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UniProtKB - B6VQ60 (BRCA1_CAEEL)

Entry version 93 (31 Jul 2019)
Sequence version 1 (16 Dec 2008)
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Protein

Breast cancer type 1 susceptibility protein homolog

Gene

brc-1

Organism
Caenorhabditis elegans
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

E3 ubiquitin-protein ligase that specifically mediates the formation of polyubiquitin chains and plays a central role in DNA repair (PubMed:16628214). Plays a role in triggering cellular responses at damage sites in response to DNA damage that may be induced by UV and ionizing radiation for example (PubMed:14711411, PubMed:16628214, PubMed:24424777, PubMed:26903030). Functions in double-strand break repair, and is required for homologous recombination between sister chromatids in meiotic and mitotic cells (PubMed:18219312, PubMed:19646877, PubMed:24424777, PubMed:26903030). In particular, protects against chromosome non-disjunction and nuclear fragmentation during meiotic double-strand break repair to ensure sister chromatid recombination and aid chromosome stability (PubMed:14711411, PubMed:18219312, PubMed:24424777). Required for normal cell cycle progression (PubMed:20207739). Along with brap-2 modulates the expression of cell cycle arrest protein cki-1 in response to increased levels of reactive oxygen species (PubMed:20207739). Constituent of the CeBCD complex that possesses E3 ubiquitin-protein ligase activity (PubMed:14711411). When bound to chromatin, the brc-1-brd-1 heterodimer within the CeBCD complex is inactive during normal conditions, but in response to DNA damage, the brc-1-brd-1 heterodimer associates with other proteins such as the recombinase rad-51 or the E2-ubiquitin-conjugating enzyme let-70, which activate the CeBCD complex as an E3-ubiquitin ligase (PubMed:16628214). Moreover, association between the brc-1-brd-1 heterodimer and rad-51 and let-70, probably requires DNA checkpoint proteins such as atl-1 and mre-11 in order to induce ubiquitination at DNA damage sites (PubMed:16628214). To this end, the brc-1-brd-1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:14711411).7 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

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.1 Publication EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

E3 ubiquitin-protein ligase activity of CeBCD complexes occurs at DNA damage sites. Following DNA damage, E3 ubiquitin-protein ligase activity is reduced by caffeine treatment (inhibitor of ATM and ATK kinase activity).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri21 – 61RING-typePROSITE-ProRule annotationAdd BLAST41

<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 functionTransferase
Biological processCell cycle, DNA damage, DNA repair
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-CEL-3108214 SUMOylation of DNA damage response and repair proteins
R-CEL-5685938 HDR through Single Strand Annealing (SSA)
R-CEL-5693607 Processing of DNA double-strand break ends

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

<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:
Breast cancer type 1 susceptibility protein homologBy similarity (EC:2.3.2.271 Publication)
Alternative name(s):
RING-type E3 ubiquitin transferase BRCA1By similarity
<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:brc-11 PublicationImported
ORF Names:C36A4.8Imported
<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>OrganismiCaenorhabditis elegansImported
<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 identifieri6239 [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 lineageiEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditina › Rhabditomorpha › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis
<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
  • UP000001940 <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 III

Organism-specific databases

WormBase

More...WormBasei		C36A4.8a ; CE43190 ; WBGene00000264 ; brc-1
C36A4.8b ; CE43228 ; WBGene00000264 ; brc-1

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, 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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Animals are viable (PubMed:18219312, PubMed:19646877). However, there is defective double strand break repair (PubMed:18219312, PubMed:19646877, PubMed:26903030). During the early stages of meiosis, this is characterized by impaired homologous recombination in germ cells with increased apoptosis and increased numbers of rad-51-positive foci (PubMed:18219312, PubMed:19646877). Increased sensitivity to UV and IR irradiation and topoisomerase inhibitor camptothecin compared to wild-type (PubMed:24424777, PubMed:26903030). Following either IR irradiation or camptothecin treatment, there is reduced egg hatching (PubMed:26903030). Furthermore, there are also DNA damage repair defects following ionizing radiation and UV irradiation characterized by reduced ubiquitination at DNA damage sites and reduced rad-51-positive foci, respectively (PubMed:16628214, PubMed:24424777, PubMed:26903030). RNAi-mediated knockdown results in high X chromosome non-disjunction leading to a high incidence of males (him) phenotype (PubMed:14711411). RNAi-mediated knockdown in addition to gamma-irradiation at the L4 stage of larval development, results in reduced progeny, increased cep-1/p53-dependent germ cell death, chromosome fragmentation and DNA repair defects (PubMed:14711411).6 Publications

