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Protein

BRCA1-associated RING domain protein 1

Gene

BARD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.3 Publications

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.2 Publications

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 fingeri50 – 87RING-typePROSITE-ProRule annotationAdd BLAST38

GO - Molecular functioni

  • kinase binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA binding Source: MGI
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell cycle arrest Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA double-strand break processing Source: Reactome
  • DNA replication Source: Reactome
  • DNA synthesis involved in DNA repair Source: Reactome
  • double-strand break repair via nonhomologous end joining Source: Reactome
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of mRNA 3'-end processing Source: UniProtKB
  • negative regulation of protein export from nucleus Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of protein catabolic process Source: UniProtKB
  • protein K6-linked ubiquitination Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • regulation of phosphorylation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • strand displacement Source: Reactome
  • tissue homeostasis Source: UniProtKB
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

BioCyciZFISH:ENSG00000138376-MONOMER.
ReactomeiR-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5689603. UCH proteinases.
R-HSA-5689901. Metalloprotease DUBs.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ99728.
SIGNORiQ99728.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
BRCA1-associated RING domain protein 1 (EC:2.3.2.272 Publications)
Short name:
BARD-1
Alternative name(s):
RING-type E3 ubiquitin transferase BARD1Curated
Gene namesi
Name:BARD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:952. BARD1.

Subcellular locationi

  • Nucleus

  • Note: During S phase of the cell cycle, colocalizes with BRCA1 into discrete subnuclear foci. 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.

GO - Cellular componenti

  • BRCA1-A complex Source: UniProtKB
  • BRCA1-BARD1 complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi580.
MalaCardsiBARD1.
OpenTargetsiENSG00000138376.
Orphaneti145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA25256.

Polymorphism and mutation databases

BioMutaiBARD1.
DMDMi116241265.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000558191 – 777BRCA1-associated RING domain protein 1Add BLAST777

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei186PhosphoserineCombined sources1
Modified residuei299PhosphothreonineCombined sources1
Modified residuei391PhosphoserineCombined sources1
Modified residuei394PhosphothreonineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99728.
MaxQBiQ99728.
PaxDbiQ99728.
PeptideAtlasiQ99728.
PRIDEiQ99728.

PTM databases

iPTMnetiQ99728.
PhosphoSitePlusiQ99728.

Expressioni

Gene expression databases

BgeeiENSG00000138376.
CleanExiHS_BARD1.
ExpressionAtlasiQ99728. baseline and differential.
GenevisibleiQ99728. HS.

Organism-specific databases

HPAiCAB034106.
HPA035354.
HPA044864.

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 UBXN1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P383989EBI-473181,EBI-349905
CEP126Q9P2H02EBI-473181,EBI-473176
CEP70Q8NHQ13EBI-473181,EBI-739624
CHD3Q128732EBI-473181,EBI-523590
CSTF1Q050484EBI-473181,EBI-1789619
CSTF2P332408EBI-473181,EBI-711360
EXOC5Q8IW243EBI-473181,EBI-10171392
FAM9BQ8IZU03EBI-473181,EBI-10175124
GIT1Q9Y2X72EBI-473181,EBI-466061
GOLGA2Q083793EBI-473181,EBI-618309
KAT7O952512EBI-473181,EBI-473199
KRT40Q6A1623EBI-473181,EBI-10171697
LDOC1O957515EBI-473181,EBI-740738
PARNO954534EBI-473181,EBI-372832
TCERG1O147762EBI-473181,EBI-473271

GO - Molecular functioni

  • kinase binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi107056. 268 interactors.
DIPiDIP-5972N.
IntActiQ99728. 42 interactors.
MINTiMINT-207047.
STRINGi9606.ENSP00000260947.

Chemistry databases

BindingDBiQ99728.

