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UniProtKB - Q95153 (BRCA1_CANLF)

Entry version 153 (23 Feb 2022)
Sequence version 1 (01 Feb 1997)
Previous versions | rss
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Protein

Breast cancer type 1 susceptibility protein homolog

Gene

BRCA1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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>-Protein inferred from homologyi <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 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 appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Required for FANCD2 targeting to sites of DNA damage. 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

<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

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 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

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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›
<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
  • UP000002254 <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

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

Keywords - Cellular componenti

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_00000558281 – 1878Breast cancer type 1 susceptibility protein homologAdd BLAST1878

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-linki298Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei392PhosphoserineBy similarity1
Modified residuei395PhosphoserineBy similarity1
Modified residuei420PhosphoserineBy similarity1
Modified residuei431PhosphoserineBy similarity1
Cross-linki456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki516Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki581Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei692PhosphoserineBy similarity1
Modified residuei712PhosphoserineBy similarity1
Modified residuei751PhosphoserineBy similarity1
Modified residuei987Phosphoserine; by CHEK2By similarity1
Modified residuei1008PhosphoserineBy similarity1
Cross-linki1079Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1144PhosphoserineBy similarity1
Modified residuei1190PhosphoserineBy similarity1
Modified residuei1192PhosphoserineBy similarity1
Modified residuei1212PhosphoserineBy similarity1
Modified residuei1218PhosphoserineBy similarity1
Modified residuei1219PhosphoserineBy similarity1
Modified residuei1281PhosphoserineBy similarity1
Modified residuei1331PhosphoserineBy similarity1
Modified residuei1344PhosphoserineBy similarity1
Modified residuei1391PhosphoserineBy similarity1
Modified residuei1398PhosphothreonineBy similarity1
Modified residuei1427PhosphoserineBy similarity1
Modified residuei1460PhosphoserineBy similarity1
Modified residuei1527PhosphoserineBy similarity1
Modified residuei1545PhosphoserineBy 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

Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Phosphorylation at Ser-987 by CHEK2 regulates mitotic spindle assembly. Phosphorylation by AURKA regulates centrosomal microtubule nucleation.By similarity
Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation (By similarity).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		Q95153

<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, 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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9612.ENSCAFP00000021534

<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

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

More...SMRi		Q95153

Database of comparative protein structure models

More...ModBasei		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%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>Domaini1652 – 1739BRCT 1PROSITE-ProRule annotationAdd BLAST88
Domaini1764 – 1863BRCT 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>Regioni303 – 329DisorderedSequence analysisAdd BLAST27
Regioni349 – 368DisorderedSequence analysisAdd BLAST20
Regioni548 – 614DisorderedSequence analysisAdd BLAST67
Regioni1134 – 1154DisorderedSequence analysisAdd BLAST21
Regioni1183 – 1221DisorderedSequence analysisAdd BLAST39
Regioni1315 – 1401DisorderedSequence analysisAdd BLAST87
Regioni1401 – 1428Interaction with PALB2By similarityAdd BLAST28
Regioni1419 – 1504DisorderedSequence analysisAdd BLAST86
Regioni1570 – 1590DisorderedSequence analysisAdd BLAST21
Regioni1743 – 1764DisorderedSequence analysisAdd BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi303 – 320Polar residuesSequence analysisAdd BLAST18
Compositional biasi556 – 581Basic and acidic residuesSequence analysisAdd BLAST26
Compositional biasi582 – 603Polar residuesSequence analysisAdd BLAST22
Compositional biasi1134 – 1151Polar residuesSequence analysisAdd BLAST18
Compositional biasi1183 – 1201Polar residuesSequence analysisAdd BLAST19
Compositional biasi1315 – 1331Polar residuesSequence analysisAdd BLAST17
Compositional biasi1341 – 1364Acidic residuesSequence analysisAdd BLAST24
Compositional biasi1374 – 1401Polar residuesSequence analysisAdd BLAST28
Compositional biasi1424 – 1504Polar residuesSequence analysisAdd BLAST81

<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).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

More...InParanoidi		Q95153

Database of Orthologous Groups

More...OrthoDBi		496760at2759

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
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

More...PANTHERi		PTHR13763, PTHR13763, 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

More...PIRSFi		PIRSF001734, BRCA1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00493, BRSTCANCERI

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%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>Sequencei

<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.

