RN169_BOVIN
ID RN169_BOVIN Reviewed; 689 AA.
AC F1MRW8;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=E3 ubiquitin-protein ligase RNF169;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 169;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF169 {ECO:0000305};
GN Name=RNF169;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase that acts as a regulator
CC of double-strand breaks (DSBs) repair following DNA damage. Functions
CC in a non-canonical fashion to harness RNF168-mediated protein
CC recruitment to DSB-containing chromatin, thereby contributing to
CC regulation of DSB repair pathway utilization. Once recruited to DSB
CC repair sites by recognizing and binding ubiquitin catalyzed by RNF168,
CC competes with TP53BP1 and BRCA1 for association with RNF168-modified
CC chromatin, thereby favouring homologous recombination repair (HRR) and
CC single-strand annealing (SSA) instead of non-homologous end joining
CC (NHEJ) mediated by TP53BP1. E3 ubiquitin-protein ligase activity is not
CC required for regulation of DSBs repair. {ECO:0000250|UniProtKB:Q8NCN4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DYRK1B. {ECO:0000250|UniProtKB:Q8NCN4}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8NCN4}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NCN4}. Note=Localizes to
CC sites of double-strand breaks (DSBs) following DNA damage. Recruited to
CC DSBs via recognition of RNF168-dependent ubiquitin products.
CC {ECO:0000250|UniProtKB:Q8NCN4}.
CC -!- DOMAIN: The MIU motif (motif interacting with ubiquitin) mediates the
CC interaction with both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains.
CC The UMI motif also mediates interaction with ubiquitin. The specificity
CC for different types of ubiquitin is mediated by juxtaposition of
CC ubiquitin-binding motifs (MIU and UMI motifs) with LR motifs (LRMs).
CC {ECO:0000250|UniProtKB:Q8NCN4}.
CC -!- PTM: Phosphorylated by DYRK1A; phosphorylation increases RNF169 ability
CC to block accumulation of TP53BP1 at the DSB sites.
CC {ECO:0000250|UniProtKB:Q8NCN4}.
CC -!- SIMILARITY: Belongs to the RNF169 family. {ECO:0000305}.
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DR EMBL; DAAA02041058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02041059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002693509.1; XM_002693463.2.
DR RefSeq; XP_015322062.1; XM_015466576.1.
DR AlphaFoldDB; F1MRW8; -.
DR SMR; F1MRW8; -.
DR STRING; 9913.ENSBTAP00000000969; -.
DR PaxDb; F1MRW8; -.
DR eggNOG; KOG4159; Eukaryota.
DR InParanoid; F1MRW8; -.
DR OrthoDB; 1189777at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA damage; DNA repair; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..689
FT /note="E3 ubiquitin-protein ligase RNF169"
FT /id="PRO_0000418008"
FT ZN_FING 49..88
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 95..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..194
FT /note="UMI motif"
FT MOTIF 646..663
FT /note="MIU motif"
FT MOTIF 670..682
FT /note="LR motif"
FT COMPBIAS 95..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT CROSSLNK 267
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT CROSSLNK 343
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
SQ SEQUENCE 689 AA; 75630 MW; EED38AD9E60643CF CRC64;
MSGRAKVAGE EALVGVAAPQ PVPAGILDEC TNVTVSQPPS PPRPEESDCA GCLETPGEAA
ALPCGHSLCR GCAQRAADAA GPCCPRCRAR GAGWARRRAR DDWQADAEVL GERARRGPPE
RCRPRRDGGA AAAGPRPEQE SRAAPAEPEF IFRAPIKLSK PGEFREEYES LRKLREEKLQ
EEKTSEDQIH KLLPEDTEIG KRKMDEQKKR DEPVVLKTNL EHCPARLSDS ENEEPSRGKM
IQTHRSAFVS KSSSYSLAFL AGNLNSKMER SQSCSDTGQD RAKSRLRAAP TSKAKATAMT
PTSNPIIGVL LSTRNHRCLS APDLTVEKRL PFSSLSALAS LHKPERSISP ESNDSISEEL
NHFKPIVCSP CTPPKRLPDG RVLSPLIIKS TPRNLNRSLQ KQTSYEASPR ILKKWEQIFQ
ERQIKKTLSK ATLTSLAPET GDDLLVSEVT QSNKEKPLLA LNTRLSSGQV LSECTGPTAP
DLDYFSSVSQ TKAEQGSDRK KNTEIPLETC CSSELPVGAS GTSLEREQSE RSGSSPDAKL
DKTRITASMK ISAVNSVLPK NSVLGGVLKT KKQLKTVNHF DLPNGVLADN LGDEPLPSLR
RGRKRRCKTK HLEQNGSLKK LRQSSGEVGL APTDPVLREM EQKLQQEEED RQLALQLQRM
FDNERRTVSR RKGSVDQYLL RSSSMAGAK
