RN169_HUMAN
ID RN169_HUMAN Reviewed; 708 AA.
AC Q8NCN4; Q6N015;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12056414; DOI=10.1093/dnares/9.2.47;
RA Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S.,
RA Takahashi Y., Kitajima S., Saga Y., Koseki H.;
RT "Characterization of size-fractionated cDNA libraries generated by the in
RT vitro recombination-assisted method.";
RL DNA Res. 9:47-57(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-708.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-485, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-249; THR-554 AND
RP SER-693, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND THR-554, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-409 AND THR-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP FUNCTION, MIU MOTIF, UBIQUITIN-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=22733822; DOI=10.1074/jbc.m112.373530;
RA Chen J., Feng W., Jiang J., Deng Y., Huen M.S.;
RT "Ring finger protein RNF169 antagonises the ubiquitin-dependent signaling
RT cascade at sites of DNA Damage.";
RL J. Biol. Chem. 287:27715-27722(2012).
RN [9]
RP FUNCTION, MIU MOTIF, UBIQUITIN-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=22492721; DOI=10.1083/jcb.201109100;
RA Poulsen M., Lukas C., Lukas J., Bekker-Jensen S., Mailand N.;
RT "Human RNF169 is a negative regulator of the ubiquitin-dependent response
RT to DNA double-strand breaks.";
RL J. Cell Biol. 197:189-199(2012).
RN [10]
RP FUNCTION, UBIQUITIN-BINDING, LR MOTIF, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-68; ALA-673; ARG-689; LYS-691; TYR-697 AND
RP 699-LEU-ARG-700.
RX PubMed=22742833; DOI=10.1016/j.molcel.2012.05.045;
RA Panier S., Ichijima Y., Fradet-Turcotte A., Leung C.C., Kaustov L.,
RA Arrowsmith C.H., Durocher D.;
RT "Tandem protein interaction modules organize the ubiquitin-dependent
RT response to DNA double-strand breaks.";
RL Mol. Cell 47:383-395(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-247; SER-339; SER-644
RP AND SER-693, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-286; LYS-362 AND LYS-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30104380; DOI=10.1073/pnas.1804823115;
RA An L., Dong C., Li J., Chen J., Yuan J., Huang J., Chan K.M., Yu C.H.,
RA Huen M.S.Y.;
RT "RNF169 limits 53BP1 deposition at DSBs to stimulate single-strand
RT annealing repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E8286-E8295(2018).
RN [15]
RP FUNCTION, PHOSPHORYLATION AT SER-368 AND SER-403, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-368 AND SER-403.
RX PubMed=30773093; DOI=10.1080/15384101.2019.1577525;
RA Menon V.R., Ananthapadmanabhan V., Swanson S., Saini S., Sesay F.,
RA Yakovlev V., Florens L., DeCaprio J.A., Washburn M.P., Dozmorov M.,
RA Litovchick L.;
RT "DYRK1A regulates the recruitment of 53BP1 to the sites of DNA damage in
RT part through interaction with RNF169.";
RL Cell Cycle 18:531-551(2019).
RN [16]
RP INTERACTION WITH DYRK1B.
RX PubMed=33469661; DOI=10.1093/nar/gkaa1290;
RA Dong C., An L., Yu C.H., Huen M.S.Y.;
RT "A DYRK1B-dependent pathway suppresses rDNA transcription in response to
RT DNA damage.";
RL Nucleic Acids Res. 49:1485-1496(2021).
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 (PubMed:22492721,
CC PubMed:30773093). Once recruited to DSB repair sites by recognizing and
CC binding ubiquitin catalyzed by RNF168, competes with TP53BP1 and BRCA1
CC for association with RNF168-modified chromatin, thereby favouring
CC homologous recombination repair (HRR) and single-strand annealing (SSA)
CC instead of non-homologous end joining (NHEJ) mediated by TP53BP1
CC (PubMed:30104380, PubMed:30773093). E3 ubiquitin-protein ligase
CC activity is not required for regulation of DSBs repair.
CC {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822,
CC ECO:0000269|PubMed:22742833, ECO:0000269|PubMed:30104380,
CC ECO:0000269|PubMed:30773093}.
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:0000269|PubMed:33469661}.