<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_00004425811 – 612Breast cancer type 1 susceptibility protein homologCuratedAdd BLAST612

<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

Phosphorylation of CeBCD complexes is required for E3 ubiquitin-protein ligase activity.1 Publication

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		B6VQ60

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

More...PaxDbi		B6VQ60

PeptideAtlas

More...PeptideAtlasi		B6VQ60

<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

More...Bgeei		WBGene00000264 Expressed in 5 organ(s), highest expression level in adult organism

<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

Heterodimer (via RING-type zinc finger) with brd-1 to form the core CeBCD complex (PubMed:14711411, PubMed:16628214). Brc-1-brd-1 heterodimer-containing CeBCD complexes bound to chromatin are activated as an E3-ubiquitin ligase in response to DNA damage (PubMed:16628214). The heterodimer interacts with the recombinase rad-51 following ionizing irradiation; the interaction is direct (PubMed:16628214). The heterodimer interacts the E2-ubiquitin-conjugating enzyme let-70 following ionizing irradiation (PubMed:16628214).

2 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

WithEntry#Exp.IntActNotes
brd-1Q212094EBI-3895496,EBI-3895480

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-375 brc-1/brd-1 complex

Protein interaction database and analysis system

More...IntActi		B6VQ60, 1 interactor

STRING: functional protein association networks

More...STRINGi		6239.C36A4.8a

<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>Domaini415 – 477BRCT 1PROSITE-ProRule annotationAdd BLAST63
Domaini505 – 603BRCT 2PROSITE-ProRule annotationAdd BLAST99

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri21 – 61RING-typePROSITE-ProRule annotationAdd BLAST41

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4362 Eukaryota
ENOG41120NI LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00440000034289

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000199539

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		B6VQ60

Identification of Orthologs from Complete Genome Data

More...OMAi		MMNSEGR

Database of Orthologous Groups

More...OrthoDBi		472443at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 1 hit
3.40.50.10190, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011364 BRCA1
IPR031099 BRCA1-associated
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR018957 Znf_C3HC4_RING-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

The PANTHER Classification System

More...PANTHERi		PTHR13763 PTHR13763, 2 hits
PTHR13763:SF0 PTHR13763:SF0, 2 hits

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16589 BRCT_2, 1 hit
PF00097 zf-C3HC4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00292 BRCT, 2 hits
SM00184 RING, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52113 SSF52113, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50172 BRCT, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_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_length">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_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 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
Isoform aImported (identifier: B6VQ60-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><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
MADVALRITE TVARLQKELK CGICCSTYKD PILSTCFHIF CRSCINACFE 
        60         70         80         90        100
RKRKVQCPIC RSVLDKRSCR DTYQITMAVQ NYLKLSEAFK KDIENMNTFK 
       110        120        130        140        150
SLPPEKMFME SQMPLDITII PENDGKRCAP DFAIPFLPVR RKRPSRPQPP 
       160        170        180        190        200
SAFAEEPAEP VEPPEPATKQ PVELQSRVFP LEKLKKDVET STETYKISRE 
       210        220        230        240        250
ELKNVDIEEY INTLRENSTE IDEIDALFQL MPTMRQFLRN NINQLMEKFH 
       260        270        280        290        300
VAPPKKSEKP ANRRVSFASS QDLENIKIMT ASESLETPPE PIQKLAQKPE 
       310        320        330        340        350
VFKSTQNLID LNLNTAVKKP VVVASDDDEV VEDSEGELQI DEDDLANVTC 
       360        370        380        390        400
ATSSTTLDAD RTPKAIQDDE DRIDDELSQV PKTIVCSRIH NDADEVVGLE 
       410        420        430        440        450
LLSDFYHKFL SNACRFAEDV NEHTTHLVMM NSEGRSISQK STAYLYAIAR 
       460        470        480        490        500
KCVIVGRQWL VDCITTGLLL SEADYTITSC SSTIPVKIPP SIGSEMGWLR 
       510        520        530        540        550
SRNDEHGKLF AGRRFMILRK FTMNPYFDYK QLIELVQQCG GEILSCYENL 
       560        570        580        590        600
SPEKLYIIFS KHSKAIEESK NIENLYKCDV VTMEWVLDSI SEYLILPTQP 
       610 
YKAVDSIGCL QD
Length:612
Mass (Da):69,718
Last modified:December 16, 2008 - 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:i159B448AEE153B8B
GO
Isoform bImported (identifier: B6VQ60-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-495: Missing.

