RNF169
entrez
254225
canonical
uniprot
Q8NCN4
canonical
ensembl
ENSG00000166439
resolver
ensp
ENSP00000299563
resolver
ensp
ENSP00000581326
resolver
enst
ENST00000299563
resolver
genesymbol
RNF169
resolver
genesymbol_syn
KIAA1991
resolver
hgnc
HGNC:26961
resolver
uniprot
Q6N015
resolver
uniprot_entry
RN169_HUMAN
resolver
uniprot_sec
Q6N015
resolver
amino_acid_sequence
MAAAGPSTRASSAAAAAALSRRGRRGRCDETAAAKTGAPGPASGPSLLVLSPPLLQPPLPPRPEESGCAGCLEPPGEAAALPCGHSLCRGCAQRAADAAGPGCPRCRARGPGWARRRARDDGQADSEVLGECARRSQPERCRPRRDGGAAAAGPRPEQEPRAAPAEPDFIFRAPIKLSKPGELREEYESLRKLREEKLQEEKPSEDQIHKLLPEDTETGKRKMDEQKKRDEPLVLKTNLERCPARLSDSENEEPSRGQMTQTHRSAFVSKNNSYSLAFLAGKLNSKVERSQSCSDTAQERAKSRVRAVPGNKAKVTTMTPASNPIIGVLLSTQNNRCVSAPDLTIEKRLPFSSLSSLASLHKPERSVSPESNDSISEELNHFKPIVCSPCTPPKRLPDGRVLSPLIIKSTPRNLNRSLQKQTSYEASPRILKKWEQIFQERQIKKTLSKATLTSLAPEMGEELLGSEGIHSSKEKPLVAVNTRLSGGQVLSEYTGPTSADLDHFPSVSQTKAEQDSDNKSSTEIPLETCCSSELKGGGSGTSLEREQFEGLGSTPDAKLDKTCISRAMKITTVNSVLPQNSVLGGVLKTKQQLKTLNHFDLTNGVLVESLSEEPLPSLRRGRKRHCKTKHLEQNGSLKKLRQTSGEVGLAPTDPVLREMEQKLQQEEEDRQLALQLQRMFDNERRTVSRRKGSVDQYLLRSSNMAGAK
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization (PubMed:22492721, PubMed:30773093). Once recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby favouring homologous recombination repair (HRR) and single-strand annealing (SSA) instead of non-homologous end joining (NHEJ) mediated by TP53BP1 (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair. {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822, ECO:0000269|PubMed:22742833, ECO:0000269|PubMed:30104380, ECO:0000269|PubMed:30773093}.
uniprot
proteins
mass_dalton
77194
uniprot
proteins
mutagenesis
MUTAGEN 68; /note="C->S: Does not affect recruitment to DSBs nor ability to inhibit DSBs repair."; /evidence="ECO:0000269|PubMed:22742833"; MUTAGEN 368; /note="S->A: About 90% loss of phosphorylation by DYRK1A; when associated with A-403."; /evidence="ECO:0000269|PubMed:30773093"; MUTAGEN 403; /note="S->A: About 90% loss of phosphorylation by DYRK1A; when associated with A-368."; /evidence="ECO:0000269|PubMed:30773093"; MUTAGEN 673; /note="A->G: Abolishes ubiquitin-binding."; /evidence="ECO:0000269|PubMed:22742833"; MUTAGEN 689; /note="R->A: Impairs recruitment to DSBs."; /evidence="ECO:0000269|PubMed:22742833"; MUTAGEN 691; /note="K->A: Impairs recruitment to DSBs."; /evidence="ECO:0000269|PubMed:22742833"; MUTAGEN 697; /note="Y->A: Impairs recruitment to DSBs."; /evidence="ECO:0000269|PubMed:22742833"; MUTAGEN 699..700; /note="LR->AA: Does not affect ubiquitin-binding but abolishes recruitment to DSBs."; /evidence="ECO:0000269|PubMed:22742833
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by DYRK1A; phosphorylation increases RNF169 ability to block accumulation of TP53BP1 at the DSB sites. {ECO:0000269|PubMed:33469661}.
uniprot
proteins
protein_family
RNF169 family
uniprot
proteins
pubmed
12056414
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
22492721
uniprot
proteins
pubmed
22733822
uniprot
proteins
pubmed
22742833
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30104380
uniprot
proteins
pubmed
30773093
uniprot
proteins
pubmed
33469661
uniprot
proteins
sequence_length
708
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30104380, ECO:0000269|PubMed:30773093}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822, ECO:0000269|PubMed:22742833}. Note=Localizes to sites of double-strand breaks (DSBs) following DNA damage. Recruited to DSBs via recognition of RNF168-dependent ubiquitin products. {ECO:0000269|PubMed:30104380}.
uniprot
proteins