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Protein

BRCA1-associated RING domain protein 1

Gene

Bard1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Probable 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).By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri44 – 8138RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
BRCA1-associated RING domain protein 1 (EC:6.3.2.-)
Short name:
BARD-1
Gene namesi
Name:Bard1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621072. Bard1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 768768BRCA1-associated RING domain protein 1PRO_0000055821Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei380 – 3801PhosphoserineBy similarity
Modified residuei383 – 3831PhosphothreonineBy similarity
Cross-linki413 – 413Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9QZH2.
PRIDEiQ9QZH2.

Interactioni

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, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. Interacts with UBXN1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020414.

Structurei

3D structure databases

ProteinModelPortaliQ9QZH2.
SMRiQ9QZH2. Positions 20-116, 415-536, 559-768.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati417 – 44933ANK 1Add
BLAST
Repeati450 – 48233ANK 2Add
BLAST
Repeati483 – 51533ANK 3Add
BLAST
Repeati516 – 53621ANK 4; degenerateAdd
BLAST
Domaini551 – 64494BRCT 1PROSITE-ProRule annotationAdd
BLAST
Domaini658 – 768111BRCT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 11394Required for BRCA1 bindingBy similarityAdd
BLAST
Regioni544 – 5485Flexible linkerBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi532 – 5354Poly-Leu

Sequence similaritiesi

Contains 4 ANK repeats.PROSITE-ProRule annotation
Contains 2 BRCT domains.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri44 – 8138RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4362. Eukaryota.
ENOG41120NI. LUCA.
HOGENOMiHOG000237306.
HOVERGENiHBG050662.
InParanoidiQ9QZH2.
KOiK10683.
PhylomeDBiQ9QZH2.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR033097. BARD1.
IPR001357. BRCT_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR24171:SF8. PTHR24171:SF8. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 3 hits.
SM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEiPS50297. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i9EBB22374910B49A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182946 mRNA. Translation: AAF00500.1.
RefSeqiNP_072144.1. NM_022622.1.
UniGeneiRn.48735.

Genome annotation databases

GeneIDi64557.
KEGGirno:64557.
UCSCiRGD:621072. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF182946 mRNA. Translation: AAF00500.1.
RefSeqiNP_072144.1. NM_022622.1.
UniGeneiRn.48735.

3D structure databases

ProteinModelPortaliQ9QZH2.
SMRiQ9QZH2. Positions 20-116, 415-536, 559-768.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020414.

Proteomic databases

PaxDbiQ9QZH2.
PRIDEiQ9QZH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64557.
KEGGirno:64557.
UCSCiRGD:621072. rat.

Organism-specific databases

CTDi580.
RGDi621072. Bard1.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4362. Eukaryota.
ENOG41120NI. LUCA.
HOGENOMiHOG000237306.
HOVERGENiHBG050662.
InParanoidiQ9QZH2.
KOiK10683.
PhylomeDBiQ9QZH2.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi613468.
PROiQ9QZH2.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR033097. BARD1.
IPR001357. BRCT_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR24171:SF8. PTHR24171:SF8. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 3 hits.
SM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEiPS50297. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of an apoptotic cleavage product of BARD1 as an autoantigen: a potential factor in the antitumoral response mediated by apoptotic bodies."
    Gautier F., Irminger-Finger I., Gregoire M., Meflah K., Harb J.
    Cancer Res. 60:6895-6900(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Carcinoma.

Entry informationi

Entry nameiBARD1_RAT
AccessioniPrimary (citable) accession number: Q9QZH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.