P38398 (BRCA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Breast cancer type 1 susceptibility protein
EC=6.3.2.-

Alternative name(s):
RING finger protein 53

Gene names

Name:	BRCA1
Synonyms:	RNF53

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	1863 AA.
Sequence status	Complete.
Protein existence	Evidence 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 and COBRA1. Interacts (via BRCT domains) with BRIP1 (phosphorylated form). Interacts with FANCD2 (ubiquitinated form). Interacts with BAP1. Interacts with DCLRE1C and CLSPN. Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts with CHEK1 and CHEK2. Interacts with BRCC3. Interacts (via the BRCT domains) with ACACA (phosphorylated form); the interaction prevents dephosphorylation of ACACA. Interacts with AURKA. Interacts with UBXN1. Part of a trimeric 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. Interacts with KIAA0101/PAF15. 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.52 Ref.54 Ref.58 Ref.59 Ref.60
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.58 Isoform 3: Cytoplasm Ref.3 Ref.10 Ref.11 Ref.41 Ref.58. Isoform 5: Cytoplasm Ref.3 Ref.10 Ref.11 Ref.41 Ref.58.
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.62 The RING-type zinc finger domain interacts with BAP1. Ref.62
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 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.17 Ref.56 Ref.58 Ref.61 Ref.64 Ref.65 Ref.66 Ref.67 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Ref.75 Ref.79 Ref.80 Ref.83 Familial breast-ovarian cancer 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.68 Ref.69 Ref.80 Ref.83 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.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA recombination DNA repair Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Ubl conjugation pathway
Cellular component	Chromosome Cytoplasm Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Disease	Disease mutation Tumor suppressor
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Traceable author statement PubMed 10918303. Source: UniProtKB 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 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 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-dependent 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 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 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 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 III promoter Traceable author statement PubMed 10918303. Source: UniProtKB response to estrogen stimulus 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_component	BRCA1-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 gamma-tubulin ring complex Non-traceable author statement PubMed 12214252. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay PubMed 21282464. Source: BHF-UCL ribonucleoprotein complex Inferred from direct assay PubMed 18809582. Source: MGI ruffle Inferred from direct assay PubMed 21282464. Source: BHF-UCL
Molecular_function	RNA binding Inferred from direct assay PubMed 12419249. Source: MGI androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB 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 activity Inferred from direct assay Ref.26PubMed 19117993Ref.49. Source: UniProtKB zinc ion binding Traceable author statement PubMed 8944023. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACACA	Q13085	2	EBI-349905,EBI-717681
BAP1	Q92560	3	EBI-349905,EBI-1791447
BARD1	Q99728	8	EBI-349905,EBI-473181
BRAP	Q7Z569	3	EBI-349905,EBI-349900
BRIP1	Q9BX63	3	EBI-349905,EBI-3509650
CCND1	P24385	3	EBI-349905,EBI-375001
CCNE1	P24864	2	EBI-349905,EBI-519526
CHEK1	O14757	3	EBI-349905,EBI-974488
ESR1	P03372	12	EBI-349905,EBI-78473
FAM175A	Q6UWZ7	10	EBI-349905,EBI-1263451
GTF2I	P78347	5	EBI-349905,EBI-359622
HSPD1	P10809	2	EBI-349905,EBI-352528
IFI16	Q16666	9	EBI-349905,EBI-2867186
KPNA2	P52292	3	EBI-349905,EBI-349938
NELFB	Q8WX92	5	EBI-349905,EBI-347721
PPP1CA	P62136	2	EBI-349905,EBI-357253
PPP1CB	P62140	3	EBI-349905,EBI-352350
PPP1CC	P36873	2	EBI-349905,EBI-356283
RBBP8	Q99708	9	EBI-349905,EBI-745715
TRRAP	Q9Y4A5	8	EBI-349905,EBI-399128
UIMC1	Q96RL1	9	EBI-349905,EBI-725300
ZCCHC8	Q6NZY4	2	EBI-349905,EBI-1263058
ZNF350	Q9GZX5	3	EBI-349905,EBI-396421

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:
     71-71: R → M

Isoform 3 (identifier: P38398-3)

Also known as: Delta11b;

The sequence of this isoform differs from the canonical sequence as follows:
     264-1366: 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1863

