BLM
entrez
641
canonical
uniprot
P54132
canonical
ensembl
ENSG00000197299
resolver
ensp
ENSP00000347232
resolver
ensp
ENSP00000454158
resolver
ensp
ENSP00000506117
resolver
ensp
ENSP00000606507
resolver
ensp
ENSP00000606510
resolver
ensp
ENSP00000606514
resolver
ensp
ENSP00000731785
resolver
enst
ENST00000355112
resolver
enst
ENST00000560509
resolver
enst
ENST00000680772
resolver
enst
ENST00000936448
resolver
enst
ENST00000936451
resolver
enst
ENST00000936455
resolver
genesymbol
BLM
resolver
genesymbol_syn
RECQ2
resolver
genesymbol_syn
RECQL3
resolver
hgnc
HGNC:1058
resolver
uniprot
B7ZKN7
resolver
uniprot
H0YNU5
resolver
uniprot
Q52M96
resolver
uniprot_entry
B7ZKN7_HUMAN
resolver
uniprot_entry
BLM_HUMAN
resolver
uniprot_entry
H0YNU5_HUMAN
resolver
uniprot_sec
Q52M96
resolver
activity_regulation
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). {ECO:0000269|PubMed:18426915}.
uniprot
proteins
amino_acid_sequence
MAAVPQNNLQEQLERHSARTLNNKLSLSKPKFSGFTFKKKTSSDNNVSVTNVSVAKTPVLRNKDVNVTEDFSFSEPLPNTTNQQRVKDFFKNAPAGQETQRGGSKSLLPDFLQTPKEVVCTTQNTPTVKKSRDTALKKLEFSSSPDSLSTINDWDDMDDFDTSETSKSFVTPPQSHFVRVSTAQKSKKGKRNFFKAQLYTTNTVKTDLPPPSSESEQIDLTEEQKDDSEWLSSDVICIDDGPIAEVHINEDAQESDSLKTHLEDERDNSEKKKNLEEAELHSTEKVPCIEFDDDDYDTDFVPPSPEEIISASSSSSKCLSTLKDLDTSDRKEDVLSTSKDLLSKPEKMSMQELNPETSTDCDARQISLQQQLIHVMEHICKLIDTIPDDKLKLLDCGNELLQQRNIRRKLLTEVDFNKSDASLLGSLWRYRPDSLDGPMEGDSCPTGNSMKELNFSHLPSNSVSPGDCLLTTTLGKTGFSATRKNLFERPLFNTHLQKSFVSSNWAETPRLGKKNESSYFPGNVLTSTAVKDQNKHTASINDLERETQPSYDIDNFDIDDFDDDDDWEDIMHNLAASKSSTAAYQPIKEGRPIKSVSERLSSAKTDCLPVSSTAQNINFSESIQNYTDKSAQNLASRNLKHERFQSLSFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHFNNLYSMVHYCENITECRRIQLLAYFGENGFNPDFCKKHPDVSCDNCCKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNIKHVGPSGRFTMNMLVDIFLGSKSAKIQSGIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQAIAYVMLGNKAQTVLNGNLKVDFMETENSSSVKKQKALVAKVSQREEMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKYSEWTSPAEDSSPGISLSSSRGPGRSAAEELDEEIPVSSHYFASKTRNERKRKKMPASQRSKRRKTASSGSKAKGGSATCRKISSKTKSSSIIGSSSASHTSQATSGANSKLGIMAPPKPINRPFLKPSYAFS
uniprot
proteins
disease_involvement
DISEASE: 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. {ECO:0000269|PubMed:10862105, ECO:0000269|PubMed:17407155, ECO:0000269|PubMed:7585968, ECO:0000269|PubMed:9285778}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
5.6.2.4
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:O88700, ECO:0000269|PubMed:12019152, ECO:0000269|PubMed:18426915, ECO:0000269|PubMed:20639533, ECO:0000269|PubMed:21325134, ECO:0000269|PubMed:23509288, ECO:0000269|PubMed:24257077, ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030, ECO:0000269|PubMed:34606619, ECO:0000269|PubMed:9388193, ECO:0000269|PubMed:9765292}.; FUNCTION: (Microbial infection) Eliminates nuclear HIV-1 cDNA, thereby suppressing immune sensing and proviral hyper-integration. {ECO:0000269|PubMed:32690953}.
