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Protein

Breast cancer type 1 susceptibility protein homolog

Gene

Brca1

Organism
Mus musculus (Mouse)
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 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator (By similarity). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation.By similarity1 Publication

<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.By similarity EC:2.3.2.27

<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.
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 ‘Function’ 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 fingeri24 – 65RING-typePROSITE-ProRule annotationAdd BLAST42

<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 functionActivator, DNA-binding, Transferase
Biological processCell cycle, DNA damage, DNA recombination, DNA repair, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transcription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-5685938 HDR through Single Strand Annealing (SSA)
R-MMU-5685942 HDR through Homologous Recombination (HRR)
R-MMU-5689901 Metalloprotease DUBs
R-MMU-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-MMU-5693571 Nonhomologous End-Joining (NHEJ)
R-MMU-5693579 Homologous DNA Pairing and Strand Exchange
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-69473 G2/M DNA damage checkpoint

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 homolog (EC:2.3.2.27By similarity)
Alternative name(s):
RING-type E3 ubiquitin transferase BRCA1Curated
<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:Brca1
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:104537 Brca1

<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

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

Keywords - Diseasei

Tumor suppressor

<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_00000558321 – 1812Breast cancer type 1 susceptibility protein homologAdd BLAST1812

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 residuei1N-acetylmethionineBy similarity1
<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-linki109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei114PhosphoserineBy similarity1
Cross-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei305PhosphoserineBy similarity1
Cross-linki336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei392PhosphoserineBy similarity1
Cross-linki440Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei686PhosphoserineBy similarity1
Modified residuei706PhosphoserineCombined sources1
Modified residuei717PhosphoserineCombined sources1
Modified residuei831PhosphoserineCombined sources1
Modified residuei971Phosphoserine; by CHEK2By similarity1
Modified residuei992PhosphoserineBy similarity1
Cross-linki1048Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1152PhosphoserineBy similarity1
Modified residuei1154PhosphoserineBy similarity1
Modified residuei1174PhosphoserineBy similarity1
Modified residuei1180PhosphoserineBy similarity1
Modified residuei1241PhosphoserineBy similarity1
Modified residuei1297PhosphoserineBy similarity1
Modified residuei1303PhosphoserineBy similarity1
Modified residuei1343PhosphoserineBy similarity1
Modified residuei1350PhosphothreonineBy similarity1
Modified residuei1413PhosphoserineBy similarity1
Modified residuei1481PhosphoserineBy similarity1
Modified residuei1495PhosphoserineBy similarity1

<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 IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Phosphorylation at Ser-971 by CHEK2 regulates mitotic spindle assembly.By similarity
Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P48754

MaxQB - The MaxQuant DataBase

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MaxQBi
P48754

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

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PaxDbi
P48754

PeptideAtlas

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PeptideAtlasi
P48754

PRoteomics IDEntifications database

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PRIDEi
P48754

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P48754

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

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PhosphoSitePlusi
P48754

<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

In the embryo, expressed in otic vesicles at day 9.5. At day 10.5, this expression decreases and high levels are found in the neuroectoderm. At days 11-12.5, high levels in differentiating keratinocytes and whisker pad primordia. At days 14-17, expression also observed in kidney epithelial cells. In the adult, highest levels found in spleen, thymus, lymph nodes, epithelial organs, and alveolar and ductal epithelial cells of the mammary gland. Very low levels in brain, kidney, and skin. No expression in heart, liver or lung.

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In the mammary gland, expression increases dramatically during pregnancy. Levels fall during lactation and increase again during post-lactational regression of the mammary gland.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000017146 Expressed in 243 organ(s), highest expression level in zygote

CleanEx database of gene expression profiles

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CleanExi
MM_BRCA1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P48754 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P48754 MM

<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 with BARD1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Component of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Interacts (via the BRCT domains) with ABRAXAS1 (phosphorylated form); this is important for recruitment to sites of DNA damage. Can form a heterotetramer with two molecules of ABRAXAS1 (phosphorylated form). Component of the BRCA1-RBBP8 complex. Interacts (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the interaction ubiquitinates RBBP8, regulates CHEK1 activation, and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Associates with RNA polymerase II holoenzyme. Interacts with SMC1A, COBRA1, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, AURKA, UBXN1 and PCLAF. Interacts (via BRCT domains) with BRIP1 (phosphorylated form). Interacts with FANCD2 (ubiquitinated form). Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts (via the BRCT domains) with ACACA (phosphorylated form); the interaction prevents dephosphorylation of ACACA. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2; the interaction is essential for its function in HRR. Interacts directly with BRCA2; the interaction occurs only in the presence of PALB2 which serves as the bridging protein. Interacts (via the BRCT domains) with LMO4; the interaction represses the transcriptional activity of BRCA1. Interacts (via the BRCT domains) with CCAR2 (via N-terminus); the interaction represses the transcriptional activator activity of BRCA1 (By similarity). Interacts with EXD2 (By similarity). Interacts (via C-terminus) with DHX9; this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
198383, 43 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-972 BRCC ubiquitin ligase complex