1863

Breast cancer type 1 susceptibility protein

PRO_0000055830

Regions

Domain

1642 – 1736

95

BRCT 1

Domain

1756 – 1855

100

BRCT 2

Zinc finger

24 – 65

42

RING-type

Region

1397 – 1424

28

Interaction with PALB2

Compositional bias

651 – 654

4

Poly-Lys

Amino acid modifications

Modified residue

114

1

Phosphoserine Ref.51 Ref.53

Modified residue

308

1

Phosphoserine; by AURKA Ref.30

Modified residue

395

1

Phosphoserine Ref.43 Ref.48

Modified residue

398

1

Phosphoserine Ref.43 Ref.48

Modified residue

423

1

Phosphoserine Ref.51

Modified residue

694

1

Phosphoserine Ref.51

Modified residue

753

1

Phosphoserine Ref.43

Modified residue

988

1

Phosphoserine; by CHEK2 Ref.16 Ref.50

Modified residue

1143

1

Phosphoserine; by ATR; in vitro Ref.15

Modified residue

1211

1

Phosphoserine Ref.43

Modified residue

1217

1

Phosphoserine Ref.43

Modified residue

1218

1

Phosphoserine Ref.43 Ref.53

Modified residue

1280

1

Phosphoserine; by ATR; in vitro Ref.15

Modified residue

1328

1

Phosphoserine Ref.51

Modified residue

1336

1

Phosphoserine Ref.33 Ref.51 Ref.53

Modified residue

1342

1

Phosphoserine Ref.51 Ref.53

Modified residue

1387

1

Phosphoserine; by ATM and ATR Ref.15

Modified residue

1394

1

Phosphothreonine; by ATR; in vitro Ref.15

Modified residue

1423

1

Phosphoserine; by ATM and ATR Ref.15

Modified residue

1457

1

Phosphoserine; by ATR; in vitro Ref.15

Modified residue

1524

1

Phosphoserine; by ATM

Natural variations

Alternative sequence

1 – 17

17

Missing in isoform 4.

VSP_035396

Alternative sequence

71

1

R → M in isoform 2.

VSP_035397

Alternative sequence

224 – 1365

1142

Missing in isoform 5.

VSP_035398

Alternative sequence

264 – 1366

1103

Missing in isoform 3 and isoform 6.

VSP_035399

Alternative sequence

1453

1

Missing in isoform 6.

VSP_043797

Alternative sequence

1778 – 1863

86

DQLEW…PHSHY → GCPPNCGCAARCLDRGQWLP CNWADV in isoform 6.

VSP_043798

Natural variant

10

1

E → K in BC and BROVCA1. Ref.83

VAR_020679

Natural variant

11

1

V → A Unclassified.

VAR_007754

Natural variant

18

1

M → T in BC; unknown pathological significance. Ref.86

VAR_063899

Natural variant

21

1

I → V Unclassified.

VAR_007755

Natural variant

22

1

L → S in BC. Ref.73

VAR_007756

Natural variant

23

1

E → K in BC and BROVCA1. Ref.83

VAR_020680

Natural variant

30

1

L → F in a breast cancer sample; somatic mutation. Ref.85

VAR_035947

Natural variant

61

1

C → G in BC and ovarian cancer; no interaction with BAP1. Ref.11 Ref.66 Ref.67 Ref.71 Ref.80 Ref.82
Corresponds to variant rs28897672 [ dbSNP | Ensembl ].

VAR_007757

Natural variant

64

1

C → G in BC; no interaction with BAP1. Ref.11 Ref.65 Ref.72

VAR_007758

Natural variant

64

1

C → Y Unclassified.
Corresponds to variant rs55851803 [ dbSNP | Ensembl ].

VAR_007759

Natural variant

71

1

R → K in BC; unknown pathological significance. Ref.80

VAR_020681

Natural variant

153

1

S → R.
Corresponds to variant rs28897674 [ dbSNP | Ensembl ].

VAR_052077

Natural variant

227

1

E → K in ovarian cancer; unknown pathological significance.

VAR_008759

Natural variant

239

1

H → R. Ref.3 Ref.71

VAR_007760

Natural variant

271

1

V → M in BC. Ref.70

VAR_007761

Natural variant

275

1

G → S. Ref.6
Corresponds to variant rs8176153 [ dbSNP | Ensembl ].

VAR_019944

Natural variant

346

1

P → S in BC; unknown pathological significance. Ref.75

VAR_008760

Natural variant

356

1

Q → R Common polymorphism. Ref.5 Ref.6 Ref.66
Corresponds to variant rs1799950 [ dbSNP | Ensembl ].

VAR_007762

Natural variant

369

1

Missing in BC.

VAR_007763

Natural variant

379

1

I → M Unclassified.
Corresponds to variant rs56128296 [ dbSNP | Ensembl ].

VAR_007764

Natural variant

461

1

F → L in BC. Ref.73
Corresponds to variant rs56046357 [ dbSNP | Ensembl ].

VAR_007765

Natural variant

465

1

Y → D in BC. Ref.73

VAR_007766

Natural variant

507

1

R → I Unclassified.

VAR_007767

Natural variant

552

1

G → V in BC. Ref.73

VAR_007768

Natural variant

656

1

N → I. Ref.78

VAR_020682

Natural variant

693

1

D → N Rare polymorphism. Ref.6 Ref.81
Corresponds to variant rs4986850 [ dbSNP | Ensembl ].

VAR_007769

Natural variant

723

1

N → D.
Corresponds to variant rs4986845 [ dbSNP | Ensembl ].

