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Protein

BRCA1-associated RING domain protein 1

Gene

Bard1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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

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

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
Zinc fingeri44 – 81RING-typePROSITE-ProRule annotationAdd BLAST38

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5689603. UCH proteinases.
R-MMU-5689901. Metalloprotease DUBs.
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69473. G2/M DNA damage checkpoint.
UniPathwayiUPA00143.

Names & Taxonomyi

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
Gene namesi
Name:Bard1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1328361. Bard1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00000558201 – 765BRCA1-associated RING domain protein 1Add BLAST765

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei378PhosphoserineBy similarity1
Modified residuei381PhosphothreonineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO70445.
MaxQBiO70445.
PaxDbiO70445.
PeptideAtlasiO70445.
PRIDEiO70445.

PTM databases

iPTMnetiO70445.
PhosphoSitePlusiO70445.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026196.
CleanExiMM_BARD1.
GenevisibleiO70445. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198301. 3 interactors.
IntActiO70445. 4 interactors.
MINTiMINT-4084475.
STRINGi10090.ENSMUSP00000027393.

Structurei

3D structure databases

ProteinModelPortaliO70445.
SMRiO70445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati415 – 447ANK 1Add BLAST33
Repeati448 – 480ANK 2Add BLAST33
Repeati481 – 513ANK 3Add BLAST33
Repeati514 – 534ANK 4; degenerateAdd BLAST21
Domaini549 – 641BRCT 1PROSITE-ProRule annotationAdd BLAST93
Domaini655 – 765BRCT 2PROSITE-ProRule annotationAdd BLAST111

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 113Required for BRCA1 bindingBy similarityAdd BLAST94
Regioni542 – 546Flexible linkerBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi530 – 533Poly-Leu4

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)DescriptionActionsGraphical viewLength
Zinc fingeri44 – 81RING-typePROSITE-ProRule annotationAdd BLAST38

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4362. Eukaryota.
ENOG410Z0YV. LUCA.
GeneTreeiENSGT00760000119090.
HOGENOMiHOG000237306.
HOVERGENiHBG050662.
InParanoidiO70445.
KOiK10683.
OMAiKKNSIKM.
OrthoDBiEOG091G0JNZ.
PhylomeDBiO70445.
TreeFamiTF326440.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
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.

O70445-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRRPPRVCS GNQPAPVPAM EPATDGLWAH SRAALARLEK LLRCSRCANI
60 70 80 90 100
LKEPVCLGGC EHIFCSGCIS DCVGSGCPVC YTPAWILDLK INRQLDSMIQ
110 120 130 140 150
LSSKLQNLLH DNKDSKDNTS RASLFGDAER KKNSIKMWFS PRSKKVRYVV
160 170 180 190 200
TKVSVQTQPQ KAKDDKAQEA SMYEFVSATP PVAVPKSAKT ASRTSAKKHP
210 220 230 240 250
KKSVAKINRE ENLRPETKDS RFDSKEELKE EKVVSCSQIP VMERPRVNGE
260 270 280 290 300
IDLLASGSVV EPECSGSLTE VSLPLAEHIV SPDTVSKNEE TPEKKVCVKD
310 320 330 340 350
LRSGGSNGNR KGCHRPTTST SDSCGSNIPS TSRGIGEPAL LAENVVLVDC
360 370 380 390 400
SSLPSGQLQV DVTLRRKSNA SDDPLSLSPG TPPPLLNNST HRQMMSSPST
410 420 430 440 450
VKLSSGMPAR KRNHRGETLL HIASIKGDIP SVEYLLQNGN DPNVKDHAGW
460 470 480 490 500
TPLHEACSHG HLKVVELLLQ HNALVNTPGY QNDSPLHDAV KSGHIDIVKV
510 520 530 540 550
LLSHGASRNA VNIFGVRPVD YTDNENIRSL LLLPEENESF STSQCSIVNT
560 570 580 590 600
GQRKNGPLVF IGSGLSSQQQ KMLSKLETVL KAKKCMEFDS TVTHVIVPDE
610 620 630 640 650
EAQSTLKCML GILSGCWILK FDWVKACLDS KVREQEEKYE VPGGPQRSRL
660 670 680 690 700
NREQLLPKLF DGCYFFLGGN FKHHPRDDLL KLIAAAGGKV LSRKPKPDSD
710 720 730 740 750
VTQTINTVAY HAKPESDQRF CTQYIVYEDL FNCHPERVRQ GKVWMAPSTW
760
LISCIMAFEL LPLDS
Length:765
Mass (Da):84,254
Last modified:August 1, 1998 - v1
Checksum:iC43DD0625F2F1AE9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF057157 mRNA. Translation: AAC18095.1.
BC128370 mRNA. Translation: AAI28371.1.
BC128371 mRNA. Translation: AAI28372.1.
CCDSiCCDS15029.1.
RefSeqiNP_031551.1. NM_007525.3.
UniGeneiMm.10764.
Mm.490738.

Genome annotation databases

EnsembliENSMUST00000027393; ENSMUSP00000027393; ENSMUSG00000026196.
GeneIDi12021.
KEGGimmu:12021.
UCSCiuc007bjm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF057157 mRNA. Translation: AAC18095.1.
BC128370 mRNA. Translation: AAI28371.1.
BC128371 mRNA. Translation: AAI28372.1.
CCDSiCCDS15029.1.
RefSeqiNP_031551.1. NM_007525.3.
UniGeneiMm.10764.
Mm.490738.

3D structure databases

ProteinModelPortaliO70445.
SMRiO70445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198301. 3 interactors.
IntActiO70445. 4 interactors.
MINTiMINT-4084475.
STRINGi10090.ENSMUSP00000027393.

PTM databases

iPTMnetiO70445.
PhosphoSitePlusiO70445.

Proteomic databases

EPDiO70445.
MaxQBiO70445.
PaxDbiO70445.
PeptideAtlasiO70445.
PRIDEiO70445.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027393; ENSMUSP00000027393; ENSMUSG00000026196.
GeneIDi12021.
KEGGimmu:12021.
UCSCiuc007bjm.2. mouse.

Organism-specific databases

CTDi580.
MGIiMGI:1328361. Bard1.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4362. Eukaryota.
ENOG410Z0YV. LUCA.
GeneTreeiENSGT00760000119090.
HOGENOMiHOG000237306.
HOVERGENiHBG050662.
InParanoidiO70445.
KOiK10683.
OMAiKKNSIKM.
OrthoDBiEOG091G0JNZ.
PhylomeDBiO70445.
TreeFamiTF326440.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5689603. UCH proteinases.
R-MMU-5689901. Metalloprotease DUBs.
R-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-5693579. Homologous DNA Pairing and Strand Exchange.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69473. G2/M DNA damage checkpoint.

Miscellaneous databases

ChiTaRSiBard1. mouse.
PROiO70445.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026196.
CleanExiMM_BARD1.
GenevisibleiO70445. MM.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
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...

Entry informationi

Entry nameiBARD1_MOUSE
AccessioniPrimary (citable) accession number: O70445
Secondary accession number(s): A2VCQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 147 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.