Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q99728 (BARD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BRCA1-associated RING domain protein 1

Short name=BARD-1
EC=6.3.2.-
Gene names
Name:BARD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length777 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.15

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.13 Ref.15 Ref.16 Ref.18

Subcellular location

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.

Post-translational modification

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

Sequence similarities

Contains 4 ANK repeats.

Contains 2 BRCT domains.

Contains 1 RING-type zinc finger.

Caution

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainANK repeat
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle arrest

Non-traceable author statement PubMed 15632137. Source: UniProtKB

cellular response to DNA damage stimulus

Non-traceable author statement PubMed 15905410. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 15265711. Source: UniProtKB

negative regulation of mRNA 3'-end processing

Non-traceable author statement PubMed 15905410. Source: UniProtKB

negative regulation of protein export from nucleus

Inferred from direct assay PubMed 15265711. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 15782130. Source: UniProtKB

positive regulation of protein catabolic process

Non-traceable author statement PubMed 15905410. Source: UniProtKB

protein K6-linked ubiquitination

Inferred from direct assay Ref.7Ref.15. Source: UniProtKB

protein ubiquitination

Non-traceable author statement PubMed 15905410. Source: UniProtKB

regulation of phosphorylation

Inferred from mutant phenotype PubMed 15782130. Source: UniProtKB

tissue homeostasis

Traceable author statement PubMed 15782130. Source: UniProtKB

   Cellular_componentBRCA1-A complex

Inferred from direct assay PubMed 17525342PubMed 19261748Ref.13. Source: UniProtKB

BRCA1-BARD1 complex

Inferred from direct assay Ref.7PubMed 15265711PubMed 19117993Ref.15. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 15265711. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 15265711. Source: UniProtKB

ubiquitin ligase complex

Non-traceable author statement Ref.8. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from direct assay PubMed 12419249. Source: MGI

kinase binding

Non-traceable author statement PubMed 15782130. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 15265711. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction PubMed 15265711. Source: UniProtKB

ubiquitin-protein ligase activity

Non-traceable author statement PubMed 15905410. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 777777BRCA1-associated RING domain protein 1
PRO_0000055819

Regions

Repeat427 – 45933ANK 1
Repeat460 – 49233ANK 2
Repeat493 – 52533ANK 3
Repeat526 – 54621ANK 4; degenerate
Domain560 – 65394BRCT 1
Domain667 – 777111BRCT 2
Zinc finger50 – 8738RING-type
Region26 – 11994Interaction with BRCA1
Region554 – 5585Flexible linker
Compositional bias400 – 4034Poly-Ser
Compositional bias542 – 5454Poly-Leu

Amino acid modifications

Modified residue3911Phosphoserine Ref.11
Modified residue3941Phosphothreonine Ref.11
Cross-link423Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Natural variations

Natural variant241P → S Common polymorphism in Caucasians; less frequent in Africans. Ref.2
Corresponds to variant rs1048108 [ dbSNP | Ensembl ].
VAR_010354
Natural variant1531K → E. Ref.2
VAR_010355
Natural variant1861S → G.
Corresponds to variant rs16852741 [ dbSNP | Ensembl ].
VAR_038371
Natural variant2411S → C.
Corresponds to variant rs3738885 [ dbSNP | Ensembl ].
VAR_020109
Natural variant3781R → S. Ref.2
Corresponds to variant rs2229571 [ dbSNP | Ensembl ].
VAR_024611
Natural variant5071V → M. Ref.2
Corresponds to variant rs2070094 [ dbSNP | Ensembl ].
VAR_010356
Natural variant5571C → S Rare polymorphism in Caucasians. Ref.2
Corresponds to variant rs28997576 [ dbSNP | Ensembl ].
VAR_010357
Natural variant5641Q → H in an ovarian clear cell adenocarcinoma. Ref.2
VAR_010358
Natural variant6451C → R.
Corresponds to variant rs34744268 [ dbSNP | Ensembl ].
VAR_038372
Natural variant6581R → C Rare polymorphism in Caucasians; absent in Africans. Ref.2
Corresponds to variant rs3738888 [ dbSNP | Ensembl ].
VAR_010359
Natural variant6951V → L in a breast cancer sample; somatic mutation. Ref.2
VAR_010360
Natural variant7281S → F.
Corresponds to variant rs13389423 [ dbSNP | Ensembl ].
VAR_028309
Natural variant7611S → N in an uterine cancer sample; somatic mutation. Ref.2
Corresponds to variant rs142155101 [ dbSNP | Ensembl ].
VAR_010361

Experimental info

Sequence conflict4061R → Q in AAB38316. Ref.1

Secondary structure

.......................................................................... 777
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99728 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 95E2D904046B5646

FASTA77786,648
        10         20         30         40         50         60 
MPDNRQPRNR QPRIRSGNEP RSAPAMEPDG RGAWAHSRAA LDRLEKLLRC SRCTNILREP 

