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Protein

Bloom syndrome protein

Gene

BLM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction (PubMed:9388193, PubMed:24816114, PubMed:25901030). Participates in DNA replication and repair (PubMed:12019152, PubMed:21325134, PubMed:23509288). 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). Negatively regulates sister chromatid exchange (SCE) (PubMed:25901030). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (PubMed:25901030). Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (PubMed:20639533, PubMed:24257077, PubMed:25901030).8 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.2 Publications

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei7173' overhang DNA-binding1 Publication1
Sitei8083' overhang DNA-binding1 Publication1
Sitei9203' overhang DNA-binding; via amide nitrogenCombined sources2 Publications1
Sitei9463' overhang DNA-bindingCombined sources2 Publications1
Sitei9683' overhang DNA-bindingCombined sources2 Publications1
Binding sitei982ATPCombined sources1 Publication1
Metal bindingi1036ZincCombined sources2 Publications1
Metal bindingi1055ZincCombined sources2 Publications1
Metal bindingi1063ZincCombined sources2 Publications1
Metal bindingi1066ZincCombined sources2 Publications1
Sitei11103' overhang DNA-bindingCombined sources2 Publications1
Binding sitei1242ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi668 – 672ATPCombined sources2 Publications5
Nucleotide bindingi692 – 696ATPCombined sources2 Publications5

GO - Molecular functioni

  • 8-hydroxy-2'-deoxyguanosine DNA binding Source: BHF-UCL
  • annealing helicase activity Source: UniProtKB
  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • ATP-dependent 3'-5' DNA helicase activity Source: GO_Central
  • ATP-dependent DNA helicase activity Source: UniProtKB
  • ATP-dependent helicase activity Source: UniProtKB
  • bubble DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA-dependent ATPase activity Source: UniProtKB
  • DNA helicase activity Source: BHF-UCL
  • forked DNA-dependent helicase activity Source: UniProtKB
  • four-way junction DNA binding Source: UniProtKB
  • four-way junction helicase activity Source: UniProtKB
  • G-quadruplex DNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB
  • p53 binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • telomeric D-loop binding Source: BHF-UCL
  • telomeric G-quadruplex DNA binding Source: BHF-UCL
  • Y-form DNA binding Source: BHF-UCL
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular response to camptothecin Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to hydroxyurea Source: UniProtKB
  • cellular response to ionizing radiation Source: UniProtKB
  • DNA double-strand break processing Source: UniProtKB
  • DNA duplex unwinding Source: UniProtKB
  • DNA recombination Source: UniProtKB
  • DNA repair Source: UniProtKB
  • DNA replication Source: BHF-UCL
  • DNA synthesis involved in DNA repair Source: Reactome
  • double-strand break repair via homologous recombination Source: GO_Central
  • G-quadruplex DNA unwinding Source: BHF-UCL
  • mitotic G2 DNA damage checkpoint Source: UniProtKB
  • negative regulation of cell division Source: UniProtKB
  • negative regulation of DNA recombination Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • protein complex oligomerization Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein oligomerization Source: UniProtKB
  • regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  • regulation of DNA-dependent DNA replication Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • replication fork processing Source: UniProtKB
  • replication fork protection Source: UniProtKB
  • response to X-ray Source: UniProtKB
  • strand displacement Source: Reactome
  • t-circle formation Source: BHF-UCL
  • telomeric D-loop disassembly Source: BHF-UCL

Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA repair, DNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-912446. Meiotic recombination.
SIGNORiP54132.

