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Entry version 162 (12 Aug 2020)
Sequence version 1 (01 Jun 1998)
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Protein

Breast cancer type 1 susceptibility protein homolog

Gene

Brca1

Organism
Rattus norvegicus (Rat)
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. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. 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).By similarity

<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

  • 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%5Fsection">'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 <a href="http://www.uniprot.org/help/function%5Fsection">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 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-RNO-3108214, SUMOylation of DNA damage response and repair proteins
R-RNO-5685938, HDR through Single Strand Annealing (SSA)
R-RNO-5685942, HDR through Homologous Recombination (HRR)
R-RNO-5689901, Metalloprotease DUBs
R-RNO-5693554, Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-5693568, Resolution of D-loop Structures through Holliday Junction Intermediates
R-RNO-5693571, Nonhomologous End-Joining (NHEJ)
R-RNO-5693579, Homologous DNA Pairing and Strand Exchange
R-RNO-5693607, Processing of DNA double-strand break ends
R-RNO-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation
R-RNO-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%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:
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%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:Brca1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2218, 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 & 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

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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000558351 – 1817Breast cancer type 1 susceptibility protein homologAdd BLAST1817

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%5Fprocessing%5Fsection">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-linki299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei306Phosphoserine; by AURKABy similarity1
Cross-linki337Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei393PhosphoserineBy similarity1
Cross-linki457Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki513Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki578Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei686PhosphoserineBy similarity1
Modified residuei706PhosphoserineBy similarity1
Modified residuei717PhosphoserineBy similarity1
Modified residuei975Phosphoserine; by CHEK2By similarity1
Cross-linki1049Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1153PhosphoserineBy similarity1
Modified residuei1155PhosphoserineBy similarity1
Modified residuei1181PhosphoserineBy similarity1
Modified residuei1242PhosphoserineBy similarity1
Modified residuei1298PhosphoserineBy similarity1
Modified residuei1304PhosphoserineBy similarity1
Modified residuei1344PhosphoserineBy similarity1
Modified residuei1351PhosphothreonineBy similarity1
Modified residuei1380PhosphoserineBy similarity1
Modified residuei1414PhosphoserineBy similarity1
Modified residuei1482PhosphoserineBy similarity1

<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

Phosphorylation at Ser-306 by AURKA is required for normal cell cycle progression from G2 to mitosis. Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Phosphorylation at Ser-975 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

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

More...
PaxDbi
O54952

PRoteomics IDEntifications database

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PRIDEi
O54952

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O54952

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

More...
PhosphoSitePlusi
O54952

<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

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, NELFB, 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 H2AX (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 similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000028109

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

Secondary structure

11817
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
O54952

Database of comparative protein structure models

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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
O54952

<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>Domaini1588 – 1682BRCT 1PROSITE-ProRule annotationAdd BLAST95
Domaini1701 – 1800BRCT 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>Regioni1354 – 1381Interaction with PALB2By similarityAdd BLAST28

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>Motifi497 – 503Nuclear localization signalSequence analysis7

<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

More...
eggNOGi
KOG4362, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O54952

KEGG Orthology (KO)

