ID A0AAZ3SQE4_ONCTS Unreviewed; 773 AA.
AC A0AAZ3SQE4;
DT 05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 1.
DT 28-JAN-2026, entry version 5.
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:ENSOTSP00005155357.1};
OS Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=74940 {ECO:0000313|Ensembl:ENSOTSP00005155357.1, ECO:0000313|Proteomes:UP000694402};
RN [1] {ECO:0000313|Proteomes:UP000694402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29621340;
RA Christensen K.A., Leong J.S., Sakhrani D., Biagi C.A., Minkley D.R.,
RA Withler R.E., Rondeau E.B., Koop B.F., Devlin R.H.;
RT "Chinook salmon (Oncorhynchus tshawytscha) genome and transcriptome.";
RL PLoS ONE 13:e0195461-e0195461(2018).
RN [2] {ECO:0000313|Ensembl:ENSOTSP00005155357.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSOTSP00005155357.1}
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; A0AAZ3SQE4; -.
DR Ensembl; ENSOTST00005176826.1; ENSOTSP00005155357.1; ENSOTSG00005068823.1.
DR GeneTree; ENSGT00390000014178; -.
DR Proteomes; UP000694402; 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; 4.
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:UP000694402};
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 35..75
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 271..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..330
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..470
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 86406 MW; 5FDBD74FE3A04C30 CRC64;
VYHSTVYPYG LYTSKSLLAC TATIQQSRGI GERNCVLCCQ ELDIFALGKC DHPVCYRCST
KMRVLCDQKY CAVCREQLDK VLFVQKLVAF SSQPLQTLQV ERKHDIYFTD SKIYAQFSLT
CPVCPESLLM LYLSIFSHER KWYNRKDLAR HRTHGDPDDT SHRGHPLCKF CDDRYLDNDE
LLKHLRRDHY FCHFCDADGA QEYYSDYQYL SEHFREAHYL CEEGRCATEQ FTHAFRSQID
YKAHKASAHS KNRAEARQNR HIDLQFSYAP RQTRRNDGET GYCARPERME RPERMEPGGW
RGRADGAGWS GPSGWSGPSG WSGPSGWSGP RPERMERPER METEERHRSI PVKPPAEAPP
VRTMKSNPLT GDDFPALLGA APPPALKTPA QVPLKEDDFP SLSASMVMTP MTPAYSAQPR
KHSSFQEEDF PALVSKIRPP RPAGGATSAW SQASSSSNTS KTVILPSSSS RPPPNNPPLP
LPAGPQLLSS SSRRKKHPVR RPSPPSDDDN CVAKTMQEHR AVPTMLDISS LLIVKGPSKS
APTASKPLQL TAKPLPPTSK PSPVTSNPTP IPAPSPPSKT AKKKKQATPP PSSFGNQVPV
LMETVSRSPG VYLAPENFQQ RNMELIQSIK NLLQNDQSRF NQFKDYSGQF RQGLMSAVLY
HQSCRTLLGD NFGGVFNELL VLLPDTRKQQ ELLTAHADNR AMERQGGGGT RKNRKSAWQT
PSSAISNAAA LDCQVCPTCC QVLDPKDFNS HKTLHLGDNE DFPSLQDISR IIS
//
