GenomeNet

Database: UniProt
Entry: A0A3P8YQ06_ESOLU
LinkDB: A0A3P8YQ06_ESOLU
Original site: A0A3P8YQ06_ESOLU 
ID   A0A3P8YQ06_ESOLU        Unreviewed;       517 AA.
AC   A0A3P8YQ06;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=RING-type E3 ubiquitin transferase RAD18 {ECO:0000256|ARBA:ARBA00031783};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000018635.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000018635.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000018635.2}
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RAD18 family.
CC       {ECO:0000256|ARBA:ARBA00009506}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_019910753.1; XM_020055194.1.
DR   AlphaFoldDB; A0A3P8YQ06; -.
DR   Ensembl; ENSELUT00000040657.2; ENSELUP00000018635.2; ENSELUG00000000733.2.
DR   GeneID; 105017026; -.
DR   GeneTree; ENSGT00390000011230; -.
DR   InParanoid; A0A3P8YQ06; -.
DR   OMA; IPNTGPR; -.
DR   OrthoDB; 6177at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000265140; LG17.
DR   Bgee; ENSELUG00000000733; Expressed in ovary and 14 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006301; P:postreplication repair; IEA:InterPro.
DR   GO; GO:0006513; P:protein monoubiquitination; IEA:InterPro.
DR   CDD; cd16529; RING-HC_RAD18; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039577; Rad18.
DR   InterPro; IPR006642; Rad18_UBZ4.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR14134; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR   PANTHER; PTHR14134:SF2; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR   Pfam; PF02037; SAP; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00513; SAP; 1.
DR   SMART; SM00734; ZnF_Rad18; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51908; ZF_UBZ4; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW   ProRule:PRU01256};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW   ProRule:PRU01256}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          25..63
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          227..254
FT                   /note="UBZ4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51908"
FT   DOMAIN          275..309
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
SQ   SEQUENCE   517 AA;  57099 MW;  F7A54F802349F8C4 CRC64;
     MANFNIAELQ PNLTCLKNVD TLLRCPICFE FLNIPMMTKC SHNFCSLCIR KFLSYKLLCP
     VCNSITTEQD LRNNRILDDL ITTFQIARQQ MSKAHFDTPP ISPKTPSSTI KCKTPGMYRG
     PKKEGSILNH FFQKAPTTSS SAVTTAAVPT PRGKRQSGAL ECSQTMKESP RHTLNVNADS
     SLQVSVKEEP MDLEIPAQSV KMMNISTGLV SLANSQSTSQ DIKPLIKVEC PVCSVGISEQ
     FINKHLDICL TRGEKHDSLR SSLGAKRKPM GKLVYTLLSM QELKRRLKEC HLSVQGNRDQ
     LVRRHQDFVH MYNAQCDALE PKPAESIAKE VEANEKARNQ LKGKTKSAMV FSKNQSVAEI
     GEIHSTYIKQ HSHEFSQLIA EVRGRRETTK KMKQEMGVSG GEEGQGVCSS STDKAAVQEQ
     SKAIPNEPGA YCLLMSTPVK EPSEEQHQPS LEDVIARSPS PCLSDRSISS SISDVFVDRC
     FERSAPTQAC QGVCSPATSG GTSSLLMLGQ QRKCLIP
//
DBGET integrated database retrieval system