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Protein Page:
BRCA2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
BRCA2 involved in double-strand break repair and/or homologous recombination. May participate in S phase checkpoint activation. Interacts with RAD51 and DSS1. Interacts with ubiquitinated FANCD2. Interacts with PALB2, enables the recombinational repair and checkpoint functions. Interacts with WDR16. Defects in BRCA2 are a cause of genetic susceptibility to breast cancer and may underlie susceptibility to uveal melanoma. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; Nuclear receptor co-regulator
Cellular Component: nucleoplasm; centrosome; protein complex; cytoplasm; nucleolus; BRCA2-MAGE-D1 complex; nucleus; secretory granule
Molecular Function: protein binding; gamma-tubulin binding; H4 histone acetyltransferase activity; histone acetyltransferase activity; protease binding; H3 histone acetyltransferase activity; single-stranded DNA binding
Biological Process: positive regulation of transcription, DNA-dependent; cytokinesis; cell aging; positive regulation of mitotic cell cycle; DNA repair; regulation of cytokinesis; oocyte maturation; inner cell mass cell proliferation; negative regulation of mammary gland epithelial cell proliferation; response to UV-C; double-strand break repair via homologous recombination; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; male meiosis I; nucleotide-excision repair; double-strand break repair; response to gamma radiation; replication fork protection; spermatogenesis; hemopoiesis; brain development; DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; centrosome duplication; female gonad development; response to X-ray
Reference #:  P51587 (UniProtKB)
Alt. Names/Synonyms: BRCA1/BRCA2-containing complex, subunit 2; BRCA2; BRCC2; breast and ovarian cancer susceptibility gene, early onset; breast cancer 2 tumor suppressor; breast cancer 2, early onset; breast cancer susceptibility protein BRCA2; Breast cancer type 2 susceptibility protein; BROVCA2; FACD; FAD; FAD1; FANCB; FANCD; FANCD1; Fanconi anemia group D1 protein; GLM3; PNCA2
Gene Symbols: BRCA2
Molecular weight: 384,225 Da
Basal Isoelectric point: 6.3  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

BRCA2

Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S3291‑p
chromatin organization, altered: S3291‑p
molecular association, regulation: S3291‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 9 S70-p KTPQRKPsyNQLASt
0 3 Y71-p TPQRKPsyNQLAStP
1 3 T77-p syNQLAStPIIFKEQ
0 4 S93-p LTLPLYQsPVKELDK
0 6 T167-p VCGSLFHtPKFVKGR
2 1 S193-p AEVDPDMsWSSSLAT
1 1 T203-p SSLATPPtLsstVLI
1 1 S205-p LATPPtLsstVLIVR
1 1 S206-p ATPPtLsstVLIVRN
1 1 T207-p TPPtLsstVLIVRNE
0 1 F221 EEASETVFPHDTTAN
0 1 T225 ETVFPHDTTANVKSY
1 1 S239-p YFSNHDEsLKKNDRF
0 1 S384-p ESGSDKIsKEVVPSL
0 1 S445-p DFLTSENsLPRISSL
0 1 K454-a PRISSLPkSEKPLNE
0 1 S492-p KQAISGTsPVASSFQ
0 1 S497 GTsPVASSFQGIKKS
0 2 S519-p PKETFNAsFSGHMTD
0 2 S683-p CSNNTVIsQDLDYKE
0 1 S755-p YSDTDFQsQKSLLYD
0 6 S805-p LKGNNYEsDVELTKN
0 2 Y949-p SIKKDLVyVLAEENK
0 2 K1536-a GKKVKIAkESLDKVK
0 1 K1872-u IFTDSFSkVIKENNE
0 1 S1926-p KVFADIQsEEILQHN
0 1 S1943-p MSGLEKVskISPCDV
0 2 K1944-u SGLEKVskISPCDVS
0 1 S1970-p GKLHKSVsSANTCGI
0 2 T2035-p EENTAIRtPEHLISQ
0 1 S2095-p TEHSLHYsPTSRQNV
0 2 K2316 STPDGTIKDRRLFMH
0 1 R3005 SLLTEGKRYRIyHLA
0 1 Y3009-p EGKRYRIyHLATSKS
0 5 T3242-p AKRKSVStPVSAQMT
4 0 S3291-p SPICTFVsPAAQKAF
0 1 S3319-p IKKKELNsPQMTPFK
  mouse

 
P70 KTPQRNPPYHQFAST
Y71 TPQRNPPYHQFASTP
T77 PYHQFASTPIMFKER
S93 QTLPLDQSPFRELGK
T160 VSGSLFYTPKLKEGQ
S185 VEVDPDMSWTSSLAT
T195 SSLATPPTLSSTVLI
S197 LATPPTLSSTVLIAR
S198 ATPPTLSSTVLIARD
T199 TPPTLSSTVLIARDE
T213-p EEARSSVtPADsPAT
S217-p SSVtPADsPATLKSC
S231 CFSNHNESPQKNDRS
C376 YSQNEEICNEAVQCS
S435 GSITSEKSLPHISSL
E444 PHISSLPEPEKMFSE
S481 KQMVSRTSQAACLsP
S487-p TSQAACLsPSIRKSI
V508 LDETLGTVFSDSMTN
S666 SYIHALISQDLNDKE
S735 LSSISFESQENPLGD
V784 LQCESCKVNIELSKN
H930 SDSLAVVHDYTEKSR
Q1510 GKKVKIMQESLDKVK
K1834 IVTDNCYKIVEQNRQ
- gap
- gap
K1898 QSMSGLKKAATPPVG
H1923 REPPQAAHPSRTYGI
S1988 RENSVVHSTQGVLSL
S2048-p TEHTLQHsPIPEDVS
K2264-u STPDGTVkDRSLFTH
R2924-m2 SLLTEGKrYRIYHLA
Y2928 EGKrYRIYHLAVSKS
L3165 LKGKSMPLAHSAQMA
S3214 SPICTFVSPAAQKAF
P3242 IKKEPSSPRRRTPFQ
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