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Entry version 150 (11 Dec 2019)
Sequence version 1 (01 May 2000)
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Protein

BRCA1-associated RING domain protein 1

Gene

Bard1

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 transcript 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. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.By similarity

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri44 – 81RING-typePROSITE-ProRule annotationAdd BLAST38

<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 functionTransferase
Biological processDNA damage, DNA repair, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-5685938 HDR through Single Strand Annealing (SSA)
R-RNO-5685942 HDR through Homologous Recombination (HRR)
R-RNO-5689603 UCH proteinases
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_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:
BRCA1-associated RING domain protein 1 (EC:2.3.2.27By similarity)
Short name:
BARD-1
Alternative name(s):
RING-type E3 ubiquitin transferase BARD1Curated
<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:Bard1
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
621072 Bard1

<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

Cytoplasm, Nucleus

<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_00000558211 – 768BRCA1-associated RING domain protein 1Add BLAST768

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
<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 residuei380PhosphoserineBy similarity1
Modified residuei383PhosphothreonineBy similarity1
Cross-linki413Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

<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

Processed during apoptosis. The homodimer is more susceptible to proteolytic cleavage than the BARD1/BRCA1 heterodimer.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q9QZH2

PRoteomics IDEntifications database

More...
PRIDEi
Q9QZH2

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9QZH2

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

More...
PhosphoSitePlusi
Q9QZH2

<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

Homo- and heterodimer. Heterodimer (RING-type zinc finger) with BRCA1. Heterodimer (via ANK repeats and BRCT domains) with CSTF1/CSTF-50.

Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1.

Interacts with UBXN1.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000020414

<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
Q9QZH2

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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati417 – 449ANK 1Add BLAST33
Repeati450 – 482ANK 2Add BLAST33
Repeati483 – 515ANK 3Add BLAST33
Repeati516 – 536ANK 4; degenerateAdd BLAST21
<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>Domaini551 – 644BRCT 1PROSITE-ProRule annotationAdd BLAST94
Domaini658 – 768BRCT 2PROSITE-ProRule annotationAdd BLAST111

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>Regioni20 – 113Required for BRCA1 bindingBy similarityAdd BLAST94
Regioni544 – 548Flexible linkerBy similarity5

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 biasi532 – 535Poly-Leu4

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri44 – 81RING-typePROSITE-ProRule annotationAdd BLAST38

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0504 Eukaryota
KOG4362 Eukaryota
ENOG41120NI LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000237306

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9QZH2

KEGG Orthology (KO)

More...
KOi
K10683

Database of Orthologous Groups

More...
OrthoDBi
854133at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9QZH2

Family and domain databases

Conserved Domains Database

More...
CDDi
cd16496 RING-HC_BARD1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.20, 1 hit
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
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR039503 BARD1_Znf-RING
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12796 Ank_2, 1 hit
PF14835 zf-RING_6, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415 ANKYRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248 ANK, 3 hits
SM00292 BRCT, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48403 SSF48403, 1 hit
SSF52113 SSF52113, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 3 hits
PS50172 BRCT, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>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 2 potential isoforms that are computationally mapped.Show allAlign All

