HUMAN:BRCA2

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Species (Taxon ID)	Homo sapiens (Human). ([1])
Gene Name(s)	BRCA2 (synonyms: FACD, FANCD1)
Protein Name(s)	Breast cancer type 2 susceptibility protein Fanconi anemia group D1 protein
External Links
EMBL	X95152 X95153 X95154 X95155 X95156 X95157 X95158 X95159 X95160 X95161 X95162 X95163 X95164 X95165 X95166 X95167 X95168 X95169 X95170 X95171 X95172 X95173 X95174 X95175 X95176 X95177 U43746 AY436640 AL137247 AL445212 AL445212 AL137247 Z74739 Z73359
IPI	IPI00412408
PIR	G02334
RefSeq	NP_000050.2
UniGene	Hs.34012
PDB	1N0W 3EU7
PDBsum	1N0W 3EU7
ProteinModelPortal	P51587
SMR	P51587
DIP	DIP-24214N
IntAct	P51587
MINT	MINT-1540184
STRING	P51587
PhosphoSite	P51587
PRIDE	P51587
Ensembl	ENST00000380152
GeneID	675
KEGG	hsa:675
NMPDR	fig\|9606.3.peg.8705
CTD	675
GeneCards	GC13P013701
HGNC	HGNC:1101
HPA	HPA026815
MIM	114480 227650 600185 605724 612555 613029 613347
neXtProt	NX_P51587
Orphanet	1333 1331 84 145 654
PharmGKB	PA25412
HOGENOM	HBG283145
HOVERGEN	HBG050731
InParanoid	P51587
OrthoDB	EOG4ZCT3K
Pathway_Interaction_DB	foxm1pathway
Reactome	REACT_216 REACT_27271
NextBio	2780
ArrayExpress	P51587
Bgee	P51587
CleanEx	HS_BRCA2
Genevestigator	P51587
GermOnline	ENSG00000139618
GO	GO:0033593 GO:0005813 GO:0005654 GO:0030141 GO:0043015 GO:0010484 GO:0010485 GO:0002020 GO:0003697 GO:0033205 GO:0051298 GO:0000724 GO:0033600 GO:0006289 GO:0045893 GO:0007090
InterPro	IPR015525 IPR015187 IPR015188 IPR002093 IPR011370 IPR015252 IPR016027 IPR015205
PANTHER	PTHR11289
Pfam	PF09169 PF09103 PF09104 PF00634 PF09121
PIRSF	PIRSF002397
SUPFAM	SSF81872 SSF50249
PROSITE	PS50138

