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Q99728

- BARD1_HUMAN

UniProt

Q99728 - BARD1_HUMAN

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Protein

BRCA1-associated RING domain protein 1

Gene

BARD1

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

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri50 – 8738RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. kinase binding Source: UniProtKB
  2. ligase activity Source: UniProtKB-KW
  3. protein heterodimerization activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. RNA binding Source: MGI
  6. ubiquitin-protein transferase activity Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell cycle arrest Source: UniProtKB
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. DNA repair Source: UniProtKB-KW
  4. negative regulation of apoptotic process Source: UniProtKB
  5. negative regulation of mRNA 3'-end processing Source: UniProtKB
  6. negative regulation of protein export from nucleus Source: UniProtKB
  7. positive regulation of apoptotic process Source: UniProtKB
  8. positive regulation of protein catabolic process Source: UniProtKB
  9. protein K6-linked ubiquitination Source: UniProtKB
  10. protein ubiquitination Source: UniProtKB
  11. regulation of phosphorylation Source: UniProtKB
  12. tissue homeostasis Source: UniProtKB
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

SignaLinkiQ99728.
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: 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

  1. BRCA1-A complex Source: UniProtKB
  2. BRCA1-BARD1 complex Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. intracellular membrane-bounded organelle Source: HPA
  5. nucleolus Source: HPA
  6. nucleus Source: UniProtKB
  7. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

Orphaneti145. Hereditary breast and ovarian cancer syndrome.
PharmGKBiPA25256.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 777777BRCA1-associated RING domain protein 1PRO_0000055819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei391 – 3911Phosphoserine1 Publication
Modified residuei394 – 3941Phosphothreonine1 Publication
Cross-linki423 – 423Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

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

MaxQBiQ99728.
PaxDbiQ99728.
PeptideAtlasiQ99728.
PRIDEiQ99728.

PTM databases

PhosphoSiteiQ99728.

Expressioni

Gene expression databases

BgeeiQ99728.
CleanExiHS_BARD1.
ExpressionAtlasiQ99728. baseline and differential.
GenevestigatoriQ99728.

Organism-specific databases

HPAiCAB034106.
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
CHD3Q128732EBI-473181,EBI-523590
CSTF1Q050484EBI-473181,EBI-1789619
CSTF2P332408EBI-473181,EBI-711360
GIT1Q9Y2X72EBI-473181,EBI-466061
KAT7O952512EBI-473181,EBI-473199
KIAA1377Q9P2H02EBI-473181,EBI-473176
PARNO954534EBI-473181,EBI-372832
TCERG1O147762EBI-473181,EBI-473271

Protein-protein interaction databases

BioGridi107056. 245 interactions.
DIPiDIP-5972N.
IntActiQ99728. 29 interactions.
MINTiMINT-207047.
STRINGi9606.ENSP00000260947.

Structurei

Secondary structure

1
777
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 4612Combined sources
Beta strandi51 – 533Combined sources
Beta strandi65 – 673Combined sources
Turni72 – 743Combined sources
Helixi75 – 784Combined sources
Turni79 – 813Combined sources
Beta strandi84 – 863Combined sources
Helixi99 – 11618Combined sources
Helixi431 – 4388Combined sources
Helixi441 – 4499Combined sources
Helixi464 – 4707Combined sources
Helixi474 – 4829Combined sources
Helixi492 – 4943Combined sources
Helixi497 – 5037Combined sources
Helixi507 – 5159Combined sources
Helixi530 – 5334Combined sources
Helixi537 – 5437Combined sources
Beta strandi571 – 5766Combined sources
Helixi579 – 59113Combined sources
Beta strandi595 – 5995Combined sources
Beta strandi606 – 6138Combined sources
Helixi618 – 6258Combined sources
Beta strandi629 – 6324Combined sources
Helixi634 – 6429Combined sources
Helixi648 – 6503Combined sources
Helixi656 – 66510Combined sources
Turni671 – 6744Combined sources
Beta strandi676 – 6794Combined sources
Beta strandi684 – 6863Combined sources
Helixi688 – 69710Combined sources
Beta strandi701 – 7055Combined sources
Helixi709 – 7113Combined sources
Helixi713 – 7153Combined sources
Helixi729 – 7313Combined sources
Beta strandi735 – 7395Combined sources
Beta strandi750 – 7523Combined sources
Beta strandi755 – 7595Combined sources
Helixi760 – 76910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 26-122, 376-777.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99728.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati427 – 45933ANK 1Add
BLAST
Repeati460 – 49233ANK 2Add
BLAST
Repeati493 – 52533ANK 3Add
BLAST
Repeati526 – 54621ANK 4; degenerateAdd
BLAST
Domaini560 – 65394BRCT 1PROSITE-ProRule annotationAdd
BLAST
Domaini667 – 777111BRCT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 11994Interaction with BRCA1Add
BLAST
Regioni554 – 5585Flexible linker

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi400 – 4034Poly-Ser
Compositional biasi542 – 5454Poly-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 fingeri50 – 8738RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000119090.
HOGENOMiHOG000237306.
HOVERGENiHBG050662.
InParanoidiQ99728.
KOiK10683.
OMAiKKNSIKM.
OrthoDBiEOG779NXN.
PhylomeDBiQ99728.
TreeFamiTF326440.