Names & Taxonomyi

Protein namesi
Recommended name:
Bloom syndrome protein (EC:3.6.4.122 Publications)
Alternative name(s):
DNA helicase, RecQ-like type 2
Short name:
RecQ2
RecQ protein-like 3
Gene namesi
Name:BLM
Synonyms:RECQ2, RECQL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000197299.10.
HGNCiHGNC:1058. BLM.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Bloom syndrome (BLM)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:210900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_006901672Q → R in BLM. 1 PublicationCorresponds to variant dbSNP:rs747281324Ensembl.1
Natural variantiVAR_016032841I → T in BLM. Corresponds to variant dbSNP:rs767086502Ensembl.1
Natural variantiVAR_006902843T → I in BLM. 1 PublicationCorresponds to variant dbSNP:rs137853152Ensembl.1
Natural variantiVAR_016033878C → R in BLM. 1 Publication1
Natural variantiVAR_009138891G → E in BLM. 1
Natural variantiVAR_009139901C → Y in BLM. Corresponds to variant dbSNP:rs758311406Ensembl.1
Natural variantiVAR_0091401036C → F in BLM. 1 PublicationCorresponds to variant dbSNP:rs137853153Ensembl.1
Natural variantiVAR_0069031055C → S in BLM. 1 PublicationCorresponds to variant dbSNP:rs367543029Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi666H → 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. 1 Publication1
Mutagenesisi729S → 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. 1 Publication1
Mutagenesisi1094 – 1103Missing : Decreased DNA Holliday junction binding. 1 Publication10
Mutagenesisi1121S → A: Decreased slightly DNA Holliday junction binding. 1 Publication1
Mutagenesisi1125K → A: Decreased DNA Holliday junction binding. 1 Publication1
Mutagenesisi1139R → A: Decreased strongly DNA Holliday junction binding. 1 Publication1
Mutagenesisi1164N → A: Reduced strongly DNA helicase activity. 1 Publication1
Mutagenesisi1227K → E: Reduced ssDNA binding. No change in DNA Holliday junction binding. 1 Publication1
Mutagenesisi1237Y → A: No change in ssDNA binding. Increased DNA Holliday junction binding. 1 Publication1
Mutagenesisi1239N → D: Reduced ssDNA binding. No change in DNA Holliday junction binding. 1 Publication1
Mutagenesisi1243T → A: No change in ssDNA binding. Decreased DNA Holliday junction binding. 1 Publication1
Mutagenesisi1244V → A: Reduced ssDNA binding. Increased DNA Holliday junction binding. 1 Publication1
Mutagenesisi1270K → V: Reduced intramolecular interaction between both the helicase ATP-binding domain and the helicase C-terminal domain with the HRDC domain. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi641.
GeneReviewsiBLM.
MalaCardsiBLM.
MIMi210900. phenotype.
OpenTargetsiENSG00000197299.
Orphaneti125. Bloom syndrome.
PharmGKBiPA25369.

Chemistry databases

ChEMBLiCHEMBL1293237.

Polymorphism and mutation databases

BioMutaiBLM.
DMDMi1705486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002050391 – 1417Bloom syndrome proteinAdd BLAST1417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei28PhosphoserineCombined sources1
Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei48PhosphoserineCombined sources1
Cross-linki56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei57PhosphothreonineCombined sources1
Cross-linki63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki91Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei114PhosphothreonineCombined sources1
Cross-linki116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei168PhosphoserineCombined sources1
Modified residuei171PhosphothreonineCombined sources1
Cross-linki195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei328PhosphoserineCombined sources1
Cross-linki331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei338PhosphoserineCombined sources1
Cross-linki344Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei358PhosphoserineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei422PhosphoserineCombined sources1
Modified residuei426PhosphoserineCombined sources1
Cross-linki451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei464PhosphoserineCombined sources1
Cross-linki476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki484Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki498Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei499PhosphoserineCombined sources1
Modified residuei508PhosphothreonineCombined sources1
Cross-linki513Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki514Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki535Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki588Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki604Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei863N6-acetyllysineCombined sources1
Cross-linki1125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1197PhosphoserineCombined sources1
Cross-linki1199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1207Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1295PhosphoserineCombined sources1
Modified residuei1296PhosphoserineCombined sources1
Modified residuei1310PhosphoserineCombined sources1
Cross-linki1329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1372Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1395Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP54132.
MaxQBiP54132.
PaxDbiP54132.
PeptideAtlasiP54132.
PRIDEiP54132.

PTM databases

iPTMnetiP54132.
PhosphoSitePlusiP54132.

Miscellaneous databases

PMAP-CutDBiP54132.

Expressioni

Gene expression databases

BgeeiENSG00000197299.
CleanExiHS_BLM.
ExpressionAtlasiP54132. baseline and differential.
GenevisibleiP54132. HS.

Organism-specific databases

HPAiHPA005689.

Interactioni

Subunit structurei

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 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.9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • p53 binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi107110. 135 interactors.
CORUMiP54132.
DIPiDIP-33322N.
ELMiP54132.
IntActiP54132. 43 interactors.
MINTiMINT-131918.
STRINGi9606.ENSP00000347232.

Chemistry databases

BindingDBiP54132.

