RN169_MOUSE
ID RN169_MOUSE Reviewed; 694 AA.
AC E9Q7F2; Q69Z47;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
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; Synonyms=Kiaa1991;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-694.
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AC113298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173319; BAD32597.1; -; mRNA.
DR CCDS; CCDS52322.1; -.
DR RefSeq; NP_780597.2; NM_175388.3.
DR AlphaFoldDB; E9Q7F2; -.
DR SMR; E9Q7F2; -.
DR BioGRID; 224481; 5.
DR STRING; 10090.ENSMUSP00000079631; -.
DR iPTMnet; E9Q7F2; -.
DR PhosphoSitePlus; E9Q7F2; -.
DR EPD; E9Q7F2; -.
DR jPOST; E9Q7F2; -.
DR MaxQB; E9Q7F2; -.
DR PaxDb; E9Q7F2; -.
DR PeptideAtlas; E9Q7F2; -.
DR PRIDE; E9Q7F2; -.
DR ProteomicsDB; 300444; -.
DR Antibodypedia; 31103; 84 antibodies from 19 providers.
DR Ensembl; ENSMUST00000080817; ENSMUSP00000079631; ENSMUSG00000058761.
DR GeneID; 108937; -.
DR KEGG; mmu:108937; -.
DR UCSC; uc009img.3; mouse.
DR CTD; 254225; -.
DR MGI; MGI:1920257; Rnf169.
DR VEuPathDB; HostDB:ENSMUSG00000058761; -.
DR eggNOG; ENOG502RJVX; Eukaryota.
DR GeneTree; ENSGT00940000153680; -.
DR HOGENOM; CLU_024691_1_0_1; -.
DR InParanoid; E9Q7F2; -.
DR OMA; QMTQTHR; -.
DR OrthoDB; 1189777at2759; -.
DR TreeFam; TF332796; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 108937; 1 hit in 109 CRISPR screens.
DR ChiTaRS; Rnf169; mouse.
DR PRO; PR:E9Q7F2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9Q7F2; protein.
DR Bgee; ENSMUSG00000058761; Expressed in manus and 220 other tissues.
DR Genevisible; E9Q7F2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
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:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
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..694
FT /note="E3 ubiquitin-protein ligase RNF169"
FT /id="PRO_0000415820"
FT ZN_FING 61..97
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 192..200
FT /note="UMI motif"
FT MOTIF 651..668
FT /note="MIU motif"
FT MOTIF 675..687
FT /note="LR motif"
FT COMPBIAS 103..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 326
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 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT CROSSLNK 349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NCN4"
SQ SEQUENCE 694 AA; 75796 MW; F39A950118ED7398 CRC64;
MAAAGPSTRA SSAAAAAALS RRGRRGRCDE MAAAKAGAPG PASSPALLVL RSAPRPEESG
CTGCLETPGE VAALPCSHSR CRGCASRAAG PGCRRCRPRG SGWARRRARD DGQAAAELMG
ERARRGQPEP CRPRRDGGAA ASGPRPEPEP LAEPEFIFRT PIKLSKPGEL SEEYGCLRKL
RGEKLQEEKD CDDQIHKLLQ EDSEMGKRKA DEQKKRDEAV VLKTSLEQCP ARLSDSENEE
PSRGQMMQTH RSAFVSKNSS CSLAFLAGKL NTKVQRSQSC SDTVQDRVRS RLRTAPPNRA
KITTITPGST PIIGVLLSTQ NNRCLSAPDL TIEKRLPFGS LSSLASLHKP ERSISPESND
SISEELNHFK PIVCSPCTPP KRLPDGRVLS PLIIKSTPRN LTRSLQKQTS YEASPRILKK
WEQIFQERQI KKTLSKATLT SLAPEAGEEF PGSDTIHSSK ERPSLAFNTR LSRVQVLSEC
AGPTSTALEC FPSVNQTKVE QDCVRKRSRE FSLETCHSSE HGGASSGPSL EREQCEESGS
TVDATLVKTC ISTVMKTAAV NSLLPKNDVL GGVLKTKQQL KTLNHFDLGN GILVNSLGEE
PIPSLRRGRK RRCKTKHLEQ NGVKKLRPPS SDMDLAPKDP GLLEVGRKLQ QEEEDQQLAL
QSHRMFDSER RTMSRRKGSV DQYLLRSSSL AGAK
