Q99728 (BARD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
BRCA1-associated RING domain protein 1
Short name=BARD-1
EC=6.3.2.-

Gene names

Name:

BARD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	777 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14
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.12 Ref.14 Ref.15 Ref.17
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 process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cell cycle arrest Non-traceable author statement PubMed 15632137. 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.14. Source: UniProtKB regulation of phosphorylation Inferred from mutant phenotype PubMed 15782130. Source: UniProtKB response to DNA damage stimulus Non-traceable author statement PubMed 15905410. Source: UniProtKB tissue homeostasis Traceable author statement PubMed 15782130. Source: UniProtKB
Cellular_component	BRCA1-A complex Inferred from direct assay PubMed 17525342PubMed 19261748Ref.12. Source: UniProtKB BRCA1-BARD1 complex Inferred from direct assay Ref.7PubMed 15265711PubMed 19117993Ref.14. Source: UniProtKB cytoplasm Inferred from direct assay PubMed 15265711. Source: UniProtKB
Molecular_function	RNA binding Inferred from direct assay PubMed 12419249. Source: MGI kinase binding Non-traceable author statement PubMed 15782130. 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	8	EBI-473181,EBI-349905
CHD3	Q12873	2	EBI-473181,EBI-523590
CSTF1	Q05048	4	EBI-473181,EBI-1789619
CSTF2	P33240	5	EBI-473181,EBI-711360
GIT1	Q9Y2X7	2	EBI-473181,EBI-466061
KAT7	O95251	2	EBI-473181,EBI-473199
KIAA1377	Q9P2H0	2	EBI-473181,EBI-473176
TCERG1	O14776	2	EBI-473181,EBI-473271

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 777

777

BRCA1-associated RING domain protein 1

PRO_0000055819

Regions

Repeat

427 – 459

33

ANK 1

Repeat

460 – 492

33

ANK 2

Repeat

493 – 525

33

ANK 3

Repeat

526 – 546

21

ANK 4; degenerate

Domain

560 – 653

94

BRCT 1

Domain

667 – 777

111

BRCT 2

Zinc finger

50 – 87

38

RING-type

Region

26 – 119

94

Interaction with BRCA1

Region

554 – 558

5

Flexible linker

Compositional bias

400 – 403

4

Poly-Ser

Compositional bias

542 – 545

4

Poly-Leu

Amino acid modifications

Modified residue

391

1

Phosphoserine Ref.11

Modified residue

394

1

Phosphothreonine Ref.11

Cross-link

423

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Natural variations

Natural variant

24

1

P → S Common polymorphism in Caucasians; less frequent in Africans. Ref.2
Corresponds to variant rs1048108 [ dbSNP | Ensembl ].

VAR_010354

Natural variant

153

1

K → E. Ref.2

VAR_010355

Natural variant

186

1

S → G.
Corresponds to variant rs16852741 [ dbSNP | Ensembl ].

VAR_038371

Natural variant

241

1

S → C.
Corresponds to variant rs3738885 [ dbSNP | Ensembl ].

VAR_020109

Natural variant

378

1

R → S. Ref.2
Corresponds to variant rs2229571 [ dbSNP | Ensembl ].

VAR_024611

Natural variant

507

1

V → M. Ref.2
Corresponds to variant rs2070094 [ dbSNP | Ensembl ].

VAR_010356

Natural variant

557

1

C → S Rare polymorphism in Caucasians. Ref.2
Corresponds to variant rs28997576 [ dbSNP | Ensembl ].

VAR_010357

Natural variant

564

1

Q → H in an ovarian clear cell adenocarcinoma. Ref.2

VAR_010358

Natural variant

645

1

C → R.
Corresponds to variant rs34744268 [ dbSNP | Ensembl ].

VAR_038372

Natural variant

658

1

R → C Rare polymorphism in Caucasians; absent in Africans. Ref.2
Corresponds to variant rs3738888 [ dbSNP | Ensembl ].

VAR_010359

Natural variant

695

1

V → L in a breast cancer sample; somatic mutation. Ref.2

VAR_010360

Natural variant

728

1

S → F.
Corresponds to variant rs13389423 [ dbSNP | Ensembl ].

