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P38398 (BRCA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 194. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Breast cancer type 1 susceptibility protein

EC=6.3.2.-
Alternative name(s):
RING finger protein 53
Gene names
Name:BRCA1
Synonyms:RNF53
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1863 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Ref.13 Ref.16 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.34 Ref.35 Ref.37 Ref.41 Ref.44 Ref.47 Ref.49 Ref.50

Enzyme regulation

The E3 ubiquitin-protein ligase activity is inhibited by phosphorylation by AURKA. Activity is increased by phosphatase treatment. Ref.37

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Heterodimer with BARD1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Component of the BRCA1-A complex, at least composed of the BRCA1, BARD1, UIMC1, BRCC3, BRE and BABAM1. Interacts (via the BRCT domains) with FAM175A. Component of the BRCA1-RBBP8 complex. Interacts (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the interaction ubiquitinates RBBP8, regulates CHEK1 activation, and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Associates with RNA polymerase II holoenzyme. Interacts with SMC1A, COBRA1, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, AURKA, UBXN1 and KIAA0101/PAF15. Interacts (via BRCT domains) with BRIP1 (phosphorylated form). Interacts with FANCD2 (ubiquitinated form). Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts (via the BRCT domains) with ACACA (phosphorylated form); the interaction prevents dephosphorylation of ACACA. Part of a BRCA complex containing BRCA1, BRCA2 and PALB2. Interacts directly with PALB2; the interaction is essential for its function in HRR. Interacts directly with BRCA2; the interaction occurs only in the presence of PALB2 which serves as the bridging protein. Interacts (via the BRCT domains) with LMO4; the interaction represses the transcriptional activity of BRCA1. Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.41 Ref.44 Ref.45 Ref.46 Ref.47 Ref.49 Ref.53 Ref.56 Ref.60 Ref.61 Ref.62

Subcellular location

Nucleus. Chromosome By similarity. Note: Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. Ref.3 Ref.10 Ref.11 Ref.41 Ref.52 Ref.60

Isoform 3: Cytoplasm Ref.3 Ref.10 Ref.11 Ref.41 Ref.52 Ref.60.

Isoform 5: Cytoplasm Ref.3 Ref.10 Ref.11 Ref.41 Ref.52 Ref.60.

Tissue specificity

Isoform 1 and isoform 3 are widely expressed. Isoform 3 is reduced or absent in several breast and ovarian cancer cell lines. Ref.3

Domain

The BRCT domains recognize and bind phosphorylated pSXXF motif on proteins. The interaction with the phosphorylated pSXXF motif of FAM175A/Abraxas, recruits BRCA1 at DNA damage sites. Ref.64

The RING-type zinc finger domain interacts with BAP1. Ref.64

Post-translational modification

Phosphorylation at Ser-308 by AURKA is required for normal cell cycle progression from G2 to mitosis. Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Phosphorylation at Ser-988 by CHEK2 regulates mitotic spindle assembly. Ref.15 Ref.16 Ref.20 Ref.30 Ref.37 Ref.50 Ref.52

Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation.

Polymorphism

There is evidence that the presence of the rare form of Gln-356-Arg and Leu-871-Pro polymorphisms may be associated with an increased risk for developing ovarian cancer.

Involvement in disease

Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Mutations in BRCA1 are thought to be responsible for 45% of inherited breast cancer. Moreover, BRCA1 carriers have a 4-fold increased risk of colon cancer, whereas male carriers face a 3-fold increased risk of prostate cancer. Cells lacking BRCA1 show defects in DNA repair by homologous recombination. Ref.1 Ref.15 Ref.17 Ref.58 Ref.60 Ref.63 Ref.66 Ref.67 Ref.68 Ref.69 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.77 Ref.81 Ref.82 Ref.85 Ref.90

Breast-ovarian cancer, familial, 1 (BROVCA1) [MIM:604370]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Mutations in BRCA1 are thought to be responsible for more than 80% of inherited breast-ovarian cancer. Ref.70 Ref.71 Ref.82 Ref.85

Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Pancreatic cancer 4 (PNCA4) [MIM:614320]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.42

Sequence similarities

Contains 2 BRCT domains.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAB61673.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA recombination
DNA repair
Fatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Ubl conjugation pathway
   Cellular componentChromosome
Cytoplasm
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseDisease mutation
Tumor suppressor
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Traceable author statement PubMed 10918303. Source: UniProtKB

DNA repair

Traceable author statement. Source: Reactome

G2 DNA damage checkpoint

Inferred from mutant phenotype Ref.41Ref.39Ref.44. Source: UniProtKB

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

apoptotic process

Traceable author statement PubMed 10918303. Source: UniProtKB

cellular response to DNA damage stimulus

Traceable author statement PubMed 10910365. Source: ProtInc

cellular response to indole-3-methanol

Inferred from direct assay PubMed 10868478. Source: UniProtKB

chromosome segregation

Inferred from mutant phenotype PubMed 15965487. Source: UniProtKB

double-strand break repair

Inferred from mutant phenotype Ref.41Ref.39Ref.44. Source: UniProtKB

double-strand break repair via homologous recombination

Inferred from direct assay PubMed 17349954. Source: HGNC

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 14654789. Source: MGI

negative regulation of centriole replication

Non-traceable author statement PubMed 12214252. Source: UniProtKB

negative regulation of fatty acid biosynthetic process

Inferred from mutant phenotype Ref.35. Source: UniProtKB

negative regulation of histone H3-K9 methylation

Inferred from direct assay PubMed 20820192. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16288014. Source: UniProtKB

positive regulation of DNA repair

Inferred from mutant phenotype Ref.41Ref.39Ref.44. Source: UniProtKB

positive regulation of cell cycle arrest

Inferred from direct assay PubMed 21102443. Source: BHF-UCL

positive regulation of histone H3-K4 methylation

Inferred from direct assay PubMed 20820192. Source: BHF-UCL

positive regulation of histone H3-K9 acetylation

Inferred from direct assay PubMed 20820192. Source: BHF-UCL

positive regulation of histone H4-K16 acetylation

Inferred from direct assay PubMed 20820192. Source: BHF-UCL

positive regulation of histone H4-K20 methylation

Inferred from direct assay PubMed 20820192. Source: BHF-UCL

positive regulation of histone acetylation

Inferred from direct assay PubMed 20820192. Source: BHF-UCL

positive regulation of protein ubiquitination

Inferred from direct assay PubMed 15965487. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16331276. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

postreplication repair

Inferred from direct assay PubMed 17349954. Source: HGNC

protein K6-linked ubiquitination

Inferred from direct assay Ref.26Ref.49. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.26Ref.49. Source: UniProtKB

protein ubiquitination

Inferred from direct assay PubMed 17349954. Source: HGNC

regulation of apoptotic process

Traceable author statement PubMed 10918303. Source: UniProtKB

regulation of cell motility

Inferred from direct assay PubMed 21282464. Source: BHF-UCL

regulation of cell proliferation

Traceable author statement PubMed 10918303. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 10910365. Source: ProtInc

regulation of transcription from RNA polymerase III promoter

Traceable author statement PubMed 10918303. Source: UniProtKB

response to estrogen

Inferred from direct assay PubMed 8895509. Source: UniProtKB

response to ionizing radiation

Inferred from mutant phenotype Ref.41Ref.39Ref.44. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from direct assay PubMed 21282464. Source: BHF-UCL

   Cellular_componentBRCA1-A complex

Inferred from direct assay Ref.41PubMed 17525341PubMed 17525342Ref.44Ref.45. Source: UniProtKB

BRCA1-BARD1 complex

Inferred from direct assay Ref.26PubMed 15265711PubMed 19117993Ref.49. Source: UniProtKB

chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

gamma-tubulin ring complex

Non-traceable author statement PubMed 12214252. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.41Ref.39. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 21282464. Source: BHF-UCL

protein complex

Inferred from direct assay PubMed 9774970. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

ruffle

Inferred from direct assay PubMed 21282464. Source: BHF-UCL

ubiquitin ligase complex

Non-traceable author statement Ref.29. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 9662397. Source: ProtInc

RNA binding

Inferred from direct assay PubMed 12419249. Source: MGI

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 15965487. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11. Source: IntAct

transcription coactivator activity

Non-traceable author statement PubMed 15572661. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 20820192. Source: BHF-UCL

tubulin binding

Non-traceable author statement PubMed 12214252. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 17873885. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.26PubMed 19117993Ref.49. Source: UniProtKB

zinc ion binding

Traceable author statement PubMed 8944023. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: P38398-1)

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.
Isoform 2 (identifier: P38398-2)