Structurei

Secondary structure

11417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi365 – 384Combined sources20
Helixi388 – 391Combined sources4
Helixi397 – 411Combined sources15
Helixi643 – 645Combined sources3
Helixi652 – 661Combined sources10
Helixi672 – 680Combined sources9
Beta strandi685 – 688Combined sources4
Helixi697 – 705Combined sources9
Beta strandi706 – 713Combined sources8
Helixi717 – 729Combined sources13
Beta strandi734 – 741Combined sources8
Helixi743 – 753Combined sources11
Beta strandi755 – 757Combined sources3
Beta strandi762 – 765Combined sources4
Helixi769 – 772Combined sources4
Helixi774 – 785Combined sources12
Beta strandi789 – 795Combined sources7
Helixi797 – 800Combined sources4
Helixi811 – 820Combined sources10
Beta strandi826 – 830Combined sources5
Helixi835 – 845Combined sources11
Beta strandi851 – 853Combined sources3
Beta strandi862 – 868Combined sources7
Helixi871 – 873Combined sources3
Helixi874 – 885Combined sources12
Beta strandi891 – 894Combined sources4
Helixi898 – 910Combined sources13
Beta strandi915 – 919Combined sources5
Helixi924 – 935Combined sources12
Beta strandi941 – 945Combined sources5
Helixi947 – 950Combined sources4
Beta strandi960 – 965Combined sources6
Helixi970 – 977Combined sources8
Turni979 – 983Combined sources5
Beta strandi987 – 993Combined sources7
Helixi995 – 1005Combined sources11
Helixi1015 – 1031Combined sources17
Helixi1037 – 1044Combined sources8
Helixi1054 – 1057Combined sources4
Helixi1059 – 1061Combined sources3
Helixi1064 – 1067Combined sources4
Turni1069 – 1071Combined sources3
Beta strandi1074 – 1076Combined sources3
Helixi1078 – 1090Combined sources13
Beta strandi1096 – 1099Combined sources4
Helixi1111 – 1119Combined sources9
Turni1129 – 1136Combined sources8
Helixi1139 – 1151Combined sources13
Beta strandi1154 – 1161Combined sources8
Beta strandi1163 – 1166Combined sources4
Beta strandi1167 – 1173Combined sources7
Helixi1177 – 1181Combined sources5
Beta strandi1188 – 1190Combined sources3
Helixi1195 – 1197Combined sources3
Beta strandi1207 – 1209Combined sources3
Helixi1210 – 1233Combined sources24
Helixi1237 – 1239Combined sources3
Helixi1243 – 1252Combined sources10
Helixi1257 – 1260Combined sources4
Beta strandi1263 – 1265Combined sources3
Helixi1268 – 1283Combined sources16
Turni1284 – 1288Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KV2NMR-A1210-1294[»]
2MH9NMR-A1067-1210[»]
2RRDNMR-A1200-1295[»]
3WE2X-ray2.70A/B1068-1209[»]
3WE3X-ray2.90A/B1068-1209[»]
4CDGX-ray2.79A/B636-1298[»]
4CGZX-ray3.20A636-1298[»]
4O3MX-ray2.30A640-1298[»]
5LUPX-ray2.03A/B/C/D/E/F/G/I/J/K/L362-414[»]
H367-414[»]
5MK5X-ray2.16A/B/C/D362-414[»]
ProteinModelPortaliP54132.
SMRiP54132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54132.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini676 – 851Helicase ATP-bindingPROSITE-ProRule annotation1 PublicationAdd BLAST176
Domaini877 – 1024Helicase C-terminalPROSITE-ProRule annotation1 PublicationAdd BLAST148
Domaini1212 – 1292HRDCPROSITE-ProRule annotation1 Publication1 PublicationAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni301 – 600Necessary for interaction with SPIDR1 PublicationAdd BLAST300
Regioni362 – 414Necessary for dimerization and homooligomerization1 PublicationAdd BLAST53
Regioni870 – 8733' overhang DNA-binding1 Publication4
Regioni897 – 8993' overhang DNA-bindingCombined sources2 Publications3
Regioni1000 – 10033' overhang DNA-bindingCombined sources2 Publications4
Regioni1094 – 1139DNA Holliday junction binding1 PublicationAdd BLAST46
Regioni1110 – 11123' overhang DNA-bindingCombined sources2 Publications3
Regioni1121 – 11253' overhang DNA-bindingCombined sources2 Publications5
Regioni1160 – 11663' overhang DNA-bindingCombined sources2 Publications7
Regioni1227 – 1244Necessary for ssDNA and DNA Holliday junction binding1 PublicationAdd BLAST18

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi795 – 798DEAH box4
Motifi1334 – 1349Nuclear localization signalSequence analysisAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi292 – 299Poly-Asp8
Compositional biasi310 – 316Poly-Ser7
Compositional biasi557 – 566Poly-Asp10

Domaini

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).3 Publications

Sequence similaritiesi

Belongs to the helicase family. RecQ subfamily.Curated

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000095239.
HOVERGENiHBG004850.
InParanoidiP54132.
KOiK10901.
OMAiCENITEC.
OrthoDBiEOG091G021X.
PhylomeDBiP54132.
TreeFamiTF317801.

