BARD1_RAT
ID BARD1_RAT Reviewed; 768 AA.
AC Q9QZH2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=BRCA1-associated RING domain protein 1;
DE Short=BARD-1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q99728};
DE AltName: Full=RING-type E3 ubiquitin transferase BARD1 {ECO:0000305};
GN Name=Bard1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Carcinoma;
RX PubMed=11156388;
RA Gautier F., Irminger-Finger I., Gregoire M., Meflah K., Harb J.;
RT "Identification of an apoptotic cleavage product of BARD1 as an
RT autoantigen: a potential factor in the antitumoral response mediated by
RT apoptotic bodies.";
RL Cancer Res. 60:6895-6900(2000).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer
CC specifically mediates the formation of 'Lys-6'-linked polyubiquitin
CC chains and coordinates a diverse range of cellular pathways such as DNA
CC damage repair, ubiquitination and transcriptional regulation to
CC maintain genomic stability. Plays a central role in the control of the
CC cell cycle in response to DNA damage. Acts by mediating ubiquitin E3
CC ligase activity that is required for its tumor suppressor function.
CC Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing
CC and RNAP II stability by inhibiting pre-mRNA 3' cleavage.
CC {ECO:0000250|UniProtKB:Q99728}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q99728};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homo- and heterodimer. Heterodimer (RING-type zinc finger)
CC with BRCA1. Heterodimer (via ANK repeats and BRCT domains) with
CC CSTF1/CSTF-50. Component of the BRCA1-A complex, at least composed of
CC the BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and
CC BABAM1/NBA1. Interacts with UBXN1. {ECO:0000250|UniProtKB:Q99728}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O70445}. Cytoplasm
CC {ECO:0000250|UniProtKB:O70445}. Note=Can translocate to the cytoplasm.
CC Localizes at sites of DNA damage at double-strand breaks (DSBs);
CC recruitment to DNA damage sites is mediated by the BRCA1-A complex.
CC {ECO:0000250|UniProtKB:Q99728}.
CC -!- PTM: Processed during apoptosis. The homodimer is more susceptible to
CC proteolytic cleavage than the BARD1/BRCA1 heterodimer.
CC {ECO:0000250|UniProtKB:Q99728}.
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DR EMBL; AF182946; AAF00500.1; -; mRNA.
DR RefSeq; NP_072144.1; NM_022622.1.
DR AlphaFoldDB; Q9QZH2; -.
DR SMR; Q9QZH2; -.
DR STRING; 10116.ENSRNOP00000020414; -.
DR iPTMnet; Q9QZH2; -.
DR PhosphoSitePlus; Q9QZH2; -.
DR PaxDb; Q9QZH2; -.
DR PRIDE; Q9QZH2; -.
DR GeneID; 64557; -.
DR KEGG; rno:64557; -.
DR UCSC; RGD:621072; rat.
DR CTD; 580; -.
DR RGD; 621072; Bard1.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4362; Eukaryota.
DR InParanoid; Q9QZH2; -.
DR OrthoDB; 854133at2759; -.
DR PhylomeDB; Q9QZH2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9QZH2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070531; C:BRCA1-A complex; ISO:RGD.
DR GO; GO:0070532; C:BRCA1-B complex; ISO:RGD.
DR GO; GO:0031436; C:BRCA1-BARD1 complex; ISS:UniProtKB.
DR GO; GO:0070533; C:BRCA1-C complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR GO; GO:0042325; P:regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR CDD; cd16496; RING-HC_BARD1; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR039503; BARD1_Znf-RING.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF14835; zf-RING_6; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; DNA damage; DNA repair; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..768
FT /note="BRCA1-associated RING domain protein 1"
FT /id="PRO_0000055821"
FT REPEAT 417..449
FT /note="ANK 1"
FT REPEAT 450..482
FT /note="ANK 2"
FT REPEAT 483..515
FT /note="ANK 3"
FT REPEAT 516..536
FT /note="ANK 4; degenerate"
FT DOMAIN 551..644
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 658..768
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT ZN_FING 44..81
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 20..113
FT /note="Required for BRCA1 binding"
FT /evidence="ECO:0000250"
FT REGION 188..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..548
FT /note="Flexible linker"
FT /evidence="ECO:0000250"
FT COMPBIAS 207..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99728"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99728"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99728"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99728"
FT CROSSLNK 538
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99728"
SQ SEQUENCE 768 AA; 84548 MW; 9EBB22374910B49A CRC64;
MPRRPPRVCS GNKPPPVPAM EPATDGLWAH SRAALARLEK LLRCSRCANI LREPVCLGGC
EHIFCSGCIS DCVGSGCPVC HTPAWILDLK INRQLDSMIQ LYSKLQNLLH DNKGSDSKDD
TSRASLFGDA ERKKNSVKMW FSPRSKKIRC VVNKVSVQTQ PQKAKDDKAQ EASVFEFVSA
TPPVVVSTRA KTASRTSAKK HPKKSVAKIN REGNFRPETR DSRFDSKEKL KEEKVVSFSQ
TLVMENSRVN GEIDLLASGS VVESVFSGSF AEVSLPLAEH IVSPDTVSKS EEAPEKKVCV
EDRCPVGSDG NPKGCHRPPT STSKKCGSNV PSASGEIREP TLLAENVVLV DCSSLPSGRL
QVDVTLRRQS NASDDSLSLS PGTPPSLLNN STHRQMMSKP STVKLSSGIP ARKRNHRGET
LLHIASIKGD ISSVEYLLQN GNDPNVKDHA GWTPLHEACS HGHLKIVELL LQHNALVNTT
GYHNDSPLHD AAKNGHIDIV KVLLSHGASR NAVNIFGERP VDYTDAENIR SLLLLPEKTD
SFSTSQCSVQ VNTGQRKSGP LVLIGSGLSS QQQKLLSKLE TVLKAKKCAE FDNTVTHVIV
PDEEAQSTLK CMLGILNGCW VLKFDWVKAC LDSQEREQEE KYEVPGGPQR SRLNREQLLP
KLFDGCYFFL GGNFKHHPKE DLLKLIAAAG GRILSRKPKP DSDVTQTINT VAYHAKPDSD
QRFCTQYIVY EDLFNCHPER VRQGKVWMAP STWLISCVMA FELLPLDS