The sequence of this isoform differs from the canonical sequence as follows:
     64-1863: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: P38398-3)

Also known as: Delta11b;

The sequence of this isoform differs from the canonical sequence as follows:
     264-1366: Missing.
     1453-1453: Missing.
Isoform 4 (identifier: P38398-4)

Also known as: DeltaBRCA1(17aa);

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
Note: Produced by alternative initiation at Met-18 of isoform 1.
Isoform 5 (identifier: P38398-5)

Also known as: Delta11; Delta772-3095;

The sequence of this isoform differs from the canonical sequence as follows:
     224-1365: Missing.
Isoform 6 (identifier: P38398-6)

The sequence of this isoform differs from the canonical sequence as follows:
     264-1366: Missing.
     1453-1453: Missing.
     1778-1863: DQLEWMVQLC...LIPQIPHSHY → GCPPNCGCAARCLDRGQWLPCNWADV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18631863Breast cancer type 1 susceptibility protein
PRO_0000055830

Regions

Domain1642 – 173695BRCT 1
Domain1756 – 1855100BRCT 2
Zinc finger24 – 6542RING-type
Region1397 – 142428Interaction with PALB2
Compositional bias651 – 6544Poly-Lys

Amino acid modifications

Modified residue11N-acetylmethionine Ref.55
Modified residue1141Phosphoserine Ref.51 Ref.54
Modified residue3081Phosphoserine; by AURKA Ref.30
Modified residue3951Phosphoserine Ref.43 Ref.48
Modified residue3981Phosphoserine Ref.43 Ref.48
Modified residue4231Phosphoserine Ref.51
Modified residue6941Phosphoserine Ref.51
Modified residue7531Phosphoserine Ref.43
Modified residue8401Phosphoserine By similarity
Modified residue9881Phosphoserine; by CHEK2 Ref.16 Ref.50
Modified residue11431Phosphoserine; by ATR; in vitro Ref.15
Modified residue12111Phosphoserine Ref.43
Modified residue12171Phosphoserine Ref.43
Modified residue12181Phosphoserine Ref.43 Ref.54
Modified residue12801Phosphoserine; by ATR; in vitro Ref.15
Modified residue13281Phosphoserine Ref.51
Modified residue13361Phosphoserine Ref.33 Ref.51 Ref.54
Modified residue13421Phosphoserine Ref.51 Ref.54
Modified residue13871Phosphoserine; by ATM and ATR Ref.15
Modified residue13941Phosphothreonine; by ATR; in vitro Ref.15
Modified residue14231Phosphoserine; by ATM and ATR Ref.15
Modified residue14571Phosphoserine; by ATR; in vitro Ref.15
Modified residue15241Phosphoserine; by ATM Ref.52

