Sequence Browser (P38398-3)

UniProt (Ref Seq)
Displayed Structure
Experimental Tertiary/Complex (PDB:XRay/EM)
Experimental Tertiary/Complex (PDB:NMR)
Modelled Tertiary (Phyre)
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1
1863
Isoform
Remark
Ref
May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
VSP_047891
No experimental confirmation available. Ref.8 (AAI15038) sequence is in conflict in position: 1461:N->D.
VSP_055404
No experimental confirmation available.
VSP_035399 VSP_043797 VSP_043798
P38398-3  
VSP_035399 VSP_043797
No experimental confirmation available. The N-terminus is confirmed by several cDNAs.
VSP_057569
Produced by alternative initiation at Met-18 of isoform 1.
VSP_035396
VSP_035398
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Protein:
Other Names:
RING finger protein 53, RING-type E3 ubiquitin transferase BRCA1
Primary Accession:
Other Accessions:
E9PFZ0, O15129, Q1RMC1, Q3LRJ0, Q3LRJ6, Q6IN79, Q7KYU9
Gene :
BRCA1*, synonyms (RNF53)
Organism :
Human
Entry Name :
Length :
1,863
Mass (Da) :
207,721
Last modified :
01-Jan-1995
Version :
v2
Isoforms :
8 
Structures :
Experimental 0 | Phyre prediction 4

E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor 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. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. 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. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator (PubMed:20160719).