Q95153-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDLSADRVEE VQNVLNAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK 
        60         70         80         90        100
LLNQRKGPSQ CPLCKNDITK RSLQESTRFS QLVEELLKII HAFELDTGLQ 
       110        120        130        140        150
FADSYNFSKK ENNSPEHLKE EVSIIQSMGY RNRAKRLRQS EPENPTLETS 
       160        170        180        190        200
LSVQLSNLGI VRSLRTKQQI QPQNKSVYIE LGSDSSEDTV NKASSCSVGD 
       210        220        230        240        250
DELEITSQGA RAEASLNPAK KAACEFSGDI TNIEHHQSSN KDLTTTEKHA 
       260        270        280        290        300
TKKHPEKYQG ISVSNLHVEP CGTNTHASSL QHENSSLLLT KHRMNVEKAE 
       310        320        330        340        350
ICNNSKQPGL ARSQQSRWAE SKETCNDRQI PSTEKKVVVN ADLLCGRKEL 
       360        370        380        390        400
NKQKPPHSDS PRDSQDVPWI TLNSSIRKVN EWFSRSDEIL TSDDSHDRGS 
       410        420        430        440        450
ELNTEVGGAV EVPNEVGEYS GSSEKIDLMA SDPQDAFICE SERVHTKPVG 
       460        470        480        490        500
GNIEDKIFGK TYRRKASLPK VSHTTEVLTI GACAIEPQTM QTHPFMNKAE 
       510        520        530        540        550
HKRRTTSSLH PEDFIKKVEL GIVPKTPEKL IEGINQIKRD GHVINITNNG 
       560        570        580        590        600
PENETEGDYV QKEKNANPTE SLEKESAFRT KTEPMSSRIS NMELELNSSS 
       610        620        630        640        650
SKAPKKNRLR RKSSARHTCA LEFVVNRNLN PPDHSELQIE SCSSSEEMKK 
       660        670        680        690        700
QHLDQVPVRH NKTLQLMQDK EPAGRAKKSS KPGEQINKRL ASHAFPELTL 
       710        720        730        740        750
TNVSGFFANY SSSSKPQECI NPGLRREEIE ESRRMTQVSD STRDPKELVL 
       760        770        780        790        800
SGGRGLQTER SVESTSISLV LDTDYGTQDS ISLLEADTLR KAKTVSNQQA 
       810        820        830        840        850
NLCATIENPK EPIHGCSKDT RNDTEGFVVP LTCKDNHTQE TSIEMEESEL 
       860        870        880        890        900
DTQCLRNMFK VSKRQSFALF SYPRDPEEDC VTVCPRSGAF GKQGPKVTLE 
       910        920        930        940        950
CGQKEESQGK KESEIRHVQA VHTNAGFSAV SQKAKKPGDF AKCSIKGVSR 
       960        970        980        990       1000
LCLSSQFKGK ETELLIANYH GISQNPYHIP PLSPIRSCVK TLCQENLSEE 
      1010       1020       1030       1040       1050
KFEQHSMSPE RAVGNERVIQ STVSTISQNN IRECASKEVG SSSVNEVVSS 
      1060       1070       1080       1090       1100
TNEVGSSVNE VGSSGENIQA ELGRNRGPKL NAMLRLGLMQ PEVCKQSLSL 
      1110       1120       1130       1140       1150
SNCKHPEMKW QGQSEGAVLS VSADFSPCLI SDNPEQPMGS SRSSQVCSET 
      1160       1170       1180       1190       1200
PDDLLNGDKI KGKVSFAESD IKEKSAVFSK SVQSGEFSRS PSPSDHTRLA 
      1210       1220       1230       1240       1250
QGYQRGTKKL ESSEENMSSE EEELPCFQHL IFGKVTNMPS QSTSHNAVAA 
      1260       1270       1280       1290       1300
EGLSNKTEEN LDSLKNSLSD ISNQVPSAKA SQEHHLSEEA RCSGSLFSSQ 
      1310       1320       1330       1340       1350
CSALEDLTVN TNTQDPFSMF DPTSKQVRHQ SENLDVLNDK ELVSDDDDER 
      1360       1370       1380       1390       1400
EPGLEEDSPQ EEQSVDSDLG EVASGYESET SLSEDCSRLS SQSDILTTQQ 
      1410       1420       1430       1440       1450
RDTMQDNLIK LQQEMAELEA VLEQHESQPS NSSPSLIADS CSPEDLLNPE 
      1460       1470       1480       1490       1500
QNASERVLTS EKSSDSPISQ NPESLSTDKF QVFLDSSTSK NGEPGMIRSS 
      1510       1520       1530       1540       1550
PSQSRLLDTR WYVHSCPRSL QDTNCPSQKE LTKVVSMEEQ QPTESEARDL 
      1560       1570       1580       1590       1600
MEQSYLSRPD LEGAPYLESG ISLFSDDPES DPSSHRASEL AHVSSMPTST 
      1610       1620       1630       1640       1650
SALKLPQFQV EESAKSTAAV HIASTAGYNK SEDSVGIEKP EVISSTRGVN 
      1660       1670       1680       1690       1700
KRISMVASGL TPKEFMLVHK FARKHHISLT NLISEETTHV IMKTDAEFVC 
      1710       1720       1730       1740       1750
ERTLKYFLGI AGGKWVVSYF WVTQSIKERK ILDEHDFEVR GDVVNGRNHQ 
      1760       1770       1780       1790       1800
GPKRARESQD RESQDRKIFR GLEICCYGPF TNMPTDQLEW MVHLCGASVV 
      1810       1820       1830       1840       1850
KEPSLFTLSK GTHPVVVVQP DAWTEDSGFH AIGQMCEAPV VTREWVLDSV 
      1860       1870 
ALYQCQELDT YLIPQIPRTA ADSSQPCV
Length:1,878
Mass (Da):208,447
Last modified:February 1, 1997 - 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:i4799B65030327C4F
GO

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
U50709 Genomic DNA Translation: AAC48663.1

NCBI Reference Sequences

More...RefSeqi		NP_001013434.1, NM_001013416.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		403437

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cfa:403437

<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
U50709 Genomic DNA Translation: AAC48663.1
RefSeqiNP_001013434.1, NM_001013416.1

3D structure databases

SMRiQ95153
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9612.ENSCAFP00000021534

Proteomic databases

PaxDbiQ95153

Genome annotation databases

GeneIDi403437
KEGGicfa:403437

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		672

Phylogenomic databases

eggNOGiKOG4362, Eukaryota
InParanoidiQ95153
OrthoDBi496760at2759

Enzyme and pathway databases

UniPathwayiUPA00143

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
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

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_CANLF
<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: Q95153
<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: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 23, 2022
This is version 153 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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