Natural variations

Alternative sequence1 – 1717Missing in isoform 4.
VSP_035396
Alternative sequence64 – 18631800Missing in isoform 2.
VSP_047891
Alternative sequence224 – 13651142Missing in isoform 5.
VSP_035398
Alternative sequence264 – 13661103Missing in isoform 3 and isoform 6.
VSP_035399
Alternative sequence14531Missing in isoform 3 and isoform 6.
VSP_043797
Alternative sequence1778 – 186386DQLEW…PHSHY → GCPPNCGCAARCLDRGQWLP CNWADV in isoform 6.
VSP_043798
Natural variant41S → F in BC; unknown pathological significance. Ref.90
VAR_070458
Natural variant101E → K in BC and BROVCA1. Ref.85
VAR_020679
Natural variant111V → A Unclassified.
VAR_007754
Natural variant181M → T in BC; unknown pathological significance. Ref.88 Ref.90
VAR_063899
Natural variant211I → V Unclassified.
VAR_007755
Natural variant221L → S in BC. Ref.75
VAR_007756
Natural variant231E → K in BC and BROVCA1. Ref.85
VAR_020680
Natural variant301L → F in a breast cancer sample; somatic mutation. Ref.87
VAR_035947
Natural variant451K → Q in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070459
Natural variant611C → G in BC and ovarian cancer; no interaction with BAP1. Ref.11 Ref.68 Ref.69 Ref.73 Ref.82 Ref.84 Ref.90
Corresponds to variant rs28897672 [ dbSNP | Ensembl ].
VAR_007757
Natural variant641C → G in BC; no interaction with BAP1. Ref.11 Ref.67 Ref.74 Ref.90
VAR_007758
Natural variant641C → Y Unclassified.
Corresponds to variant rs55851803 [ dbSNP | Ensembl ].
VAR_007759
Natural variant671D → Y in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070460
Natural variant711R → K in BC; unknown pathological significance. Ref.82
VAR_020681
Natural variant1051Y → C. Ref.90
VAR_070461
Natural variant1321N → K in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070462
Natural variant1421P → H in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070463
Natural variant1471L → F in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070464
Natural variant1531S → R.
Corresponds to variant rs28897674 [ dbSNP | Ensembl ].
VAR_052077
Natural variant1651L → P in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070465
Natural variant1701R → W in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070466
Natural variant1861S → Y in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070467
Natural variant1911V → I in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070468
Natural variant2271E → K in ovarian cancer; unknown pathological significance.
VAR_008759
Natural variant2311T → M in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070469
Natural variant2391H → R. Ref.3 Ref.73
VAR_007760
Natural variant2451D → V in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070470
Natural variant2461L → V in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070471
Natural variant2711V → L in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070472
Natural variant2711V → M in BC. Ref.72
Corresponds to variant rs80357244 [ dbSNP | Ensembl ].
VAR_007761
Natural variant2751G → S. Ref.6
Corresponds to variant rs8176153 [ dbSNP | Ensembl ].
VAR_019944
Natural variant3461P → S in BC; unknown pathological significance. Ref.77
VAR_008760
Natural variant3561Q → R Common polymorphism. Ref.5 Ref.6 Ref.68
Corresponds to variant rs1799950 [ dbSNP | Ensembl ].
VAR_007762
Natural variant3691Missing in BC.
VAR_007763
Natural variant3791I → M Unclassified.
Corresponds to variant rs56128296 [ dbSNP | Ensembl ].
VAR_007764
Natural variant4611F → L in BC. Ref.75
Corresponds to variant rs56046357 [ dbSNP | Ensembl ].
VAR_007765
Natural variant4651Y → D in BC. Ref.75
VAR_007766
Natural variant5071R → I Unclassified.
VAR_007767
Natural variant5521G → V in BC. Ref.75
VAR_007768
Natural variant6561N → I. Ref.80
VAR_020682
Natural variant6681L → F in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070473
Natural variant6931D → N Rare polymorphism. Ref.6 Ref.83
Corresponds to variant rs4986850 [ dbSNP | Ensembl ].
VAR_007769
Natural variant6951D → N in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070474
Natural variant7231N → D.
Corresponds to variant rs4986845 [ dbSNP | Ensembl ].
VAR_020110
Natural variant7491D → Y in BC. Ref.81
VAR_020683
Natural variant7581L → F in a breast cancer sample; somatic mutation. Ref.87
VAR_035948
Natural variant7721V → A Rare polymorphism. Ref.67 Ref.74
VAR_007770
Natural variant7781G → C in a breast cancer sample; somatic mutation. Ref.87
VAR_035949
Natural variant7981P → L in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070475
Natural variant8101N → Y in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070476
Natural variant8201K → E Rare polymorphism. Ref.74
Corresponds to variant rs56082113 [ dbSNP | Ensembl ].
VAR_007771
Natural variant8261T → K in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
Corresponds to variant rs28897683 [ dbSNP | Ensembl ].
VAR_007772
Natural variant8351H → Y in BROVCA1; unknown pathological significance. Ref.82
VAR_020684
Natural variant8411R → Q in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070477
Natural variant8411R → W in BROVCA1; unknown pathological significance. Ref.70 Ref.73
Corresponds to variant rs1800709 [ dbSNP | Ensembl ].
VAR_007773
Natural variant8561Y → H in a patient with sporadic breast cancer; unknown pathological significance. Ref.86 Ref.90
Corresponds to variant rs80356892 [ dbSNP | Ensembl ].
VAR_020685
Natural variant8661R → C. Ref.90
VAR_070478
Natural variant8661R → Q in BC; unknown pathological significance. Ref.82
VAR_020686
Natural variant8711P → L Common polymorphism. Ref.6 Ref.77 Ref.80 Ref.86
Corresponds to variant rs799917 [ dbSNP | Ensembl ].
VAR_007774
Natural variant8881H → Y in BC; unknown pathological significance. Ref.82
VAR_020687
Natural variant8921L → S in BC. Ref.75
VAR_007775
Natural variant9251I → L.
Corresponds to variant rs4986847 [ dbSNP | Ensembl ].
VAR_021913
Natural variant9601G → D in BC. Ref.75
VAR_007776
Natural variant9891F → S.
Corresponds to variant rs4986848 [ dbSNP | Ensembl ].
VAR_020111
Natural variant10081M → I Common polymorphism.
Corresponds to variant rs1800704 [ dbSNP | Ensembl ].
VAR_007777
Natural variant10251T → I in BC. Ref.75
VAR_007778
Natural variant10381E → G Common polymorphism. Ref.6 Ref.68 Ref.77 Ref.86
Corresponds to variant rs16941 [ dbSNP | Ensembl ].
VAR_007779
Natural variant10401S → N Rare polymorphism. Ref.6 Ref.67 Ref.68 Ref.74 Ref.83
Corresponds to variant rs4986852 [ dbSNP | Ensembl ].
VAR_007780
Natural variant10471V → A in BC. Ref.75
VAR_007781
Natural variant10601E → A. Ref.83 Ref.90
VAR_020688
Natural variant11011S → N in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070479
Natural variant11391S → I in BC; unknown pathological significance. Ref.82
VAR_020689
Natural variant11401S → G in BC; unknown pathological significance; functionally neutral in vitro. Ref.6 Ref.90
Corresponds to variant rs2227945 [ dbSNP | Ensembl ].
VAR_019945
Natural variant11401S → N in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070480
Natural variant11501P → S in BC. Ref.72
Corresponds to variant rs80357272 [ dbSNP | Ensembl ].
VAR_007782
Natural variant11831K → R Common polymorphism. Ref.6 Ref.68 Ref.77 Ref.85 Ref.86
Corresponds to variant rs16942 [ dbSNP | Ensembl ].
VAR_007783
Natural variant11871S → I in BC and BROVCA1. Ref.85
VAR_020690
Natural variant12001Q → H in BC and BROVCA1. Ref.85
Corresponds to variant rs56214134 [ dbSNP | Ensembl ].
VAR_020691
Natural variant12041R → I in BC. Ref.85
VAR_020692
Natural variant12071K → N in BC. Ref.85
VAR_020693
Natural variant12101E → G in BC; unknown pathological significance. Ref.82
VAR_020694
Natural variant12141E → K in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070481
Natural variant12171S → Y in BC and BROVCA1. Ref.85
VAR_020695
Natural variant12191E → D Unclassified.
VAR_007784
Natural variant12261F → L in BROVCA1. Ref.85
VAR_020696
Natural variant12361N → K in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
Corresponds to variant rs28897687 [ dbSNP | Ensembl ].
VAR_052078
Natural variant12431R → G in BROVCA1. Ref.85
VAR_020697
Natural variant12501E → K. Ref.90
Corresponds to variant rs28897686 [ dbSNP | Ensembl ].
VAR_052079
Natural variant12671L → S in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070482
Natural variant12821E → V in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070483
Natural variant12971S → P in BC; unknown pathological significance. Ref.82
VAR_020698
Natural variant12971Missing in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070484
Natural variant13011S → R in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070485
Natural variant13461E → K in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070486
Natural variant13471R → G. Ref.79
Corresponds to variant rs28897689 [ dbSNP | Ensembl ].
VAR_007785
Natural variant13781V → I in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070487
Natural variant14001M → V in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070488
Natural variant14061K → N Polymorphism.
Corresponds to variant rs1800707 [ dbSNP | Ensembl ].
VAR_008761
Natural variant14071L → P in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070489
Natural variant14111M → T in BC and ovarian cancer; unknown pathological significance; decreased interaction with PALB2. Ref.84 Ref.90
VAR_020699
Natural variant14311S → P.
VAR_007786
Natural variant14431R → G in BC; unknown pathological significance; functionally neutral in vitro. Ref.67 Ref.74 Ref.90
VAR_007787
Natural variant14431R → Q.
Corresponds to variant rs4986849 [ dbSNP | Ensembl ].
VAR_020112
Natural variant14481S → G in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070490
Natural variant14861S → C in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070491
Natural variant14951R → M in BC; unknown pathological significance. Ref.88
VAR_063900
Natural variant15121S → I. Ref.73 Ref.74 Ref.79
Corresponds to variant rs1800744 [ dbSNP | Ensembl ].
VAR_007788
Natural variant15341V → M in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070492
Natural variant15611T → I Found in breast cancer; unknown pathological significance.
Corresponds to variant rs56158747 [ dbSNP | Ensembl ].
VAR_007789
Natural variant15891R → P in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070493
Natural variant16061K → E Found in breast cancer; unknown pathological significance.
VAR_007790
Natural variant16131S → G Common polymorphism. Ref.3 Ref.6 Ref.68 Ref.77 Ref.80
Corresponds to variant rs1799966 [ dbSNP | Ensembl ].
VAR_007791
Natural variant16201T → A. Ref.6
Corresponds to variant rs8176219 [ dbSNP | Ensembl ].
VAR_019946
Natural variant16231A → G Could be associated with cancer susceptibility; major splicing aberration identified with this mutant. Ref.88 Ref.89
VAR_063901
Natural variant16281M → T in some patients with sporadic breast cancer; unknown pathological significance. Ref.86 Ref.90
Corresponds to variant rs4986854 [ dbSNP | Ensembl ].
VAR_007793
Natural variant16281M → V Unclassified.
VAR_007792
Natural variant16371P → L Rare polymorphism. Ref.66 Ref.74
VAR_007794
Natural variant16411A → P in ovarian cancer; unknown pathological significance.
Corresponds to variant rs1800726 [ dbSNP | Ensembl ].
VAR_008762
Natural variant16511S → F in BC; unknown pathological significance. Ref.90
VAR_070494
Natural variant16511S → P in BC; unknown pathological significance. Ref.90
VAR_070495
Natural variant16521M → I Rare polymorphism. Ref.74 Ref.79 Ref.90
Corresponds to variant rs1799967 [ dbSNP | Ensembl ].
VAR_007795
Natural variant16551S → F in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070496
Natural variant16621F → C.
Corresponds to variant rs28897695 [ dbSNP | Ensembl ].
VAR_052080
Natural variant16651V → M. Ref.83
VAR_020700
Natural variant16851T → A in BC; unknown pathological significance. Ref.88
VAR_063902
Natural variant16851T → I Could be associated with cancer susceptibility; multifactorial likelihood analysis provides evidence for pathogenicity. Ref.88 Ref.89
VAR_063903
Natural variant16861H → Q in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070497
Natural variant16861H → R in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070498
Natural variant16881Missing in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070499
Natural variant16891M → R in BC; unknown pathological significance. Ref.88
VAR_063904
Natural variant16901K → Q in some patients with sporadic breast cancer; unknown pathological significance. Ref.86
VAR_020701
Natural variant16911T → I in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070500
Natural variant16921D → N in ovarian cancer; unknown pathological significance.
VAR_008763
Natural variant16971C → R in ovarian cancer. Ref.84
VAR_020702
Natural variant16991R → Q in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070501
Natural variant16991R → W in BC and ovarian cancer; functionally impaired in vitro. Ref.84 Ref.88 Ref.90
VAR_020703
Natural variant17061G → A in BC; unknown pathological significance. Ref.90
VAR_070502
Natural variant17061G → E in BC; unknown pathological significance. Ref.88 Ref.90
Corresponds to variant rs80356860 [ dbSNP | Ensembl ].
VAR_063905
Natural variant17081A → E in BC; abolishes ACACA binding. Ref.66 Ref.88 Ref.90
Corresponds to variant rs28897696 [ dbSNP | Ensembl ].
VAR_007796
Natural variant17131V → G. Ref.86
VAR_007797
Natural variant17151S → R in BC; unknown pathological significance. Ref.88
VAR_063906
Natural variant17181W → C in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070503
Natural variant17201T → A in BC; unknown pathological significance; functionally neutral in vitro; no effect on in vitro phosphorylation by ATR. Ref.15 Ref.90
VAR_070504
Natural variant17351E → K in BC; unknown pathological significance. Ref.90
VAR_070505
Natural variant17361V → A in BC; unknown pathological significance. Ref.90
VAR_070506
Natural variant17381G → R in BC; unknown pathological significance. Ref.88
VAR_063907
Natural variant17391D → G in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070507
Natural variant17391D → V in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070508
Natural variant17461H → Q in BC; unknown pathological significance. Ref.90
VAR_070509
Natural variant17491P → R in ovarian cancer; unknown pathological significance; abolishes ACACA binding and strongly reduces BRIP1 binding. Ref.17 Ref.60 Ref.76
VAR_007798
Natural variant17531R → T in BC; unknown pathological significance. Ref.90
VAR_070510
Natural variant17641L → P in BC; unknown pathological significance; functionally impaired in vitro. Ref.88 Ref.90
VAR_063908
Natural variant17661I → S in BC; unknown pathological significance. Ref.88
VAR_063909
Natural variant17671C → S in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070511
Natural variant17701G → V in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070512
Natural variant17751M → K in BC; strongly reduced transcription transactivation; abolishes interaction with BRIP1 and RBBP8. Ref.63
VAR_063212
Natural variant17751M → R in BC; alters protein stability and abolishes ACACA and BRIP1 binding. Ref.1 Ref.17 Ref.58 Ref.60 Ref.66
VAR_007799
Natural variant17761P → S in ovarian cancer; unknown pathological significance.
Corresponds to variant rs1800757 [ dbSNP | Ensembl ].
VAR_008764
Natural variant17821W → C in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070513
Natural variant17861L → P in BROVCA1; unknown pathological significance. Ref.82
VAR_020704
Natural variant17881G → V in BC; unknown pathological significance. Ref.88
VAR_063910
Natural variant17891A → T in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070514
Natural variant17941E → D in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070515
Natural variant18041V → D in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070516
Natural variant18121P → R in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070517
Natural variant18121P → S in ovarian cancer; unknown pathological significance.
Corresponds to variant rs1800751 [ dbSNP | Ensembl ].
VAR_008765
Natural variant18371W → R in BC; unknown pathological significance; functionally impaired in vitro. Ref.90
VAR_070518
Natural variant18621H → L in BC; unknown pathological significance; functionally neutral in vitro. Ref.90
VAR_070519