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KOi
K10605

Database for complete collections of gene phylogenies

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PhylomeDBi
O54952

Family and domain databases

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

More...
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%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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O54952-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDLSAVRIQE VQNVLHAMQK ILECPICLEL IKEPVSTQCD HIFCKFCMLK
60 70 80 90 100
LLNQKKGPSQ CPLCKNEITK RSLQGSARFS QLVEELLKII DAFELDTGMQ
110 120 130 140 150
CANGFSFSKK KNSSSELLNE DASIIQSVGY RNRVKKLQQI ESGSATLKDS
160 170 180 190 200
LSVQLSNLGI VRSMKKNRQT QPQNKSVYIA LESDSSEERV NAPDGCSVRD
210 220 230 240 250
QELFQIAPGG AGDEGKLNSA KKAACDFSEG IRNIEHHQCS DKDLNPTENH
260 270 280 290 300
ATERHPEKCP RISVANVHVE PCGTDARASS LQRGTRSLLF TEDRLDAEKA
310 320 330 340 350
EFCDRSKQSG AAVSQQSRWA DSKETCNGRP VPRTEGKADP NVDSLCGRKQ
360 370 380 390 400
WNHPKSLCPE NSGATTDVPW ITLNSSIQKV NEWFSRTGEM LTSDNASDRR
410 420 430 440 450
PASNAEAAVV LEVSNEVDGC FSSSKKIDLV APDPDNAVMC TSGRDFSKPV
460 470 480 490 500
ENIINDKIFG KTYQRKGSRP HLNHVTEIIG TFTTEPQIIQ EQPFTNKLKR
510 520 530 540 550
KRSTCLHPED FIKKADLTVV QRISENLNQG TDQMEPNDQA MSITSNGQEN
560 570 580 590 600
RATGNDLQRG RNAHPIESLR KEPAFTAKAK SISNSISDLE VELNVHSSKA
610 620 630 640 650
PKKNRLRRKS TRCVLPLEPI SRNPSPPTCA ELQIESCGSS EETKKNNSNQ
660 670 680 690 700
TPAGHIREPQ LIEDTEPAAD AKKNEPNEHI RKRSASDAFP EEKLMNKAGL
710 720 730 740 750
LTSCSSPRKP QGPVNPSPER KGIEQLEMCQ MPDNNKELGD LVLGGEPSGK
760 770 780 790 800
PTEPSEESTS VSLVPDTDYD TQNSVSILEA NTVRYARTGS VQCMTQFVAS
810 820 830 840 850
ENPKELVHGS NNAGSGSECF KHPLRHELNH NQETIEMEDS ELDTQYLQNT
860 870 880 890 900
FQVSKRQSFA LFSKLRSPQK DCTLVGARSV PSREPSPKVT SRGEQKERQG
910 920 930 940 950
QEESEISHVQ AVTVTVGLPV PCQEGKPGAV TMCADVSRLC PSSHYRSCEN
960 970 980 990 1000
GLNTTDKSGI SQNSHFRQSV SPLRSSIKTD NRKTLTEGRF EKHTERGMGN
1010 1020 1030 1040 1050
ETAVQSTIHT ISLNNRGDAC LEASSGSVIE VHSTGENVQG QLDRNRGPKV
1060 1070 1080 1090 1100
NTVSLLDSTQ PGVSKQSAPV SDKYLEIKQE SKAVSADFSP CLFSDHLEKP
1110 1120 1130 1140 1150
MRSDKTFQVC SETPDDLLDD VEIQENASFG EGGITEKSAI FNGSVLRRES
1160 1170 1180 1190 1200
SRSPSPVTHA SKSRSLHRGS RKLEFSEESD STEDEDLPCF QHLLSRVSST
1210 1220 1230 1240 1250
PELTRCSSVV TQRVPEKAKG TQAPRKSSIS DCNNEVILGE ASQEYQFSED
1260 1270 1280 1290 1300
AKCSGSMFSS QHSAALGSPA NALSQDPDFN PPSKQRRHQA ENEEAFLSDK
1310 1320 1330 1340 1350
ELISDHEDMA ACLEEASDQE EDSIIPDSVA SGYESEANLS EDCSQSDILT
1360 1370 1380 1390 1400
TQQRATMKDN LIKLQQEMAQ LEAVLEQHGS QPSGHPPCLP ADPCALEDLP
1410 1420 1430 1440 1450
DPEQNRSGTA ILTSKNINEN PVSQNPKRAC DDKSQPQPPD GLPSGDKESG
1460 1470 1480 1490 1500
MRRPSPFKSP LTSSRCSARG HSRSLQNRNS TSQEELLQPA XLEKSCEPHN
1510 1520 1530 1540 1550
LTGRSCLPRQ DLEGTPYPES GIRLVSSRDP DSESPKVSAL VCTAPASTSA
1560 1570 1580 1590 1600
LKISQGQVAG SCRSPAAGGA DTAVVEIVSK IKPEVTSPKE RAERDISMVV
1610 1620 1630 1640 1650
SGLTPKEVMI VQKFAEKYRL ALTDVITEET THVIIKTDAE FVCERTLKYF
1660 1670 1680 1690 1700
LGIAGGKWIV SYSWVIKSIQ ERKLLSVHEF EVKGDVVTGS NHQGPRRSRE
1710 1720 1730 1740 1750
SQEKLFEGLQ IYCCEPFTNM PKDELERMLQ LCGASVVKEL PLLTRDTGAH
1760 1770 1780 1790 1800
PIVLVQPSAW TEDNDCPDIG QLCKGRLVMW DWVLDSISVY RCRDLDAYLV
1810
QNITCGRDGS EPQDSND
Length:1,817
Mass (Da):199,879
Last modified:June 1, 1998 - 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:iC0B4760F0E349A01
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V8S5G3V8S5_RAT
Breast cancer type 1 susceptibility...
Brca1 rCG_34321
1,817Annotation 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 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 conflicti38Q → K in AAB40387 (PubMed:8761410).Curated1
Sequence conflicti38Q → K in AAB37501 (PubMed:8761410).Curated1
Sequence conflicti192A → M in AAB40387 (PubMed:8761410).Curated1
Sequence conflicti192A → M in AAB37501 (PubMed:8761410).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