CC -!- INTERACTION:
CC Q8NCN4; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-6380946, EBI-739624;
CC Q8NCN4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-6380946, EBI-618309;
CC Q8NCN4; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-6380946, EBI-10961706;
CC Q8NCN4; O75031: HSF2BP; NbExp=3; IntAct=EBI-6380946, EBI-7116203;
CC Q8NCN4; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-6380946, EBI-14066006;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:30104380,
CC ECO:0000269|PubMed:30773093}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:22492721, ECO:0000269|PubMed:22733822,
CC ECO:0000269|PubMed:22742833}. Note=Localizes to sites of double-strand
CC breaks (DSBs) following DNA damage. Recruited to DSBs via recognition
CC of RNF168-dependent ubiquitin products. {ECO:0000269|PubMed:30104380}.
CC -!- DOMAIN: The MIU motif (motif interacting with ubiquitin) mediates the
CC interaction with both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains
CC (PubMed:22733822 and PubMed:22492721). The UMI motif also mediates
CC interaction with ubiquitin. The specificity for different types of
CC ubiquitin is mediated by juxtaposition of ubiquitin-binding motifs (MIU
CC and UMI motifs) with LR motifs (LRMs) (PubMed:22742833).
CC {ECO:0000269|PubMed:22742833}.
CC -!- PTM: Phosphorylated by DYRK1A; phosphorylation increases RNF169 ability
CC to block accumulation of TP53BP1 at the DSB sites.
CC {ECO:0000269|PubMed:33469661}.
CC -!- SIMILARITY: Belongs to the RNF169 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC02700.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB082522; BAC02700.1; ALT_INIT; mRNA.
DR EMBL; BX640750; CAE45858.1; -; mRNA.
DR CCDS; CCDS41691.1; -.
DR RefSeq; NP_001092108.1; NM_001098638.1.
DR PDB; 5GG4; X-ray; 3.11 A; E/F/G/H=620-632.
DR PDB; 5VEY; NMR; -; C=653-708.
DR PDBsum; 5GG4; -.
DR PDBsum; 5VEY; -.
DR AlphaFoldDB; Q8NCN4; -.
DR SMR; Q8NCN4; -.
DR BioGRID; 129022; 56.
DR IntAct; Q8NCN4; 51.
DR MINT; Q8NCN4; -.
DR STRING; 9606.ENSP00000299563; -.
DR GlyGen; Q8NCN4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NCN4; -.
DR PhosphoSitePlus; Q8NCN4; -.
DR BioMuta; RNF169; -.
DR DMDM; 110287945; -.
DR EPD; Q8NCN4; -.
DR jPOST; Q8NCN4; -.
DR MassIVE; Q8NCN4; -.
DR MaxQB; Q8NCN4; -.
DR PaxDb; Q8NCN4; -.
DR PeptideAtlas; Q8NCN4; -.
DR PRIDE; Q8NCN4; -.
DR ProteomicsDB; 72913; -.
DR Antibodypedia; 31103; 84 antibodies from 19 providers.
DR DNASU; 254225; -.
DR Ensembl; ENST00000299563.5; ENSP00000299563.4; ENSG00000166439.6.
DR GeneID; 254225; -.
DR KEGG; hsa:254225; -.
DR MANE-Select; ENST00000299563.5; ENSP00000299563.4; NM_001098638.2; NP_001092108.1.
DR UCSC; uc001ovl.4; human.
DR CTD; 254225; -.
DR DisGeNET; 254225; -.
DR GeneCards; RNF169; -.
DR HGNC; HGNC:26961; RNF169.
DR HPA; ENSG00000166439; Low tissue specificity.
DR MIM; 618650; gene.
DR neXtProt; NX_Q8NCN4; -.
DR OpenTargets; ENSG00000166439; -.
DR PharmGKB; PA142671054; -.
DR VEuPathDB; HostDB:ENSG00000166439; -.
DR eggNOG; KOG4159; Eukaryota.
DR GeneTree; ENSGT00940000153680; -.
DR HOGENOM; CLU_024691_1_0_1; -.
DR InParanoid; Q8NCN4; -.
DR OMA; QMTQTHR; -.
DR OrthoDB; 1189777at2759; -.
DR PhylomeDB; Q8NCN4; -.
DR TreeFam; TF332796; -.
DR PathwayCommons; Q8NCN4; -.