Experimental info

Mutagenesis261I → A: Disrupts the interaction with E2 enzymes, thereby abolishing the E3 ubiquitin-protein ligase activity. Ref.34 Ref.49
Mutagenesis261I → E: No ubiquitination of RBBP8. No restoration RBBP8-mediated focus formation or G2/M checkpoint control upon DNA damage. Ref.34 Ref.49
Mutagenesis711R → G: No effect on interaction with BAP1. Ref.11
Mutagenesis3081S → N: Abolishes phosphorylation by AURKA and interferes with cell cycle progression from G2 to mitosis. Ref.30
Mutagenesis11431S → A: Reduces in vitro phosphorylation by ATR. Ref.15
Mutagenesis12391S → A: No effect on in vitro phosphorylation by ATR. Ref.15
Mutagenesis12801S → A: Reduces in vitro phosphorylation by ATR. Ref.15
Mutagenesis12981S → A: No effect on in vitro phosphorylation by ATR. Ref.15
Mutagenesis13301S → A: No effect on in vitro phosphorylation by ATR. Ref.15
Mutagenesis13871S → A: Loss of IR-induced S-phase checkpoint. Reduces in vitro phosphorylation by ATR. Ref.15 Ref.20
Mutagenesis13941T → A: Reduces in vitro phosphorylation by ATR. Ref.15
Mutagenesis14231S → A: Inhibition of the infrared-induced G2 arrest. Reduces phosphorylation by ATR. Ref.15 Ref.20
Mutagenesis14571S → A: Reduces in vitro phosphorylation by ATR. Ref.15
Mutagenesis14661S → A: No effect on in vitro phosphorylation by ATR. Ref.15
Mutagenesis15241S → A: No change in infrared S-phase delay; when associated with A-1387. No effect on in vitro phosphorylation by ATR. Ref.15 Ref.20
Mutagenesis16551S → A: Abolishes interaction with BRIP1. Ref.60
Mutagenesis17021K → M: Abolishes interaction with BRIP1. Ref.60
Mutagenesis17381G → E: Abolishes interaction with BRIP1. Ref.60
Mutagenesis17551S → A: No effect on in vitro phosphorylation by ATR. Ref.15
Sequence conflict891I → T in AAB61673. Ref.4
Sequence conflict1481Missing in AAB61673. Ref.4
Sequence conflict2531A → V in AAC00049. Ref.3
Sequence conflict10771G → R in AAB61673. Ref.4
Sequence conflict14261S → P in AAC00049. Ref.3

Secondary structure

...................................................................... 1863
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 89C6D83FF56312AF

FASTA1,863207,721
        10         20         30         40         50         60 
MDLSALRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ 

        70         80         90        100        110        120 
CPLCKNDITK RSLQESTRFS QLVEELLKII CAFQLDTGLE YANSYNFAKK ENNSPEHLKD 

       130        140        150        160        170        180 
EVSIIQSMGY RNRAKRLLQS EPENPSLQET SLSVQLSNLG TVRTLRTKQR IQPQKTSVYI 

       190        200        210        220        230        240 
ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTRDEISLDS AKKAACEFSE TDVTNTEHHQ 

       250        260        270        280        290        300 
PSNNDLNTTE KRAAERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSSL LLTKDRMNVE 

       310        320        330        340        350        360 
KAEFCNKSKQ PGLARSQHNR WAGSKETCND RRTPSTEKKV DLNADPLCER KEWNKQKLPC 

       370        380        390        400        410        420 
SENPRDTEDV PWITLNSSIQ KVNEWFSRSD ELLGSDDSHD GESESNAKVA DVLDVLNEVD 

       430        440        450        460        470        480 
EYSGSSEKID LLASDPHEAL ICKSERVHSK SVESNIEDKI FGKTYRKKAS LPNLSHVTEN 

       490        500        510        520        530        540 
LIIGAFVTEP QIIQERPLTN KLKRKRRPTS GLHPEDFIKK ADLAVQKTPE MINQGTNQTE 

       550        560        570        580        590        600 
QNGQVMNITN SGHENKTKGD SIQNEKNPNP IESLEKESAF KTKAEPISSS ISNMELELNI 

       610        620        630        640        650        660 
HNSKAPKKNR LRRKSSTRHI HALELVVSRN LSPPNCTELQ IDSCSSSEEI KKKKYNQMPV 

       670        680        690        700        710        720 
RHSRNLQLME GKEPATGAKK SNKPNEQTSK RHDSDTFPEL KLTNAPGSFT KCSNTSELKE 

       730        740        750        760        770        780 
FVNPSLPREE KEEKLETVKV SNNAEDPKDL MLSGERVLQT ERSVESSSIS LVPGTDYGTQ 

       790        800        810        820        830        840 
ESISLLEVST LGKAKTEPNK CVSQCAAFEN PKGLIHGCSK DNRNDTEGFK YPLGHEVNHS 

       850        860        870        880        890        900 
RETSIEMEES ELDAQYLQNT FKVSKRQSFA PFSNPGNAEE ECATFSAHSG SLKKQSPKVT 

       910        920        930        940        950        960 
FECEQKEENQ GKNESNIKPV QTVNITAGFP VVGQKDKPVD NAKCSIKGGS RFCLSSQFRG 

       970        980        990       1000       1010       1020 
NETGLITPNK HGLLQNPYRI PPLFPIKSFV KTKCKKNLLE ENFEEHSMSP EREMGNENIP 

      1030       1040       1050       1060       1070       1080 
STVSTISRNN IRENVFKEAS SSNINEVGSS TNEVGSSINE IGSSDENIQA ELGRNRGPKL 

      1090       1100       1110       1120       1130       1140 
NAMLRLGVLQ PEVYKQSLPG SNCKHPEIKK QEYEEVVQTV NTDFSPYLIS DNLEQPMGSS 

      1150       1160       1170       1180       1190       1200 
HASQVCSETP DDLLDDGEIK EDTSFAENDI KESSAVFSKS VQKGELSRSP SPFTHTHLAQ 

      1210       1220       1230       1240       1250       1260 
GYRRGAKKLE SSEENLSSED EELPCFQHLL FGKVNNIPSQ STRHSTVATE CLSKNTEENL 

      1270       1280       1290       1300       1310       1320 
LSLKNSLNDC SNQVILAKAS QEHHLSEETK CSASLFSSQC SELEDLTANT NTQDPFLIGS 

      1330       1340       1350       1360       1370       1380 
SKQMRHQSES QGVGLSDKEL VSDDEERGTG LEENNQEEQS MDSNLGEAAS GCESETSVSE 

      1390       1400       1410       1420       1430       1440 
DCSGLSSQSD ILTTQQRDTM QHNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIISDSSALE 

      1450       1460       1470       1480       1490       1500 
DLRNPEQSTS EKAVLTSQKS SEYPISQNPE GLSADKFEVS ADSSTSKNKE PGVERSSPSK 

      1510       1520       1530       1540       1550       1560 
CPSLDDRWYM HSCSGSLQNR NYPSQEELIK VVDVEEQQLE ESGPHDLTET SYLPRQDLEG 

      1570       1580       1590       1600       1610       1620 
TPYLESGISL FSDDPESDPS EDRAPESARV GNIPSSTSAL KVPQLKVAES AQSPAAAHTT 

      1630       1640       1650       1660       1670       1680 
DTAGYNAMEE SVSREKPELT ASTERVNKRM SMVVSGLTPE EFMLVYKFAR KHHITLTNLI 

      1690       1700       1710       1720       1730       1740 
TEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV 

      1750       1760       1770       1780       1790       1800 
VNGRNHQGPK RARESQDRKI FRGLEICCYG PFTNMPTDQL EWMVQLCGAS VVKELSSFTL 

      1810       1820       1830       1840       1850       1860 
GTGVHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH 


SHY 

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Isoform 2 [UniParc].

