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InterPro: IPR001357 BRCT

Protein matches Help

UniProtKB

Matches:

4502 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

IPR001357 BRCT

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00533	BRCT	3578
PROSITE profile	PS50172	BRCT	4035
SMART	SM00292	BRCT	3791
SuperFamily	SSF52113	BRCT	4267
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001679 NAD-dependent DNA ligase
IPR001726 DNA nucleotidylexotransferase
IPR002378 Breast cancer type I susceptibility protein
IPR008288 NAD+ ADP-ribosyltransferase
IPR011364 BRCA1
IPR012112 DNA repair protein, Rev1
IPR012178 DNA replication factor C, large subunit
IPR016592 Nibrin

GO Term annotation Help

Component

GO:0005622 intracellular

InterPro annotation

Entry Details in BioMart

Abstract

The BRCT domain (after the C_terminal domain of a breast cancer susceptibility protein) is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage [1], for example as found in the breast cancer DNA-repair protein BRCA1. The domain is an approximately 100 amino acid tandem repeat, which appears to act as a phospho-protein binding domain [2].

A chitin biosynthesis protein from yeast also seems to belong to this group.

Structural links Help

PDB - click here

SCOP: a.60.2.2 , c.15.1.1 , c.15.1.2 , c.15.1.3 , c.15.1.4 , c.15.1.5

CATH: 1.10.150.20 , 3.40.50.10190

Database links Help

Enzyme: EC:6.5.1

PROSITE doc: PDOC50172

PANDIT: PF00533

Blocks: IPB001357

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001357

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00541 Pescadillo homolog

P09838 DNA nucleotidylexotransferase

P11938 DNA-binding protein RAP1

P35600 Replication factor C subunit 1

P41882 Ankyrin repeat-containing protein F37A4.4

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002054	DNA-directed DNA polymerase, family X
IPR014778	Myb, DNA-binding
IPR013725	DNA replication factor RFC1, C-terminal
IPR012287	Homeodomain-related
IPR012178	DNA replication factor C, large subunit
IPR001005	SANT, DNA-binding
IPR002110	Ankyrin repeat
IPR001357	BRCT
IPR019843	DNA polymerase family X, binding site
IPR003125	Protein of unknown function WSN
IPR003959	ATPase, AAA-type, core
IPR010996	DNA-directed DNA polymerase, family X, beta-like, N-terminal
IPR002934	Nucleotidyltransferase
IPR003593	ATPase, AAA+ type, core
IPR008921	DNA polymerase III, clamp loader complex, gamma/delta/delta subunit, C-terminal
IPR017930	HTH transcriptional regulator, Myb-type, DNA-binding
IPR020683	Ankyrin repeat-containing domain
IPR001726	DNA nucleotidylexotransferase
IPR015280	Rap1, DNA-binding
IPR018944	DNA polymerase lambda, fingers domain
IPR010613	Pescadillo, N-terminal
IPR009057	Homeodomain-like
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Bork P, Hofmann K, Bucher P, Neuwald AF, Altschul SF, Koonin EV. A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins. FASEB J. 11 68-76 1997 [PubMed: 9034168] http://www.fasebj.org/cgi/content/abstract/11/1/68
2.	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
	Oishi H, Kitagawa H, Wada O, Takezawa S, Tora L, Kouzu-Fujita M, Takada I, Yano T, Yanagisawa J, Kato S. An hGCN5/TRRAP histone acetyltransferase complex co-activates BRCA1 transactivation function through histone modification. J. Biol. Chem. 281 2006 20-6 [PubMed: 16260778] http://dx.doi.org/10.1074/jbc.M510157200
	Simbulan-Rosenthal CM, Rosenthal DS, Luo R, Samara R, Espinoza LA, Hassa PO, Hottiger MO, Smulson ME. PARP-1 binds E2F-1 independently of its DNA binding and catalytic domains, and acts as a novel coactivator of E2F-1-mediated transcription during re-entry of quiescent cells into S phase. Oncogene 22 2003 8460-71 [PubMed: 14627987] http://dx.doi.org/10.1038/sj.onc.1206897
	Zhang X, Morera S, Bates PA, Whitehead PC, Coffer AI, Hainbucher K, Nash RA, Sternberg MJ, Lindahl T, Freemont PS. Structure of an XRCC1 BRCT domain: a new protein-protein interaction module. EMBO J. 17 1998 6404-11 [PubMed: 9799248] http://dx.doi.org/10.1093/emboj/17.21.6404
	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
	Williams RS, Lee MS, Hau DD, Glover JN. Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1. Nat. Struct. Mol. Biol. 11 2004 519-25 [PubMed: 15133503] http://dx.doi.org/10.1038/nsmb776
	Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25 1997 3389-402 [PubMed: 9254694] http://dx.doi.org/10.1093/nar/25.17.3389
	Callebaut I, Mornon JP. From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair. FEBS Lett. 400 1997 25-30 [PubMed: 9000507] http://dx.doi.org/10.1016/S0014-5793(96)01312-9
	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
	Koonin EV, Altschul SF, Bork P. BRCA1 protein products ... Functional motifs... Nat. Genet. 13 1996 266-8 [PubMed: 8673121] http://dx.doi.org/10.1038/ng0796-266
	Du LL, Moser BA, Russell P. Homo-oligomerization is the essential function of the tandem BRCT domains in the checkpoint protein Crb2. J. Biol. Chem. 279 2004 38409-14 [PubMed: 15229228] http://dx.doi.org/10.1074/jbc.M403326200
	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
	Schmidt U, Wollmann Y, Franke C, Grosse F, Saluz HP, Hanel F. Characterization of the interaction between the human DNA topoisomerase IIbeta-binding protein 1 (TopBP1) and the cell division cycle 45 (Cdc45) protein. Biochem. J. 409 2008 169-77 [PubMed: 17887956] http://dx.doi.org/10.1042/BJ20070872
	Moreau K, Dizin E, Ray H, Luquain C, Lefai E, Foufelle F, Billaud M, Lenoir GM, Venezia ND. BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase. J. Biol. Chem. 281 2006 3172-81 [PubMed: 16326698] http://dx.doi.org/10.1074/jbc.M504652200

InterPro 23.1