ID A0A674DWC8_SALTR Unreviewed; 983 AA.
AC A0A674DWC8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
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:ENSSTUP00000099849.1};
GN Synonyms=LOC115188868 {ECO:0000313|Ensembl:ENSSTUP00000099849.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000099849.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000099849.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSTUP00000099849.1}
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 AlphaFoldDB; A0A674DWC8; -.
DR Ensembl; ENSSTUT00000107138.1; ENSSTUP00000099849.1; ENSSTUG00000044728.1.
DR GeneTree; ENSGT00390000014178; -.
DR Proteomes; UP000472277; Unassembled WGS sequence.
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:UP000472277};
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 12..52
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 250..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..559
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 983 AA; 110205 MW; BD16791B983BA76E CRC64;
MESTSNNYER NCVLCCQELD IFALGKCDHP VCYRCSTKMR VLCDQKYCAV CREELDKVLF
VQKLVAFSSL PLQTLQVERK HDIYFTDSKI YAQFRTLLLS KCPVCPESKV FSKFEELEQH
MRKQHELFCC KLCTKHLQIF SHERKWYNRK DLARHRSHGD PEDTSHRGHP LCKFCDDRYL
DNDELLKHLR RDHYFCHFCD ADGAQEYYSD YQYLSEHFRE AHYLCEEGRC ATEQFTHAFR
SQIDYKAHKA SAHSKNRAEA RQNRHIDLQF SYAPRQTRRN DGGMVSGEDY EEVRSGRGGR
ERNQGNQQNT RGSWRYNREE EDRELAVAVR ASMMQQRRQE DRGRDTQDRS GAPKHRKEEM
PERTGRPERT GRPERPERPE RPERTERPER PERPERTERP ERTERTERME RMETEERMER
MEPEERHRSV PIKPPAETPP VRTMKSNPLT GDDFPALLGA AAPTLSVKAP PALKTPAQVP
LKEDDFPSLS AATVTTPMNP AYSAQPRKHS SFQEEDFPAL VSKIRPPRPA GGATSAWSQA
SSSSSKTVIL PSSSSRPSSN NPPLPLPAGP QLLSSSSSRR KKLSARRPSP PSDDDNCVAK
TMQEHRAIPT MLDISSLLIV KGPSKPLPPT SKPLPPTSKP SPVTSNPAPS PTSKSAKKKK
QVTPPPPFGN QVHVPTETVS RVQKENVPES RASKPLVAVM TAALKTAVKA TVKTSGLANG
HLDKPVTVAP LPKAQPDPPL EVEEEFPALI SKKPPPGFKS SFVLKSSAPP NVLSPSPPGL
GGAPPPSKPP PGFTGIPLNS NVVEPAPPAS SPRSPQSPGV YLAPENFQQR NMELIQSIKN
LLQNDQSRFN QFKDYSGQFR QGLMSAVLYH RSCKTLLGDN FVGVFNELLV LLPDTGKQQE
LLTAHADDQA TERPGGGGAR KNKKKSAWQT PSSAISNAAA LDCQVCPTCC QVLDPKDFNS
HKTLHLGDNE DFPSLQAISR IIS
//
