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InterPro: IPR011364 BRCA1

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UniProtKB

Matches:

858 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR011364 BRCA1

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF001734	BRCA1	34
PANTHER	PTHR13763	BRCA1	857
Signatures in BioMart

InterPro Relationships Help

Children

IPR002378 Breast cancer type I susceptibility protein

Contains

IPR001357 BRCT
IPR001841 Zinc finger, RING-type
IPR017907 Zinc finger, RING-type, conserved site
IPR018957 Zinc finger, C3HC4 RING-type

GO Term annotation Help

Process

GO:0006281 DNA repair

Function

GO:0003677 DNA binding
GO:0008270 zinc ion binding

Component

GO:0005634 nucleus

InterPro annotation

Entry Details in BioMart

Abstract

This group represents a DNA-damage repair protein, BRCA1 [1, 2]. Germline mutations of the tumour-suppressor gene product BRCA1 lead to 50% familial breast cancer. The protein contains the BRCT C-terminal domain, an approximately 100 amino acid tandem repeat, which appears to act as a phospho-protein binding domain [3].

Structural links Help

PDB - click here

SCOP: c.15.1.3 , g.44.1.1

CATH: 3.30.40.10 , 3.40.50.10190

Database links Help

Enzyme: EC:6.3.2

CluSTr: ALLvsALL:14169:42.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011364

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O54952 Breast cancer type 1 susceptibility protein homolog

P38398 Breast cancer type 1 susceptibility protein

P48754 Breast cancer type 1 susceptibility protein homolog

Q8RXD4 Protein BREAST CANCER SUSCEPTIBILITY 1 homolog

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011364	BRCA1
IPR018957	Zinc finger, C3HC4 RING-type
IPR002378	Breast cancer type I susceptibility protein
IPR017907	Zinc finger, RING-type, conserved site
IPR001357	BRCT
IPR001841	Zinc finger, RING-type
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Xu X, Weaver Z, Linke SP, Li C, Gotay J, Wang XW, Harris CC, Ried T, Deng CX. Centrosome amplification and a defective G2-M cell cycle checkpoint induce genetic instability in BRCA1 exon 11 isoform-deficient cells. Mol. Cell 3 389-95 1999 [PubMed: 10198641] http://dx.doi.org/10.1016/S1097-2765(00)80466-9
2.	Khavari PA, Peterson CL, Tamkun JW, Mendel DB, Crabtree GR. BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription. Nature 366 170-4 1993 [PubMed: 8232556] http://dx.doi.org/10.1038/366170a0
3.	Yu X, Chini CC, He M, Mer G, Chen J. The BRCT domain is a phospho-protein binding domain. Science 302 639-42 2003 [PubMed: 14576433] http://dx.doi.org/10.1126/science.1088753

Additional Reading Open in usermanual
	Shiozaki EN, Gu L, Yan N, Shi Y. Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling. Mol. Cell 14 2004 405-12 [PubMed: 15125843] http://dx.doi.org/10.1016/S1097-2765(04)00238-2
	Shen Y, Tong L. Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1. Biochemistry 47 2008 5767-73 [PubMed: 18452305] http://dx.doi.org/10.1021/bi800314m
	Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ. Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer. Nat. Struct. Mol. Biol. 11 2004 512-8 [PubMed: 15133502] http://dx.doi.org/10.1038/nsmb775
	Tischkowitz M, Hamel N, Carvalho MA, Birrane G, Soni A, van Beers EH, Joosse SA, Wong N, Novak D, Quenneville LA, Grist SA; kConFab, Nederlof PM, Goldgar DE, Tavtigian SV, Monteiro AN, Ladias JA, Foulkes WD. Pathogenicity of the BRCA1 missense variant M1775K is determined by the disruption of the BRCT phosphopeptide-binding pocket: a multi-modal approach. Eur. J. Hum. Genet. 16 2008 820-32 [PubMed: 18285836] http://dx.doi.org/10.1038/ejhg.2008.13
	Varma AK, Brown RS, Birrane G, Ladias JA. Structural basis for cell cycle checkpoint control by the BRCA1-CtIP complex. Biochemistry 44 2005 10941-6 [PubMed: 16101277] http://dx.doi.org/10.1021/bi0509651

InterPro 23.1