ID A0A6P7N908_BETSP Unreviewed; 923 AA.
AC A0A6P7N908;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, 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=znf598 {ECO:0000313|RefSeq:XP_029016026.1};
OS Betta splendens (Siamese fighting fish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Osphronemidae; Betta.
OX NCBI_TaxID=158456 {ECO:0000313|Proteomes:UP000515150, ECO:0000313|RefSeq:XP_029016026.1};
RN [1] {ECO:0000313|RefSeq:XP_029016026.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-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_029016026.1; XM_029160193.3.
DR AlphaFoldDB; A0A6P7N908; -.
DR FunCoup; A0A6P7N908; 1186.
DR GeneID; 114861150; -.
DR KEGG; bspl:114861150; -.
DR CTD; 90850; -.
DR InParanoid; A0A6P7N908; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000515150; Chromosome 8.
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:UP000515150};
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 274..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..587
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 102932 MW; 7960AA39EE748E82 CRC64;
MDSTTTKEAE KHCVLCCQEV DIFALGKCDH PVCFRCSTKM RVLCEQKYCA VCREELDKVV
FVKKLATFSS LPYQQFPSEK KHDIYFGDEK IYAQYRHLLL SECVHCPESK VFSRFEELEQ
HMRKQHQLFT CKLCTKHLKI FSYERKWYNR KELARHRAHG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DADGSQEYYS DYKYLSEHFR ESHYLCEEGR CATEQFTHAF
RSEIDYKAHK AAAHSKNRAE ARQNRHIDLQ FNYTPRQQRR NEGLTGEDYE EVRHNRGGRE
RPHGGQKSWR YSREDEDRQM EAAIRASIAQ RRQEERGAVQ QRSTPKYFRE EKTERIEPEE
PTHRTGHIKP TSKPPVRTMK STSPEDDFPV LGATAAAAAS IVKPAPVAVV ASQQPPKEDD
FPSLSAVAAV PLMTPVYSGQ SRKASSFLEE DFPALVSKIR PHKPAGGTKS AWSNSTAVSK
PITNPPPSRP TPPLSSVASA PQLLCSSTSS TSRRKKKVGE NVKAAFTRTP SSSDDESGGL
TQQEFRSVPT MLDISSLLTV KGGNSKPSPV TSSSPNPAPS TSLPAAKGNK KKKPQKTTAA
PSTSVSSLSG MATPVNTIPV ETVAQKENVP EKNVNKPLSS VVTAPLSSGL ANGQPDKSPP
INKKTDTGTI HSNTDPPLQK EEEFPALITK KPPPGFKSSF PMKASAPPSS TTVTPPPPGL
GVSGTRPPPG FTGIPLNSNV VEPGDSAVNL PPKVSNCGYL VPEDFNQRNL ELIQSIKKYL
NNDESKFNQF KNYSAQFRQG VISAAQYHHS CKDLLGDNFN RIFNELLVLL PDTGKQQELL
TAHGDCKALE KQSGAGVGKK NKNKKNVWQT PTTVSHVAAE LDCQVCPTCR QVVAHKDFNS
HKTLHLRETE EFPSLQSISR IIS
//