Structurei

Secondary structure

1777
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 46Combined sources12
Beta strandi51 – 53Combined sources3
Beta strandi65 – 67Combined sources3
Turni72 – 74Combined sources3
Helixi75 – 78Combined sources4
Turni79 – 81Combined sources3
Beta strandi84 – 86Combined sources3
Helixi99 – 116Combined sources18
Helixi431 – 438Combined sources8
Helixi441 – 449Combined sources9
Helixi464 – 470Combined sources7
Helixi474 – 482Combined sources9
Helixi492 – 494Combined sources3
Helixi497 – 503Combined sources7
Helixi507 – 515Combined sources9
Helixi530 – 533Combined sources4
Helixi537 – 543Combined sources7
Beta strandi571 – 576Combined sources6
Helixi579 – 591Combined sources13
Beta strandi595 – 599Combined sources5
Beta strandi606 – 613Combined sources8
Helixi618 – 625Combined sources8
Beta strandi629 – 632Combined sources4
Helixi634 – 642Combined sources9
Helixi648 – 650Combined sources3
Helixi656 – 665Combined sources10
Turni671 – 674Combined sources4
Beta strandi676 – 679Combined sources4
Beta strandi684 – 686Combined sources3
Helixi688 – 697Combined sources10
Beta strandi701 – 705Combined sources5
Helixi709 – 711Combined sources3
Helixi713 – 715Combined sources3
Helixi729 – 731Combined sources3
Beta strandi735 – 739Combined sources5
Beta strandi750 – 752Combined sources3
Beta strandi755 – 759Combined sources5
Helixi760 – 769Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JM7NMR-B26-140[»]
2NTEX-ray1.90A/B568-777[»]
2R1ZX-ray2.10A/B569-777[»]
3C5RX-ray2.00A/B425-555[»]
3FA2X-ray2.20A/B566-777[»]
ProteinModelPortaliQ99728.
SMRiQ99728.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99728.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati427 – 459ANK 1Add BLAST33
Repeati460 – 492ANK 2Add BLAST33
Repeati493 – 525ANK 3Add BLAST33
Repeati526 – 546ANK 4; degenerateAdd BLAST21
Domaini560 – 653BRCT 1PROSITE-ProRule annotationAdd BLAST94
Domaini667 – 777BRCT 2PROSITE-ProRule annotationAdd BLAST111

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 119Interaction with BRCA1Add BLAST94
Regioni554 – 558Flexible linker5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi400 – 403Poly-Ser4
Compositional biasi542 – 545Poly-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 fingeri50 – 87RING-typePROSITE-ProRule annotationAdd BLAST38

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4362. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00760000119090.
HOGENOMiHOG000237306.
HOVERGENiHBG050662.
InParanoidiQ99728.
KOiK10683.
OMAiKKNSIKM.
OrthoDBiEOG091G0JNZ.
PhylomeDBiQ99728.
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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99728-1) [UniParc]FASTAAdd to basket
Also known as: FL

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPDNRQPRNR QPRIRSGNEP RSAPAMEPDG RGAWAHSRAA LDRLEKLLRC
60 70 80 90 100
SRCTNILREP VCLGGCEHIF CSNCVSDCIG TGCPVCYTPA WIQDLKINRQ
110 120 130 140 150
LDSMIQLCSK LRNLLHDNEL SDLKEDKPRK SLFNDAGNKK NSIKMWFSPR
160 170 180 190 200
SKKVRYVVSK ASVQTQPAIK KDASAQQDSY EFVSPSPPAD VSERAKKASA
210 220 230 240 250
RSGKKQKKKT LAEINQKWNL EAEKEDGEFD SKEESKQKLV SFCSQPSVIS
260 270 280 290 300
SPQINGEIDL LASGSLTESE CFGSLTEVSL PLAEQIESPD TKSRNEVVTP
310 320 330 340 350
EKVCKNYLTS KKSLPLENNG KRGHHNRLSS PISKRCRTSI LSTSGDFVKQ
360 370 380 390 400
TVPSENIPLP ECSSPPSCKR KVGGTSGRKN SNMSDEFISL SPGTPPSTLS
410 420 430 440 450
SSSYRRVMSS PSAMKLLPNM AVKRNHRGET LLHIASIKGD IPSVEYLLQN
460 470 480 490 500
GSDPNVKDHA GWTPLHEACN HGHLKVVELL LQHKALVNTT GYQNDSPLHD
510 520 530 540 550
AAKNGHVDIV KLLLSYGASR NAVNIFGLRP VDYTDDESMK SLLLLPEKNE
560 570 580 590 600
SSSASHCSVM NTGQRRDGPL VLIGSGLSSE QQKMLSELAV ILKAKKYTEF
610 620 630 640 650
DSTVTHVVVP GDAVQSTLKC MLGILNGCWI LKFEWVKACL RRKVCEQEEK
660 670 680 690 700
YEIPEGPRRS RLNREQLLPK LFDGCYFYLW GTFKHHPKDN LIKLVTAGGG
710 720 730 740 750
QILSRKPKPD SDVTQTINTV AYHARPDSDQ RFCTQYIIYE DLCNYHPERV
760 770
RQGKVWKAPS SWFIDCVMSF ELLPLDS
Length:777
Mass (Da):86,648
Last modified:October 17, 2006 - v2
Checksum:i95E2D904046B5646
GO
Isoform alpha (identifier: Q99728-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     54-72: Missing.