Checksum: F488196D90AE5BAE
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FASTA637,177
Isoform 3 (Delta11b) [UniParc].

Checksum: 29C7B9FF1660BD5C
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FASTA75985,001
Isoform 4 (DeltaBRCA1(17aa)) [UniParc].

Checksum: 3C16437DF10FA4D1
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FASTA1,846205,838
Isoform 5 (Delta11) (Delta772-3095) [UniParc].

Checksum: A4EED8A734FCB619
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FASTA72180,590
Isoform 6 [UniParc].

Checksum: 67C7F5031F0ED6F3
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FASTA69978,165

References

« Hide 'large scale' references
[1]"A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1."
Miki Y., Swensen J., Shattuck-Eidens D., Futreal P.A., Harshman K., Tavtigian S., Liu Q., Cochran C., Bennett L.M., Ding W., Bell R., Rosenthal J., Hussey C., Tran T., McClure M., Frye C., Hattier T., Phelps R. expand/collapse author list , Haugen-Strano A., Katcher H., Yakumo K., Gholami Z., Shaffer D., Stone S., Bayer S., Wray C., Bogden R., Dayananth P., Ward J., Tonin P., Narod S., Bristow P.K., Norris F.H., Helvering L., Morrison P., Rosteck P., Lai M., Barrett J.C., Lewis C., Neuhausen S., Cannon-Albright L., Godlgar D., Wiseman R., Kamb A., Skolnick M.H.
Science 266:66-71(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT BC ARG-1775.
[2]"Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1."
Smith T.M., Lee M.K., Szabo C.I., Jerome N., McEuen M., Taylor M., Hood L., King M.-C.
Genome Res. 6:1029-1049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Differential subcellular localization, expression and biological toxicity of BRCA1 and the splice variant BRCA1-delta11b."
Wilson C.A., Payton M.N., Elliott G.S., Buaas F.W., Cajulis E.E., Grosshans D., Ramos L., Reese D.M., Slamon D.J., Calzone F.J.
Oncogene 14:1-16(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 2), VARIANTS ARG-239 AND GLY-1613, TISSUE SPECIFICITY (ISOFORMS 1 AND 3).
Tissue: Mammary gland.
[4]Holt J.T., Robinson-Benion C.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Testis.
[5]Raymond C.K., Paddock M., Subramanian S., Deodato C., Zhou Y., Haugen E., Kaul R., Olson M.V.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-356.
[6]NIEHS SNPs program
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-275; ARG-356; ASN-693; LEU-871; GLY-1038; ASN-1040; GLY-1140; ARG-1183; GLY-1613 AND ALA-1620.
[7]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 6).
Tissue: PNS.
[9]"Initiation of translation from a downstream in-frame AUG codon on BRCA1 can generate the novel isoform protein DeltaBRCA1(17aa)."
Liu J., Prolla G., Rostagno A., Chiarle R., Feiner H., Inghirami G.
Oncogene 19:2767-2773(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 6-18 (ISOFORM 1), PROTEIN SEQUENCE OF 18-26 (ISOFORM 4), ALTERNATIVE INITIATION (ISOFORM 4).
[10]"Localization of BRCA1 and a splice variant identifies the nuclear localization signal."
Thakur S., Zhang H.B., Peng Y., Le H., Carroll B., Ward T., Yao J., Farid L.M., Couch F.J., Wilson R.B., Weber B.L.
Mol. Cell. Biol. 17:444-452(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 5), SUBCELLULAR LOCATION (ISOFORM 5).
[11]"BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression."
Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I., Chodosh L.A., Ishov A.M., Tommerup N., Vissing H., Sekido Y., Minna J., Borodovsky A., Schultz D.C., Wilkinson K.D., Maul G.G., Barlev N., Berger S., Prendergast G.C., Rauscher F.J. III
Oncogene 16:1097-1112(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAP1, SUBCELLULAR LOCATION, VARIANTS GLY-61 AND GLY-64, MUTAGENESIS OF ARG-71.
[12]"Characterization of a carboxy-terminal BRCA1 interacting protein."
Wong A.K., Ormonde P.A., Pero R., Chen Y., Lian L., Salada G., Berry S., Lawrence Q., Dayananth P., Ha P., Tavtigian S.V., Teng D.H., Bartel P.L.
Oncogene 17:2279-2285(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBBP8.
[13]"RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination."
Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S., Weissman A.M.
Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE.
[14]"BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures."
Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.
Genes Dev. 14:927-939(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BASC COMPLEX.
[15]"Functional interactions between BRCA1 and the checkpoint kinase ATR during genotoxic stress."
Tibbetts R.S., Cortez D., Brumbaugh K.M., Scully R., Livingston D., Elledge S.J., Abraham R.T.
Genes Dev. 14:2989-3002(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1143; SER-1280; SER-1387; THR-1394; SER-1423 AND SER-1457, MUTAGENESIS OF SER-1143; SER-1239; SER-1280; SER-1298; SER-1330; SER-1387; THR-1394; SER-1423; SER-1457; SER-1466; SER-1524 AND SER-1755, CHARACTERIZATION OF VARIANT BC ALA-1720.
[16]"hCds1-mediated phosphorylation of BRCA1 regulates the DNA damage response."
Lee J.S., Collins K.M., Brown A.L., Lee C.H., Chung J.H.
Nature 404:201-204(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-988 BY CHEK2, INTERACTION WITH CHEK2.
[17]"BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function."
Cantor S.B., Bell D.W., Ganesan S., Kass E.M., Drapkin R., Grossman S., Wahrer D.C.R., Sgroi D.C., Lane W.S., Haber D.A., Livingston D.M.
Cell 105:149-160(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRIP1, CHARACTERIZATION OF VARIANT OVARIAN CANCER ARG-1749, CHARACTERIZATION OF VARIANT BC ARG-1775.
[18]"BRCA1-induced large-scale chromatin unfolding and allele-specific effects of cancer-predisposing mutations."
Ye Q., Hu Y.-F., Zhong H., Nye A.C., Belmont A.S., Li R.
J. Cell Biol. 155:911-921(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NELFB.
[19]"Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway."
Garcia-Higuera I., Taniguchi T., Ganesan S., Meyn M.S., Timmers C., Hejna J., Grompe M., D'Andrea A.D.
Mol. Cell 7:249-262(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FANCD2.
[20]"Phosphorylation of serine 1387 in BRCA1 is specifically required for the Atm-mediated S-phase checkpoint after ionizing irradiation."
Xu B., O'Donnell A.H., Kim S.-T., Kastan M.B.
Cancer Res. 62:4588-4591(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY ATM, MUTAGENESIS OF SER-1387; SER-1423 AND SER-1524.
[21]"NBS1 localizes to gamma-H2AX foci through interaction with the FHA/BRCT domain."
Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K., Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.
Curr. Biol. 12:1846-1851(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH H2AFX.
[22]"SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint."
Yazdi P.T., Wang Y., Zhao S., Patel N., Lee E.Y.-H.P., Qin J.
Genes Dev. 16:571-582(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMC1A.
[23]"The LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor suppressor BRCA1 and inhibits BRCA1 activity."
Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J., Visvader J.E.
J. Biol. Chem. 277:7849-7856(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LMO4.
[24]"BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage."
Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., Brody L.C.
Nat. Genet. 30:285-289(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHEK1.
[25]"BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."
Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.
Oncogene 21:6729-6739(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACACA.
[26]"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, UBIQUITINATION, INTERACTION WITH BARD1.
[27]"BRCA1-independent ubiquitination of FANCD2."
Vandenberg C.J., Gergely F., Ong C.Y., Pace P., Mallery D.L., Hiom K., Patel K.J.
Mol. Cell 12:247-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair."
Dong Y., Hakimi M.-A., Chen X., Kumaraswamy E., Cooch N.S., Godwin A.K., Shiekhattar R.
Mol. Cell 12:1087-1099(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRCC3.
[29]"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.
[30]"BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M transition."
Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A., Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.
J. Biol. Chem. 279:19643-19648(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AURKA, FUNCTION, MUTAGENESIS OF SER-308, PHOSPHORYLATION AT SER-308.
[31]"Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response."
Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., Legerski R.J.
Mol. Cell. Biol. 24:9207-9220(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLRE1C.
[32]"Human claspin works with BRCA1 to both positively and negatively regulate cell proliferation."
Lin S.-Y., Li K., Stewart G.S., Elledge S.J.
Proc. Natl. Acad. Sci. U.S.A. 101:6484-6489(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLSPN.
[33]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP."
Yu X., Fu S., Lai M., Baer R., Chen J.
Genes Dev. 20:1721-1726(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RBBP8, MUTAGENESIS OF ILE-26.
[35]"BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase."
Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F., Billaud M., Lenoir G.M., Venezia N.D.
J. Biol. Chem. 281:3172-3181(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACACA.
[36]"ACCA phosphopeptide recognition by the BRCT repeats of BRCA1."
Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.
J. Mol. Biol. 359:973-982(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACACA.
[37]"Aurora-A kinase regulates breast cancer associated gene 1 inhibition of centrosome-dependent microtubule nucleation."
Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.
Cancer Res. 67:11186-11194(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY AURKA, ENZYME REGULATION.
[38]"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: INTERACTION WITH FAM175A.
[39]"CCDC98 targets BRCA1 to DNA damage sites."
Liu Z., Wu J., Yu X.
Nat. Struct. Mol. Biol. 14:716-720(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FAM175A.
[40]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[41]"Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response."
Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S., Elledge S.J.
Science 316:1194-1198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A.
[42]"Germline BRCA1 mutations predispose to pancreatic adenocarcinoma."
Al-Sukhni W., Rothenmund H., Borgida A.E., Zogopoulos G., O'Shea A.M., Pollett A., Gallinger S.
Hum. Genet. 124:271-278(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PNCA4.
[43]"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-395; SER-398; SER-753; SER-1211; SER-1217 AND SER-1218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[44]"MERIT40 facilitates BRCA1 localization and DNA damage repair."
Feng L., Huang J., Chen J.
Genes Dev. 23:719-728(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX.
[45]"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.
[46]"MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks."
Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y., Greenberg R.A.
Genes Dev. 23:740-754(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
[47]"PALB2 is an integral component of the BRCA complex required for homologous recombination repair."
Sy S.M., Huen M.S., Chen J.
Proc. Natl. Acad. Sci. U.S.A. 106:7155-7160(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH PALB2, IDENTIFICATION IN A BRCA COMPLEX WITH BRCA1 AND PALB2, CHARACTERIZATION OF VARIANT OVARIAN CANCER 1411-THR.
[48]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[49]"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 BARD1 AND UBXN1, UBIQUITINATION, MUTAGENESIS OF ILE-26.
[50]"The CHK2-BRCA1 tumour suppressor pathway ensures chromosomal stability in human somatic cells."
Stolz A., Ertych N., Kienitz A., Vogel C., Schneider V., Fritz B., Jacob R., Dittmar G., Weichert W., Petersen I., Bastians H.
Nat. Cell Biol. 12:492-499(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CHROMOSOMAL STABILITY, PHOSPHORYLATION AT SER-988 BY CHEK2.
[51]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-423; SER-694; SER-1328; SER-1336 AND SER-1342, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[52]"Protein phosphatase 5 is necessary for ATR-mediated DNA repair."
Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y., Jun J.Y., You H.J.
Biochem. Biophys. Res. Commun. 404:476-481(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1524, SUBCELLULAR LOCATION.
[53]"KIAA0101 interacts with BRCA1 and regulates centrosome number."
Kais Z., Barsky S.H., Mathsyaraja H., Zha A., Ransburgh D.J., He G., Pilarski R.T., Shapiro C.L., Huang K., Parvin J.D.
Mol. Cancer Res. 9:1091-1099(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIAA0101.
