ID A0A3B3T033_9TELE Unreviewed; 461 AA.
AC A0A3B3T033;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000036025.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000036025.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3T033; -.
DR STRING; 1676925.ENSPKIP00000036025; -.
DR Ensembl; ENSPKIT00000016965.1; ENSPKIP00000036025.1; ENSPKIG00000014751.1.
DR GeneTree; ENSGT00940000153680; -.
DR OrthoDB; 2919223at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261540; Unplaced.
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; 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 21..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 100..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..151
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 331..365
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 114..132
FT /note="LR motif 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT MOTIF 147..155
FT /note="UMI motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT MOTIF 377..388
FT /note="LR motif 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03066"
FT COMPBIAS 240..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 51434 MW; 2236397D3A0E479E CRC64;
MPPVAEAEGR PGGLSRADCL CPICLDIFLE PVTLPCSHTF CKPCFLETVD KANLSCPLCR
KRVSSWARMH SRNKTLVNVE LWSRVQETFP AQCEQRLSGR DTGDMAAVSS RPRVSQPGEL
RKEYEDQISR LAAEKRALEE AEQAASEQYI QRLLAEDEEH LAEEWRRQEE KQLEDDEKLA
RILSMELNSS PAPEAQKQVR STGKISAKKI TNTGDIERFL LPLAQRGPVS SSTEVERSRL
DVYGGNEAER GEPDTRVSQP EQNDSTASVP AEMDSTASVP AEMDSTAAAS WMGHDGDLGD
HGTMWVREQP PGKRKSTEVG SEGADSHARK RSCHADLLVD LEEKLQNQQQ QQEEDRQLAL
RLQQQLDREE ALRVVNRRKG SPDQYQLRQR PSNVPADPSS RGRSQSGPEQ KQEKLRVRQR
GSSCGGPRAQ RGEPASESPL PVVHKACKQT TLTEIFPSLN S
//
