DNA helicase BLM
- GeneBlm
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1416 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
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
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 676-680 | ATP (UniProtKB | ChEBI) | ||||
Sequence: FRTNQ | ||||||
Binding site | 700-704 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GGGKS | ||||||
Site | 725 | 3' overhang DNA-binding | ||||
Sequence: R | ||||||
Site | 816 | 3' overhang DNA-binding | ||||
Sequence: R | ||||||
Site | 928 | 3' overhang DNA-binding; via amide nitrogen | ||||
Sequence: A | ||||||
Site | 954 | 3' overhang DNA-binding | ||||
Sequence: T | ||||||
Site | 976 | 3' overhang DNA-binding | ||||
Sequence: K | ||||||
Binding site | 990 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1044 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1063 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1071 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1074 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 1115 | 3' overhang DNA-binding | ||||
Sequence: T | ||||||
Binding site | 1247 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRecQ-like DNA helicase BLM
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO88700
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized to DNA replication forks, especially after DNA damage.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 264 | Reduces TRIM25-mediated ubiquitination in response to DNA damage. Reduces recruitment of BLM to replication forks and impairs the restart of stalled replication forks. | ||||
Sequence: K → R | ||||||
Mutagenesis | 680 | Reduced ATPase and helicase activities. | ||||
Sequence: Q → P | ||||||
Mutagenesis | 703 | Reduced ATPase and helicase activities. | ||||
Sequence: K → A | ||||||
Mutagenesis | 849 | Reduced ATPase and helicase activities. | ||||
Sequence: I → T | ||||||
Mutagenesis | 1063 | Reduced ATPase and helicase activities. | ||||
Sequence: C → S |
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.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000205040 | 1-1416 | RecQ-like DNA helicase BLM | |||
Sequence: MAAVPLNNLQEQLQRHSARKLNNQPSLSKPKSLGFTFKKKTSEGDVSVTSVSVVKTPALSDKDVNVSEAFSFTESPLHKPKQQAKIEGFFKHFPGRQQSKGTCSEPSLPATVQTAQDTLCTTPKTPTAKKLPVAVFKKLEFSSSADSLSDWADMDDFDMSASDAFASLAKNPATRVSTAQKMKKTKRNFFKPPPRKANAVKTDLTPPSPECLQVDLTKESEEEEEEEEEAEGADCLSRDVICIDNDSASEELTEKDTQESQSLKAHLGAERGDSEKKSHEDEAVFHSVQNTEYFEHNDNDYDIDFVPPSPEEIISTASSSLKCSSMLKDLDDSDKEKGILSTSEELLSKPEEMTTHKSDAGTSKDCDAQQIRIQQQLIHVMEHICKLVDTVPTDELEALNCGTELLQQRNIRRKLLAEAGFNGNDVRLLGSLWRHRPDSLDNTVQGDSCPVGHPNKELNSPYLLSHSPSTEECLPTTTPGKTGFSATPKNLFERPLLNSHLQKSFVSSNWAETPRMENRNESTDFPGSVLTSTTVKAQSKQAASGWNVERHGQASYDIDNFNIDDFDDDDDDDDWENIMHNFPASKSSTATYPPIKEGGPVKSLSERISSAKAKFLPVVSTAQNTNLSESIQNCSDKLAQNLSSKNPKHEHFQSLNFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNYHTKETHVNNLYSMVHYCENITECRRIQLLAYFGEKGFNPDFCKKYPDVSCDNCCKTKDYKTKDVTDDVKNIIRFVQEHSSSPGTRNIGPAGRFTLNMLVDIFLGSKSAKVKSGIFGKGTTYSRHNAERLFKKLILDKILDEDLYINANDQPIAYVMLGTKAHSVLSGHLKVDFMETENSSSIKKQKALVAKVSQREEVVKKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVLQKYSEWTVPAEDGSPGARGAPEDTEEEEEEAPVSSHYFANQTRNERKRKKMSATHKPKRRRTSYGGFRAKGGSTTCRKTTSKSKFYGVTGSRSASCASQATSSASRKLGIMAPPKPVNRTFLRPSYAFS | ||||||
Modified residue | 28 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 31 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 38 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 47 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 55 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 56 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 62 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 91 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 114 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 129 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 191 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 201 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 247 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 249 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 264 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Modified residue | 333 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 343 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 349 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 363 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 431 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 456 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 469 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 481 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 489 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 503 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 504 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 513 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 536 