        70         80         90        100        110        120 
VCLGGCEHIF CSNCVSDCIG TGCPVCYTPA WIQDLKINRQ LDSMIQLCSK LRNLLHDNEL 

       130        140        150        160        170        180 
SDLKEDKPRK SLFNDAGNKK NSIKMWFSPR SKKVRYVVSK ASVQTQPAIK KDASAQQDSY 

       190        200        210        220        230        240 
EFVSPSPPAD VSERAKKASA RSGKKQKKKT LAEINQKWNL EAEKEDGEFD SKEESKQKLV 

       250        260        270        280        290        300 
SFCSQPSVIS SPQINGEIDL LASGSLTESE CFGSLTEVSL PLAEQIESPD TKSRNEVVTP 

       310        320        330        340        350        360 
EKVCKNYLTS KKSLPLENNG KRGHHNRLSS PISKRCRTSI LSTSGDFVKQ TVPSENIPLP 

       370        380        390        400        410        420 
ECSSPPSCKR KVGGTSGRKN SNMSDEFISL SPGTPPSTLS SSSYRRVMSS PSAMKLLPNM 

       430        440        450        460        470        480 
AVKRNHRGET LLHIASIKGD IPSVEYLLQN GSDPNVKDHA GWTPLHEACN HGHLKVVELL 

       490        500        510        520        530        540 
LQHKALVNTT GYQNDSPLHD AAKNGHVDIV KLLLSYGASR NAVNIFGLRP VDYTDDESMK 

       550        560        570        580        590        600 
SLLLLPEKNE SSSASHCSVM NTGQRRDGPL VLIGSGLSSE QQKMLSELAV ILKAKKYTEF 

       610        620        630        640        650        660 
DSTVTHVVVP GDAVQSTLKC MLGILNGCWI LKFEWVKACL RRKVCEQEEK YEIPEGPRRS 

       670        680        690        700        710        720 
RLNREQLLPK LFDGCYFYLW GTFKHHPKDN LIKLVTAGGG QILSRKPKPD SDVTQTINTV 

       730        740        750        760        770 
AYHARPDSDQ RFCTQYIIYE DLCNYHPERV RQGKVWKAPS SWFIDCVMSF ELLPLDS 

« Hide

References

« Hide 'large scale' references
[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], 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]"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. expand/collapse author list , 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].
[4]"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].
Tissue: Brain.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND THR-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"Crystal structure of the BARD1 BRCT domains."
Birrane G., Varma A.K., Soni A., Ladias J.A.
Biochemistry 46:7706-7712(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 568-777.
[18]"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.
[19]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76638 mRNA. Translation: AAB38316.1.
AF038042 expand/collapse EMBL AC list , AF038034, AF038035, AF038036, AF038037, AF038038, AF038039, AF038040, AF038041 Genomic DNA. Translation: AAB99978.1.
AC016708 Genomic DNA. Translation: AAX93130.1.
BC126426 mRNA. Translation: AAI26427.1.
RefSeqNP_000456.2. NM_000465.3.
NP_001269472.1. NM_001282543.1.
UniGeneHs.591642.
Hs.597413.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ99728.
SMRQ99728. Positions 26-122, 376-777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107056. 244 interactions.
DIPDIP-5972N.
IntActQ99728. 29 interactions.
MINTMINT-207047.
STRING9606.ENSP00000260947.

Chemistry

BindingDBQ99728.

PTM databases

PhosphoSiteQ99728.

Polymorphism databases

DMDM116241265.

Proteomic databases

PaxDbQ99728.
PeptideAtlasQ99728.
PRIDEQ99728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260947; ENSP00000260947; ENSG00000138376.
GeneID580.
KEGGhsa:580.
UCSCuc002veu.2. human.

Organism-specific databases

CTD580.
GeneCardsGC02M215556.
H-InvDBHIX0030010.
HGNCHGNC:952. BARD1.
HPACAB034106.
HPA044864.
MIM601593. gene.
neXtProtNX_Q99728.
Orphanet145. Hereditary breast and ovarian cancer syndrome.
PharmGKBPA25256.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000237306.
HOVERGENHBG050662.
InParanoidQ99728.
KOK10683.
OMAKKNSIKM.
OrthoDBEOG779NXN.
PhylomeDBQ99728.
TreeFamTF326440.

Enzyme and pathway databases

SignaLinkQ99728.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ99728.
BgeeQ99728.
CleanExHS_BARD1.
GenevestigatorQ99728.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001357. BRCT_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00023. Ank. 3 hits.
PF00533. BRCT. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 3 hits.
SM00292. BRCT. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF52113. SSF52113. 2 hits.
PROSITEPS50297. 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]
ProtoNetSearch...

Other

ChiTaRSBARD1. human.
EvolutionaryTraceQ99728.
GeneWikiBARD1.
GenomeRNAi580.
NextBio2367.
PROQ99728.
SOURCESearch...

Entry information

Entry nameBARD1_HUMAN
AccessionPrimary (citable) accession number: Q99728
Secondary accession number(s): O43574, Q53SS5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM