ID A0A6P6NDD6_CARAU Unreviewed; 952 AA.
AC A0A6P6NDD6;
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_026106206.1};
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957 {ECO:0000313|Proteomes:UP000515129, ECO:0000313|RefSeq:XP_026106206.1};
RN [1] {ECO:0000313|RefSeq:XP_026106206.1}
RP IDENTIFICATION.
RC STRAIN=Wakin {ECO:0000313|RefSeq:XP_026106206.1};
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_026106206.1};
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_026106206.1; XM_026250421.1.
DR AlphaFoldDB; A0A6P6NDD6; -.
DR KEGG; caua:113078111; -.
DR CTD; 90850; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000515129; Unplaced.
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:UP000515129};
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 61..101
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 326..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..362
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..539
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 107283 MW; DAC5B07F79A9592C CRC64;
MHCAERSRAQ ERASPGLAAR TVVYQPSRFR RTTARTLPQH NRPVPPDSMR SSARRDAENS
CVLCCQDIEL FAVGKCDHPV CYRCSTKMRV LCEQNYCAVC REQLDKVVFI KKLEPFAALN
IHQYQFEKKY DVYFADGKIY AQFRKILLHE CPQCPEPKVF FKFEELEQHM RKQHELFCCK
LCAKHLKIFS YERKWYNRKE LARHRTQGDP DDTSHRGHPL CKFCDDRYLD NDELLKHLRR
DHYFCHFCDA DGAQEYYSDY QYLSEHFRES HYLCQEGHCS TEQFTHAFRT EIDYKAHKAA
AHSKNRAEAR QNRQIDIQFN YASRQQQRRN DGLIVGGDDY EEGDRFSRQG RPGRARAPGG
QQNVRSWRYS REEENREIAA ALRASIVSHQ EERSHVQERS SVKPRKEEKM EPDDMRNNRS
TAKQTNEMQA RPVRSNPPSA AQDFPVLGAA APPAPIQSKI KQASVPLKED DFPSLSGSVV
SSPMTPAYTN QPKKHSSFQE EDFPALVSKI KPLKPQSNTT SAWSQAGSKP VVVSNKPVVL
PTKTAPTVSS SILSASDPPP SGSVPQPLTA SSSRRKKKLT SAETHRAPPK VKCPSSSDDE
DPQTGKTAQE IRTVPTMLDI STLLTVKDGS SQPNPKTNKK KKPATASSLG SPSHTFESVS
KMAHKENVPE MKPPDNSLPS KTNSFINGLV EKPTEALSPT SFPENIPSPL KQSVTDQPPP
PKEEEFPALI SKKPPPGFKS AFPLKSTPNV LPPPPPGLGP VVSKPPPGFT GVPLNSNVEE
SAVNRVTPAI GSYLIPDNFQ QRNMDLIQSI KNYLQNDETK FNEFKNYSGQ FRQGIIPAVQ
YYKSCQELLG ENFNGVFNEL LVLLPDTRKQ QELLTAHGDF KALEKQQQGS KPKKTKKKAW
QTGTTSISLD LDCQVCPTCK QVLALKDFNT HKTLHIGDED FPSLQAISKI IS
//