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0000724	double-strand break repair via homologous recombination	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015187	P	Seeded From UniProt
	GO:0000724	double-strand break repair via homologous recombination	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015252	P	Seeded From UniProt
	GO:0000724	double-strand break repair via homologous recombination	PMID:20729832^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0000724	double-strand break repair via homologous recombination	Reactome:REACT_1874	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0002020	protease binding	PMID:15314155^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P51784	F	Seeded From UniProt
	GO:0003677	DNA binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0238	F	Seeded From UniProt
	GO:0003697	single-stranded DNA binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015252	F	Seeded From UniProt
	GO:0003697	single-stranded DNA binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000001475	F	Seeded From UniProt
	GO:0003697	single-stranded DNA binding	PMID:20729832^[1]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10373512^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P60896	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10373512^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P60896	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11597317^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q06609	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12242698^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P38398	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:12242698^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9GKK8	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15115758^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BXW9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15930293^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y5V3	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15967112^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q8N1V2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16099937^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P02768	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16275750^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q8N137	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17515903^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q06609	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18212739^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BXW9-2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19303847^[13]	IPI: Inferred from Physical Interaction	UniProtKB:Q06609	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19423707^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q86YC2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20729832^[1]	IPI: Inferred from Physical Interaction	UniProtKB:Q06609	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20729832^[1]	IPI: Inferred from Physical Interaction	UniProtKB:Q14565	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21399666^[15]	IPI: Inferred from Physical Interaction	UniProtKB:Q9P0W2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9774970^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P38398	F	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015252	C	Seeded From UniProt
	GO:0005634	nucleus	PMID:17286961^[17]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:18029348^[18]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:9560268^[19]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:9774970^[16]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005654	nucleoplasm	Reactome:REACT_1612	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005654	nucleoplasm	Reactome:REACT_21405	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:18029348^[18]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005813	centrosome	PMID:17286961^[17]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0006281	DNA repair	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011370	P	Seeded From UniProt
	GO:0006281	DNA repair	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0234	P	Seeded From UniProt
	GO:0006281	DNA repair	Reactome:REACT_216	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006289	nucleotide-excision repair	PMID:16845393^[20]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0006302	double-strand break repair	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002093	P	Seeded From UniProt
	GO:0006302	double-strand break repair	PMID:16845393^[20]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0006302	double-strand break repair	Reactome:REACT_2054	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006310	DNA recombination	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015252	P	Seeded From UniProt
	GO:0006310	DNA recombination	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0233	P	Seeded From UniProt
	GO:0006310	DNA recombination	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000001475	P	Seeded From UniProt
	GO:0006974	response to DNA damage stimulus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0227	P	Seeded From UniProt
	GO:0007049	cell cycle	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0131	P	Seeded From UniProt
	GO:0007090	regulation of S phase of mitotic cell cycle	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015252	P	Seeded From UniProt
	GO:0007090	regulation of S phase of mitotic cell cycle	PMID:9774970^[16]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0007283	spermatogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000001475	P	Seeded From UniProt