[54]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-1218; SER-1336 AND SER-1342, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[55]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[56]"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 1-110 IN COMPLEX WITH ZINC IONS AND BARD1, SUBUNIT.
[57]"Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1."
Williams R.S., Green R., Glover J.N.
Nat. Struct. Biol. 8:838-842(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1646-1859, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
[58]"Structural consequences of a cancer-causing BRCA1-BRCT missense mutation."
Williams R.S., Glover J.N.
J. Biol. Chem. 278:2630-2635(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1646-1859 OF VARIANT BC ARG-1775, CHARACTERIZATION OF VARIANT BC ARG-1775, CIRCULAR DICHROISM.
[59]"Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1."
Gaiser O.J., Ball L.J., Schmieder P., Leitner D., Strauss H., Wahl M., Kuhne R., Oschkinat H., Heinemann U.
Biochemistry 43:15983-15995(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1755-1863.
[60]"Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer."
Clapperton J.A., Manke I.A., Lowery D.M., Ho T., Haire L.F., Yaffe M.B., Smerdon S.J.
Nat. Struct. Mol. Biol. 11:512-518(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1649-1859 IN COMPLEX WITH WITH PHOSPHORYLATED BRIP1 PEPTIDE, MUTAGENESIS OF SER-1655; LYS-1702 AND GLY-1738, CHARACTERIZATION OF VARIANT OVARIAN CANCER ARG-1749, CHARACTERIZATION OF VARIANT BC ARG-1775, SUBCELLULAR LOCATION, INTERACTION WITH PHOSPHORYLATED BRIP1.
[61]"Structural basis for cell cycle checkpoint control by the BRCA1-CtIP complex."
Varma A.K., Brown R.S., Birrane G., Ladias J.A.
Biochemistry 44:10941-10946(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH PHOSPHORYLATED RBBP8 PEPTIDE, SUBUNIT.
[62]"Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1."
Shen Y., Tong L.
Biochemistry 47:5767-5773(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH PHOSPHORYLATED ACACA PEPTIDE, SUBUNIT.
[63]"Pathogenicity of the BRCA1 missense variant M1775K is determined by the disruption of the BRCT phosphopeptide-binding pocket: a multi-modal approach."
Tischkowitz M., Hamel N., Carvalho M.A., Birrane G., Soni A., van Beers E.H., Joosse S.A., Wong N., Novak D., Quenneville L.A., Grist S.A., Nederlof P.M., Goldgar D.E., Tavtigian S.V., Monteiro A.N., Ladias J.A., Foulkes W.D.
Eur. J. Hum. Genet. 16:820-832(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1649-1859 OF VARIANT BC LYS-1775, VARIANT BC LYS-1775, CHARACTERIZATION OF VARIANT BC LYS-1775.
[64]"Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1."
Campbell S.J., Edwards R.A., Glover J.N.
Structure 18:167-176(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1646-1859 IN COMPLEX WITH PHOSPHORYLATED PEPTIDES, DOMAIN.
[65]"Mutations and polymorphisms in the familial early-onset breast cancer (BRCA1) gene."
Couch F.J., Weber B.L.
Hum. Mutat. 8:8-18(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[66]"BRCA1 mutations in primary breast and ovarian carcinomas."
Futreal P.A., Liu Q., Shattuck-Eidens D., Cochran C., Harshman K., Tavtigian S., Bennett L.M., Haugen-Strano A., Swensen J., Miki Y., Eddington K., McClure M., Frye C., Weaver-Felhaus J., Ding W., Gholami Z., Soederkvist P., Terry L. expand/collapse author list , Jhanwar S., Berchuk A., Iglehart J.D., Marks J., Ballinger D.G., Barrett J.C., Skolnick M.H., Kamb A., Wiseman R.
Science 266:120-122(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BC ARG-1775, VARIANTS LEU-1637 AND GLU-1708.
[67]"Mutations in the BRCA1 gene in families with early-onset breast and ovarian cancer."
Castilla L.H., Couch F.J., Erdos M.R., Hoskins K.F., Calzone K., Garber J.E., Boyd J., Lubin M.B., Deshano M.L., Brody L.C., Collins F.S., Weber B.L.
Nat. Genet. 8:387-391(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BC GLY-64, VARIANTS ALA-772; ASN-1040 AND GLY-1443.
[68]"Confirmation of BRCA1 by analysis of germline mutations linked to breast and ovarian cancer in ten families."
Friedman L.S., Ostermeyer E.A., Szabo C.I., Dowd P., Lynch E.D., Rowell S.E., King M.-C.
Nat. Genet. 8:399-404(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BC GLY-61, VARIANTS ARG-356; GLY-1038; ASN-1040; ARG-1183 AND GLY-1613.
[69]"A high incidence of BRCA1 mutations in 20 breast-ovarian cancer families."
Serova O., Montagna M., Torchard D., Narod S.A., Tonin P., Sylla B., Lynch H.T., Feunteun J., Lenoir G.M.
Am. J. Hum. Genet. 58:42-51(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BC GLY-61.
[70]"BRCA1 R841W: a strong candidate for a common mutation with moderate phenotype."
Barker D.F., Almeida E.F.A., Casey G., Fain P.R., Liao S.-Y., Masunaka I., Noble B., Kurosaki T., Anton-Culver H.
Genet. Epidemiol. 13:595-604(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BROVCA1 TRP-841.
[71]"Comparison of BRCA1 polymorphisms, rare sequence variants and/or missense mutations in unaffected and breast/ovarian cancer populations."
Durocher F., Shattuck-Eidens D., McClure M., Labrie F., Skolnick M.H., Goldgar D.E., Simard J.
Hum. Mol. Genet. 5:835-842(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BC AND BROVCA1.
[72]"Mutations in the BRCA1 gene in Japanese breast cancer patients."
Katagiri T., Emi M., Ito I., Kobayashi K., Yoshimoto M., Iwase T., Kasumi F., Miki Y., Skolnick M.H., Nakamura Y.
Hum. Mutat. 7:334-339(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BC MET-271 AND SER-1150.
[73]"A high proportion of mutations in the BRCA1 gene in German breast/ovarian cancer families with clustering of mutations in the 3' third of the gene."
Dong J., Chang-Claude J., Wu Y., Schumacher V., Debatin I., Tonin P., Royer-Pokora B.
Hum. Genet. 103:154-161(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BC GLY-61, VARIANTS ARG-239; TRP-841 AND ILE-1512.
[74]"Constant denaturant gel electrophoresis (CDGE) in BRCA1 mutation screening."
Andersen T.I., Eiken H.G., Couch F., Kaada G., Skrede M., Johnsen H., Aloysius T.A., Tveit K.M., Tranebjaerg L., Doerum A., Moeller P., Weber B.L., Boerresen-Dale A.-L.
Hum. Mutat. 11:166-174(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BC GLY-64, VARIANTS ALA-772; GLU-820; ASN-1040; GLY-1443; ILE-1512; LEU-1637 AND ILE-1652.
[75]"High proportion of missense mutations of the BRCA1 and BRCA2 genes in Japanese breast cancer families."
Katagiri T., Kasumi F., Yoshimoto M., Nomizu T., Asaishi K., Abe R., Tsuchiya A., Sugano M., Takai S., Yoneda M., Fukutomi T., Nanba K., Makita M., Okazaki H., Hirata K., Okazaki M., Furutsuma Y., Morishita Y. expand/collapse author list , Iino Y., Karino T., Ayabe H., Hara S., Kajiwara T., Houga S., Shimizu T., Toda M., Yamazaki Y., Uchida T., Kunitomo K., Sonoo H., Kurebayashi J., Shimotsuma K., Nakamura Y., Miki Y.
J. Hum. Genet. 43:42-48(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BC SER-22; LEU-461; ASP-465; VAL-552; SER-892; ASP-960; ILE-1025 AND ALA-1047.
[76]"The contribution of germline BRCA1 and BRCA2 mutations to familial ovarian cancer: no evidence for other ovarian cancer-susceptibility genes."
Gayther S.A., Russell P., Harrington P., Antoniou A.C., Easton D.F., Ponder B.A.J.
Am. J. Hum. Genet. 65:1021-1029(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OVARIAN CANCER ARG-1749.
[77]"Molecular characterization of germline mutations in the BRCA1 and BRCA2 genes from breast cancer families in Taiwan."
Li S.S.-L., Tseng H.-M., Yang T.-P., Liu C.-H., Teng S.-J., Huang H.-W., Chen L.-M., Kao H.-W., Chen J.H., Tseng J.-N., Chen A., Hou M.-F., Huang T.-J., Chang H.-T., Mok K.-T., Tsai J.-H.
Hum. Genet. 104:201-204(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BC SER-346, VARIANTS LEU-871; GLY-1038; ARG-1183 AND GLY-1613.
[78]"Germline BRCA1 alterations in a population-based series of ovarian cancer cases."
Janezic S.A., Ziogas A., Krumroy L.M., Krasner M., Plummer S.J., Cohen P., Gildea M., Barker D., Haile R., Casey G., Anton-Culver H.
Hum. Mol. Genet. 8:889-897(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OVARIAN CANCER, VARIANTS.
[79]"Characterization of common BRCA1 and BRCA2 variants."
Deffenbaugh A.M., Frank T.S., Hoffman M., Cannon-Albright L., Neuhausen S.L.
Genet. Test. 6:119-121(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLY-1347; ILE-1512 AND ILE-1652.
[80]"BRCA1 and BRCA2 sequence variants in Chinese breast cancer families."
Zhi X., Szabo C., Chopin S., Suter N., Wang Q.-S., Ostrander E.A., Sinilnikova O.M., Lenoir G.M., Goldgar D., Shi Y.-R.
Hum. Mutat. 20:474-474(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-656; LEU-871 AND GLY-1613.
[81]"BRCA1 and BRCA2 mutation analysis of early-onset and familial breast cancer cases in Mexico."
Ruiz-Flores P., Sinilnikova O.M., Badzioch M., Calderon-Garciduenas A.L., Chopin S., Fabrice O., Gonzalez-Guerrero J.F., Szabo C., Lenoir G., Goldgar D.E., Barrera-Saldana H.A.
Hum. Mutat. 20:474-475(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BC TYR-749.
[82]"Twenty-three novel BRCA1 and BRCA2 sequence alterations in breast and/or ovarian cancer families in Southern Germany."
Meyer P., Voigtlaender T., Bartram C.R., Klaes R.
Hum. Mutat. 22:259-259(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BC GLY-61; LYS-71; GLN-866; TYR-888; ILE-1139; GLY-1210 AND PRO-1297, VARIANTS BROVCA1 TYR-835 AND PRO-1786.
[83]"BRCA1 and BRCA2 germline mutation spectrum and frequencies in Belgian breast/ovarian cancer families."
Claes K., Poppe B., Coene I., De Paepe A., Messiaen L.
Br. J. Cancer 90:1244-1251(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASN-693; ASN-1040; ALA-1060 AND MET-1665.
[84]"One in 10 ovarian cancer patients carry germ line BRCA1 or BRCA2 mutations: results of a prospective study in Southern Sweden."
Malander S., Ridderheim M., Masbaeck A., Loman N., Kristoffersson U., Olsson H., Nilbert M., Borg A.
Eur. J. Cancer 40:422-428(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OVARIAN CANCER GLY-61; THR-1411; ARG-1697 AND TRP-1699.
[85]"Novel germline mutations in the BRCA1 and BRCA2 genes in Indian breast and breast-ovarian cancer families."
Valarmathi M.T., Sawhney M., Deo S.S.V., Shukla N.K., Das S.N.
Hum. Mutat. 23:205-205(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BC/BROVCA1 LYS-10; LYS-23; ILE-1187; HIS-1200 AND TYR-1217, VARIANTS BC ILE-1204 AND ASN-1207, VARIANTS BROVCA1 LEU-1226 AND GLY-1243, VARIANT ARG-1183.
[86]"BRCA1 and BRCA2 germline mutations in Korean patients with sporadic breast cancer."
Seo J.H., Cho D.-Y., Ahn S.-H., Yoon K.-S., Kang C.-S., Cho H.M., Lee H.S., Choe J.J., Choi C.W., Kim B.S., Shin S.W., Kim Y.H., Kim J.S., Son G.-S., Lee J.-B., Koo B.H.
Hum. Mutat. 24:350-350(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-856; LEU-871; GLY-1038; ARG-1183; THR-1628; GLN-1690 AND GLY-1713.
[87]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-30; PHE-758 AND CYS-778.
[88]"A systematic genetic assessment of 1,433 sequence variants of unknown clinical significance in the BRCA1 and BRCA2 breast cancer-predisposition genes."
Easton D.F., Deffenbaugh A.M., Pruss D., Frye C., Wenstrup R.J., Allen-Brady K., Tavtigian S.V., Monteiro A.N.A., Iversen E.S., Couch F.J., Goldgar D.E.
Am. J. Hum. Genet. 81:873-883(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-18; MET-1495; GLY-1623; ILE-1685; ALA-1685; ARG-1689; TRP-1699; GLU-1706; GLU-1708; ARG-1715; ARG-1738; PRO-1764; SER-1766 AND VAL-1788.
[89]"Detection of splicing aberrations caused by BRCA1 and BRCA2 sequence variants encoding missense substitutions: implications for prediction of pathogenicity."
Walker L.C., Whiley P.J., Couch F.J., Farrugia D.J., Healey S., Eccles D.M., Lin F., Butler S.A., Goff S.A., Thompson B.A., Lakhani S.R., Da Silva L.M., Tavtigian S.V., Goldgar D.E., Brown M.A., Spurdle A.B.
Hum. Mutat. 31:E1484-E1505(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS GLY-1623 AND ILE-1685.
[90]"A high-throughput functional complementation assay for classification of BRCA1 missense variants."
Bouwman P., van der Gulden H., van der Heijden I., Drost R., Klijn C.N., Prasetyanti P., Pieterse M., Wientjens E., Seibler J., Hogervorst F.B., Jonkers J.
Cancer Discov. 3:1142-1155(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS BC PHE-4; THR-18; GLN-45; GLY-61; GLY-64; TYR-67; LYS-132; HIS-142; PHE-147; PRO-165; TRP-170; TYR-186; ILE-191; MET-231; VAL-245; VAL-246; LEU-271; PHE-668; ASN-695; LEU-798; TYR-810; LYS-826; GLN-841; HIS-856; ASN-1101; ASN-1140; GLY-1140; LYS-1214; LYS-1236; SER-1267; VAL-1282; SER-1297 DEL; ARG-1301; LYS-1346; ILE-1378; VAL-1400; PRO-1407; THR-1411; GLY-1443; GLY-1448; CYS-1486; MET-1534; PRO-1589; THR-1628; PRO-1651; PHE-1651; PHE-1655; ARG-1686; GLN-1686; VAL-1688 DEL; ILE-1691; TRP-1699; GLN-1699; GLU-1706; ALA-1706; GLU-1708; CYS-1718; ALA-1720; LYS-1735; ALA-1736; GLY-1739; VAL-1739; GLN-1746; THR-1753; PRO-1764; SER-1767; VAL-1770; CYS-1782; THR-1789; ASP-1794; ASP-1804; ARG-1812; ARG-1837 AND LEU-1862, VARIANTS CYS-105; CYS-866; ALA-1060; LYS-1250 AND ILE-1652.
+Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

