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Protein

Bloom syndrome protein

Gene

BLM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei982ATPCombined sources1 Publication1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi668 – 672ATPCombined sources2 Publications5
Nucleotide bindingi692 – 696ATPCombined sources2 Publications5

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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

SIGNOR Signaling Network Open Resource

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SIGNORi
P54132

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:BLM
Synonyms:RECQ2, RECQL3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000197299.10

Human Gene Nomenclature Database

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HGNCi
HGNC:1058 BLM

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
604610 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P54132

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_006901672Q → R in BLM. 1 PublicationCorresponds to variant dbSNP:rs747281324EnsemblClinVar.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:rs137853153EnsemblClinVar.1
Natural variantiVAR_0069031055C → S in BLM. 1 PublicationCorresponds to variant dbSNP:rs367543029EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
641

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
BLM

MalaCards human disease database

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MalaCardsi
BLM
MIMi210900 phenotype

Open Targets

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OpenTargetsi
ENSG00000197299

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
125 Bloom syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA25369

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1293237

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
BLM

Domain mapping of disease mutations (DMDM)

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DMDMi
1705486

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002050391 – 1417Bloom syndrome proteinAdd BLAST1417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
P54132

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P54132

MaxQB - The MaxQuant DataBase

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MaxQBi
P54132

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P54132

PeptideAtlas

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PeptideAtlasi
P54132

PRoteomics IDEntifications database

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PRIDEi
P54132

ProteomicsDB human proteome resource

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ProteomicsDBi
56649

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P54132

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P54132

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P54132

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000197299 Expressed in 154 organ(s), highest expression level in parotid gland

CleanEx database of gene expression profiles

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CleanExi
HS_BLM

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P54132 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P54132 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA005689

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107110, 150 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3301 BTR double Holliday Junction dissolution complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P54132

Database of interacting proteins

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DIPi
DIP-33322N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P54132

Protein interaction database and analysis system

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IntActi
P54132, 48 interactors

Molecular INTeraction database

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MINTi
P54132

STRING: functional protein association networks

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STRINGi
9606.ENSP00000347232

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P54132

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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/H/I/J/K/L362-414[»]
5M1VX-ray2.01A/B/C/D362-414[»]
5MK5X-ray2.16A/B/C/D362-414[»]
5U6KX-ray2.60L/M/N/O297-309[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P54132

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P54132

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P54132

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi795 – 798DEAH box4
Motifi1334 – 1349Nuclear localization signalSequence analysisAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi292 – 299Poly-Asp8
Compositional biasi310 – 316Poly-Ser7
Compositional biasi557 – 566Poly-Asp10

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the helicase family. RecQ subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0351 Eukaryota
COG0514 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156800

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000095239

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004850

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P54132

KEGG Orthology (KO)

More...
KOi
K10901

Identification of Orthologs from Complete Genome Data

More...
OMAi
HHPHDSG

Database of Orthologous Groups

More...
OrthoDBi
664798at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P54132

TreeFam database of animal gene trees

More...
TreeFami
TF317801

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00079 HELICc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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_sf
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

