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Details on Person UniProt:P54132 BLM
| Class:Id | ReferenceGeneProduct:50864 |
|---|---|
| _chainChangeLog | chain:1-1417 added on Fri February 6 2015 |
| _displayName | UniProt:P54132 BLM |
| _timestamp | 2025-05-21 21:04:09 |
| chain | chain:1-1417 |
| checksum | 423DF5F381194E11 |
| comment | FUNCTION ATP-dependent DNA helicase that unwinds double-stranded (ds)DNA in a 3'-5' direction (PubMed:24816114, PubMed:25901030, PubMed:9388193, PubMed:9765292). Participates in DNA replication and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288, PubMed:34606619). 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:21325134). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA), forked duplex DNA and Holliday junction DNA (PubMed:20639533, PubMed:24257077, PubMed:25901030). Unwinds G-quadruplex DNA; unwinding occurs in the 3'-5' direction and requires a 3' single-stranded end of at least 7 nucleotides (PubMed:18426915, PubMed:9765292). Helicase activity is higher on G-quadruplex substrates than on duplex DNA substrates (PubMed:9765292). Telomeres, immunoglobulin heavy chain switch regions and rDNA are notably G-rich; formation of G-quadruplex DNA would block DNA replication and transcription (PubMed:18426915, PubMed:9765292). Negatively regulates sister chromatid exchange (SCE) (PubMed:25901030). Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks (By similarity).FUNCTION (Microbial infection) Eliminates nuclear HIV-1 cDNA, thereby suppressing immune sensing and proviral hyper-integration.CATALYTIC ACTIVITY Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.CATALYTIC ACTIVITY ATP + H2O = ADP + phosphate + H(+)COFACTOR Binds 1 zinc ion per subunit.ACTIVITY REGULATION Helicase activity on forked duplex DNA is not inhibited by telomestatin (TMS); TMS does inhibit helicase activity on G-quadruplex DNA (PubMed:18426915).SUBUNIT Monomer (PubMed:28228481). Homodimer (via N-terminus) (PubMed:28228481). Homotetramer (via N-terminus); dimer of dimers (PubMed:28228481). Homohexamer (via N-terminus) (PubMed:28228481). Self-association negatively regulates DNA unwinding amplitude and rate. Oligomeric complexes dissociate into monomer in presence of ATP (PubMed:28228481). 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 KHDC3L/FILIA-OOEP/FLOPED scaffold complex and TRIM25 at DNA replication forks (By similarity). Interacts with ubiquitinated FANCD2 (PubMed:15257300). Interacts with SUPV3L1 (PubMed:17961633). 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.INTERACTION 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.DOMAIN The N-terminal region mediates dimerization and homooligomerization (PubMed:28228481). Both the helicase ATP-binding domain and the helicase C-terminal domain form intramolecular interactions with the HRDC domain in a ATP-dependent manner (PubMed:25901030). The HRDC domain is required for single-stranded DNA (ssDNA) and DNA Holliday junction binding (PubMed:20639533).PTM Poly-ubiquitinated by TRIM25 at Lys-259 (By similarity). Deubiquitinated by USP37; leading to stabilization in order to sustain the DNA damage response (PubMed:34606619).PTM Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1.PTM (Microbial infection) Sumoylation of BLM is decreased by HIV-1 Vpu protein, unleashing end degradation of viral cDNA.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the helicase family. RecQ subfamily.ONLINE INFORMATION BLM mutation db |
| description | recommendedName: fullName evidence="31"RecQ-like DNA helicase BLM ecNumber evidence="21 22 28 29"5.6.2.4 alternativeName: Bloom syndrome protein alternativeName: fullName evidence="31"DNA 3'-5' helicase BLM alternativeName: DNA helicase, RecQ-like type 2 shortName: RecQ2 alternativeName: RecQ protein-like 3 |
| geneName | BLM RECQ2 RECQL3 |
| identifier | P54132 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation ATP-binding Disease variant DNA damage DNA repair DNA replication DNA-binding Dwarfism Helicase Hydrolase Isomerase Isopeptide bond Metal-binding Nucleotide-binding Nucleus Phosphoprotein Proteomics identification Reference proteome Ubl conjugation Zinc |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9909836] Weiser, Joel, 2024-05-14 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 |
| name | BLM |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9002830] ENSEMBL:ENSG00000197299 BLM [Homo sapiens] |
| secondaryIdentifier | BLM_HUMAN Q52M96 |
| sequenceLength | 1417 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:174881] BLM [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:4568883] 4SUMO2,3-BLM [nucleoplasm] [Homo sapiens] |
| (referenceSequence) | [GroupModifiedResidue:4568842] sumoylated lysine (polySUMO2,3 [nucleoplasm]) at 347 [GroupModifiedResidue:4568854] sumoylated lysine (polySUMO2,3 [nucleoplasm]) at 331 [GroupModifiedResidue:4568859] sumoylated lysine (polySUMO2,3 [nucleoplasm]) at 317 [GroupModifiedResidue:4568885] sumoylated lysine (polySUMO2,3 [nucleoplasm]) at 344 |
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No pathways have been reviewed or authored by UniProt:P54132 BLM (50864)
