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UniProtKB - Q9BX63 (FANCJ_HUMAN)

Entry version 185 (25 May 2022)
Sequence version 2 (10 Oct 2018)
Previous versions | rss
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Protein

Fanconi anemia group J protein

Gene

BRIP1

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

DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination. Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1.

4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi283Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi298Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi310Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi350Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi185 – 192ATPPROSITE-ProRule annotation8

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHelicase, Hydrolase
Biological processDNA damage, DNA repair
Ligand4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.4.12, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9BX63

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2564830, Cytosolic iron-sulfur cluster assembly
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-9701192, Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function
R-HSA-9704331, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function
R-HSA-9704646, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q9BX63

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9BX63

<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%5Fand%5Ftaxonomy%5Fsection">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:
Fanconi anemia group J proteinCurated (EC:3.6.4.131 Publication)
Short name:
Protein FACJ
Alternative name(s):
ATP-dependent RNA helicase BRIP1
BRCA1-associated C-terminal helicase 1
BRCA1-interacting protein C-terminal helicase 1
Short name:
BRCA1-interacting protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:BRIP1Imported
Synonyms:BACH1, FANCJ
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 17

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:20473, BRIP1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605882, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9BX63

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000136492

<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

Keywords - Cellular componenti

Cytoplasm, 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

Breast cancer (BC)2 Publications
Disease susceptibility is associated with variants affecting the gene represented in this entry.
Disease descriptionA common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.
Related information in OMIM
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_02089647P → A in BC; early onset; loss of ATPase and helicase activities. 2 PublicationsCorresponds to variant dbSNP:rs28903098EnsemblClinVar.1
Natural variantiVAR_020900299M → I in BC; early onset; reduces helicase efficiency on longer substrates. 2 PublicationsCorresponds to variant dbSNP:rs137852985EnsemblClinVar.1
Fanconi anemia complementation group J (FANCJ)3 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023700255Q → H in FANCJ. 1 Publication1
Natural variantiVAR_023702349A → P in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity. 2 PublicationsCorresponds to variant dbSNP:rs149364097EnsemblClinVar.1
Natural variantiVAR_023703647W → C in FANCJ; associated with C-707. 1 PublicationCorresponds to variant dbSNP:rs786202760EnsemblClinVar.1
Natural variantiVAR_023704707R → C in FANCJ; associated with C-647. 1 PublicationCorresponds to variant dbSNP:rs764803896EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi52K → R: Disrupts BRCA1-mediated double-strand break repair. Loss of ATPase and DNA helicase activities. 3 Publications1
Mutagenesisi986S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi988S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi989T → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi990S → A: Disrupts the interaction with BRCA1. 1 Publication1
Mutagenesisi991P → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. 1 Publication1
Mutagenesisi992T → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi993F → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. 1 Publication1
Mutagenesisi997T → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1001S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1003S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1004S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1007S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1011Y → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1013T → A: Does not affect the interaction with BRCA1. 1 Publication1

Keywords - Diseasei

Disease variant, Fanconi anemia

Organism-specific databases

DisGeNET

More...DisGeNETi		83990

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

More...GeneReviewsi		BRIP1

MalaCards human disease database

More...MalaCardsi		BRIP1
MIMi114480, phenotype
609054, phenotype

Open Targets

More...OpenTargetsi		ENSG00000136492

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

More...Orphaneti		84, Fanconi anemia
145, Hereditary breast and ovarian cancer syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA134906421

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9BX63, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		BRIP1

Domain mapping of disease mutations (DMDM)

More...DMDMi		57012613

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000551731 – 1249Fanconi anemia group J proteinAdd BLAST1249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei505PhosphoserineCombined sources1
Modified residuei927PhosphoserineCombined sources1
Modified residuei930PhosphoserineCombined sources1
Modified residuei956PhosphoserineCombined sources1
Modified residuei990PhosphoserineCombined sources1 Publication1
Modified residuei1004PhosphoserineCombined sources1
Modified residuei1032PhosphoserineCombined sources1
Modified residuei1237PhosphoserineCombined sources1
Modified residuei1249N6-acetyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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. Phosphorylation is necessary for interaction with BRCA1, and is cell-cycle regulated.1 Publication
Acetylation at Lys-1249 facilitates DNA end processing required for repair and checkpoint signaling.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-3220
CPTAC-3221
CPTAC-3222
CPTAC-3281
CPTAC-918