VAR_020110

Natural variant

749

1

D → Y in BC. Ref.79

VAR_020683

Natural variant

758

1

L → F in a breast cancer sample; somatic mutation. Ref.85

VAR_035948

Natural variant

772

1

V → A Rare polymorphism. Ref.65 Ref.72

VAR_007770

Natural variant

778

1

G → C in a breast cancer sample; somatic mutation. Ref.85

VAR_035949

Natural variant

820

1

K → E Rare polymorphism. Ref.72

VAR_007771

Natural variant

826

1

T → K in BC.

VAR_007772

Natural variant

835

1

H → Y in BROVCA1; unknown pathological significance. Ref.80

VAR_020684

Natural variant

841

1

R → W in BROVCA1; unknown pathological significance. Ref.68 Ref.71
Corresponds to variant rs1800709 [ dbSNP | Ensembl ].

VAR_007773

Natural variant

856

1

Y → H in a patient with sporadic breast cancer; unknown pathological significance. Ref.84

VAR_020685

Natural variant

866

1

R → Q in BC; unknown pathological significance. Ref.80

VAR_020686

Natural variant

871

1

P → L Common polymorphism. Ref.6 Ref.75 Ref.78 Ref.84
Corresponds to variant rs799917 [ dbSNP | Ensembl ].

VAR_007774

Natural variant

888

1

H → Y in BC; unknown pathological significance. Ref.80

VAR_020687

Natural variant

892

1

L → S in BC. Ref.73

VAR_007775

Natural variant

925

1

I → L.
Corresponds to variant rs4986847 [ dbSNP | Ensembl ].

VAR_021913

Natural variant

960

1

G → D in BC. Ref.73

VAR_007776

Natural variant

989

1

F → S.
Corresponds to variant rs4986848 [ dbSNP | Ensembl ].

VAR_020111

Natural variant

1008

1

M → I Common polymorphism.
Corresponds to variant rs1800704 [ dbSNP | Ensembl ].

VAR_007777

Natural variant

1025

1

T → I in BC. Ref.73

VAR_007778

Natural variant

1038

1

E → G Common polymorphism. Ref.6 Ref.66 Ref.75 Ref.84
Corresponds to variant rs16941 [ dbSNP | Ensembl ].

VAR_007779

Natural variant

1040

1

S → N Rare polymorphism. Ref.6 Ref.65 Ref.66 Ref.72 Ref.81
Corresponds to variant rs4986852 [ dbSNP | Ensembl ].

VAR_007780

Natural variant

1047

1

V → A in BC. Ref.73

VAR_007781

Natural variant

1060

1

E → A. Ref.81

VAR_020688

Natural variant

1139

1

S → I in BC; unknown pathological significance. Ref.80

VAR_020689

Natural variant

1140

1

S → G. Ref.6
Corresponds to variant rs2227945 [ dbSNP | Ensembl ].

VAR_019945

Natural variant

1150

1

P → S in BC. Ref.70

VAR_007782

Natural variant

1183

1

K → R Common polymorphism. Ref.6 Ref.66 Ref.75 Ref.83 Ref.84
Corresponds to variant rs16942 [ dbSNP | Ensembl ].

VAR_007783

Natural variant

1187

1

S → I in BC and BROVCA1. Ref.83

VAR_020690

Natural variant

1200

1

Q → H in BC and BROVCA1. Ref.83

VAR_020691

Natural variant

1204

1

R → I in BC. Ref.83

VAR_020692

Natural variant

1207

1

K → N in BC. Ref.83

VAR_020693

Natural variant

1210

1

E → G in BC; unknown pathological significance. Ref.80

VAR_020694

Natural variant

1217

1

S → Y in BC and BROVCA1. Ref.83

VAR_020695

Natural variant

1219

1

E → D Unclassified.

VAR_007784

Natural variant

1226

1

F → L in BROVCA1. Ref.83

VAR_020696

Natural variant

1236

1

N → K.
Corresponds to variant rs28897687 [ dbSNP | Ensembl ].

VAR_052078

Natural variant

1243

1

R → G in BROVCA1. Ref.83

VAR_020697

Natural variant

1250

1

E → K.
Corresponds to variant rs28897686 [ dbSNP | Ensembl ].

VAR_052079

Natural variant

1297

1

S → P in BC; unknown pathological significance. Ref.80

VAR_020698

Natural variant

1347

1

R → G. Ref.77

VAR_007785

Natural variant

1406

1

K → N Polymorphism.
Corresponds to variant rs1800707 [ dbSNP | Ensembl ].

VAR_008761

Natural variant

1411

1

M → T in ovarian cancer; unknown pathological significance; decreased interaction with PALB2. Ref.82

VAR_020699

Natural variant

1431

1

S → P.

