Reviewed, UniProtKB/Swiss-Prot P38398 (BRCA1_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1863 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Plays a central role in DNA repair by facilitating cellular response to DNA repair. 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.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBN protein 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/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1. Interacts (via BRCT domains) with FAM175A/Abraxas and RBBP8. Associates with RNA polymerase II holoenzyme. Interacts with SMC1A and COBRA1/NELFB. Interacts (via BRCT domains) with BRIP1. Interacts with FANCD2 (ubiquitinated). Interacts with BAP1. Interacts with DCLRE1C/Artemis and CLSPN. Interacts with H2AFX (phosphorylated on 'Ser-140'). Interacts with CHEK1/CHK1. Interacts with BRCC3. Interacts (via BRCT domains) with ACACA (phosphorylated); the interaction prevents dephosphorylation of ACACA. Ref.19 Ref.26 Ref.8 Ref.9 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.22 Ref.23 Ref.24 Ref.27
Subcellular location	Nucleus. 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.8 Ref.3 Ref.7 Isoform 3: Cytoplasm. Ref.8 Ref.3 Ref.7 Isoform 5: Cytoplasm. Ref.8 Ref.3 Ref.7
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. The RING-type zinc finger domain interacts with BAP1.
Post-translational modification	Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Ref.12 Ref.16 Ref.25 Ref.31 Ref.33 Ref.34
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	Defects in BRCA1 are a cause of genetic susceptibility to breast cancer (BC) [MIM:113705, 114480]. BC is an extremely common malignancy, affecting one in eight women during their lifetime. A positive family history has been identified as major contributor to risk of development of the disease, and this link is striking for early-onset breast cancer. 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.13 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.49 Ref.53 Ref.54 Ref.57 Defects in BRCA1 are a cause of susceptibility to familial breast-ovarian cancer type 1 (BROVCA1) [MIM:604370]. Mutations in BRCA1 are thought to be responsible for more than 80% of inherited breast-ovarian cancer. Defects in BRCA1 are a cause of genetic susceptibility to ovarian cancer [MIM:113705].
Sequence similarities	Contains 2 BRCT domains. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair Fatty acid biosynthesis Lipid synthesis Ubl conjugation pathway
Cellular component	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
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Traceable author statement. Source: UniProtKB DNA damage response, signal transduction resulting in induction of apoptosis Inferred from direct assay. Source: MGI G2/M transition DNA damage checkpoint Ref.30 Ref.32 Ref.35 Inferred from mutant phenotype. Source: UniProtKB androgen receptor signaling pathway Non-traceable author statement. Source: UniProtKB apoptosis Traceable author statement. Source: UniProtKB chromosome segregation Inferred from mutant phenotype. Source: UniProtKB double-strand break repair via homologous recombination Inferred from direct assay. Source: HGNC fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of centriole replication Non-traceable author statement. Source: UniProtKB negative regulation of fatty acid biosynthetic process Ref.26 Inferred from mutant phenotype. Source: UniProtKB negative regulation of transcription Inferred from direct assay. Source: UniProtKB positive regulation of DNA repair Ref.30 Ref.32 Ref.35 Inferred from mutant phenotype. Source: UniProtKB positive regulation of protein ubiquitination Inferred from direct assay. Source: UniProtKB positive regulation of transcription, DNA-dependent Non-traceable author statement. Source: UniProtKB postreplication repair Inferred from direct assay. Source: HGNC protein ubiquitination Non-traceable author statement. Source: UniProtKB regulation of cell proliferation Traceable author statement. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc regulation of transcription from RNA polymerase III promoter Traceable author statement. Source: UniProtKB response to estrogen stimulus Inferred from direct assay. Source: UniProtKB response to ionizing radiation Ref.30 Ref.32 Ref.35 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	BRCA1-A complex Ref.32 Ref.35 Ref.36 Inferred from direct assay. Source: UniProtKB BRCA1-BARD1 complex Inferred from direct assay. Source: UniProtKB gamma-tubulin ring complex Non-traceable author statement. Source: UniProtKB nucleoplasm Inferred from Experiment. Source: Reactome ribonucleoprotein complex Inferred from direct assay. Source: MGI
Molecular function	androgen receptor binding Non-traceable author statement. Source: UniProtKB enzyme binding Inferred from physical interaction. Source: UniProtKB identical protein binding Inferred from physical interaction. Source: IntAct ligase activity Inferred from electronic annotation. Source: UniProtKB-KW transcription coactivator activity Non-traceable author statement. Source: UniProtKB tubulin binding Non-traceable author statement. Source: UniProtKB zinc ion binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-349905,EBI-349905
ACACA	Q13085	2	EBI-349905,EBI-717681
BACH1	O14867	1	EBI-349905,EBI-1263541
BAP1	Q92560	1	EBI-349905,EBI-1791447
BAP1	Q92560	1	EBI-2015072,EBI-1791447
Bap1	Q99PU7	2	EBI-349905,EBI-1791471	From a different organism.
BARD1	Q99728	5	EBI-349905,EBI-473181
BRAP	Q7Z569	1	EBI-349905,EBI-349900
CCND1	P24385	2	EBI-349905,EBI-375001
CCNE1	P24864	2	EBI-349905,EBI-519526
CHEK1	O14757	1	EBI-349905,EBI-974488
COBRA1	Q8WX92	3	EBI-349905,EBI-347721
ESR1	P03372	4	EBI-349905,EBI-78473
FAM175A	Q6UWZ7	4	EBI-349905,EBI-1263451
H2AFX	P16104	1	EBI-349905,EBI-494830
KPNA2	P52292	1	EBI-349905,EBI-349938
MDC1	Q14676	1	EBI-349905,EBI-495644
NCK1	P16333	1	EBI-349905,EBI-389883
ORC3L	Q9UBD5	1	EBI-349905,EBI-374916
PIK3R1	P27986	1	EBI-349905,EBI-79464
PPP1CA	P62136	2	EBI-349905,EBI-357253
PPP1CB	P62140	2	EBI-349905,EBI-352350
PPP1CC	P36873	2	EBI-349905,EBI-356283
RBBP8	Q99708	5	EBI-349905,EBI-1263531
SMC1A	Q14683	1	EBI-349905,EBI-80690
TP53BP1	Q12888	1	EBI-349905,EBI-396540
TRRAP	Q9Y4A5	2	EBI-349905,EBI-399128
UIMC1	Q96RL1	4	EBI-349905,EBI-725300
ZCCHC8	Q6NZY4	2	EBI-349905,EBI-1263058
ZNF350	Q9GZX5	2	EBI-349905,EBI-396421

Alternative products

This entry describes 5 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.

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

Compositional bias

651 – 654

4

Poly-Lys

Amino acid modifications

Modified residue

395

1

Phosphoserine Ref.34

Modified residue

398

1

Phosphoserine Ref.34

Modified residue

403

1

Phosphoserine Ref.34

Modified residue

753

1

Phosphoserine Ref.34

Modified residue

840

1

Phosphoserine By similarity

Modified residue

1143

1

Phosphoserine; by ATR; in vitro Ref.12

Modified residue

1211

1

Phosphoserine Ref.25 Ref.34

Modified residue

1212

1

Phosphoserine Ref.25

Modified residue

1217

1

Phosphoserine Ref.25 Ref.34

Modified residue

1218

1

Phosphoserine Ref.25 Ref.34

Modified residue

1239

1

Phosphoserine Ref.31

Modified residue

1245

1

Phosphoserine Ref.31

Modified residue

1280

1

Phosphoserine; by ATR; in vitro Ref.12

Modified residue

1330

1

Phosphoserine Ref.31

Modified residue

1336

1

Phosphoserine Ref.25 Ref.31

Modified residue

1342

1

Phosphoserine Ref.31

Modified residue

1387

1

Phosphoserine; by ATM and ATR Ref.12

Modified residue

1394

1

Phosphothreonine; by ATR; in vitro Ref.12

Modified residue

1423

1

Phosphoserine; by ATM and ATR Ref.12

Modified residue

1457

1

Phosphoserine; by ATR; in vitro Ref.12 Ref.31

Modified residue

1466

1

Phosphoserine Ref.31

Modified residue

1524

1

Phosphoserine; by ATM Ref.31

Modified residue

1542

1

Phosphoserine Ref.33

Modified residue

1700

1

Phosphothreonine Ref.31

Modified residue

1720

1

Phosphothreonine Ref.31

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.

VSP_035399

Natural variant

10

1

E → K in BC and BROVCA1.

VAR_020679

Natural variant

11

1

V → A Unclassified.

VAR_007754

Natural variant

21

1

I → V Unclassified.

VAR_007755

Natural variant

22

1

L → S in BC. Ref.47

VAR_007756

Natural variant

23

1

E → K in BC and BROVCA1.

VAR_020680

Natural variant

30

1

L → F in a breast cancer sample; somatic mutation. Ref.59

VAR_035947

Natural variant

61

1

C → G in BC and ovarian cancer; no interaction with BAP1. dbSNP rs28897672.

VAR_007757

Natural variant

64

1

C → G in BC; no interaction with BAP1. Ref.39 Ref.46

VAR_007758

Natural variant

64

1

C → Y Unclassified. dbSNP rs55851803.

VAR_007759

Natural variant

71

1

R → K in BC; unknown pathological significance. Ref.54

VAR_020681

Natural variant

153

1

S → R: dbSNP rs28897674.

VAR_052077

Natural variant

227

1

E → K in ovarian cancer; could be a polymorphism.

VAR_008759

Natural variant

239

1

H → R Ref.3 Ref.45

VAR_007760

Natural variant

271

1

V → M in BC. Ref.44

VAR_007761

Natural variant

275

1

G → S: dbSNP rs8176153. Ref.5

VAR_019944

Natural variant

346

1

P → S in BC; could be a polymorphism. Ref.49

VAR_008760

Natural variant

356

1

Q → R Common polymorphism. dbSNP rs1799950. Ref.40 Ref.5

VAR_007762

Natural variant

369

1

Missing in BC.

VAR_007763

Natural variant

379

1

I → M Unclassified. dbSNP rs56128296.

VAR_007764

Natural variant

461

1

F → L in BC. dbSNP rs56046357.

VAR_007765

Natural variant

465

1

Y → D in BC. Ref.47

VAR_007766

Natural variant

507

1

R → I Unclassified.

VAR_007767

Natural variant

552

1

G → V in BC. Ref.47

VAR_007768

Natural variant

656

1

N → I Ref.52

VAR_020682

Natural variant

693

1

D → N Rare polymorphism. dbSNP rs4986850. Ref.5 Ref.55

VAR_007769

Natural variant

723

1

N → D: dbSNP rs4986845.

VAR_020110

Natural variant

749

1

D → Y in BC. Ref.53

VAR_020683

Natural variant

758

1

L → F in a breast cancer sample; somatic mutation. Ref.59

VAR_035948

Natural variant

772

1

V → A Rare polymorphism. Ref.39 Ref.46

VAR_007770

Natural variant

778

1

G → C in a breast cancer sample; somatic mutation. Ref.59

VAR_035949

Natural variant

820

1

K → E Rare polymorphism. Ref.46

VAR_007771

Natural variant

826

1

T → K in BC.

VAR_007772

Natural variant

835

1

H → Y in BROVCA1; unknown pathological significance.

VAR_020684

Natural variant

841

1

R → W in BROVCA1; could be a rare polymorphism. dbSNP rs1800709.

VAR_007773

Natural variant

856

1

Y → H in a patient with sporadic breast cancer; unknown pathological significance. Ref.58

VAR_020685

Natural variant

866

1

R → Q in BC; unknown pathological significance. Ref.54

VAR_020686

Natural variant

871

1

P → L Common polymorphism. dbSNP rs799917. Ref.49 Ref.5 Ref.52 Ref.58

VAR_007774

Natural variant

888

1

H → Y in BC; unknown pathological significance. Ref.54

VAR_020687

Natural variant

892

1

L → S in BC. Ref.47

VAR_007775

Natural variant

925

1

I → L: dbSNP rs4986847.

VAR_021913

Natural variant

960

1

G → D in BC. Ref.47

VAR_007776

Natural variant

989

1

F → S: dbSNP rs4986848.

VAR_020111

Natural variant

1008

1

M → I Common polymorphism. dbSNP rs1800704.

VAR_007777

Natural variant

1025

1

T → I in BC. Ref.47

VAR_007778

Natural variant

1038

1

E → G Common polymorphism. dbSNP rs16941. Ref.40 Ref.49 Ref.5 Ref.58

VAR_007779

Natural variant

1040

1

S → N Rare polymorphism. dbSNP rs4986852. Ref.39 Ref.40 Ref.46 Ref.5 Ref.55

VAR_007780

Natural variant

1047

1

V → A in BC. Ref.47

VAR_007781

Natural variant

1060

1

E → A Ref.55

VAR_020688

Natural variant

1139

1

S → I in BC; unknown pathological significance. Ref.54

VAR_020689

Natural variant

1140

1

S → G: dbSNP rs2227945. Ref.5

VAR_019945

Natural variant

1150

1

P → S in BC. Ref.44

VAR_007782

Natural variant

1183

1

K → R Common polymorphism. dbSNP rs16942. Ref.40 Ref.49 Ref.57 Ref.5 Ref.58

VAR_007783

Natural variant

1187

1

S → I in BC and BROVCA1.

VAR_020690

Natural variant

1200

1

Q → H in BC and BROVCA1.

VAR_020691

Natural variant

1204

1

R → I in BC. Ref.57

VAR_020692

Natural variant

1207

1

K → N in BC. Ref.57

VAR_020693

Natural variant

1210

1

E → G in BC; unknown pathological significance. Ref.54

VAR_020694

Natural variant

1217

1

S → Y in BC and BROVCA1.

VAR_020695

Natural variant

1219

1

E → D Unclassified.

VAR_007784

Natural variant

1226

1

F → L in BROVCA1.

VAR_020696

Natural variant

1236

1

N → K: dbSNP rs28897687.

VAR_052078

Natural variant

1243

1

R → G in BROVCA1.

VAR_020697

Natural variant

1250

1

E → K: dbSNP rs28897686.

VAR_052079

Natural variant

1297

1

S → P in BC; unknown pathological significance. Ref.54

VAR_020698

Natural variant

1347

1

R → G Ref.51

VAR_007785

Natural variant

1406

1

K → N Polymorphism. dbSNP rs1800707.

VAR_008761

Natural variant

1411

1

M → T in ovarian cancer; unknown pathological significance. Ref.56

VAR_020699

Natural variant

1431

1

S → P

VAR_007786

Natural variant

1443

1

R → G Rare polymorphism. Ref.39 Ref.46

VAR_007787

Natural variant

1443

1

R → Q: dbSNP rs4986849. Ref.39 Ref.46

VAR_020112

Natural variant

1512

1

S → I: dbSNP rs1800744. Ref.45 Ref.46 Ref.51

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. dbSNP rs1799966. Ref.3 Ref.40 Ref.49 Ref.5 Ref.52

VAR_007791

Natural variant

1620

1

T → A: dbSNP rs8176219. Ref.5

VAR_019946

Natural variant

1628

1

M → T in some patients with sporadic breast cancer; unknown pathological significance. dbSNP rs4986854. Ref.58

VAR_007793

Natural variant

1628

1

M → V Unclassified. Ref.58

VAR_007792

Natural variant

1637

1

P → L Rare polymorphism. Ref.46 Ref.38

VAR_007794

Natural variant

1641

1

A → P in ovarian cancer; could be a polymorphism. dbSNP rs1800726.

VAR_008762

Natural variant

1652

1

M → I Rare polymorphism. dbSNP rs1799967. Ref.46 Ref.51

VAR_007795

Natural variant

1662

1

F → C: dbSNP rs28897695.

VAR_052080

Natural variant

1665

1

V → M Ref.55

VAR_020700

Natural variant

1690

1

K → Q in some patients with sporadic breast cancer; unknown pathological significance. Ref.58

VAR_020701

Natural variant

1692

1

D → N in ovarian cancer; could be a polymorphism.

VAR_008763

Natural variant

1697

1

C → R in ovarian cancer. Ref.56

VAR_020702

Natural variant

1699

1

R → W in ovarian cancer. Ref.56

VAR_020703

Natural variant

1708

1

A → E in BC; abolishes ACACA binding.

VAR_007796

Natural variant

1713

1

V → G Ref.58

VAR_007797

Natural variant

1749

1

P → R in ovarian cancer; could be a polymorphism; abolishes ACACA binding and reduces BRIP1 binding. Ref.13 Ref.48

VAR_007798

Natural variant

1775

1

M → R in BC; abolishes ACACA and BRIP1 binding. Ref.13

VAR_007799

Natural variant

1776

1

P → S in ovarian cancer; could be a polymorphism. dbSNP rs1800757.

VAR_008764

Natural variant

1786

1

L → P in BROVCA1; unknown pathological significance.

VAR_020704

Natural variant

1812

1

P → S in ovarian cancer; could be a polymorphism. dbSNP rs1800751.

VAR_008765

Experimental info

Mutagenesis

71

1

R → G: No effect on interaction with BAP1. Ref.8

Mutagenesis

1143

1

S → A: Reduces in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1239

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1280

1

S → A: Reduces in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1298

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1330

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1387

1

S → A: Loss of IR-induced S-phase checkpoint. Reduces in vitro phosphorylation by ATR. Ref.12 Ref.16

Mutagenesis

1394

1

T → A: Reduces in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1423

1

S → A: Inhibition of the IR-induced G2 arrest. Reduces phosphorylation by ATR. Ref.12 Ref.16

Mutagenesis

1457

1

S → A: Reduces in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1466

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1524

1

S → A: No change in IR S-phase delay; when associated with A-1387. No effect on in vitro phosphorylation by ATR. Ref.12 Ref.16

Mutagenesis

1720

1

T → A: No effect on in vitro phosphorylation by ATR. Ref.12

Mutagenesis

1755

1

S → A: No effect on in vitro phosphorylation by ATR. Ref.12

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

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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

1686 – 1689

4

Beta strand

1695 – 1697

3

Helix

1701 – 1708

8

Beta strand

1712 – 1715

4

Helix

1717 – 1724

8

Helix

1731 – 1734

4

Turn

1740 – 1742

3

Helix

1748 – 1753

6

Turn

1760 – 1763

4

Beta strand

1765 – 1768

4

Beta strand

1773 – 1775

3

Helix

1777 – 1786

10

Helix

1795 – 1797

3

Beta strand

1806 – 1810

5

Helix

1812 – 1814

3

Helix

1819 – 1822

4

Turn

1825 – 1827

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. 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). 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)). 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). 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

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: 7545954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 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: 8938427] [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: 9010228] [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]	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.
[6]	"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: 10851077] [Abstract] Cited for: PROTEIN SEQUENCE OF 6-18 (ISOFORM 1), PROTEIN SEQUENCE OF 18-26 (ISOFORM 4), ALTERNATIVE INITIATION (ISOFORM 4).
[7]	"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: 8972225] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 5), SUBCELLULAR LOCATION (ISOFORM 5).
[8]	"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: 9528852] [Abstract] Cited for: INTERACTION WITH BAP1, SUBCELLULAR LOCATION, VARIANTS GLY-61 AND GLY-64, MUTAGENESIS OF ARG-71.
[9]	"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: 9811458] [Abstract] Cited for: INTERACTION WITH RBBP8.
[10]	"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: 10500182] [Abstract] Cited for: FUNCTION AS A E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE.
[11]	"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: 10783165] [Abstract] Cited for: IDENTIFICATION IN THE BASC COMPLEX.
[12]	"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: 11114888] [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.
[13]	"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: 11301010] [Abstract] Cited for: INTERACTION WITH BRIP1, CHARACTERIZATION OF VARIANT OVARIAN CANCER ARG-1749, CHARACTERIZATION OF VARIANT BC ARG-1775.
[14]	"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: 11739404] [Abstract] Cited for: INTERACTION WITH NELFB.
[15]	"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: 11239454] [Abstract] Cited for: INTERACTION WITH FANCD2.
[16]	"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: 12183412] [Abstract] Cited for: PHOSPHORYLATION BY ATM, MUTAGENESIS OF SER-1387; SER-1423 AND SER-1524.
[17]	"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: 12419185] [Abstract] Cited for: INTERACTION WITH H2AFX.
[18]	"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: 11877377] [Abstract] Cited for: INTERACTION WITH SMC1A.
[19]	"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: 11836499] [Abstract] Cited for: FUNCTION, INTERACTION WITH CHEK1.
[20]	"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: 12360400] [Abstract] Cited for: INTERACTION WITH ACACA.
[21]	"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: 12887909] [Abstract] Cited for: FUNCTION.
[22]	"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: 14636569] [Abstract] Cited for: INTERACTION WITH BRCC3.
[23]	"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: 15456891] [Abstract] Cited for: INTERACTION WITH DCLRE1C.
[24]	"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: 15096610] [Abstract] Cited for: INTERACTION WITH CLSPN.
[25]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1211; SER-1212; SER-1217; SER-1218 AND SER-1336, MASS SPECTROMETRY. Tissue: Epithelium.
[26]	"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: 16326698] [Abstract] Cited for: FUNCTION, INTERACTION WITH ACACA.
[27]	"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: 16698035] [Abstract] Cited for: INTERACTION WITH ACACA.
[28]	"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: 8807330] [Abstract] Cited for: REVIEW ON VARIANTS.
[29]	"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: 17643122] [Abstract] Cited for: INTERACTION WITH FAM175A.
[30]	"CCDC98 targets BRCA1 to DNA damage sites." Liu Z., Wu J., Yu X. Nat. Struct. Mol. Biol. 14:716-720(2007) [PubMed: 17643121] [Abstract] Cited for: INTERACTION WITH FAM175A.
[31]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1239; SER-1245; SER-1330; SER-1336; SER-1342; SER-1457; SER-1466; SER-1524; THR-1700 AND THR-1720, MASS SPECTROMETRY.
[32]	"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: 17525340] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FAM175A.
[33]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1542, MASS SPECTROMETRY.
[34]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-398; SER-403; SER-753; SER-1211; SER-1217 AND SER-1218, MASS SPECTROMETRY.
[35]	"MERIT40 facilitates BRCA1 localization and DNA damage repair." Feng L., Huang J., Chen J. Genes Dev. 23:719-728(2009) [PubMed: 19261748] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX.
[36]	"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: 19261749] [Abstract] Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
[37]	"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: 19261746] [Abstract] Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
[38]	"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: 7939630] [Abstract] Cited for: VARIANTS LEU-1637; GLU-1708 AND ARG-1775.
[39]	"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: 7894491] [Abstract] Cited for: VARIANT BC GLY-64, VARIANTS ALA-772; ASN-1040 AND GLY-1443.
[40]	"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: 7894493] [Abstract] Cited for: VARIANT BC GLY-61, VARIANTS ARG-356; GLY-1038; ASN-1040; ARG-1183 AND GLY-1613.
[41]	"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: 8554067] [Abstract] Cited for: VARIANT BC GLY-61.
[42]	"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: 8968716] [Abstract] Cited for: VARIANT BROVCA1 TRP-841.
[43]	"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: 8776600] [Abstract] Cited for: VARIANTS BC AND BROVCA1.
[44]	"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: 8723683] [Abstract] Cited for: VARIANTS BC MET-271 AND SER-1150.
[45]	"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: 9760198] [Abstract] Cited for: VARIANT BC GLY-61, VARIANTS ARG-239; TRP-841 AND ILE-1512.
[46]	"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: 9482581] [Abstract] Cited for: VARIANT BC GLY-64, VARIANTS ALA-772; GLU-820; ASN-1040; GLY-1443; ILE-1512; LEU-1637 AND ILE-1652.
[47]	"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: 9609997] [Abstract] Cited for: VARIANTS BC SER-22; LEU-461; ASP-465; VAL-552; SER-892; ASP-960; ILE-1025 AND ALA-1047.
[48]	"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: 10486320] [Abstract] Cited for: VARIANT OVARIAN CANCER ARG-1749.
[49]	"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: 10323242] [Abstract] Cited for: VARIANT BC SER-346, VARIANTS LEU-871; GLY-1038; ARG-1183 AND GLY-1613.
[50]	"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: 10196379] [Abstract] Cited for: VARIANTS OVARIAN CANCER, VARIANTS.
[51]	"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: 12215251] [Abstract] Cited for: VARIANTS GLY-1347; ILE-1512 AND ILE-1652.
[52]	"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: 12442274] [Abstract] Cited for: VARIANTS ILE-656; LEU-871 AND GLY-1613.
[53]	"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: 12442275] [Abstract] Cited for: VARIANT BC TYR-749.
[54]	"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: 12938098] [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.
[55]	"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: 15026808] [Abstract] Cited for: VARIANTS ASN-693; ASN-1040; ALA-1060 AND MET-1665.
[56]	"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: 14746861] [Abstract] Cited for: VARIANTS OVARIAN CANCER GLY-61; THR-1411; ARG-1697 AND TRP-1699.
[57]	"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: 14722926] [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.
[58]	"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: 15365993] [Abstract] Cited for: VARIANTS HIS-856; LEU-871; GLY-1038; ARG-1183; THR-1628; GLN-1690 AND GLY-1713.
[59]	"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: 16959974] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-30; PHE-758 AND CYS-778.
+	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

EMBLGenBankDDBJ

U14680 mRNA. Translation: AAA73985.1.
L78833 Genomic DNA. Translation: AAC37594.1.
U64805 mRNA. Translation: AAC00049.1.
AF005068 mRNA. Translation: AAB61673.1.
AY273801 Genomic DNA. Translation: AAP12647.1.

IPI

IPI00027277.
IPI00185298.
IPI00218982.
IPI00375507.
IPI00909467.

PIR

A58881.

RefSeq

NP_009225.1.
NP_009226.1.
NP_009227.1.
NP_009228.1.
NP_009235.2.

UniGene

Hs.194143

3D structure databases

PDBPDBe

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	[»]

DisProt

DP00238.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5971N.

IntAct

P38398. 42 interactions.

PTM databases

PhosphoSite

P38398.

Proteomic databases

PRIDE

P38398.

Genome annotation databases

Ensembl

ENSG00000012048. Homo sapiens. [Contig view]

GeneID

672.

KEGG

hsa:672.

UCSC

uc002ico.1. human.

Organism-specific databases

GeneCards

GC17M038450.

H-InvDB

HIX0039035.

HGNC

HGNC:1100. BRCA1.

HPA

CAB001946.

MIM

113705. gene.
114480. phenotype.
604370. phenotype.

Orphanet

145. Breast cancer, familial.
1331. Prostate cancer, familial.

PharmGKB

PA25411.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P38398.

HOVERGEN

P38398.

OMA

P38398. CMLKLLN.

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_216. DNA Repair.

Gene expression databases

ArrayExpress

P38398.

Bgee

P38398.

CleanEx

HS_BRCA1.

GermOnline

ENSG00000012048. Homo sapiens.

Family and domain databases

InterPro

IPR011364. BRCA1.
IPR001357. BRCT.
IPR002378. Brst_cancerI.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]

PANTHER

PTHR13763. BRCA1. 1 hit.

Pfam

PF00533. BRCT. 2 hits.
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]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

2752.

PMAP-CutDB

P38398.

SOURCE

Search...

Entry information

Entry name

BRCA1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	February 1, 1995
Last modified:	July 7, 2009
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)