DR SignaLink; Q8NCN4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 254225; 12 hits in 1122 CRISPR screens.
DR ChiTaRS; RNF169; human.
DR GenomeRNAi; 254225; -.
DR Pharos; Q8NCN4; Tbio.
DR PRO; PR:Q8NCN4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NCN4; protein.
DR Bgee; ENSG00000166439; Expressed in epithelial cell of pancreas and 189 other tissues.
DR ExpressionAtlas; Q8NCN4; baseline and differential.
DR Genevisible; Q8NCN4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA: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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA damage; DNA repair; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..708
FT /note="E3 ubiquitin-protein ligase RNF169"
FT /id="PRO_0000245598"
FT ZN_FING 68..107
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 205..213
FT /note="UMI motif"
FT MOTIF 665..682
FT /note="MIU motif"
FT MOTIF 689..701
FT /note="LR motif"
FT COMPBIAS 113..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30773093,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30773093,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 554
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 511
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 68
FT /note="C->S: Does not affect recruitment to DSBs nor
FT ability to inhibit DSBs repair."
FT /evidence="ECO:0000269|PubMed:22742833"
FT MUTAGEN 368
FT /note="S->A: About 90% loss of phosphorylation by DYRK1A;
FT when associated with A-403."
FT /evidence="ECO:0000269|PubMed:30773093"
FT MUTAGEN 403
FT /note="S->A: About 90% loss of phosphorylation by DYRK1A;
FT when associated with A-368."
FT /evidence="ECO:0000269|PubMed:30773093"
FT MUTAGEN 673
FT /note="A->G: Abolishes ubiquitin-binding."
FT /evidence="ECO:0000269|PubMed:22742833"
FT MUTAGEN 689
FT /note="R->A: Impairs recruitment to DSBs."
FT /evidence="ECO:0000269|PubMed:22742833"
FT MUTAGEN 691
FT /note="K->A: Impairs recruitment to DSBs."
FT /evidence="ECO:0000269|PubMed:22742833"
FT MUTAGEN 697
FT /note="Y->A: Impairs recruitment to DSBs."
FT /evidence="ECO:0000269|PubMed:22742833"
FT MUTAGEN 699..700
FT /note="LR->AA: Does not affect ubiquitin-binding but
FT abolishes recruitment to DSBs."
FT /evidence="ECO:0000269|PubMed:22742833"
FT HELIX 654..683
FT /evidence="ECO:0007829|PDB:5VEY"
SQ SEQUENCE 708 AA; 77194 MW; 95988AC8D440B8AD CRC64;
MAAAGPSTRA SSAAAAAALS RRGRRGRCDE TAAAKTGAPG PASGPSLLVL SPPLLQPPLP
PRPEESGCAG CLEPPGEAAA LPCGHSLCRG CAQRAADAAG PGCPRCRARG PGWARRRARD
DGQADSEVLG ECARRSQPER CRPRRDGGAA AAGPRPEQEP RAAPAEPDFI FRAPIKLSKP
GELREEYESL RKLREEKLQE EKPSEDQIHK LLPEDTETGK RKMDEQKKRD EPLVLKTNLE
RCPARLSDSE NEEPSRGQMT QTHRSAFVSK NNSYSLAFLA GKLNSKVERS QSCSDTAQER
AKSRVRAVPG NKAKVTTMTP ASNPIIGVLL STQNNRCVSA PDLTIEKRLP FSSLSSLASL
HKPERSVSPE SNDSISEELN HFKPIVCSPC TPPKRLPDGR VLSPLIIKST PRNLNRSLQK
QTSYEASPRI LKKWEQIFQE RQIKKTLSKA TLTSLAPEMG EELLGSEGIH SSKEKPLVAV
NTRLSGGQVL SEYTGPTSAD LDHFPSVSQT KAEQDSDNKS STEIPLETCC SSELKGGGSG
TSLEREQFEG LGSTPDAKLD KTCISRAMKI TTVNSVLPQN SVLGGVLKTK QQLKTLNHFD
LTNGVLVESL SEEPLPSLRR GRKRHCKTKH LEQNGSLKKL RQTSGEVGLA PTDPVLREME
QKLQQEEEDR QLALQLQRMF DNERRTVSRR KGSVDQYLLR SSNMAGAK