Show »
Length:758
Mass (Da):84,574
Checksum:iF45B73AF6EDB602D
GO
Isoform beta (identifier: Q99728-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MPDNRQPRNRQPRIRSGNEPRSAP → MVAVPGPTVAPRSTAWRSCCAARV
     25-121: Missing.

Show »
Length:680
Mass (Da):75,474
Checksum:iD710F909D260F2F3
GO
Isoform gamma (identifier: Q99728-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-127: DLKEDK → GRHTFC
     128-777: Missing.

Show »
Length:127
Mass (Da):14,362
Checksum:iFEA9852C92F33975
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti85V → A in AEF57473 (PubMed:18089818).Curated1
Sequence conflicti406R → Q in AAB38316 (PubMed:8944023).Curated1
Sequence conflicti406R → Q in AEF57471 (PubMed:18089818).Curated1
Sequence conflicti406R → Q in AEF57472 (PubMed:18089818).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01035424P → S Common polymorphism in Caucasians; less frequent in Africans. 1 PublicationCorresponds to variant rs1048108dbSNPEnsembl.1
Natural variantiVAR_010355153K → E.1 PublicationCorresponds to variant rs753377280dbSNPEnsembl.1
Natural variantiVAR_038371186S → G.Corresponds to variant rs16852741dbSNPEnsembl.1
Natural variantiVAR_020109241S → C.Corresponds to variant rs3738885dbSNPEnsembl.1
Natural variantiVAR_024611378R → S.1 PublicationCorresponds to variant rs2229571dbSNPEnsembl.1
Natural variantiVAR_010356507V → M.1 PublicationCorresponds to variant rs2070094dbSNPEnsembl.1
Natural variantiVAR_010357557C → S Rare polymorphism in Caucasians. 1 PublicationCorresponds to variant rs28997576dbSNPEnsembl.1
Natural variantiVAR_010358564Q → H in an ovarian clear cell adenocarcinoma. 1 Publication1
Natural variantiVAR_038372645C → R.Corresponds to variant rs34744268dbSNPEnsembl.1
Natural variantiVAR_010359658R → C Rare polymorphism in Caucasians; absent in Africans. 1 PublicationCorresponds to variant rs3738888dbSNPEnsembl.1
Natural variantiVAR_010360695V → L in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs111367604dbSNPEnsembl.1
Natural variantiVAR_028309728S → F.Corresponds to variant rs13389423dbSNPEnsembl.1
Natural variantiVAR_010361761S → N in an uterine cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs142155101dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0558741 – 24MPDNR…PRSAP → MVAVPGPTVAPRSTAWRSCC AARV in isoform beta. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_05587525 – 121Missing in isoform beta. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_05587654 – 72Missing in isoform alpha. 1 PublicationAdd BLAST19
Alternative sequenceiVSP_055877122 – 127DLKEDK → GRHTFC in isoform gamma. 1 Publication6
Alternative sequenceiVSP_055878128 – 777Missing in isoform gamma. 1 PublicationAdd BLAST650

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76638 mRNA. Translation: AAB38316.1.
AF038042
, AF038034, AF038035, AF038036, AF038037, AF038038, AF038039, AF038040, AF038041 Genomic DNA. Translation: AAB99978.1.
JF790280 mRNA. Translation: AEF57471.1.
JF790281 mRNA. Translation: AEF57472.1.
JF790282 mRNA. Translation: AEF57473.1.
AC016708 Genomic DNA. Translation: AAX93130.1.
BC126426 mRNA. Translation: AAI26427.1.
CCDSiCCDS2397.1. [Q99728-1]
CCDS74646.1. [Q99728-2]
RefSeqiNP_000456.2. NM_000465.3. [Q99728-1]
NP_001269472.1. NM_001282543.1. [Q99728-2]
UniGeneiHs.591642.
Hs.597413.

Genome annotation databases

EnsembliENST00000260947; ENSP00000260947; ENSG00000138376. [Q99728-1]
ENST00000617164; ENSP00000480470; ENSG00000138376. [Q99728-2]
ENST00000620057; ENSP00000481988; ENSG00000138376. [Q99728-4]
GeneIDi580.
KEGGihsa:580.
UCSCiuc002veu.4. human. [Q99728-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76638 mRNA. Translation: AAB38316.1.
AF038042
, AF038034, AF038035, AF038036, AF038037, AF038038, AF038039, AF038040, AF038041 Genomic DNA. Translation: AAB99978.1.
JF790280 mRNA. Translation: AEF57471.1.
JF790281 mRNA. Translation: AEF57472.1.
JF790282 mRNA. Translation: AEF57473.1.
AC016708 Genomic DNA. Translation: AAX93130.1.
BC126426 mRNA. Translation: AAI26427.1.
CCDSiCCDS2397.1. [Q99728-1]
CCDS74646.1. [Q99728-2]
RefSeqiNP_000456.2. NM_000465.3. [Q99728-1]
NP_001269472.1. NM_001282543.1. [Q99728-2]
UniGeneiHs.591642.
Hs.597413.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JM7NMR-B26-140[»]
2NTEX-ray1.90A/B568-777[»]
2R1ZX-ray2.10A/B569-777[»]
3C5RX-ray2.00A/B425-555[»]
3FA2X-ray2.20A/B566-777[»]
ProteinModelPortaliQ99728.
SMRiQ99728.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107056. 268 interactors.
DIPiDIP-5972N.
IntActiQ99728. 42 interactors.
MINTiMINT-207047.
STRINGi9606.ENSP00000260947.

Chemistry databases

BindingDBiQ99728.

PTM databases

iPTMnetiQ99728.
PhosphoSitePlusiQ99728.

Polymorphism and mutation databases

BioMutaiBARD1.
DMDMi116241265.

Proteomic databases

EPDiQ99728.
MaxQBiQ99728.
PaxDbiQ99728.
PeptideAtlasiQ99728.
PRIDEiQ99728.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260947; ENSP00000260947; ENSG00000138376. [Q99728-1]
ENST00000617164; ENSP00000480470; ENSG00000138376. [Q99728-2]
ENST00000620057; ENSP00000481988; ENSG00000138376. [Q99728-4]
GeneIDi580.
KEGGihsa:580.
UCSCiuc002veu.4. human. [Q99728-1]

Organism-specific databases

CTDi580.
DisGeNETi580.
GeneCardsiBARD1.
H-InvDBHIX0030010.
HGNCiHGNC:952. BARD1.
HPAiCAB034106.
HPA035354.
HPA044864.
MalaCardsiBARD1.
MIMi601593. gene.
neXtProtiNX_Q99728.
OpenTargetsiENSG00000138376.
Orphaneti145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA25256.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4362. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00760000119090.
HOGENOMiHOG000237306.
HOVERGENiHBG050662.
InParanoidiQ99728.
KOiK10683.
OMAiKKNSIKM.
OrthoDBiEOG091G0JNZ.
PhylomeDBiQ99728.
TreeFamiTF326440.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000138376-MONOMER.
ReactomeiR-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5689603. UCH proteinases.
R-HSA-5689901. Metalloprotease DUBs.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SignaLinkiQ99728.
SIGNORiQ99728.

Miscellaneous databases

ChiTaRSiBARD1. human.
EvolutionaryTraceiQ99728.
GeneWikiiBARD1.
GenomeRNAii580.
PROiQ99728.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138376.
CleanExiHS_BARD1.
ExpressionAtlasiQ99728. baseline and differential.
GenevisibleiQ99728. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q99728
Secondary accession number(s): F6MDH7
, F6MDH8, F6MDH9, O43574, Q53SS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-26 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.