Rbbp8
entrez
225182
canonical
uniprot
Q80YR6
canonical
ensembl
ENSMUSG00000041238
resolver
ensp
ENSMUSP00000046255
resolver
ensp
ENSMUSP00000111527
resolver
ensp
ENSMUSP00000332261
resolver
enst
ENSMUST00000047322
resolver
enst
ENSMUST00000115861
resolver
genesymbol
Rbbp8
resolver
genesymbol_syn
Ctip
resolver
uniprot_entry
CTIP_MOUSE
resolver
amino_acid_sequence
MSISGSGCGSPNSADASNDFKELWTKLKEYHDKEVQGLQVKVTKLKKERILDAQRLEEFFTKNQQLRDQQKVLQETIKILEDRLRAGLCDRCAVTEEHMHKKQQEFENIRQQNLKLITELMNEKNTLQEENKKLSEQLQQKMENGQQDQVAELACEENIIPDSPVTSFSFSGINRLRKKENLHVRYVEQTHTKLERSLCTNELRKISKDSAPAPVNSEEHEILVADTCDQNHSPLSKICETSSYPTDKTSFNLDTVVAETLGLNGQEESEPQGPMSPLGSELYHCLKEDHKKHPFMESARSKEDSLRFSDSASKTPPQEFTTRASSPVFGATSTVKAHLGLNTSFSPSLLDIGKKNLLKTAPFSNIAVSRSEKVRSKSEDNALFTQHSLGSEVKVISQSFSSKQILTNKTVSDSVDEQCSADHMNTTVADKYLVPLKSLGGKASKRKRTEEESEHAVKCPQACFDKENALPFPMENQFSMNGDHVMDKPLDLSDRFAATQRQEKNHGNETSKNKLKQATIYEALKPIPKGSSSGRKALSGDCMPAKDSWETYCLQPRSLQSSSKFSPDQKTPLQIKEENPVFKTPPCSQESLETENLFGDVKGTGSLVPTKVKSRAVHGGCELASVLQLNPCRVAKTKALPSNQDTSFENIQWSVDPGADLSQYKMDVTVIDTKDSSHSRLGGETVDMDCTLVSETVLLKMKKQEQKERSPNGDIKMNDSLEDMFDRTTHEEYESCLADSFSQVPDEEELPDTTKKTNIPADKQDGVKQKAFVGPYFKDKERETSIQNFPHIEVVRKKEERRKLLGHTCKECEIYYADLPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCLERGYIKEDLDLSPRPKRRQPYNAVFSPKGKEQRT
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
FUNCTION: Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (By similarity). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (By similarity). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (By similarity). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (By similarity). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA (By similarity). Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (By similarity). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (PubMed:21131978, PubMed:21131982). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging (By similarity). {ECO:0000250|UniProtKB:Q99708, ECO:0000269|PubMed:21131978, ECO:0000269|PubMed:21131982}.
uniprot
proteins
mass_dalton
100831
uniprot
proteins
post_translational_modification
PTM: Hyperphosphorylation upon ionizing radiation results in dissociation from BRCA1. Phosphorylation at Thr-843 by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylation at Thr-843 and Thr-855 promote interaction with NBN and recruitment to double-strand breaks (DSBs). Phosphorylated on Ser-326 as cells enter G2 phase. Phosphorylated at Ser-326 as cells enter G2 phase. This phosphorylation is required for binding BRCA1 and for the G2/M DNA damage transition checkpoint control (By similarity). Phosphorylation at Thr-315 is required for PIN1-binding, while phosphorylation at Ser-276 serves as a PIN1 isomerization site. Phosphorylation at Thr-315 is cell-cycle dependent. It steadily increases during S phase, peaks at late S/G2 phase, and drops at G1 (By similarity). Phosphorylation is not required for tetramerization (By similarity). Binds to DNA more strongly when dephosphorylated (By similarity). {ECO:0000250|UniProtKB:Q99708}.; PTM: Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via its N-terminal RING domain) does not lead to its proteasomal degradation but instead the ubiquitinated RBBP8 binds to chromatin following DNA damage and may play a role in G2/M checkpoint control. Ubiquitinated by RNF138 at its N-terminus. Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation. Ubiquitinated by the E3 FZR1/APC/C complex; this modification leads to proteasomal degradation. {ECO:0000250|UniProtKB:Q99708}.
uniprot
proteins
protein_family
COM1/SAE2/CtIP family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20829486
uniprot
proteins
pubmed
21131978
uniprot
proteins
pubmed
21131982
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23353824
uniprot
proteins
pubmed
30975768
uniprot
proteins
sequence_length
893
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99708}. Chromosome {ECO:0000250|UniProtKB:Q99708}. Note=Associates with sites of DNA damage in S/G2 phase. Recruited to DSBs by the MRE11-RAD50-NBN (MRN) complex following phosphorylation by CDK1, which promotes interaction with NBN. Ubiquitinated RBBP8 binds to chromatin following DNA damage. {ECO:0000250|UniProtKB:Q99708}.
uniprot
proteins