uniprot
proteins
mass_dalton
159000
uniprot
proteins
mutagenesis
MUTAGEN 666; /note="H->A: Reduced intramolecular association between both the helicase ATP-binding domain and the helicase C-terminal domain with the HRDC domain. No change in forked duplex DNA helicase activity. No change in DNA 4-way junction branch migration and Holliday junction dissolution activities. No change in suppression of enhanced sister chromatide exchange activity."; /evidence="ECO:0000269|PubMed:25901030"; MUTAGEN 729; /note="S->A: Reduced intramolecular interaction between both the helicase ATP-binding domain and the helicase C-terminal domain with the HRDC domain. No change in forked duplex DNA helicase activity. No change in DNA 4-way junction branch migration and Holliday junction dissolution activities. No change in suppression of enhanced sister chromatide exchange activity."; /evidence="ECO:0000269|PubMed:25901030"; MUTAGEN 1094..1103; /note="Missing: Decreased DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:24257077"; MUTAGEN 1121; /note="S->A: Decreased slightly DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:24257077"; MUTAGEN 1125; /note="K->A: Decreased DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:24257077"; MUTAGEN 1139; /note="R->A: Decreased strongly DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:24257077"; MUTAGEN 1164; /note="N->A: Reduced strongly DNA helicase activity."; /evidence="ECO:0000269|PubMed:24816114"; MUTAGEN 1227; /note="K->E: Reduced ssDNA binding. No change in DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:20639533"; MUTAGEN 1237; /note="Y->A: No change in ssDNA binding. Increased DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:20639533"; MUTAGEN 1239; /note="N->D: Reduced ssDNA binding. No change in DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:20639533"; MUTAGEN 1243; /note="T->A: No change in ssDNA binding. Decreased DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:20639533"; MUTAGEN 1244; /note="V->A: Reduced ssDNA binding. Increased DNAHolliday junction binding."; /evidence="ECO:0000269|PubMed:20639533"; MUTAGEN 1270; /note="K->V: Reduced intramolecular interaction between both the helicase ATP-binding domain and the helicase C-terminal domain with the HRDC domain."; /evidence="ECO:0000269|PubMed:25901030
uniprot
proteins
post_translational_modification
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). {ECO:0000250|UniProtKB:O88700, ECO:0000269|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. {ECO:0000269|PubMed:15257300, ECO:0000269|PubMed:15775963}.; PTM: (Microbial infection) Sumoylation of BLM is decreased by HIV-1 Vpu protein, unleashing end degradation of viral cDNA. {ECO:0000269|PubMed:32690953}.
uniprot
proteins
protein_family
Helicase family
uniprot
proteins
protein_family
RecQ subfamily
uniprot
proteins
pubmed
10783165
uniprot
proteins
pubmed
10862105
uniprot
proteins
pubmed
12019152
uniprot
proteins
pubmed
15257300
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15775963
uniprot
proteins
pubmed
16595695
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17407155
uniprot
proteins
pubmed
17961633
uniprot
proteins
pubmed
18426915
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18923082
uniprot
proteins
pubmed
18923083
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20639533
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21325134
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23509288
uniprot
proteins
pubmed
24257077
uniprot
proteins
pubmed
24435566
uniprot
proteins
pubmed
24816114
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
25901030
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28228481
uniprot
proteins
pubmed
32690953
uniprot
proteins
pubmed
34606619
uniprot
proteins
pubmed
7585968
uniprot
proteins
pubmed
9285778
uniprot
proteins
pubmed
9388193
uniprot
proteins
pubmed
9388480
uniprot
proteins
pubmed
9765292
uniprot
proteins
sequence_length
1417
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23509288}. 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.
uniprot
proteins