Family and domain databases

CDDicd00079. HELICc. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiView protein in InterPro
IPR012532. BDHCT.
IPR032439. BDHCT_assoc.
IPR032437. BLM_N.
IPR011545. DEAD/DEAH_box_helicase_dom.
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.
IPR032284. RecQ_Zn-bd.
IPR018982. RQC_domain.
IPR036388. WH-like_DNA-bd_sf.
IPR036390. WH_DNA-bd_sf.
PfamiView protein in Pfam
PF08072. BDHCT. 1 hit.
PF16204. BDHCT_assoc. 1 hit.
PF16202. BLM_N. 1 hit.
PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00570. HRDC. 1 hit.
PF16124. RecQ_Zn_bind. 1 hit.
PF09382. RQC. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00341. HRDC. 1 hit.
SM00956. RQC. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF47819. SSF47819. 1 hit.
SSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiView protein in PROSITE
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50967. HRDC. 1 hit.

Sequencei

Sequence statusi: Complete.

P54132-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVPQNNLQ EQLERHSART LNNKLSLSKP KFSGFTFKKK TSSDNNVSVT
60 70 80 90 100
NVSVAKTPVL RNKDVNVTED FSFSEPLPNT TNQQRVKDFF KNAPAGQETQ
110 120 130 140 150
RGGSKSLLPD FLQTPKEVVC TTQNTPTVKK SRDTALKKLE FSSSPDSLST
160 170 180 190 200
INDWDDMDDF DTSETSKSFV TPPQSHFVRV STAQKSKKGK RNFFKAQLYT
210 220 230 240 250
TNTVKTDLPP PSSESEQIDL TEEQKDDSEW LSSDVICIDD GPIAEVHINE
260 270 280 290 300
DAQESDSLKT HLEDERDNSE KKKNLEEAEL HSTEKVPCIE FDDDDYDTDF
310 320 330 340 350
VPPSPEEIIS ASSSSSKCLS TLKDLDTSDR KEDVLSTSKD LLSKPEKMSM
360 370 380 390 400
QELNPETSTD CDARQISLQQ QLIHVMEHIC KLIDTIPDDK LKLLDCGNEL
410 420 430 440 450
LQQRNIRRKL LTEVDFNKSD ASLLGSLWRY RPDSLDGPME GDSCPTGNSM
460 470 480 490 500
KELNFSHLPS NSVSPGDCLL TTTLGKTGFS ATRKNLFERP LFNTHLQKSF
510 520 530 540 550
VSSNWAETPR LGKKNESSYF PGNVLTSTAV KDQNKHTASI NDLERETQPS
560 570 580 590 600
YDIDNFDIDD FDDDDDWEDI MHNLAASKSS TAAYQPIKEG RPIKSVSERL
610 620 630 640 650
SSAKTDCLPV SSTAQNINFS ESIQNYTDKS AQNLASRNLK HERFQSLSFP
660 670 680 690 700
HTKEMMKIFH KKFGLHNFRT NQLEAINAAL LGEDCFILMP TGGGKSLCYQ
710 720 730 740 750
LPACVSPGVT VVISPLRSLI VDQVQKLTSL DIPATYLTGD KTDSEATNIY
760 770 780 790 800
LQLSKKDPII KLLYVTPEKI CASNRLISTL ENLYERKLLA RFVIDEAHCV
810 820 830 840 850
SQWGHDFRQD YKRMNMLRQK FPSVPVMALT ATANPRVQKD ILTQLKILRP
860 870 880 890 900
QVFSMSFNRH NLKYYVLPKK PKKVAFDCLE WIRKHHPYDS GIIYCLSRRE
910 920 930 940 950
CDTMADTLQR DGLAALAYHA GLSDSARDEV QQKWINQDGC QVICATIAFG
960 970 980 990 1000
MGIDKPDVRF VIHASLPKSV EGYYQESGRA GRDGEISHCL LFYTYHDVTR
1010 1020 1030 1040 1050
LKRLIMMEKD GNHHTRETHF NNLYSMVHYC ENITECRRIQ LLAYFGENGF
1060 1070 1080 1090 1100
NPDFCKKHPD VSCDNCCKTK DYKTRDVTDD VKSIVRFVQE HSSSQGMRNI
1110 1120 1130 1140 1150
KHVGPSGRFT MNMLVDIFLG SKSAKIQSGI FGKGSAYSRH NAERLFKKLI
1160 1170 1180 1190 1200
LDKILDEDLY INANDQAIAY VMLGNKAQTV LNGNLKVDFM ETENSSSVKK
1210 1220 1230 1240 1250