Database of interacting proteins

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DIPi
DIP-41981N

Protein interaction database and analysis system

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IntActi
P48754, 16 interactors

Molecular INTeraction database

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MINTi
P48754

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000017290

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P48754

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

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SMRi
P48754

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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>Domaini1585 – 1679BRCT 1PROSITE-ProRule annotationAdd BLAST95
Domaini1698 – 1797BRCT 2PROSITE-ProRule annotationAdd BLAST100

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>Regioni1353 – 1380Interaction with PALB2By similarityAdd BLAST28

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 biasi1562 – 1567Poly-Ala6

<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 BRCT domains recognize and bind phosphorylated pSXXF motif on proteins. The interaction with the phosphorylated pSXXF motif of ABRAXAS1, recruits BRCA1 at DNA damage sites.By similarity
The RING-type zinc finger domain interacts with BAP1.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri24 – 65RING-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410ITQ6 Eukaryota
ENOG4111WR7 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00440000034289

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230969

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050730

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P48754

KEGG Orthology (KO)

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KOi
K10605

Identification of Orthologs from Complete Genome Data

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OMAi
CNDRQTP

Database of Orthologous Groups

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OrthoDBi
EOG091G0670

TreeFam database of animal gene trees

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TreeFami
TF105060

Family and domain databases

Conserved Domains Database

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CDDi
cd00027 BRCT, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.40.10, 1 hit
3.40.50.10190, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011364 BRCA1
IPR031099 BRCA1-associated
IPR025994 BRCA1_serine_dom
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

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PANTHERi
PTHR13763 PTHR13763, 1 hit
PTHR13763:SF0 PTHR13763:SF0, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00533 BRCT, 2 hits
PF12820 BRCT_assoc, 1 hit
PF00097 zf-C3HC4, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001734 BRCA1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00493 BRSTCANCERI

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52113 SSF52113, 2 hits

PROSITE; a protein domain and family database

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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>.<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

