ID I3KKU2_ORENI Unreviewed; 442 AA.
AC I3KKU2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC100691685 {ECO:0000313|Ensembl:ENSONIP00000021737.1};
GN Synonyms=RNF168 {ECO:0000256|HAMAP-Rule:MF_03066};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000021737.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000021737.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|HAMAP-Rule:MF_03066};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|HAMAP-Rule:MF_03066}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03066}.
CC Note=Localizes to double-strand breaks (DSBs) sites of DNA damage.
CC {ECO:0000256|HAMAP-Rule:MF_03066}.
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 mediates interaction with ubiquitin with a preference for
CC 'Lys-63'-linked 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). {ECO:0000256|HAMAP-
CC Rule:MF_03066}.
CC -!- SIMILARITY: Belongs to the RNF168 family. {ECO:0000256|HAMAP-
CC Rule:MF_03066}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03066}.
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DR RefSeq; XP_005462783.1; XM_005462726.2.
DR RefSeq; XP_013121271.1; XM_013265817.2.
DR AlphaFoldDB; I3KKU2; -.
DR STRING; 8128.ENSONIP00000021737; -.
DR Ensembl; ENSONIT00000021756.2; ENSONIP00000021737.1; ENSONIG00000017234.2.
DR GeneID; 100691685; -.
DR KEGG; onl:100691685; -.
DR CTD; 165918; -.
DR eggNOG; KOG4159; Eukaryota.
DR GeneTree; ENSGT00940000153680; -.
DR HOGENOM; CLU_052187_0_0_1; -.
DR InParanoid; I3KKU2; -.
DR OMA; CLCPICL; -.
DR OrthoDB; 2919223at2759; -.
DR TreeFam; TF332796; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005207; Linkage group LG14.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003682; F:chromatin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-UniRule.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:UniProtKB-UniRule.
DR CDD; cd21952; MIU2_RNF168; 1.
DR CDD; cd16550; RING-HC_RNF168; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_03066; RNF168; 1.
DR InterPro; IPR034725; RNF168.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23328:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF168; 1.
DR PANTHER; PTHR23328; UNCHARACTERIZED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03066};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_03066};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_03066};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03066};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03066};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03066};
KW Ubl conjugation pathway {ECO:0000256|HAMAP-Rule:MF_03066};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03066};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_03066}.
FT DOMAIN 28..67
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 254..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..183
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 123..141
FT /note="LR motif 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT MOTIF 156..164
FT /note="UMI motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT MOTIF 371..382
FT /note="LR motif 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT COMPBIAS 298..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 49621 MW; 9E1F3F4781ED0B31 CRC64;
MSPVSEVESS DVGGRGQETT LSKEDCLCPV CLEIFMEPVT LPCTHTFCKV CFLESVDKAT
LCCPMCRKRV STWARLHSRN NTLVNETLWR RVQTCFPRQC EHRLSGQGEV EDPHSALVCF
RRVSEPGELR QEYEDQITKL TKEKRELQEE ERKASEEYIQ RLLAEEEQLL RDERKRRDED
ERLARLLSDQ LNPPPLEDRG HVAVTPLKKK KAASVGHIEK FLSPRVAPPS STCSSTCSST
SSHVSNKENI LVSEAALPAE RRPPQLDYYG PETDLRPPEE VAERQPGSQA IRDGGCSSVK
RKSSELEATE EVTADTKRVS PHFLGSSSFS LLEAAEQELQ ERRRQEEDDR QLALILQKQL
DQEEKRCATD RSKGSTDAYQ LRPHRGAEQE GRTSIMPGRP SRRTPKNCTA KPSAASSSSS
SSSSGKGSKQ TLLTEMFSTL SS
//