Encyclopedia of Proteome Dynamics

More...EPDi		Q9BX63

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9BX63

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9BX63

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9BX63

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

More...PaxDbi		Q9BX63

PeptideAtlas

More...PeptideAtlasi		Q9BX63

PRoteomics IDEntifications database

More...PRIDEi		Q9BX63

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		79352 [Q9BX63-1]
79353 [Q9BX63-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9BX63

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

More...PhosphoSitePlusi		Q9BX63

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed, with highest levels in testis.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000136492, Expressed in lung and 132 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9BX63, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9BX63, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000136492, Tissue enhanced (bone marrow, lymphoid tissue, testis)

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds directly to the BRCT domains of BRCA1 (PubMed:15125843).

Interacts with the CIA complex components CIAO1, CIAO2B and MMS19 (PubMed:23585563).

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		123841, 73 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-4426, BRCA1-B complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9BX63

Database of interacting proteins

More...DIPi		DIP-41787N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q9BX63

Protein interaction database and analysis system

More...IntActi		Q9BX63, 25 interactors

Molecular INTeraction database

More...MINTi		Q9BX63

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000259008

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9BX63

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9BX63, protein

<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

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		Q9BX63

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

More...SMRi		Q9BX63

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9BX63

<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%5Fand%5Fdomains%5Fsection">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>Domaini11 – 442Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST432

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>Regioni102 – 131DisorderedSequence analysisAdd BLAST30
Regioni888 – 1063Interaction with BRCA11 PublicationAdd BLAST176
Regioni1018 – 1042DisorderedSequence analysisAdd BLAST25
Regioni1108 – 1127DisorderedSequence analysisAdd BLAST20

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>Motifi158 – 175Nuclear localization signalSequence analysisAdd BLAST18
Motifi393 – 396DEAH box4

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1022 – 1036Polar residuesSequence analysisAdd BLAST15
Compositional biasi1108 – 1126Basic and acidic residuesSequence analysisAdd BLAST19

<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

4Fe-4S iron-sulfur-binding is required for helicase activity.1 Publication

<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 DEAD box helicase family. DEAH subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1132, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182970

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9BX63

Identification of Orthologs from Complete Genome Data

More...OMAi		CHSKNFT

Database of Orthologous Groups

More...OrthoDBi		186062at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9BX63

TreeFam database of animal gene trees

More...TreeFami		TF329449

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.300, 3 hits

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00181

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006555, ATP-dep_Helicase_C
IPR010614, DEAD_2
IPR045028, DinG/Rad3-like
IPR014013, Helic_SF1/SF2_ATP-bd_DinG/Rad3
IPR006554, Helicase-like_DEXD_c2
IPR014001, Helicase_ATP-bd
IPR027417, P-loop_NTPase
IPR013020, Rad3/Chl1-like