Q9QZH2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPRRPPRVCS GNKPPPVPAM EPATDGLWAH SRAALARLEK LLRCSRCANI
60 70 80 90 100
LREPVCLGGC EHIFCSGCIS DCVGSGCPVC HTPAWILDLK INRQLDSMIQ
110 120 130 140 150
LYSKLQNLLH DNKGSDSKDD TSRASLFGDA ERKKNSVKMW FSPRSKKIRC
160 170 180 190 200
VVNKVSVQTQ PQKAKDDKAQ EASVFEFVSA TPPVVVSTRA KTASRTSAKK
210 220 230 240 250
HPKKSVAKIN REGNFRPETR DSRFDSKEKL KEEKVVSFSQ TLVMENSRVN
260 270 280 290 300
GEIDLLASGS VVESVFSGSF AEVSLPLAEH IVSPDTVSKS EEAPEKKVCV
310 320 330 340 350
EDRCPVGSDG NPKGCHRPPT STSKKCGSNV PSASGEIREP TLLAENVVLV
360 370 380 390 400
DCSSLPSGRL QVDVTLRRQS NASDDSLSLS PGTPPSLLNN STHRQMMSKP
410 420 430 440 450
STVKLSSGIP ARKRNHRGET LLHIASIKGD ISSVEYLLQN GNDPNVKDHA
460 470 480 490 500
GWTPLHEACS HGHLKIVELL LQHNALVNTT GYHNDSPLHD AAKNGHIDIV
510 520 530 540 550
KVLLSHGASR NAVNIFGERP VDYTDAENIR SLLLLPEKTD SFSTSQCSVQ
560 570 580 590 600
VNTGQRKSGP LVLIGSGLSS QQQKLLSKLE TVLKAKKCAE FDNTVTHVIV
610 620 630 640 650
PDEEAQSTLK CMLGILNGCW VLKFDWVKAC LDSQEREQEE KYEVPGGPQR
660 670 680 690 700
SRLNREQLLP KLFDGCYFFL GGNFKHHPKE DLLKLIAAAG GRILSRKPKP
710 720 730 740 750
DSDVTQTINT VAYHAKPDSD QRFCTQYIVY EDLFNCHPER VRQGKVWMAP
760
STWLISCVMA FELLPLDS
Length:768
Mass (Da):84,548
Last modified:May 1, 2000 - 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:i9EBB22374910B49A
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K9Y6A0A0G2K9Y6_RAT
BRCA1 associated RING domain 1
Bard1 rCG_25001
768Annotation score:

Annotation score:2 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>
G3V7X7G3V7X7_RAT
BRCA1-associated RING domain protei...
Bard1
603Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

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
AF182946 mRNA Translation: AAF00500.1

NCBI Reference Sequences

More...
RefSeqi
NP_072144.1, NM_022622.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
64557

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:64557

UCSC genome browser

More...
UCSCi
RGD:621072 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
AF182946 mRNA Translation: AAF00500.1
RefSeqiNP_072144.1, NM_022622.1

3D structure databases

SMRiQ9QZH2
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020414

PTM databases

iPTMnetiQ9QZH2
PhosphoSitePlusiQ9QZH2

Proteomic databases

PaxDbiQ9QZH2
PRIDEiQ9QZH2

Genome annotation databases

GeneIDi64557
KEGGirno:64557
UCSCiRGD:621072 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
580
RGDi621072 Bard1

Phylogenomic databases

eggNOGiKOG0504 Eukaryota
KOG4362 Eukaryota
ENOG41120NI LUCA
HOGENOMiHOG000237306
InParanoidiQ9QZH2
KOiK10683
OrthoDBi854133at2759
PhylomeDBiQ9QZH2

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-RNO-5685938 HDR through Single Strand Annealing (SSA)
R-RNO-5685942 HDR through Homologous Recombination (HRR)
R-RNO-5689603 UCH proteinases
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

Protein Ontology

More...
PROi
PR:Q9QZH2

Family and domain databases

CDDicd16496 RING-HC_BARD1, 1 hit
Gene3Di1.25.40.20, 1 hit
3.30.40.10, 1 hit
3.40.50.10190, 2 hits
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR039503 BARD1_Znf-RING
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PfamiView protein in Pfam
PF12796 Ank_2, 1 hit
PF14835 zf-RING_6, 1 hit
PRINTSiPR01415 ANKYRIN
SMARTiView protein in SMART
SM00248 ANK, 3 hits
SM00292 BRCT, 2 hits
SUPFAMiSSF48403 SSF48403, 1 hit
SSF52113 SSF52113, 2 hits
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 3 hits
PS50172 BRCT, 2 hits
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiBARD1_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: Q9QZH2
<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 21, 2001
Last sequence update: May 1, 2000
Last modified: December 11, 2019
This is version 150 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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