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DDBJi
Links Updated
AF036760 mRNA Translation: AAC36493.1
S82504 Genomic DNA No translation available.
S82502 Genomic DNA No translation available.
U60523 mRNA Translation: AAB40387.1
S82500 Genomic DNA Translation: AAB37501.1

NCBI Reference Sequences

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RefSeqi
NP_036646.1, NM_012514.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
497672

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:497672

UCSC genome browser

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UCSCi
RGD:2218, rat

<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
AF036760 mRNA Translation: AAC36493.1
S82504 Genomic DNA No translation available.
S82502 Genomic DNA No translation available.
U60523 mRNA Translation: AAB40387.1
S82500 Genomic DNA Translation: AAB37501.1
RefSeqiNP_036646.1, NM_012514.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L0BX-ray2.30A1589-1817[»]
SMRiO54952
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028109

PTM databases

iPTMnetiO54952
PhosphoSitePlusiO54952

Proteomic databases

PaxDbiO54952
PRIDEiO54952

Genome annotation databases

GeneIDi497672
KEGGirno:497672
UCSCiRGD:2218, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
672
RGDi2218, Brca1

Phylogenomic databases

eggNOGiKOG4362, Eukaryota
InParanoidiO54952
KOiK10605
PhylomeDBiO54952

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-RNO-3108214, SUMOylation of DNA damage response and repair proteins
R-RNO-5685938, HDR through Single Strand Annealing (SSA)
R-RNO-5685942, HDR through Homologous Recombination (HRR)
R-RNO-5689901, Metalloprotease DUBs
R-RNO-5693554, Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-5693568, Resolution of D-loop Structures through Holliday Junction Intermediates
R-RNO-5693571, Nonhomologous End-Joining (NHEJ)
R-RNO-5693579, Homologous DNA Pairing and Strand Exchange
R-RNO-5693607, Processing of DNA double-strand break ends
R-RNO-5693616, Presynaptic phase of homologous DNA pairing and strand exchange
R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation
R-RNO-69473, G2/M DNA damage checkpoint

Miscellaneous databases

EvolutionaryTraceiO54952

Protein Ontology

More...
PROi
PR:O54952

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
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...

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_RAT
<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: O54952
Secondary accession number(s): P97951
<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: February 2, 2004
Last sequence update: June 1, 1998
Last modified: August 12, 2020
This is version 162 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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