ID A0A8C5F716_GADMO Unreviewed; 1151 AA.
AC A0A8C5F716;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 3.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=ZNF598 {ECO:0000313|Ensembl:ENSGMOP00000011489.2};
GN Synonyms=znf598 {ECO:0000313|Ensembl:ENSGMOP00000011489.2};
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049 {ECO:0000313|Ensembl:ENSGMOP00000011489.2, ECO:0000313|Proteomes:UP000694546};
RN [1] {ECO:0000313|Ensembl:ENSGMOP00000011489.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSGMOP00000011489.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR RefSeq; XP_030205195.1; XM_030349335.1.
DR AlphaFoldDB; A0A8C5F716; -.
DR Ensembl; ENSGMOT00000011801.2; ENSGMOP00000011489.2; ENSGMOG00000010717.2.
DR GeneID; 115537412; -.
DR GeneTree; ENSGT00390000014178; -.
DR OMA; WSERHEA; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000694546; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694546};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 13..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 291..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..650
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..695
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..715
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..757
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..829
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..860
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..931
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 128567 MW; A86230AB6078CB36 CRC64;
MDSSNTKDTE KTCVLCCQDV DIFALGKCDH PVCYRCSTKM RVLCDQKYCA VCREELDKVV
FVNRLAAFST LPFQQFHCEQ SHDIYFGDAQ IHTQFRRLLL PECPHCPEPK VFPRLEELEQ
HIRKQHELFC CKLCTKHLKI FSHERKWYNR KELARHRAHG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DADGAQEYYC DYQYLSEHFR ESHYLCEEGR CATEQFTHAF
RSEIDYKAHK ASAHSKNRAE ARQNRQIDLQ FTYAPRMQRR NDGMLTGEDY EEARQSRGGG
RGGGGGGGGG RPYGGQQKSW RYNREEEERD IAAAMRASMA VRRPEDRGPP AQDRGPPQRQ
RNDERMDRMD RTERMERPER MERPERMDRT ERKERMDRPE RMDRTDRTDR PERMDRTDRI
DRPERKERMD RTDRMDRTER MDRPERMDRT ERMDRPERMD RPERMDRTER MDRPERMDRT
ERIDRTERKD RTERMDADEL RHRAGAIKNN PEPPVRTMKS KNPFGEDDDF PVLGVPVSTP
IPSSKPAPVT APRGPLKEDD FPTLSGAPPR GTLKQDDFPR LSAGPPRGPL KEDDFPSLSA
ATSAVTSPMT PAYTAPPRNS SSFQEDDFPA LVSKLRLQKP SGGSASAWSS HGKPVPPTRA
NHGPPPPEAF PAPAPPAGLQ PLSSSSSSSA SVAMSSRRKK RGGETARPAA APQRSSSDEE
DGGLTQREFR TVPTMLDISS LLTVKSGGGV SGGGGVGTSI SAGVGGRPQA PPATDSSDAI
PGLAAPKAGK KKKTQQQQPQ PQPQQKNTNL PATPSKTATS ATKTKAKATV AQKENVPEKS
KNKAAPAPAA TVTAARTGTP SQLTNGYAET AFTPATKKAS ASPAVTPHPF PEPPPADEED
FPALVTRKPP PGFKSSFPLK ATAPLAAAPP SSVVPPLPPP GLAGGPSKSP PPGFTGIPLN
SNVVEPAPPP PHRPAQLLDS YMVPENFQQR NLELIQSIRN YLHNDESHFN QFKNFSGQFR
QGVMSAAQYY RSCKELLGDN FQRIFNELLV LLPDTSRQQE LLAAHGDSRA LEKQSTGGGG
GVGKKNKSKR NAWQAPPTAN GDTAMLAELD CRVCPTCRQV LAPKDFNSHK TLHLGESEDF
PSLQSISRII S
//