VAR_007786

Natural variant

1443

1

R → G Rare polymorphism. Ref.65 Ref.72

VAR_007787

Natural variant

1443

1

R → Q.
Corresponds to variant rs4986849 [ dbSNP | Ensembl ].

VAR_020112

Natural variant

1495

1

R → M in BC; unknown pathological significance. Ref.86

VAR_063900

Natural variant

1512

1

S → I. Ref.71 Ref.72 Ref.77
Corresponds to variant rs1800744 [ dbSNP | Ensembl ].

VAR_007788

Natural variant

1561

1

T → I Unclassified.

VAR_007789

Natural variant

1606

1

K → E Unclassified.

VAR_007790

Natural variant

1613

1

S → G Common polymorphism. Ref.3 Ref.6 Ref.66 Ref.75 Ref.78
Corresponds to variant rs1799966 [ dbSNP | Ensembl ].

VAR_007791

Natural variant

1620

1

T → A. Ref.6
Corresponds to variant rs8176219 [ dbSNP | Ensembl ].

VAR_019946

Natural variant

1623

1

A → G Could be associated with cancer susceptibility; major splicing aberration identified with this mutant. Ref.86 Ref.87

VAR_063901

Natural variant

1628

1

M → T in some patients with sporadic breast cancer; unknown pathological significance. Ref.84
Corresponds to variant rs4986854 [ dbSNP | Ensembl ].

VAR_007793

Natural variant

1628

1

M → V Unclassified.

VAR_007792

Natural variant

1637

1

P → L Rare polymorphism. Ref.64 Ref.72

VAR_007794

Natural variant

1641

1

A → P in ovarian cancer; unknown pathological significance.
Corresponds to variant rs1800726 [ dbSNP | Ensembl ].

VAR_008762

Natural variant

1652

1

M → I Rare polymorphism. Ref.72 Ref.77
Corresponds to variant rs1799967 [ dbSNP | Ensembl ].

VAR_007795

Natural variant

1662

1

F → C.
Corresponds to variant rs28897695 [ dbSNP | Ensembl ].

VAR_052080

Natural variant

1665

1

V → M. Ref.81

VAR_020700

Natural variant

1685

1

T → A in BC; unknown pathological significance. Ref.86

VAR_063902

Natural variant

1685

1

T → I Could be associated with cancer susceptibility; multifactorial likelihood analysis provides evidence for pathogenicity. Ref.86 Ref.87

VAR_063903

Natural variant

1689

1

M → R in BC; unknown pathological significance. Ref.86

VAR_063904

Natural variant

1690

1

K → Q in some patients with sporadic breast cancer; unknown pathological significance. Ref.84

VAR_020701

Natural variant

1692

1

D → N in ovarian cancer; unknown pathological significance.

VAR_008763

Natural variant

1697

1

C → R in ovarian cancer. Ref.82

VAR_020702

Natural variant

1699

1

R → W in ovarian cancer. Ref.82 Ref.86

VAR_020703

Natural variant

1706

1

G → E in BC; unknown pathological significance. Ref.86

VAR_063905

Natural variant

1708

1

A → E in BC; abolishes ACACA binding. Ref.64 Ref.86

VAR_007796

Natural variant

1713

1

V → G. Ref.84

VAR_007797

Natural variant

1715

1

S → R in BC; unknown pathological significance. Ref.86

VAR_063906

Natural variant

1738

1

G → R in BC; unknown pathological significance. Ref.86

VAR_063907

Natural variant

1749

1

P → R in ovarian cancer; unknown pathological significance; abolishes ACACA binding and strongly reduces BRIP1 binding. Ref.17 Ref.58 Ref.74

VAR_007798

Natural variant

1764

1

L → P in BC; unknown pathological significance. Ref.86

VAR_063908

Natural variant

1766

1

I → S in BC; unknown pathological significance. Ref.86

VAR_063909

Natural variant

1775

1

M → K in BC; strongly reduced transcription transactivation; abolishes interaction with BRIP1 and RBBP8. Ref.61

VAR_063212

Natural variant

1775

1

M → R in BC; alters protein stability and abolishes ACACA and BRIP1 binding. Ref.1 Ref.17 Ref.56 Ref.58 Ref.64

VAR_007799

Natural variant

1776

1

P → S in ovarian cancer; unknown pathological significance.
Corresponds to variant rs1800757 [ dbSNP | Ensembl ].

VAR_008764

Natural variant

1786

1

L → P in BROVCA1; unknown pathological significance. Ref.80

VAR_020704

Natural variant

1788

1

G → V in BC; unknown pathological significance. Ref.86

VAR_063910

Natural variant

1812

1

P → S in ovarian cancer; unknown pathological significance.
Corresponds to variant rs1800751 [ dbSNP | Ensembl ].

VAR_008765

Experimental info

Mutagenesis

26

1

I → A: Disrupts the interaction with E2 enzymes, thereby abolishing the E3 ubiquitin-protein ligase activity. Ref.34 Ref.49

Mutagenesis

26

1

I → E: No ubiquitination of RBBP8. No restoration RBBP8-mediated focus formation or G2/M checkpoint control upon DNA damage. Ref.34 Ref.49

Mutagenesis

71

1

R → G: No effect on interaction with BAP1. Ref.11

Mutagenesis

308

1

S → N: Abolishes phosphorylation by AURKA and interferes with cell cycle progression from G2 to mitosis. Ref.30

Mutagenesis

1143

1

S → A: Reduces in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1239

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1280

1

S → A: Reduces in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1298

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1330

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1387

1

S → A: Loss of IR-induced S-phase checkpoint. Reduces in vitro phosphorylation by ATR. Ref.15 Ref.20

Mutagenesis

1394

1

T → A: Reduces in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1423

1

S → A: Inhibition of the infrared-induced G2 arrest. Reduces phosphorylation by ATR. Ref.15 Ref.20

Mutagenesis

1457

1

S → A: Reduces in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1466

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1524

1

S → 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

Mutagenesis

1655

1

S → A: Abolishes interaction with BRIP1. Ref.58

Mutagenesis

1702

1

K → M: Abolishes interaction with BRIP1. Ref.58

Mutagenesis

1720

1

T → A: No effect on in vitro phosphorylation by ATR. Ref.15

Mutagenesis

1738

1

G → E: Abolishes interaction with BRIP1. Ref.58

Mutagenesis

1755

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.15

Sequence conflict

89

1

I → T in AAB61673. Ref.4

Sequence conflict

148

1

Missing in AAB61673. Ref.4

Sequence conflict

253

1

A → V in AAC00049. Ref.3

Sequence conflict

1077

1

G → R in AAB61673. Ref.4

Sequence conflict

1426

1

S → P in AAC00049. Ref.3

Sequence conflict

1453

1

Missing in AAC00049. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1863

Helix Strand Turn

Details...

Helix

3 – 5

3

Helix

8 – 21

14

Beta strand

25 – 27

3

Helix

46 – 53

8

Beta strand

54 – 58

5

Turn

62 – 64

3

Turn

70 – 72

3

Beta strand

78 – 80

3

Helix

81 – 96

16

Beta strand

1651 – 1656

6

Helix

1659 – 1672

14

Beta strand

1675 – 1679

5

Beta strand

1686 – 1689

4

Beta strand

1695 – 1697

3

Helix

1701 – 1708

8

Beta strand

1712 – 1715

4

Helix

1717 – 1724

8

Beta strand

1725 – 1727

3

Helix

1731 – 1734

4

Turn

1740 – 1742

3

Beta strand

1743 – 1745

3

Helix

1748 – 1753

6

Turn

1755 – 1757

3

Turn

1760 – 1763

4

Beta strand

1765 – 1768

4

Beta strand

1770 – 1772

3

Beta strand

1773 – 1775

3

Helix

1777 – 1786

10

Beta strand

1789 – 1791

3

Helix

1795 – 1797

3

Beta strand

1801 – 1803

3

Beta strand

1806 – 1810

5

Helix

1812 – 1814

3

Helix

1819 – 1822

4

Turn

1825 – 1827

3

Beta strand

1828 – 1830

3

Beta strand

1832 – 1834

3

Helix

1835 – 1844

10

Helix

1851 – 1853

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 89C6D83FF56312AF	FASTA	1,863	207,721
	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
	Isoform 2 [UniParc]. Checksum: C358CA74EC4F2C95	FASTA	1,863	207,696
	10 20 30 40 50 60 MDLSALRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ 70 80 90 100 110 120 CPLCKNDITK MSLQESTRFS 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
	Isoform 3 (Delta11b) [UniParc]. Checksum: 0FB0AB4830BD4C74	FASTA	760	85,072
	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 YQGEAASGCE SETSVSEDCS GLSSQSDILT TQQRDTMQHN 310 320 330 340 350 360 LIKLQQEMAE LEAVLEQHGS QPSNSYPSII SDSSALEDLR NPEQSTSEKA VLTSQKSSEY 370 380 390 400 410 420 PISQNPEGLS ADKFEVSADS STSKNKEPGV ERSSPSKCPS LDDRWYMHSC SGSLQNRNYP 430 440 450 460 470 480 SQEELIKVVD VEEQQLEESG PHDLTETSYL PRQDLEGTPY LESGISLFSD DPESDPSEDR 490 500 510 520 530 540 APESARVGNI PSSTSALKVP QLKVAESAQS PAAAHTTDTA GYNAMEESVS REKPELTAST 550 560 570 580 590 600 ERVNKRMSMV VSGLTPEEFM LVYKFARKHH ITLTNLITEE TTHVVMKTDA EFVCERTLKY 610 620 630 640 650 660 FLGIAGGKWV VSYFWVTQSI KERKMLNEHD FEVRGDVVNG RNHQGPKRAR ESQDRKIFRG 670 680 690 700 710 720 LEICCYGPFT NMPTDQLEWM VQLCGASVVK ELSSFTLGTG VHPIVVVQPD AWTEDNGFHA 730 740 750 760 IGQMCEAPVV TREWVLDSVA LYQCQELDTY LIPQIPHSHY
	Isoform 4 (DeltaBRCA1(17aa)) [UniParc]. Checksum: 3C16437DF10FA4D1	FASTA	1,846	205,838
	10 20 30 40 50 60 MQKILECPIC LELIKEPVST KCDHIFCKFC MLKLLNQKKG PSQCPLCKND ITKRSLQEST 70 80 90 100 110 120 RFSQLVEELL KIICAFQLDT GLEYANSYNF AKKENNSPEH LKDEVSIIQS MGYRNRAKRL 130 140 150 160 170 180 LQSEPENPSL QETSLSVQLS NLGTVRTLRT KQRIQPQKTS VYIELGSDSS EDTVNKATYC 190 200 210 220 230 240 SVGDQELLQI TPQGTRDEIS LDSAKKAACE FSETDVTNTE HHQPSNNDLN TTEKRAAERH 250 260 270 280 290 300 PEKYQGSSVS NLHVEPCGTN THASSLQHEN SSLLLTKDRM NVEKAEFCNK SKQPGLARSQ 310 320 330 340 350 360 HNRWAGSKET CNDRRTPSTE KKVDLNADPL CERKEWNKQK LPCSENPRDT EDVPWITLNS 370 380 390 400 410 420 SIQKVNEWFS RSDELLGSDD SHDGESESNA KVADVLDVLN EVDEYSGSSE KIDLLASDPH 430 440 450 460 470 480 EALICKSERV HSKSVESNIE DKIFGKTYRK KASLPNLSHV TENLIIGAFV TEPQIIQERP 490 500 510 520 530 540 LTNKLKRKRR PTSGLHPEDF IKKADLAVQK TPEMINQGTN QTEQNGQVMN ITNSGHENKT 550 560 570 580 590 600 KGDSIQNEKN PNPIESLEKE SAFKTKAEPI SSSISNMELE LNIHNSKAPK KNRLRRKSST 610 620 630 640 650 660 RHIHALELVV SRNLSPPNCT ELQIDSCSSS EEIKKKKYNQ MPVRHSRNLQ LMEGKEPATG 670 680 690 700 710 720 AKKSNKPNEQ TSKRHDSDTF PELKLTNAPG SFTKCSNTSE LKEFVNPSLP REEKEEKLET 730 740 750 760 770 780 VKVSNNAEDP KDLMLSGERV LQTERSVESS SISLVPGTDY GTQESISLLE VSTLGKAKTE 790 800 810 820 830 840 PNKCVSQCAA FENPKGLIHG CSKDNRNDTE GFKYPLGHEV NHSRETSIEM EESELDAQYL 850 860 870 880 890 900 QNTFKVSKRQ SFAPFSNPGN AEEECATFSA HSGSLKKQSP KVTFECEQKE ENQGKNESNI 910 920 930 940 950 960 KPVQTVNITA GFPVVGQKDK PVDNAKCSIK GGSRFCLSSQ FRGNETGLIT PNKHGLLQNP 970 980 990 1000 1010 1020 YRIPPLFPIK SFVKTKCKKN LLEENFEEHS MSPEREMGNE NIPSTVSTIS RNNIRENVFK 1030 1040 1050 1060 1070 1080 EASSSNINEV GSSTNEVGSS INEIGSSDEN IQAELGRNRG PKLNAMLRLG VLQPEVYKQS 1090 1100 1110 1120 1130 1140 LPGSNCKHPE IKKQEYEEVV QTVNTDFSPY LISDNLEQPM GSSHASQVCS ETPDDLLDDG 1150 1160 1170 1180 1190 1200 EIKEDTSFAE NDIKESSAVF SKSVQKGELS RSPSPFTHTH LAQGYRRGAK KLESSEENLS 1210 1220 1230 1240 1250 1260 SEDEELPCFQ HLLFGKVNNI PSQSTRHSTV ATECLSKNTE ENLLSLKNSL NDCSNQVILA 1270 1280 1290 1300 1310 1320 KASQEHHLSE ETKCSASLFS SQCSELEDLT ANTNTQDPFL IGSSKQMRHQ SESQGVGLSD 1330 1340 1350 1360 1370 1380 KELVSDDEER GTGLEENNQE EQSMDSNLGE AASGCESETS VSEDCSGLSS QSDILTTQQR 1390 1400 1410 1420 1430 1440 DTMQHNLIKL QQEMAELEAV LEQHGSQPSN SYPSIISDSS ALEDLRNPEQ STSEKAVLTS 1450 1460 1470 1480 1490 1500 QKSSEYPISQ NPEGLSADKF EVSADSSTSK NKEPGVERSS PSKCPSLDDR WYMHSCSGSL 1510 1520 1530 1540 1550 1560 QNRNYPSQEE LIKVVDVEEQ QLEESGPHDL TETSYLPRQD LEGTPYLESG ISLFSDDPES 1570 1580 1590 1600 1610 1620 DPSEDRAPES ARVGNIPSST SALKVPQLKV AESAQSPAAA HTTDTAGYNA MEESVSREKP 1630 1640 1650 1660 1670 1680 ELTASTERVN KRMSMVVSGL TPEEFMLVYK FARKHHITLT NLITEETTHV VMKTDAEFVC 1690 1700 1710 1720 1730 1740 ERTLKYFLGI AGGKWVVSYF WVTQSIKERK MLNEHDFEVR GDVVNGRNHQ GPKRARESQD 1750 1760 1770 1780 1790 1800 RKIFRGLEIC CYGPFTNMPT DQLEWMVQLC GASVVKELSS FTLGTGVHPI VVVQPDAWTE 1810 1820 1830 1840 DNGFHAIGQM CEAPVVTREW VLDSVALYQC QELDTYLIPQ IPHSHY
	Isoform 5 (Delta11) (Delta772-3095) [UniParc]. Checksum: A4EED8A734FCB619	FASTA	721	80,590
	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 AKKGEAASGC ESETSVSEDC 250 260 270 280 290 300 SGLSSQSDIL TTQQRDTMQH NLIKLQQEMA ELEAVLEQHG SQPSNSYPSI ISDSSALEDL 310 320 330 340 350 360 RNPEQSTSEK AVLTSQKSSE YPISQNPEGL SADKFEVSAD SSTSKNKEPG VERSSPSKCP 370 380 390 400 410 420 SLDDRWYMHS CSGSLQNRNY PSQEELIKVV DVEEQQLEES GPHDLTETSY LPRQDLEGTP 430 440 450 460 470 480 YLESGISLFS DDPESDPSED RAPESARVGN IPSSTSALKV PQLKVAESAQ SPAAAHTTDT 490 500 510 520 530 540 AGYNAMEESV SREKPELTAS TERVNKRMSM VVSGLTPEEF MLVYKFARKH HITLTNLITE 550 560 570 580 590 600 ETTHVVMKTD AEFVCERTLK YFLGIAGGKW VVSYFWVTQS IKERKMLNEH DFEVRGDVVN 610 620 630 640 650 660 GRNHQGPKRA RESQDRKIFR GLEICCYGPF TNMPTDQLEW MVQLCGASVV KELSSFTLGT 670 680 690 700 710 720 GVHPIVVVQP DAWTEDNGFH AIGQMCEAPV VTREWVLDSV ALYQCQELDT YLIPQIPHSH Y
	Isoform 6 [UniParc]. Checksum: 67C7F5031F0ED6F3	FASTA	699	78,165
	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 YQGEAASGCE SETSVSEDCS GLSSQSDILT TQQRDTMQHN 310 320 330 340 350 360 LIKLQQEMAE LEAVLEQHGS QPSNSYPSII SDSSALEDLR NPEQSTSEKV LTSQKSSEYP 370 380 390 400 410 420 ISQNPEGLSA DKFEVSADSS TSKNKEPGVE RSSPSKCPSL DDRWYMHSCS GSLQNRNYPS 430 440 450 460 470 480 QEELIKVVDV EEQQLEESGP HDLTETSYLP RQDLEGTPYL ESGISLFSDD PESDPSEDRA 490 500 510 520 530 540 PESARVGNIP SSTSALKVPQ LKVAESAQSP AAAHTTDTAG YNAMEESVSR EKPELTASTE 550 560 570 580 590 600 RVNKRMSMVV SGLTPEEFML VYKFARKHHI TLTNLITEET THVVMKTDAE FVCERTLKYF 610 620 630 640 650 660 LGIAGGKWVV SYFWVTQSIK ERKMLNEHDF EVRGDVVNGR NHQGPKRARE SQDRKIFRGL 670 680 690 EICCYGPFTN MPTGCPPNCG CAARCLDRGQ WLPCNWADV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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; THR-1720 AND SER-1755.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[52]	"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.
[53]	"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, MASS SPECTROMETRY.
[54]	"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.
[55]	"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, MASS SPECTROMETRY.
[56]	"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.
[57]	"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.
[58]	"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.
[59]	"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.
[60]	"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.
[61]	"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.
[62]	"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.
[63]	"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.
[64]	"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. , 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.
[65]	"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.
[66]	"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.
[67]	"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.
[68]	"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.
[69]	"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.
[70]	"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.
[71]	"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.
[72]	"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.
[73]	"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. , 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.
[74]	"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.
[75]	"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.
[76]	"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.
[77]	"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.
[78]	"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.
[79]	"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.
[80]	"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.
[81]	"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.
[82]	"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.
[83]	"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.
[84]	"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.
[85]	"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. , 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.
[86]	"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.
[87]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

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.
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.

IPI

IPI00027272.
IPI00027277.
IPI00185298.
IPI00218982.
IPI00909467.
IPI00945705.

PIR

A58881.

RefSeq

NP_009225.1. NM_007294.3.
NP_009228.2. NM_007297.3.
NP_009229.2. NM_007298.3.
NP_009230.2. NM_007299.3.
NP_009231.2. NM_007300.3.

UniGene

Hs.194143.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JM7	NMR	-	A	1-110	[»]
1JNX	X-ray	2.50	X	1646-1859	[»]
1N5O	X-ray	2.80	X	1646-1859	[»]
1OQA	NMR	-	A	1755-1863	[»]
1T15	X-ray	1.85	A	1649-1859	[»]
1T29	X-ray	2.30	A	1646-1859	[»]
1T2U	X-ray	2.80	A	1646-1859	[»]
1T2V	X-ray	3.30	A/B/C/D/E	1646-1859	[»]
1Y98	X-ray	2.50	A	1646-1859	[»]
2ING	X-ray	3.60	X	1649-1859	[»]
3COJ	X-ray	3.21	A/B/C/D/E/F/G/X	1646-1859	[»]
3K0H	X-ray	2.70	A	1646-1859	[»]
3K0K	X-ray	2.70	A	1646-1859	[»]
3K15	X-ray	2.80	A	1646-1859	[»]
3K16	X-ray	3.00	A	1646-1859	[»]
3PXA	X-ray	2.55	A	1646-1859	[»]
3PXB	X-ray	2.50	A	1646-1859	[»]
3PXC	X-ray	2.80	X	1646-1859	[»]
3PXD	X-ray	2.80	A	1646-1859	[»]
3PXE	X-ray	2.85	A/B/C/D	1646-1859	[»]

DisProt

DP00238.

ProteinModelPortal

P38398.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5971N.

IntAct

P38398. 55 interactions.

MINT

MINT-90433.

STRING

9606.ENSP00000350283.

PTM databases

PhosphoSite

P38398.

Polymorphism databases

DMDM

728984.

Proteomic databases

PaxDb

P38398.

PRIDE

P38398.

Protocols and materials databases

DNASU

672.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000352993; ENSP00000312236; ENSG00000012048.
ENST00000357654; ENSP00000350283; ENSG00000012048.
ENST00000468300; ENSP00000417148; ENSG00000012048.

GeneID

672.

KEGG

hsa:672.

UCSC

uc002icp.4. human.
uc002icq.3. human.
uc002icu.3. human.
uc010whl.2. human.

Organism-specific databases

CTD

672.

GeneCards

GC17M041197.

HGNC

HGNC:1100. BRCA1.

HPA

CAB001946.
CAB018369.
HPA034966.

MIM

113705. gene.
114480. phenotype.
167000. phenotype.
604370. phenotype.
614320. phenotype.

neXtProt

NX_P38398.

Orphanet

1333. Familial pancreatic carcinoma.
1331. Familial prostate cancer.
145. Hereditary breast and ovarian cancer syndrome.
168829. Primary peritoneal carcinoma.

PharmGKB

PA25411.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG274496.

HOGENOM

HOG000230969.

HOVERGEN

HBG050730.

InParanoid

P38398.

KO

K10605.

OrthoDB

EOG42RD7C.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.
bard1pathway. BARD1 signaling events.
ar_pathway. Coregulation of Androgen receptor activity.
hnf3apathway. FOXA1 transcription factor network.

Reactome

REACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_216. DNA Repair.

SignaLink

P38398.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

P38398.

Bgee

P38398.

CleanEx

HS_BRCA1.

Genevestigator

P38398.

GermOnline

ENSG00000012048. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.
3.40.50.10190. 2 hits.

InterPro

IPR011364. 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]

PANTHER

PTHR13763. PTHR13763. 1 hit.

Pfam

PF00533. BRCT. 2 hits.
PF12820. BRCT_assoc. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]

PIRSF

PIRSF001734. BRCA1. 1 hit.

PRINTS

PR00493. BRSTCANCERI.

SMART

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

SUPFAM

SSF52113. BRCT. 2 hits.

PROSITE

PS50172. BRCT. 2 hits.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P38398.

ChEMBL

CHEMBL5990.

ChiTaRS

BRCA1. human.

EvolutionaryTrace

P38398.

GenomeRNAi

672.

NextBio

2752.

PMAP-CutDB

P38398.

SOURCE

Search...

Entry information

Entry name

BRCA1_HUMAN

Accession

Primary (citable) accession number: P38398
Secondary accession number(s): O15129 , Q3LRJ0, Q3LRJ6, Q6IN79, Q7KYU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 181 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.