Show »
Length:117
Mass (Da):13,737
Checksum:iA18F6013E5DB7F3E
GO

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_0592591 – 495Missing in isoform b. CuratedAdd BLAST495

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
BX284603 Genomic DNA Translation: CAR97812.1
BX284603 Genomic DNA Translation: CAR97813.1

NCBI Reference Sequences

More...RefSeqi		NP_001254881.1, NM_001267952.1 [B6VQ60-1]
NP_001254882.1, NM_001267953.1 [B6VQ60-2]

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		C36A4.8a; C36A4.8a; WBGene00000264 [B6VQ60-1]
C36A4.8b; C36A4.8b; WBGene00000264 [B6VQ60-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		175499

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cel:CELE_C36A4.8

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284603 Genomic DNA Translation: CAR97812.1
BX284603 Genomic DNA Translation: CAR97813.1
RefSeqiNP_001254881.1, NM_001267952.1 [B6VQ60-1]
NP_001254882.1, NM_001267953.1 [B6VQ60-2]

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Protein-protein interaction databases

ComplexPortaliCPX-375 brc-1/brd-1 complex
IntActiB6VQ60, 1 interactor
STRINGi6239.C36A4.8a

Proteomic databases

EPDiB6VQ60
PaxDbiB6VQ60
PeptideAtlasiB6VQ60

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC36A4.8a; C36A4.8a; WBGene00000264 [B6VQ60-1]
C36A4.8b; C36A4.8b; WBGene00000264 [B6VQ60-2]
GeneIDi175499
KEGGicel:CELE_C36A4.8

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		175499
WormBaseiC36A4.8a ; CE43190 ; WBGene00000264 ; brc-1
C36A4.8b ; CE43228 ; WBGene00000264 ; brc-1

Phylogenomic databases

eggNOGiKOG4362 Eukaryota
ENOG41120NI LUCA
GeneTreeiENSGT00440000034289
HOGENOMiHOG000199539
InParanoidiB6VQ60
OMAiMMNSEGR
OrthoDBi472443at2759

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-CEL-3108214 SUMOylation of DNA damage response and repair proteins
R-CEL-5685938 HDR through Single Strand Annealing (SSA)
R-CEL-5693607 Processing of DNA double-strand break ends

Miscellaneous databases

Protein Ontology

More...PROi		PR:B6VQ60

Gene expression databases

BgeeiWBGene00000264 Expressed in 5 organ(s), highest expression level in adult organism

Family and domain databases

Gene3Di3.30.40.10, 1 hit
3.40.50.10190, 2 hits
InterProiView protein in InterPro
IPR011364 BRCA1
IPR031099 BRCA1-associated
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR018957 Znf_C3HC4_RING-type
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR13763 PTHR13763, 2 hits
PTHR13763:SF0 PTHR13763:SF0, 2 hits
PfamiView protein in Pfam
PF16589 BRCT_2, 1 hit
PF00097 zf-C3HC4, 1 hit
SMARTiView protein in SMART
SM00292 BRCT, 2 hits
SM00184 RING, 1 hit
SUPFAMiSSF52113 SSF52113, 2 hits
PROSITEiView protein in PROSITE
PS50172 BRCT, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiBRCA1_CAEEL
<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: B6VQ60
Secondary accession number(s): B6VQ61
<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: December 20, 2017
Last sequence update: December 16, 2008
Last modified: July 31, 2019
This is version 93 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 programCaenorhabditis annotation project

<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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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