P48754-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDLSAVQIQE VQNVLHAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK
60 70 80 90 100
LLNQKKGPSQ CPLCKNEITK RSLQGSTRFS QLAEELLRIM AAFELDTGMQ
110 120 130 140 150
LTNGFSFSKK RNNSCERLNE EASIIQSVGY RNRVRRLPQV EPGNATLKDS
160 170 180 190 200
LGVQLSNLGI VRSVKKNRQT QPRKKSVYIE LDSDSSEETV TKPGDCSVRD
210 220 230 240 250
QELLQTAPQE AGDEGKLHSA EEAACEFSEG IRNIEHHQCS DDLNPTENHA
260 270 280 290 300
TERHPEKCQS ISISNVCVEP CGTDAHASSL QPETSSLLLI EDRMNAEKAE
310 320 330 340 350
FCNKSKQPGI AVSQQSRWAA SKGTCNDRQV PSTGEKVGPN ADSLSDREKW
360 370 380 390 400
THPQSLCPEN SGATTDVPWI TLNSSVQKVN EWFSRTGEML TSDSASARRH
410 420 430 440 450
ESNAEAAVVL EVSNEVDGGF SSSRKTDLVT PDPHHTLMCK SGRDFSKPVE
460 470 480 490 500
DNISDKIFGK SYQRKGSRPH LNHVTEIIGT FITEPQITQE QPFTNKLKRK
510 520 530 540 550
RSTSLQPEDF IKKADSAGVQ RTPDNINQGT DLMEPNEQAV STTSNCQENK
560 570 580 590 600
IAGSNLQKEK SAHPTESLRK EPASTAGAKS ISNSVSDLEV ELNVHSSKAP
610 620 630 640 650
KKNRLRRKSS IRCALPLEPI SRNPSPPTCA ELQIDSCGSS EETKKNHSNQ
660 670 680 690 700
QPAGHLREPQ LIEDTEPAAD AKKNEPNEHI RKRRASDAFP EEKLMNKAGL
710 720 730 740 750
LTSCSSPRKS QGPVNPSPQR TGTEQLETRQ MSDSAKELGD RVLGGEPSGK
760 770 780 790 800
TTDRSEESTS VSLVSDTDYD TQNSVSVLDA HTVRYARTGS AQCMTQFVAS
810 820 830 840 850
ENPKELVHGS NNAGSGTEGL KPPLRHALNL SQEKVEMEDS ELDTQYLQNT
860 870 880 890 900
FQVSKRQSFA LFSKPRSPQK DCAHSVPSKE LSPKVTAKGK QKERQGQEEF
910 920 930 940 950
EISHVQAVAA TVGLPVPCQE GKLAADTMCD RGCRLCPSSH YRSGENGLSA
960 970 980 990 1000
TGKSGISQNS HFKQSVSPIR SSIKTDNRKP LTEGRFERHT SSTEMAVGNE
1010 1020 1030 1040 1050
NILQSTVHTV SLNNRGNACQ EAGSGSIHEV CSTGDSFPGQ LGRNRGPKVN
1060 1070 1080 1090 1100
TVPPLDSMQP GVCQQSVPVS DKYLEIKKQE GEAVCADFSP CLFSDHLEQS
1110 1120 1130 1140 1150
MSGKVFQVCS ETPDDLLDDV EIQGHTSFGE GDIMERSAVF NGSILRRESS
1160 1170 1180 1190 1200
RSPSPVTHAS KSQSLHRASR KLESSEESDS TEDEDLPCFQ HLLSRISNTP
1210 1220 1230 1240 1250
ELTRCSSAVT QRMPEKAEGT QAPWKGSSSD CNNEVIMIEA SQEHQFSEDP
1260 1270 1280 1290 1300
RCSGSMFSSQ HSAAQGSTAN ANSQDSNFIP PSKQRSHQCG NEEAFLSDKE
1310 1320 1330 1340 1350
LISDNEEMAT CLEEDNDQEE DSIIPDSEAS GYESETNLSE DCSQSDILTT
1360 1370 1380 1390 1400
QQRATMKYNL IKLQQEMAHL EAVLEQRGNQ PSGHSPSLLA DPCALEDLPD
1410 1420 1430 1440 1450
LEPNMSGAAI LTSKNINENP VSQNLKSACD DKFQLQHLEG PTSGDDESGM
1460 1470 1480 1490 1500
GRPSPFKSPL AGSRGSAHGC SRHLQKRNSP SQEELLQPAG SEASSEPHNS
1510 1520 1530 1540 1550
TGQSCLPRRE LEGTPYLGSG ISLFSSRDPE SESPKEPAHI GTTPASTSAL
1560 1570 1580 1590 1600
KIPQGQVAFR SAAAAGADKA VVGIVSKIKP ELTSSEERAD RDISMVVSGL
1610 1620 1630 1640 1650
TPKEVMTVQK FAEKYRLTLT DAITEETTHV IIKTDAEFVC ERTLKYFLGI
1660 1670 1680 1690 1700
AGGKWIVSYS WVVRSIQERR LLNVHEFEVK GDVVTGRNHQ GPRRSRESRE
1710 1720 1730 1740 1750
KLFKGLQVYC CEPFTNMPKD ELERMLQLCG ASVVKELPSL THDTGAHLVV
1760 1770 1780 1790 1800
IVQPSAWTED SNCPDIGQLC KARLVMWDWV LDSLSSYRCR DLDAYLVQNI
1810
TCDSSEPQDS ND
Length:1,812
Mass (Da):198,795
Last modified:October 3, 2012 - v3
<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:i2B47FB55B149FD71
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
A0A087WPK5A0A087WPK5_MOUSE
Breast cancer type 1 susceptibility...
Brca1
75Annotation score:

Annotation score:3 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>
A0A087WP26A0A087WP26_MOUSE
Breast cancer type 1 susceptibility...
Brca1
79Annotation score:

Annotation score:3 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>
A0A087WPE1A0A087WPE1_MOUSE
Breast cancer type 1 susceptibility...
Brca1
177Annotation score:

Annotation score:3 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 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 conflicti93F → L in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti305S → T in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti319A → P in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti377Q → E in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti550K → Q in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti652P → A in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti765S → P in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti765S → P in AAC52323 (PubMed:7590247).Curated1
Sequence conflicti917P → L in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti933C → S in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti933C → S in AAA99742 (PubMed:8566965).Curated1
Sequence conflicti1091C → R in AAB17114 (PubMed:8634697).Curated1
Sequence conflicti1122I → K in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1206S → R in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti1212 – 1213RM → GI in AAA96393 (PubMed:8575748).Curated2
Sequence conflicti1255S → R in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti1261H → N in AAA96393 (PubMed:8575748).Curated1
Sequence conflicti1264A → V in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1269A → P in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1283K → T in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1337N → T in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1349T → P in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1352 – 1353QR → EG in AAB17113 (PubMed:8634698).Curated2
Sequence conflicti1381P → S in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1390A → G in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1400D → V in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1503Q → E in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1549A → V in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1680K → T in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1712E → D in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1721E → D in AAB17113 (PubMed:8634698).Curated1
Sequence conflicti1791D → G in AAB17114 (PubMed:8634697).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U31625 mRNA Translation: AAB17114.1
U35641 mRNA Translation: AAB17113.1
U32446 mRNA Translation: AAA96393.1
U36475 mRNA Translation: AAC52323.1
AL590996 Genomic DNA Translation: CAM21026.1
U33835 Genomic DNA Translation: AAA99742.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS25474.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I49350

NCBI Reference Sequences

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RefSeqi
NP_033894.3, NM_009764.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.244975

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000017290; ENSMUSP00000017290; ENSMUSG00000017146

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
12189

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:12189

UCSC genome browser

More...
UCSCi
uc007lpd.2 mouse

<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
U31625 mRNA Translation: AAB17114.1
U35641 mRNA Translation: AAB17113.1
U32446 mRNA Translation: AAA96393.1
U36475 mRNA Translation: AAC52323.1
AL590996 Genomic DNA Translation: CAM21026.1
U33835 Genomic DNA Translation: AAA99742.1
CCDSiCCDS25474.1
PIRiI49350
RefSeqiNP_033894.3, NM_009764.3
UniGeneiMm.244975

3D structure databases

ProteinModelPortaliP48754
SMRiP48754
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198383, 43 interactors
ComplexPortaliCPX-972 BRCC ubiquitin ligase complex
DIPiDIP-41981N
IntActiP48754, 16 interactors
MINTiP48754
STRINGi10090.ENSMUSP00000017290

PTM databases

iPTMnetiP48754
PhosphoSitePlusiP48754

Proteomic databases

EPDiP48754
MaxQBiP48754
PaxDbiP48754
PeptideAtlasiP48754
PRIDEiP48754

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017290; ENSMUSP00000017290; ENSMUSG00000017146
GeneIDi12189
KEGGimmu:12189
UCSCiuc007lpd.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
672
MGIiMGI:104537 Brca1

Phylogenomic databases

eggNOGiENOG410ITQ6 Eukaryota
ENOG4111WR7 LUCA
GeneTreeiENSGT00440000034289
HOGENOMiHOG000230969
HOVERGENiHBG050730
InParanoidiP48754
KOiK10605
OMAiCNDRQTP
OrthoDBiEOG091G0670
TreeFamiTF105060

Enzyme and pathway databases

UniPathwayi
UPA00143

ReactomeiR-MMU-3108214 SUMOylation of DNA damage response and repair proteins
R-MMU-5685938 HDR through Single Strand Annealing (SSA)
R-MMU-5685942 HDR through Homologous Recombination (HRR)
R-MMU-5689901 Metalloprotease DUBs
R-MMU-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-MMU-5693571 Nonhomologous End-Joining (NHEJ)
R-MMU-5693579 Homologous DNA Pairing and Strand Exchange
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-69473 G2/M DNA damage checkpoint

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P48754

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000017146 Expressed in 243 organ(s), highest expression level in zygote
CleanExiMM_BRCA1
ExpressionAtlasiP48754 baseline and differential
GenevisibleiP48754 MM

Family and domain databases

CDDicd00027 BRCT, 2 hits
Gene3Di3.30.40.10, 1 hit
3.40.50.10190, 2 hits
InterProiView protein in InterPro
IPR011364 BRCA1
IPR031099 BRCA1-associated
IPR025994 BRCA1_serine_dom
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, 1 hit
PTHR13763:SF0 PTHR13763:SF0, 1 hit
PfamiView protein in Pfam
PF00533 BRCT, 2 hits
PF12820 BRCT_assoc, 1 hit
PF00097 zf-C3HC4, 1 hit
PIRSFiPIRSF001734 BRCA1, 1 hit
PRINTSiPR00493 BRSTCANCERI
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...

<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_MOUSE
<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: P48754
Secondary accession number(s): A2A4Q4, Q60957, Q60983
<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: February 1, 1996
Last sequence update: October 3, 2012
Last modified: December 5, 2018
This is version 185 of the entry and version 3 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

<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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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