	GO:0007584	response to nutrient	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000001475	P	Seeded From UniProt
	GO:0010484	H3 histone acetyltransferase activity	PMID:9619837^[21]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0010485	H4 histone acetyltransferase activity	PMID:9619837^[21]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0030141	stored secretory granule	PMID:8589722^[22]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0030879	mammary gland development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000001475	P	Seeded From UniProt
	GO:0031619	homologous chromosome orientation involved in meiotic metaphase I plate congression	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000001475	P	Seeded From UniProt
	GO:0032355	response to estradiol stimulus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000001475	P	Seeded From UniProt
	GO:0033205	cell cycle cytokinesis	PMID:17286961^[17]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0033593	BRCA2-MAGE-D1 complex	PMID:15930293^[7]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0033600	negative regulation of mammary gland epithelial cell proliferation	PMID:15930293^[7]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0035264	multicellular organism growth	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000001475	P	Seeded From UniProt
	GO:0043015	gamma-tubulin binding	PMID:17286961^[17]	IPI: Inferred from Physical Interaction	UniProtKB:P23258	F	Seeded From UniProt
	GO:0043234	protein complex	PMID:9774970^[16]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0043966	histone H3 acetylation	PMID:9619837^[21]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043967	histone H4 acetylation	PMID:9619837^[21]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0045893	positive regulation of transcription, DNA-dependent	PMID:9126734^[23]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0051298	centrosome duplication	PMID:17286961^[17]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0004402	histone acetyltransferase activity	PMID:9824164^[24]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0005730	nucleolus	PMID:18029348^[18]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Jensen RB et al. (2010) Purified human BRCA2 stimulates RAD51-mediated recombination. Nature 467: 678-83 PubMed GONUTS page
↑ Schoenfeld AR et al. (2004) BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage. Mol Cell Biol 24: 7444-55 PubMed GONUTS page
↑ ^3.0 ^3.1 Marston NJ et al. (1999) Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals. Mol Cell Biol 19: 4633-42 PubMed GONUTS page
↑ Orelli BJ & Bishop DK (2001) BRCA2 and homologous recombination. Breast Cancer Res 3: 294-8 PubMed GONUTS page
↑ ^5.0 ^5.1 Daniel DC (2002) Highlight: BRCA1 and BRCA2 proteins in breast cancer. Microsc Res Tech 59: 68-83 PubMed GONUTS page
↑ Hussain S et al. (2004) Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways. Hum Mol Genet 13: 1241-8 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Tian XX et al. (2005) BRCA2 suppresses cell proliferation via stabilizing MAGE-D1. Cancer Res 65: 4747-53 PubMed GONUTS page
↑ Silva FP et al. (2005) WDRPUH, a novel WD-repeat-containing protein, is highly expressed in human hepatocellular carcinoma and involved in cell proliferation. Neoplasia 7: 348-55 PubMed GONUTS page
↑ Lowenthal MS et al. (2005) Analysis of albumin-associated peptides and proteins from ovarian cancer patients. Clin Chem 51: 1933-45 PubMed GONUTS page
↑ Zou C et al. (2005) Centrobin: a novel daughter centriole-associated protein that is required for centriole duplication. J Cell Biol 171: 437-45 PubMed GONUTS page
↑ Davies OR & Pellegrini L (2007) Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats. Nat Struct Mol Biol 14: 475-83 PubMed GONUTS page
↑ Wilson JB et al. (2008) FANCG promotes formation of a newly identified protein complex containing BRCA2, FANCD2 and XRCC3. Oncogene 27: 3641-52 PubMed GONUTS page
↑ Carreira A et al. (2009) The BRC repeats of BRCA2 modulate the DNA-binding selectivity of RAD51. Cell 136: 1032-43 PubMed GONUTS page
↑ Sy SM et al. (2009) PALB2 regulates recombinational repair through chromatin association and oligomerization. J Biol Chem 284: 18302-10 PubMed GONUTS page
↑ Lee M et al. (2011) A mitotic function for the high-mobility group protein HMG20b regulated by its interaction with the BRC repeats of the BRCA2 tumor suppressor. Oncogene 30: 3360-9 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Chen J et al. (1998) Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells. Mol Cell 2: 317-28 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 Nakanishi A et al. (2007) Interference with BRCA2, which localizes to the centrosome during S and early M phase, leads to abnormal nuclear division. Biochem Biophys Res Commun 355: 34-40 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page
↑ Chen PL et al. (1998) The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment. Proc Natl Acad Sci U S A 95: 5287-92 PubMed GONUTS page
↑ ^20.0 ^20.1 Cipak L et al. (2006) The role of BRCA2 in replication-coupled DNA interstrand cross-link repair in vitro. Nat Struct Mol Biol 13: 729-33 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 Siddique H et al. (1998) The BRCA2 is a histone acetyltransferase. Oncogene 16: 2283-5 PubMed GONUTS page
↑ Jensen RA et al. (1996) BRCA1 is secreted and exhibits properties of a granin. Nat Genet 12: 303-8 PubMed GONUTS page
↑ Milner J et al. (1997) Transcriptional activation functions in BRCA2. Nature 386: 772-3 PubMed GONUTS page
↑ Fuks F et al. (1998) BRCA2 associates with acetyltransferase activity when bound to P/CAF. Oncogene 17: 2531-4 PubMed GONUTS page