The PANTHER Classification System

More...PANTHERi		PTHR11472, PTHR11472, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF06733, DEAD_2, 1 hit
PF13307, Helicase_C_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00487, DEXDc, 1 hit
SM00488, DEXDc2, 1 hit
SM00491, HELICc2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00604, rad3, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51193, HELICASE_ATP_BIND_2, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 14 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9BX63-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS 
        60         70         80         90        100
GKSLALLCSA LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM 
       110        120        130        140        150
NQGTSRHFNY PSTPPSERNG TSSTCQDSPE KTTLAAKLSA KKQASIYRDE 
       160        170        180        190        200
NDDFQVEKKR IRPLETTQQI RKRHCFGTEV HNLDAKVDSG KTVKLNSPLE 
       210        220        230        240        250
KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK SKIPKIYFGT 
       260        270        280        290        300
RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME 
       310        320        330        340        350
LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC 
       360        370        380        390        400
PYYTARELIQ DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED 
       410        420        430        440        450
CARESASYSV TEVQLRFARD ELDSMVNNNI RKKDHEPLRA VCCSLINWLE 
       460        470        480        490        500
ANAEYLVERD YESACKIWSG NEMLLTLHKM GITTATFPIL QGHFSAVLQK 
       510        520        530        540        550
EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ NSRFADDYKI 
       560        570        580        590        600
AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF 
       610        620        630        640        650
SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT 
       660        670        680        690        700
IGSGPKGRNL CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL 
       710        720        730        740        750
LEKLKERWLS TGLWHNLELV KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG 
       760        770        780        790        800
EKDGALLVAV CRGKVSEGLD FSDDNARAVI TIGIPFPNVK DLQVELKRQY 
       810        820        830        840        850
NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG ALILVDDRFR 
       860        870        880        890        900
NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT 
       910        920        930        940        950
NIQDNESTLE VTSLKYSTSP YLLEAASHLS PENFVEDEAK ICVQELQCPK 
       960        970        980        990       1000
IITKNSPLPS SIISRKEKND PVFLEEAGKA EKIVISRSTS PTFNKQTKRV 
      1010       1020       1030       1040       1050
SWSSFNSLGQ YFTGKIPKAT PELGSSENSA SSPPRFKTEK MESKTVLPFT 
      1060       1070       1080       1090       1100
DKCESSNLTV NTSFGSCPQS ETIISSLKID ATLTRKNHSE HPLCSEEALD 
      1110       1120       1130       1140       1150
PDIELSLVSE EDKQSTSNRD FETEAEDESI YFTPELYDPE DTDEEKNDLA 
      1160       1170       1180       1190       1200
ETDRGNRLAN NSDCILAKDL FEIRTIKEVD SAREVKAEDC IDTKLNGILH 
      1210       1220       1230       1240 
IEESKIDDID GNVKTTWINE LELGKTHEIE IKNFKPSPSK NKGMFPGFK
Length:1,249
Mass (Da):140,867
Last modified:October 10, 2018 - v2
<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:i8ED691F03A442BE1
GO
Isoform 2 (identifier: Q9BX63-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     969-994: NDPVFLEEAGKAEKIVISRSTSPTFN → SMKSSSHLPLIEKSFIIFSEMIFIWV
     995-1249: Missing.

Show »
Length:994
Mass (Da):112,466
Checksum:iA92FE302C66F1790
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 14 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A804HJV4A0A804HJV4_HUMAN
Fanconi anemia group J protein
BRIP1
1,175Annotation 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>
A0A804HKS0A0A804HKS0_HUMAN
Fanconi anemia group J protein
BRIP1
970Annotation 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>
J3QKX0J3QKX0_HUMAN
Fanconi anemia group J protein
BRIP1
852Annotation 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>
A0A804HL36A0A804HL36_HUMAN
Fanconi anemia group J protein
BRIP1
872Annotation 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>
A0A804HJU1A0A804HJU1_HUMAN
Fanconi anemia group J protein
BRIP1
833Annotation 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>
A0A804HK62A0A804HK62_HUMAN
Fanconi anemia group J protein
BRIP1
870Annotation 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>
A0A804HIH9A0A804HIH9_HUMAN
Fanconi anemia group J protein
BRIP1
460Annotation 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>
A0A804HJY1A0A804HJY1_HUMAN
Fanconi anemia group J protein
BRIP1
232Annotation 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>
J3KS24J3KS24_HUMAN
Fanconi anemia group J protein
BRIP1
220Annotation 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>
J3QQP5J3QQP5_HUMAN
Fanconi anemia group J protein
BRIP1
380Annotation 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>
There are more potential isoformsShow all