VAR_028309

Natural variant

761

1

S → N in an uterine cancer sample; somatic mutation. Ref.2

VAR_010361

Experimental info

Sequence conflict

406

1

R → Q in AAB38316. Ref.1

Secondary structure

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777

Helix Strand Turn

Details...

Helix

35 – 46

12

Beta strand

51 – 53

3

Beta strand

65 – 67

3

Turn

72 – 74

3

Helix

75 – 78

4

Turn

79 – 81

3

Beta strand

84 – 86

3

Helix

99 – 116

18

Helix

431 – 438

8

Helix

441 – 449

9

Helix

464 – 470

7

Helix

474 – 482

9

Helix

492 – 494

3

Helix

497 – 503

7

Helix

507 – 515

9

Helix

530 – 533

4

Helix

537 – 543

7

Beta strand

571 – 576

6

Helix

579 – 591

13

Beta strand

595 – 599

5

Beta strand

606 – 613

8

Helix

618 – 625

8

Beta strand

629 – 632

4

Helix

634 – 642

9

Helix

648 – 650

3

Helix

656 – 665

10

Turn

671 – 674

4

Beta strand

676 – 679

4

Beta strand

684 – 686

3

Helix

688 – 697

10

Beta strand

701 – 705

5

Helix

709 – 711

3

Helix

713 – 715

3

Helix

729 – 731

3

Beta strand

735 – 739

5

Beta strand

750 – 752

3

Beta strand

755 – 759

5

Helix

760 – 769

10

Sequences

	Sequence		Length	Mass (Da)
	Q99728 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 95E2D904046B5646	FASTA	777	86,648
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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, MASS SPECTROMETRY.
[18]	"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, MASS SPECTROMETRY, DOMAINS ANK REPEATS, DOMAIN STRUCTURE.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U76638 mRNA. Translation: AAB38316.1.
AF038042 , AF038034, AF038035, AF038036, AF038037, AF038038, AF038039, AF038040, AF038041 Genomic DNA. Translation: AAB99978.1.
AC016708 Genomic DNA. Translation: AAX93130.1.
BC126426 mRNA. Translation: AAI26427.1.

IPI

IPI00017746.

RefSeq

NP_000456.2. NM_000465.2.

UniGene

Hs.591642.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q99728.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5972N.

IntAct

Q99728. 28 interactions.

MINT

MINT-207047.

STRING

9606.ENSP00000260947.

PTM databases

PhosphoSite

Q99728.

Polymorphism databases

DMDM

116241265.

Proteomic databases

PaxDb

Q99728.

PeptideAtlas

Q99728.

PRIDE

Q99728.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260947; ENSP00000260947; ENSG00000138376.

GeneID

580.

KEGG

hsa:580.

UCSC

uc002veu.2. human.

Organism-specific databases

CTD

580.

GeneCards

GC02M215556.

H-InvDB

HIX0030010.

HGNC

HGNC:952. BARD1.

HPA

CAB034106.
HPA044864.

MIM

601593. gene.

neXtProt

NX_Q99728.

Orphanet

145. Hereditary breast and ovarian cancer syndrome.

PharmGKB

PA25256.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOGENOM

HOG000237306.

HOVERGEN

HBG050662.

InParanoid

Q99728.

KO

K10683.

OMA

KKNSIKM.

OrthoDB

EOG4FFD1B.

PhylomeDB

Q99728.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q99728.

Bgee

Q99728.

CleanEx

HS_BARD1.

Genevestigator

Q99728.

GermOnline

ENSG00000138376. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.
3.30.40.10. 1 hit.

InterPro

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]

Pfam

PF00023. Ank. 3 hits.
PF00533. BRCT. 1 hit.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 3 hits.
SM00292. BRCT. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF52113. BRCT. 2 hits.

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

Q99728.

ChEMBL

CHEMBL1741211.

ChiTaRS

BARD1. human.

EvolutionaryTrace

Q99728.

GenomeRNAi

580.

NextBio

2367.

SOURCE

Search...

Entry information

Entry name

BARD1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.