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.
IPR001357. BRCT_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00023. Ank. 3 hits.
PF00533. BRCT. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 3 hits.
SM00292. BRCT. 2 hits.
SM00184. RING. 1 hit.
[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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851V → A in AEF57473. (PubMed:18089818)Curated
Sequence conflicti406 – 4061R → Q in AAB38316. (PubMed:8944023)Curated
Sequence conflicti406 – 4061R → Q in AEF57471. (PubMed:18089818)Curated
Sequence conflicti406 – 4061R → Q in AEF57472. (PubMed:18089818)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241P → S Common polymorphism in Caucasians; less frequent in Africans. 1 Publication
Corresponds to variant rs1048108 [ dbSNP | Ensembl ].
VAR_010354
Natural varianti153 – 1531K → E.1 Publication
VAR_010355
Natural varianti186 – 1861S → G.
Corresponds to variant rs16852741 [ dbSNP | Ensembl ].
VAR_038371
Natural varianti241 – 2411S → C.
Corresponds to variant rs3738885 [ dbSNP | Ensembl ].
VAR_020109
Natural varianti378 – 3781R → S.1 Publication
Corresponds to variant rs2229571 [ dbSNP | Ensembl ].
VAR_024611
Natural varianti507 – 5071V → M.1 Publication
Corresponds to variant rs2070094 [ dbSNP | Ensembl ].
VAR_010356
Natural varianti557 – 5571C → S Rare polymorphism in Caucasians. 1 Publication
Corresponds to variant rs28997576 [ dbSNP | Ensembl ].
VAR_010357
Natural varianti564 – 5641Q → H in an ovarian clear cell adenocarcinoma. 1 Publication
VAR_010358
Natural varianti645 – 6451C → R.
Corresponds to variant rs34744268 [ dbSNP | Ensembl ].
VAR_038372
Natural varianti658 – 6581R → C Rare polymorphism in Caucasians; absent in Africans. 1 Publication
Corresponds to variant rs3738888 [ dbSNP | Ensembl ].
VAR_010359
Natural varianti695 – 6951V → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_010360
Natural varianti728 – 7281S → F.
Corresponds to variant rs13389423 [ dbSNP | Ensembl ].
VAR_028309
Natural varianti761 – 7611S → N in an uterine cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs142155101 [ dbSNP | Ensembl ].
VAR_010361

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424MPDNR…PRSAP → MVAVPGPTVAPRSTAWRSCC AARV in isoform beta. 1 PublicationVSP_055874Add
BLAST
Alternative sequencei25 – 12197Missing in isoform beta. 1 PublicationVSP_055875Add
BLAST
Alternative sequencei54 – 7219Missing in isoform alpha. 1 PublicationVSP_055876Add
BLAST
Alternative sequencei122 – 1276DLKEDK → GRHTFC in isoform gamma. 1 PublicationVSP_055877
Alternative sequencei128 – 777650Missing in isoform gamma. 1 PublicationVSP_055878Add
BLAST

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]
ENST00000449967; ENSP00000406752; ENSG00000138376. [Q99728-3]
ENST00000617164; ENSP00000480470; ENSG00000138376. [Q99728-2]
ENST00000620057; ENSP00000481988; ENSG00000138376. [Q99728-4]
GeneIDi580.
KEGGihsa:580.
UCSCiuc002veu.2. human. [Q99728-1]

Polymorphism databases

DMDMi116241265.

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 .
CCDSi CCDS2397.1. [Q99728-1 ]
CCDS74646.1. [Q99728-2 ]
RefSeqi NP_000456.2. NM_000465.3. [Q99728-1 ]
NP_001269472.1. NM_001282543.1. [Q99728-2 ]
UniGenei Hs.591642.
Hs.597413.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JM7 NMR - B 26-140 [» ]
2NTE X-ray 1.90 A/B 568-777 [» ]
2R1Z X-ray 2.10 A/B 569-777 [» ]
3C5R X-ray 2.00 A/B 425-555 [» ]
3FA2 X-ray 2.20 A/B 566-777 [» ]
ProteinModelPortali Q99728.
SMRi Q99728. Positions 26-122, 376-777.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107056. 245 interactions.
DIPi DIP-5972N.
IntActi Q99728. 29 interactions.
MINTi MINT-207047.
STRINGi 9606.ENSP00000260947.

Chemistry

BindingDBi Q99728.

PTM databases

PhosphoSitei Q99728.

Polymorphism databases

DMDMi 116241265.

Proteomic databases

MaxQBi Q99728.
PaxDbi Q99728.
PeptideAtlasi Q99728.
PRIDEi Q99728.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260947 ; ENSP00000260947 ; ENSG00000138376 . [Q99728-1 ]
ENST00000449967 ; ENSP00000406752 ; ENSG00000138376 . [Q99728-3 ]
ENST00000617164 ; ENSP00000480470 ; ENSG00000138376 . [Q99728-2 ]
ENST00000620057 ; ENSP00000481988 ; ENSG00000138376 . [Q99728-4 ]
GeneIDi 580.
KEGGi hsa:580.
UCSCi uc002veu.2. human. [Q99728-1 ]

Organism-specific databases

CTDi 580.
GeneCardsi GC02M215556.
H-InvDB HIX0030010.
HGNCi HGNC:952. BARD1.
HPAi CAB034106.
HPA044864.
MIMi 601593. gene.
neXtProti NX_Q99728.
Orphaneti 145. Hereditary breast and ovarian cancer syndrome.
PharmGKBi PA25256.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000119090.
HOGENOMi HOG000237306.
HOVERGENi HBG050662.
InParanoidi Q99728.
KOi K10683.
OMAi KKNSIKM.
OrthoDBi EOG779NXN.
PhylomeDBi Q99728.
TreeFami TF326440.

Enzyme and pathway databases

UniPathwayi UPA00143 .
SignaLinki Q99728.

Miscellaneous databases

ChiTaRSi BARD1. human.
EvolutionaryTracei Q99728.
GeneWikii BARD1.
GenomeRNAii 580.
NextBioi 2367.
PROi Q99728.
SOURCEi Search...

Gene expression databases

Bgeei Q99728.
CleanExi HS_BARD1.
ExpressionAtlasi Q99728. baseline and differential.
Genevestigatori Q99728.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001357. BRCT_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF00023. Ank. 3 hits.
PF00533. BRCT. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 3 hits.
SM00292. BRCT. 2 hits.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a RING protein that can interact in vivo with the BRCA1 gene product."
    Wu L.C., Wang Z.W., Tsan J.T., Spillman M.A., Phung A., Xu X.L., Yang M.-C.W., Hwang L.-Y., Bowcock A.M., Baer R.
    Nat. Genet. 14:430-440(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: B-cell.
  2. "Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers."
    Thai T.H., Du F., Tsan J.T., Jin Y., Phung A., Spillman M.A., Massa H.F., Muller C.Y., Ashfaq R., Mathis J.M., Miller D.S., Trask B.J., Baer R., Bowcock A.M.
    Hum. Mol. Genet. 7:195-202(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-24; GLU-153; SER-378; MET-507; SER-557; HIS-564; CYS-658; LEU-695 AND ASN-761.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), ALTERNATIVE SPLICING.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. "Mapping the functional domains of BRCA1. Interaction of the ring finger domains of BRCA1 and BARD1."
    Meza J.E., Brzovic P.S., King M.-C., Klevit R.E.
    J. Biol. Chem. 274:5659-5665(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  7. "Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50."
    Kleiman F.E., Manley J.L.
    Science 285:1576-1579(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION.
  8. "The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin."
    Wu-Baer F., Lagrazon K., Yuan W., Baer R.
    J. Biol. Chem. 278:34743-34746(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRCA1.
  9. "BRCA1:BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair."
    Morris J.R., Solomon E.
    Hum. Mol. Genet. 13:807-817(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BARD1.
  10. "CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response."
    Kim H., Huang J., Chen J.
    Nat. Struct. Mol. Biol. 14:710-715(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
  11. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-423.
    Tissue: Mammary cancer.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND THR-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control."
    Wang B., Hurov K., Hofmann K., Elledge S.J.
    Genes Dev. 23:729-739(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "The UBXN1 protein associates with autoubiquitinated forms of the BRCA1 tumor suppressor and inhibits its enzymatic function."
    Wu-Baer F., Ludwig T., Baer R.
    Mol. Cell. Biol. 30:2787-2798(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRCA1.
  17. "Structure of a BRCA1-BARD1 heterodimeric RING-RING complex."
    Brzovic P.S., Rajagopal P., Hoyt D.W., King M.C., Klevit R.E.
    Nat. Struct. Biol. 8:833-837(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 26-140 IN COMPLEX WITH BRCA1 AND ZINC IONS, SUBUNIT.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 568-777.
  19. "The BARD1 C-terminal domain structure and interactions with polyadenylation factor CstF-50."
    Edwards R.A., Lee M.S., Tsutakawa S.E., Williams R.S., Nazeer I., Kleiman F.E., Tainer J.A., Glover J.N.
    Biochemistry 47:11446-11456(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 569-777, INTERACTION WITH CSTF1, DOMAIN STRUCTURE, IDENTIFICATION BY MASS SPECTROMETRY.
  20. "Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences."
    Fox D. III, Le Trong I., Rajagopal P., Brzovic P.S., Stenkamp R.E., Klevit R.E.
    J. Biol. Chem. 283:21179-21186(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 425-555, IDENTIFICATION BY MASS SPECTROMETRY, DOMAINS ANK REPEATS, DOMAIN STRUCTURE.

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 26, 2014
This is version 160 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

External Data

Dasty 3