ID A0A0F8BBR5_LARCR Unreviewed; 439 AA.
AC A0A0F8BBR5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RNF168 {ECO:0000256|HAMAP-Rule:MF_03066};
GN ORFNames=EH28_00229 {ECO:0000313|EMBL:KKF30640.1};
OS Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Larimichthys.
OX NCBI_TaxID=215358 {ECO:0000313|EMBL:KKF30640.1};
RN [1] {ECO:0000313|EMBL:KKF30640.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSNF {ECO:0000313|EMBL:KKF30640.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KKF30640.1};
RX PubMed=25835551;
RA Ao J., Mu Y., Xiang L.X., Fan D., Feng M., Zhang S., Shi Q., Zhu L.Y.,
RA Li T., Ding Y., Nie L., Li Q., Dong W.R., Jiang L., Sun B., Zhang X.,
RA Li M., Zhang H.Q., Xie S., Zhu Y., Jiang X., Wang X., Mu P., Chen W.,
RA Yue Z., Wang Z., Wang J., Shao J.Z., Chen X.;
RT "Genome Sequencing of the Perciform Fish Larimichthys crocea Provides
RT Insights into Molecular and Genetic Mechanisms of Stress Adaptation.";
RL PLoS Genet. 11:E1005118-E1005118(2015).
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 EMBL; KQ041089; KKF30640.1; -; Genomic_DNA.
DR RefSeq; XP_010746293.2; XM_010747991.2.
DR RefSeq; XP_019113430.1; XM_019257885.1.
DR AlphaFoldDB; A0A0F8BBR5; -.
DR GeneID; 104932698; -.
DR KEGG; lco:104932698; -.
DR CTD; 165918; -.
DR eggNOG; KOG4159; Eukaryota.
DR OrthoDB; 2919223at2759; -.
DR UniPathway; UPA00143; -.
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; 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; PF13923; zf-C3HC4_2; 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 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 29..68
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 253..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..195
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 128..146
FT /note="LR motif 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT MOTIF 161..169
FT /note="UMI motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT MOTIF 380..391
FT /note="LR motif 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT COMPBIAS 302..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 49433 MW; 806C56B9A3AE94E0 CRC64;
MAPVSDVEVS DRGAAGRTGG VLSLDDCRCP VCLEIFMEPV TLPCTHTFCK DCFLESVDKA
TLCCPLCRKR VSTWARLNNR NNTMVNQQLW TRIQSTFPLQ CQRRLSGQDH ANDDDLGATD
TSLCYPRVSQ PGEVRQEYED QVTKLTEEKR VLDEEERRAS EEYIQRLLAE EEELLQEDRR
RREEDERLAR QLSTQLNSAI VSQEVVTPAK KKEVSGQIEK FLCPRPSKSS SDCSFTANKE
NILVSPVKLQ AECSPPKLDY YGDTSDPPPP SGEEEEEERD LPESHRSHLT GDGGPSLAKR
KSSELETTEE EKVTKRACRS LPSSSSSYSS LEGGGSVLQG IVDWESELQS RRQQEEEDRR
LALLLQKELD QEEKQRATDR RKGSSDAYLL RQNRRGKEDA SSSQTPRRSS TKTTKTSSAS
SSRGSKQTTL TDMFSCLNS
//