BRCA1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14680 mRNA. Translation: AAA73985.1.
L78833 Genomic DNA. Translation: AAC37594.1.
U64805 mRNA. Translation: AAC00049.1.
AF005068 mRNA. Translation: AAB61673.1. Sequence problems.
DQ190450 Genomic DNA. Translation: ABA29208.1.
DQ190451 Genomic DNA. Translation: ABA29211.1.
DQ190452 Genomic DNA. Translation: ABA29214.1.
DQ190453 Genomic DNA. Translation: ABA29217.1.
DQ190454 Genomic DNA. Translation: ABA29220.1.
DQ190455 Genomic DNA. Translation: ABA29223.1.
DQ190456 Genomic DNA. Translation: ABA29226.1.
AY273801 Genomic DNA. Translation: AAP12647.1.
AC060780 Genomic DNA. No translation available.
AC135721 Genomic DNA. No translation available.
BC072418 mRNA. Translation: AAH72418.1.
CCDSCCDS11453.1. [P38398-1]
CCDS11454.2. [P38398-3]
CCDS11455.2. [P38398-6]
PIRA58881.
RefSeqNP_009225.1. NM_007294.3. [P38398-1]
NP_009228.2. NM_007297.3.
NP_009229.2. NM_007298.3. [P38398-3]
NP_009230.2. NM_007299.3. [P38398-6]
NP_009231.2. NM_007300.3.
XP_006722092.1. XM_006722029.1. [P38398-1]
XP_006722093.1. XM_006722030.1. [P38398-1]
XP_006722094.1. XM_006722031.1. [P38398-1]
XP_006722103.1. XM_006722040.1. [P38398-3]
UniGeneHs.194143.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JM7NMR-A1-110[»]
1JNXX-ray2.50X1646-1859[»]
1N5OX-ray2.80X1646-1859[»]
1OQANMR-A1755-1863[»]
1T15X-ray1.85A1646-1859[»]
1T29X-ray2.30A1646-1859[»]
1T2UX-ray2.80A1646-1859[»]
1T2VX-ray3.30A/B/C/D/E1646-1859[»]
1Y98X-ray2.50A1646-1859[»]
2INGX-ray3.60X1649-1859[»]
3COJX-ray3.21A/B/C/D/E/F/G/X1646-1859[»]
3K0HX-ray2.70A1646-1859[»]
3K0KX-ray2.70A1646-1859[»]
3K15X-ray2.80A1646-1859[»]
3K16X-ray3.00A1646-1859[»]
3PXAX-ray2.55A1646-1859[»]
3PXBX-ray2.50A1646-1859[»]
3PXCX-ray2.80X1646-1859[»]
3PXDX-ray2.80A1646-1859[»]
3PXEX-ray2.85A/B/C/D1646-1859[»]
4IFIX-ray2.20A1646-1859[»]
4IGKX-ray1.75A/B1646-1859[»]
DisProtDP00238.
ProteinModelPortalP38398.
SMRP38398. Positions 1-103, 1649-1859.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107140. 411 interactions.
DIPDIP-5971N.
IntActP38398. 72 interactions.
MINTMINT-90433.
STRING9606.ENSP00000350283.