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAC11156 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti641I → V in BAC11156 (PubMed:14702039).Curated1
Sequence conflicti767E → I AA sequence (PubMed:11301010).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02089647P → A in BC; early onset; loss of ATPase and helicase activities. 2 PublicationsCorresponds to variant dbSNP:rs28903098EnsemblClinVar.1
Natural variantiVAR_020897173R → C2 PublicationsCorresponds to variant dbSNP:rs4988345EnsemblClinVar.1
Natural variantiVAR_020898193V → I2 PublicationsCorresponds to variant dbSNP:rs4988346EnsemblClinVar.1
Natural variantiVAR_020899195L → P1 PublicationCorresponds to variant dbSNP:rs4988347EnsemblClinVar.1
Natural variantiVAR_023700255Q → H in FANCJ. 1 Publication1
Natural variantiVAR_023701264R → W1 PublicationCorresponds to variant dbSNP:rs28997569EnsemblClinVar.1
Natural variantiVAR_020900299M → I in BC; early onset; reduces helicase efficiency on longer substrates. 2 PublicationsCorresponds to variant dbSNP:rs137852985EnsemblClinVar.1
Natural variantiVAR_023702349A → P in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity. 2 PublicationsCorresponds to variant dbSNP:rs149364097EnsemblClinVar.1
Natural variantiVAR_020901419R → W1 PublicationCorresponds to variant dbSNP:rs150624408EnsemblClinVar.1
Natural variantiVAR_020902531F → V1 PublicationCorresponds to variant dbSNP:rs4988350EnsemblClinVar.1
Natural variantiVAR_020903540Q → L1 PublicationCorresponds to variant dbSNP:rs4988349EnsemblClinVar.1
Natural variantiVAR_052192633I → M. Corresponds to variant dbSNP:rs28997572EnsemblClinVar.1
Natural variantiVAR_023703647W → C in FANCJ; associated with C-707. 1 PublicationCorresponds to variant dbSNP:rs786202760EnsemblClinVar.1
Natural variantiVAR_023704707R → C in FANCJ; associated with C-647. 1 PublicationCorresponds to variant dbSNP:rs764803896EnsemblClinVar.1
Natural variantiVAR_020904832C → Y1 PublicationCorresponds to variant dbSNP:rs4988355Ensembl.1
Natural variantiVAR_020905919S → P7 PublicationsCorresponds to variant dbSNP:rs4986764EnsemblClinVar.1
Natural variantiVAR_020906935V → G1 PublicationCorresponds to variant dbSNP:rs4988356EnsemblClinVar.1
Natural variantiVAR_0209071034P → L in a patient with ovarian cancer; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1199923024EnsemblClinVar.1
Natural variantiVAR_0521931148D → E. Corresponds to variant dbSNP:rs28997573EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012540969 – 994NDPVF…SPTFN → SMKSSSHLPLIEKSFIIFSE MIFIWV in isoform 2. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_012541995 – 1249Missing in isoform 2. 1 PublicationAdd BLAST255

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
AF360549 mRNA Translation: AAK38111.1
AC002994 Genomic DNA No translation available.
AC005969 Genomic DNA No translation available.
AC060798 Genomic DNA No translation available.
CH471179 Genomic DNA Translation: EAW51430.1
CH471179 Genomic DNA Translation: EAW51432.1
CH471179 Genomic DNA Translation: EAW51431.1
CH471179 Genomic DNA Translation: EAW51433.1
BC101472 mRNA Translation: AAI01473.1
BC101474 mRNA Translation: AAI01475.1
AK074713 mRNA Translation: BAC11156.1 Different initiation.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11631.1 [Q9BX63-1]

NCBI Reference Sequences

More...RefSeqi		NP_114432.2, NM_032043.2 [Q9BX63-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000259008.7; ENSP00000259008.2; ENSG00000136492.10
ENST00000577598.5; ENSP00000464654.1; ENSG00000136492.10 [Q9BX63-2]
ENST00000682453.1; ENSP00000506943.1; ENSG00000136492.10
ENST00000683039.1; ENSP00000508303.1; ENSG00000136492.10

Database of genes from NCBI RefSeq genomes

More...GeneIDi		83990

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:83990

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000259008.7; ENSP00000259008.2; NM_032043.3; NP_114432.2

UCSC genome browser

More...UCSCi		uc002izk.3, human [Q9BX63-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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%5Freferences%5Fsection">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

Fanconi Anemia Mutation Database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF360549 mRNA Translation: AAK38111.1
AC002994 Genomic DNA No translation available.
AC005969 Genomic DNA No translation available.
AC060798 Genomic DNA No translation available.
CH471179 Genomic DNA Translation: EAW51430.1
CH471179 Genomic DNA Translation: EAW51432.1
CH471179 Genomic DNA Translation: EAW51431.1
CH471179 Genomic DNA Translation: EAW51433.1
BC101472 mRNA Translation: AAI01473.1
BC101474 mRNA Translation: AAI01475.1
AK074713 mRNA Translation: BAC11156.1 Different initiation.
CCDSiCCDS11631.1 [Q9BX63-1]
RefSeqiNP_114432.2, NM_032043.2 [Q9BX63-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T15X-ray1.85B988-995[»]
1T29X-ray2.30B985-998[»]
3AL3X-ray2.15B1129-1138[»]
AlphaFoldDBiQ9BX63
SMRiQ9BX63
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi123841, 73 interactors
ComplexPortaliCPX-4426, BRCA1-B complex
CORUMiQ9BX63
DIPiDIP-41787N
ELMiQ9BX63
IntActiQ9BX63, 25 interactors
MINTiQ9BX63
STRINGi9606.ENSP00000259008