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 540 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 596 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 602 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 612 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 871 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 1130 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1202 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 1204 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1212 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 1301 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1311 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 1371 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 1394 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
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
- PTM
Proteomic databases
PTM databases
Expression
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
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
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 13-31 | Polar residues | ||||
Sequence: LQRHSARKLNNQPSLSKPK | ||||||
Region | 13-34 | Disordered | ||||
Sequence: LQRHSARKLNNQPSLSKPKSLG | ||||||
Region | 170-237 | Disordered | ||||
Sequence: KNPATRVSTAQKMKKTKRNFFKPPPRKANAVKTDLTPPSPECLQVDLTKESEEEEEEEEEAEGADCLS | ||||||
Compositional bias | 217-233 | Acidic residues | ||||
Sequence: TKESEEEEEEEEEAEGA | ||||||
Region | 249-281 | Disordered | ||||
Sequence: SEELTEKDTQESQSLKAHLGAERGDSEKKSHED | ||||||
Region | 367-419 | Necessary for dimerization and homooligomerization | ||||
Sequence: DAQQIRIQQQLIHVMEHICKLVDTVPTDELEALNCGTELLQQRNIRRKLLAEA | ||||||
Domain | 684-859 | Helicase ATP-binding | ||||
Sequence: INAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQ | ||||||
Motif | 803-806 | DEAH box | ||||
Sequence: DEAH | ||||||
Region | 878-881 | 3' overhang DNA-binding | ||||
Sequence: KPKK | ||||||
Domain | 885-1032 | Helicase C-terminal | ||||
Sequence: DCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNYHTKETHVNNLY | ||||||
Region | 905-907 | 3' overhang DNA-binding | ||||
Sequence: SRR | ||||||
Region | 1008-1011 | 3' overhang DNA-binding | ||||
Sequence: RLKR | ||||||
Region | 1102-1144 | DNA Holliday junction binding | ||||
Sequence: SPGTRNIGPAGRFTLNMLVDIFLGSKSAKVKSGIFGKGTTYSR | ||||||
Region | 1115-1117 | 3' overhang DNA-binding | ||||
Sequence: TLN | ||||||
Region | 1126-1130 | 3' overhang DNA-binding | ||||
Sequence: SKSAK | ||||||
Region | 1165-1171 | 3' overhang DNA-binding | ||||
Sequence: YINANDQ | ||||||
Domain | 1217-1297 | HRDC | ||||
Sequence: EEVVKKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVLQKYSEWTVPA | ||||||
Region | 1232-1249 | Necessary for ssDNA and DNA Holliday junction binding | ||||
Sequence: KLLGKVFGVHYFNIFNTA | ||||||
Region | 1295-1405 | Disordered | ||||
Sequence: VPAEDGSPGARGAPEDTEEEEEEAPVSSHYFANQTRNERKRKKMSATHKPKRRRTSYGGFRAKGGSTTCRKTTSKSKFYGVTGSRSASCASQATSSASRKLGIMAPPKPVN | ||||||
Motif | 1333-1348 | Nuclear localization signal | ||||
Sequence: RKRKKMSATHKPKRRR | ||||||
Compositional bias | 1335-1352 | Basic residues | ||||
Sequence: RKKMSATHKPKRRRTSYG | ||||||
Compositional bias | 1360-1393 | Polar residues | ||||
Sequence: STTCRKTTSKSKFYGVTGSRSASCASQATSSASR |
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 statusComplete
- Length1,416
- Mass (Da)158,366
- Last updated1998-11-01 v1
- Checksum447C8110A775DD42
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PZ97 | E9PZ97_MOUSE | Blm | 1419 | ||
A0A0U1RPP0 | A0A0U1RPP0_MOUSE | Blm | 155 | ||
A0A0U1RPS3 | A0A0U1RPS3_MOUSE | Blm | 42 | ||
A0A0U1RNI0 | A0A0U1RNI0_MOUSE | Blm | 51 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 13-31 | Polar residues | ||||
Sequence: LQRHSARKLNNQPSLSKPK | ||||||
Sequence conflict | 131 | in Ref. 2; BAA32001 | ||||
Sequence: L → P | ||||||
Compositional bias | 217-233 | Acidic residues | ||||
Sequence: TKESEEEEEEEEEAEGA | ||||||
Sequence conflict | 229 | in Ref. 2; BAA32001 | ||||
Sequence: E → EE | ||||||
Sequence conflict | 535 | in Ref. 2; BAA32001 | ||||
Sequence: V → M | ||||||
Sequence conflict | 546-547 | in Ref. 2; BAA32001 | ||||
Sequence: WN → RT | ||||||
Sequence conflict | 574 | in Ref. 2; BAA32001 | ||||
Sequence: Missing | ||||||
Sequence conflict | 591 | in Ref. 2; BAA32001 | ||||
Sequence: T → A | ||||||
Sequence conflict | 621 | in Ref. 2; BAA32001 | ||||
Sequence: T → N | ||||||
Sequence conflict | 1295 | in Ref. 2; BAA32001 | ||||
Sequence: V → L | ||||||
Compositional bias | 1335-1352 | Basic residues | ||||
Sequence: RKKMSATHKPKRRRTSYG | ||||||
Compositional bias | 1360-1393 | Polar residues | ||||
Sequence: STTCRKTTSKSKFYGVTGSRSASCASQATSSASR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z98263 EMBL· GenBank· DDBJ | CAB10933.1 EMBL· GenBank· DDBJ | mRNA | ||
AB008674 EMBL· GenBank· DDBJ | BAA32001.1 EMBL· GenBank· DDBJ | mRNA |