QKALVAKVSQ REEMVKKCLG ELTEVCKSLG KVFGVHYFNI FNTVTLKKLA
1260 1270 1280 1290 1300
ESLSSDPEVL LQIDGVTEDK LEKYGAEVIS VLQKYSEWTS PAEDSSPGIS
1310 1320 1330 1340 1350
LSSSRGPGRS AAEELDEEIP VSSHYFASKT RNERKRKKMP ASQRSKRRKT
1360 1370 1380 1390 1400
ASSGSKAKGG SATCRKISSK TKSSSIIGSS SASHTSQATS GANSKLGIMA
1410
PPKPINRPFL KPSYAFS
Length:1,417
Mass (Da):159,000
Last modified:October 1, 1996 - v1
Checksum:i423DF5F381194E11
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022295137K → R1 PublicationCorresponds to variant dbSNP:rs28384988Ensembl.1
Natural variantiVAR_022296298T → M1 PublicationCorresponds to variant dbSNP:rs28384991Ensembl.1
Natural variantiVAR_022297591R → Q1 PublicationCorresponds to variant dbSNP:rs28385012Ensembl.1
Natural variantiVAR_006901672Q → R in BLM. 1 PublicationCorresponds to variant dbSNP:rs747281324Ensembl.1
Natural variantiVAR_016032841I → T in BLM. Corresponds to variant dbSNP:rs767086502Ensembl.1
Natural variantiVAR_006902843T → I in BLM. 1 PublicationCorresponds to variant dbSNP:rs137853152Ensembl.1
Natural variantiVAR_022298868P → L1 PublicationCorresponds to variant dbSNP:rs2227935Ensembl.1
Natural variantiVAR_016033878C → R in BLM. 1 Publication1
Natural variantiVAR_009138891G → E in BLM. 1
Natural variantiVAR_009139901C → Y in BLM. Corresponds to variant dbSNP:rs758311406Ensembl.1
Natural variantiVAR_0091401036C → F in BLM. 1 PublicationCorresponds to variant dbSNP:rs137853153Ensembl.1
Natural variantiVAR_0517311043A → D. Corresponds to variant dbSNP:rs2229035Ensembl.1
Natural variantiVAR_0069031055C → S in BLM. 1 PublicationCorresponds to variant dbSNP:rs367543029Ensembl.1
Natural variantiVAR_0222991205V → I. Corresponds to variant dbSNP:rs28385141Ensembl.1
Natural variantiVAR_0149121209S → T. Corresponds to variant dbSNP:rs1801256Ensembl.1
Natural variantiVAR_0223001213E → K1 PublicationCorresponds to variant dbSNP:rs28385142Ensembl.1
Natural variantiVAR_0223011321V → I1 PublicationCorresponds to variant dbSNP:rs7167216Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39817 mRNA. Translation: AAA87850.1.
AY886902 Genomic DNA. Translation: AAW62255.1.
BC093622 mRNA. Translation: AAH93622.1.
BC101567 mRNA. Translation: AAI01568.1.
BC115030 mRNA. Translation: AAI15031.1.
BC115032 mRNA. Translation: AAI15033.1.
CCDSiCCDS10363.1.
PIRiA57570.
RefSeqiNP_000048.1. NM_000057.3.
NP_001274175.1. NM_001287246.1.
NP_001274176.1. NM_001287247.1.
NP_001274177.1. NM_001287248.1.
UniGeneiHs.725208.

Genome annotation databases

EnsembliENST00000355112; ENSP00000347232; ENSG00000197299.
GeneIDi641.
KEGGihsa:641.
UCSCiuc002bpr.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiBLM_HUMAN
AccessioniPrimary (citable) accession number: P54132
Secondary accession number(s): Q52M96
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 25, 2017
This is version 185 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families