Chemistry

BindingDBP38398.
ChEMBLCHEMBL5990.

PTM databases

PhosphoSiteP38398.

Polymorphism databases

DMDM728984.

Proteomic databases

MaxQBP38398.
PaxDbP38398.
PRIDEP38398.

Protocols and materials databases

DNASU672.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000352993; ENSP00000312236; ENSG00000012048. [P38398-5]
ENST00000357654; ENSP00000350283; ENSG00000012048. [P38398-1]
ENST00000461221; ENSP00000418548; ENSG00000012048. [P38398-2]
ENST00000461798; ENSP00000417988; ENSG00000012048. [P38398-2]
ENST00000468300; ENSP00000417148; ENSG00000012048. [P38398-6]
ENST00000491747; ENSP00000420705; ENSG00000012048. [P38398-3]
GeneID672.
KEGGhsa:672.
UCSCuc002icp.4. human. [P38398-2]
uc002icq.3. human. [P38398-1]
uc002icu.3. human. [P38398-6]
uc010whq.1. human. [P38398-3]

Organism-specific databases

CTD672.
GeneCardsGC17M041197.
GeneReviewsBRCA1.
HGNCHGNC:1100. BRCA1.
HPACAB001946.
CAB018369.
HPA034966.
MIM113705. gene.
114480. phenotype.
167000. phenotype.
604370. phenotype.
614320. phenotype.
neXtProtNX_P38398.
Orphanet1333. Familial pancreatic carcinoma.
1331. Familial prostate cancer.
145. Hereditary breast and ovarian cancer syndrome.
227535. Hereditary breast cancer.
213524. Hereditary site-specific ovarian cancer syndrome.
168829. Primary peritoneal carcinoma.
PharmGKBPA25411.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG274496.
HOGENOMHOG000230969.
HOVERGENHBG050730.
InParanoidP38398.
KOK10605.
OrthoDBEOG79CXXK.
PhylomeDBP38398.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_216. DNA Repair.
SignaLinkP38398.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP38398.
BgeeP38398.
CleanExHS_BRCA1.
GenevestigatorP38398.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.
InterProIPR011364. BRCA1.
IPR025994. BRCA1_serine_dom.
IPR001357. BRCT_dom.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERPTHR13763. PTHR13763. 1 hit.
PfamPF00533. BRCT. 2 hits.
PF12820. BRCT_assoc. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
PIRSFPIRSF001734. BRCA1. 1 hit.
PRINTSPR00493. BRSTCANCERI.
SMARTSM00292. BRCT. 2 hits.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF52113. SSF52113. 2 hits.
PROSITEPS50172. BRCT. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBRCA1. human.
EvolutionaryTraceP38398.
GeneWikiBRCA1.
GenomeRNAi672.
NextBio2752.
PMAP-CutDBP38398.
PROP38398.
SOURCESearch...

Entry information

Entry nameBRCA1_HUMAN
AccessionPrimary (citable) accession number: P38398
Secondary accession number(s): O15129 expand/collapse secondary AC list , Q3LRJ0, Q3LRJ6, Q6IN79, Q7KYU9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 194 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 17

Human chromosome 17: entries, gene names and cross-references to MIM