[PMID:20729832-0] 1.0 ^1.1 ^1.2 ^1.3 Jensen RB et al. (2010) Purified human BRCA2 stimulates RAD51-mediated recombination. Nature 467: 678-83 PubMed GONUTS page

[PMID:15314155-1] Schoenfeld AR et al. (2004) BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage. Mol Cell Biol 24: 7444-55 PubMed GONUTS page

[PMID:10373512-2] 3.0 ^3.1 Marston NJ et al. (1999) Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals. Mol Cell Biol 19: 4633-42 PubMed GONUTS page

[PMID:11597317-3] Orelli BJ & Bishop DK (2001) BRCA2 and homologous recombination. Breast Cancer Res 3: 294-8 PubMed GONUTS page

[PMID:12242698-4] 5.0 ^5.1 Daniel DC (2002) Highlight: BRCA1 and BRCA2 proteins in breast cancer. Microsc Res Tech 59: 68-83 PubMed GONUTS page

[PMID:15115758-5] Hussain S et al. (2004) Direct interaction of FANCD2 with BRCA2 in DNA damage response pathways. Hum Mol Genet 13: 1241-8 PubMed GONUTS page

[PMID:15930293-6] 7.0 ^7.1 ^7.2 Tian XX et al. (2005) BRCA2 suppresses cell proliferation via stabilizing MAGE-D1. Cancer Res 65: 4747-53 PubMed GONUTS page

[PMID:15967112-7] Silva FP et al. (2005) WDRPUH, a novel WD-repeat-containing protein, is highly expressed in human hepatocellular carcinoma and involved in cell proliferation. Neoplasia 7: 348-55 PubMed GONUTS page

[PMID:16099937-8] Lowenthal MS et al. (2005) Analysis of albumin-associated peptides and proteins from ovarian cancer patients. Clin Chem 51: 1933-45 PubMed GONUTS page

[PMID:16275750-9] Zou C et al. (2005) Centrobin: a novel daughter centriole-associated protein that is required for centriole duplication. J Cell Biol 171: 437-45 PubMed GONUTS page

[PMID:17515903-10] Davies OR & Pellegrini L (2007) Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats. Nat Struct Mol Biol 14: 475-83 PubMed GONUTS page

[PMID:18212739-11] Wilson JB et al. (2008) FANCG promotes formation of a newly identified protein complex containing BRCA2, FANCD2 and XRCC3. Oncogene 27: 3641-52 PubMed GONUTS page

[PMID:19303847-12] Carreira A et al. (2009) The BRC repeats of BRCA2 modulate the DNA-binding selectivity of RAD51. Cell 136: 1032-43 PubMed GONUTS page

[PMID:19423707-13] Sy SM et al. (2009) PALB2 regulates recombinational repair through chromatin association and oligomerization. J Biol Chem 284: 18302-10 PubMed GONUTS page

[PMID:21399666-14] Lee M et al. (2011) A mitotic function for the high-mobility group protein HMG20b regulated by its interaction with the BRC repeats of the BRCA2 tumor suppressor. Oncogene 30: 3360-9 PubMed GONUTS page

[PMID:9774970-15] 16.0 ^16.1 ^16.2 ^16.3 Chen J et al. (1998) Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells. Mol Cell 2: 317-28 PubMed GONUTS page

[PMID:17286961-16] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 Nakanishi A et al. (2007) Interference with BRCA2, which localizes to the centrosome during S and early M phase, leads to abnormal nuclear division. Biochem Biophys Res Commun 355: 34-40 PubMed GONUTS page

[PMID:18029348-17] 18.0 ^18.1 ^18.2 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page

[PMID:9560268-18] Chen PL et al. (1998) The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment. Proc Natl Acad Sci U S A 95: 5287-92 PubMed GONUTS page

[PMID:16845393-19] 20.0 ^20.1 Cipak L et al. (2006) The role of BRCA2 in replication-coupled DNA interstrand cross-link repair in vitro. Nat Struct Mol Biol 13: 729-33 PubMed GONUTS page

[PMID:9619837-20] 21.0 ^21.1 ^21.2 ^21.3 Siddique H et al. (1998) The BRCA2 is a histone acetyltransferase. Oncogene 16: 2283-5 PubMed GONUTS page

[PMID:8589722-21] Jensen RA et al. (1996) BRCA1 is secreted and exhibits properties of a granin. Nat Genet 12: 303-8 PubMed GONUTS page

[PMID:9126734-22] Milner J et al. (1997) Transcriptional activation functions in BRCA2. Nature 386: 772-3 PubMed GONUTS page

[PMID:9824164-23] Fuks F et al. (1998) BRCA2 associates with acetyltransferase activity when bound to P/CAF. Oncogene 17: 2531-4 PubMed GONUTS page

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HUMAN:BRCA2

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