Pfam protein domain database

More...
Pfami
View 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

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SM00341 HRDC, 1 hit
SM00956 RQC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit
SSF47819 SSF47819, 1 hit
SSF52540 SSF52540, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00614 recQ_fam, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i423DF5F381194E11
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YNU5H0YNU5_HUMAN
Bloom syndrome protein
BLM
1,286Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YLV8H0YLV8_HUMAN
Bloom syndrome protein
BLM
413Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3B3IT82A0A3B3IT82_HUMAN
Bloom syndrome protein
BLM
1,386Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022295137K → R1 PublicationCorresponds to variant dbSNP:rs28384988EnsemblClinVar.1
Natural variantiVAR_022296298T → M1 PublicationCorresponds to variant dbSNP:rs28384991EnsemblClinVar.1
Natural variantiVAR_022297591R → Q1 PublicationCorresponds to variant dbSNP:rs28385012EnsemblClinVar.1
Natural variantiVAR_006901672Q → R in BLM. 1 PublicationCorresponds to variant dbSNP:rs747281324EnsemblClinVar.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:rs2227935EnsemblClinVar.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:rs137853153EnsemblClinVar.1
Natural variantiVAR_0517311043A → D. Corresponds to variant dbSNP:rs2229035EnsemblClinVar.1
Natural variantiVAR_0069031055C → S in BLM. 1 PublicationCorresponds to variant dbSNP:rs367543029EnsemblClinVar.1
Natural variantiVAR_0222991205V → I. Corresponds to variant dbSNP:rs28385141EnsemblClinVar.1
Natural variantiVAR_0149121209S → T. Corresponds to variant dbSNP:rs1801256EnsemblClinVar.1
Natural variantiVAR_0223001213E → K1 PublicationCorresponds to variant dbSNP:rs28385142EnsemblClinVar.1
Natural variantiVAR_0223011321V → I1 PublicationCorresponds to variant dbSNP:rs7167216EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10363.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A57570

NCBI Reference Sequences

More...
RefSeqi
NP_000048.1, NM_000057.3
NP_001274175.1, NM_001287246.1
NP_001274176.1, NM_001287247.1
NP_001274177.1, NM_001287248.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.725208

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000355112; ENSP00000347232; ENSG00000197299

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
641

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:641

UCSC genome browser

More...
UCSCi
uc002bpr.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

BLMbase

BLM mutation db

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

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

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/H/I/J/K/L362-414[»]
5M1VX-ray2.01A/B/C/D362-414[»]
5MK5X-ray2.16A/B/C/D362-414[»]
5U6KX-ray2.60L/M/N/O297-309[»]
ProteinModelPortaliP54132
SMRiP54132
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107110, 150 interactors
ComplexPortaliCPX-3301 BTR double Holliday Junction dissolution complex
CORUMiP54132
DIPiDIP-33322N
ELMiP54132
IntActiP54132, 48 interactors
MINTiP54132
STRINGi9606.ENSP00000347232

Chemistry databases

BindingDBiP54132
ChEMBLiCHEMBL1293237

PTM databases

iPTMnetiP54132
PhosphoSitePlusiP54132

Polymorphism and mutation databases

BioMutaiBLM
DMDMi1705486

Proteomic databases

EPDiP54132
jPOSTiP54132
MaxQBiP54132
PaxDbiP54132
PeptideAtlasiP54132
PRIDEiP54132
ProteomicsDBi56649

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
641
DisGeNETi641
EuPathDBiHostDB:ENSG00000197299.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
BLM
GeneReviewsiBLM
HGNCiHGNC:1058 BLM
HPAiHPA005689
MalaCardsiBLM
MIMi210900 phenotype
604610 gene
neXtProtiNX_P54132
OpenTargetsiENSG00000197299
Orphaneti125 Bloom syndrome
PharmGKBiPA25369

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0351 Eukaryota
COG0514 LUCA
GeneTreeiENSGT00940000156800
HOGENOMiHOG000095239
HOVERGENiHBG004850
InParanoidiP54132
KOiK10901
OMAiHHPHDSG
OrthoDBi664798at2759
PhylomeDBiP54132
TreeFamiTF317801

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
BLM human
EvolutionaryTraceiP54132

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Bloom_syndrome_protein

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
641
PMAP-CutDBiP54132

Protein Ontology

More...
PROi
PR:P54132

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000197299 Expressed in 154 organ(s), highest expression level in parotid gland
CleanExiHS_BLM
ExpressionAtlasiP54132 baseline and differential
GenevisibleiP54132 HS

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_sf
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, 2 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBLM_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P54132
Secondary accession number(s): Q52M96
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 16, 2019
This is version 199 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
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