Chemistry databases

BindingDBiQ9BX63

PTM databases

iPTMnetiQ9BX63
PhosphoSitePlusiQ9BX63

Genetic variation databases

BioMutaiBRIP1
DMDMi57012613

Proteomic databases

CPTACiCPTAC-3220
CPTAC-3221
CPTAC-3222
CPTAC-3281
CPTAC-918
EPDiQ9BX63
jPOSTiQ9BX63
MassIVEiQ9BX63
MaxQBiQ9BX63
PaxDbiQ9BX63
PeptideAtlasiQ9BX63
PRIDEiQ9BX63
ProteomicsDBi79352 [Q9BX63-1]
79353 [Q9BX63-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		18594, 313 antibodies from 36 providers

The CPTC Antibody Portal

More...CPTCi		Q9BX63, 5 antibodies

The DNASU plasmid repository

More...DNASUi		83990

Genome annotation databases

EnsembliENST00000259008.7; ENSP00000259008.2; ENSG00000136492.10
ENST00000577598.5; ENSP00000464654.1; ENSG00000136492.10 [Q9BX63-2]
ENST00000682453.1; ENSP00000506943.1; ENSG00000136492.10
ENST00000683039.1; ENSP00000508303.1; ENSG00000136492.10
GeneIDi83990
KEGGihsa:83990
MANE-SelectiENST00000259008.7; ENSP00000259008.2; NM_032043.3; NP_114432.2
UCSCiuc002izk.3, human [Q9BX63-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		83990
DisGeNETi83990

GeneCards: human genes, protein and diseases

More...GeneCardsi		BRIP1
GeneReviewsiBRIP1
HGNCiHGNC:20473, BRIP1
HPAiENSG00000136492, Tissue enhanced (bone marrow, lymphoid tissue, testis)
MalaCardsiBRIP1
MIMi114480, phenotype
605882, gene
609054, phenotype
neXtProtiNX_Q9BX63
OpenTargetsiENSG00000136492
Orphaneti84, Fanconi anemia
145, Hereditary breast and ovarian cancer syndrome
PharmGKBiPA134906421
VEuPathDBiHostDB:ENSG00000136492

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1132, Eukaryota
GeneTreeiENSGT00950000182970
InParanoidiQ9BX63
OMAiCHSKNFT
OrthoDBi186062at2759
PhylomeDBiQ9BX63
TreeFamiTF329449

Enzyme and pathway databases

BRENDAi3.6.4.12, 2681
PathwayCommonsiQ9BX63
ReactomeiR-HSA-2564830, Cytosolic iron-sulfur cluster assembly
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-9701192, Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function
R-HSA-9704331, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function
R-HSA-9704646, Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function
SignaLinkiQ9BX63
SIGNORiQ9BX63

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		83990, 98 hits in 1082 CRISPR screens

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

More...ChiTaRSi		BRIP1, human
EvolutionaryTraceiQ9BX63

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		BRIP1

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

More...GenomeRNAii		83990
PharosiQ9BX63, Tbio

Protein Ontology

More...PROi		PR:Q9BX63
RNActiQ9BX63, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000136492, Expressed in lung and 132 other tissues
ExpressionAtlasiQ9BX63, baseline and differential
GenevisibleiQ9BX63, HS

Family and domain databases

Gene3Di3.40.50.300, 3 hits
IDEALiIID00181
InterProiView protein in InterPro
IPR006555, ATP-dep_Helicase_C
IPR010614, DEAD_2
IPR045028, DinG/Rad3-like
IPR014013, Helic_SF1/SF2_ATP-bd_DinG/Rad3
IPR006554, Helicase-like_DEXD_c2
IPR014001, Helicase_ATP-bd
IPR027417, P-loop_NTPase
IPR013020, Rad3/Chl1-like
PANTHERiPTHR11472, PTHR11472, 1 hit
PfamiView protein in Pfam
PF06733, DEAD_2, 1 hit
PF13307, Helicase_C_2, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00488, DEXDc2, 1 hit
SM00491, HELICc2, 1 hit
SUPFAMiSSF52540, SSF52540, 2 hits
TIGRFAMsiTIGR00604, rad3, 1 hit
PROSITEiView protein in PROSITE
PS51193, HELICASE_ATP_BIND_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 nameiFANCJ_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: Q9BX63
Secondary accession number(s): A0A024QZ45, Q3MJE2, Q8NCI5
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 10, 2018
Last modified: May 25, 2022
This is version 185 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
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