ID A0A8C4XAK8_ERPCA Unreviewed; 903 AA.
AC A0A8C4XAK8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
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:ENSECRP00000017765.1};
GN Synonyms=znf598 {ECO:0000313|Ensembl:ENSECRP00000017765.1};
OS Erpetoichthys calabaricus (Rope fish) (Calamoichthys calabaricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Polypteriformes; Polypteridae; Erpetoichthys.
OX NCBI_TaxID=27687 {ECO:0000313|Ensembl:ENSECRP00000017765.1, ECO:0000313|Proteomes:UP000694620};
RN [1] {ECO:0000313|Ensembl:ENSECRP00000017765.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSECRP00000017765.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSECRP00000017765.1}
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 RefSeq; XP_028670268.1; XM_028814435.2.
DR AlphaFoldDB; A0A8C4XAK8; -.
DR Ensembl; ENSECRT00000018115.1; ENSECRP00000017765.1; ENSECRG00000011870.1.
DR GeneID; 114661221; -.
DR CTD; 90850; -.
DR GeneTree; ENSGT00390000014178; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000694620; Chromosome 11.
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:UP000694620};
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 345..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..515
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 102679 MW; 8774100822C4D7D7 CRC64;
MASKLGKESE GSCVLCCQEI DIYALGKCDH PVCFRCSTKM RVLCEQKYCA VCREELDKVL
FVKKPDQFST ITTQNFQCEK KYDIYFSDPQ FCAQFRRILQ HECPQCKELK IFNKFEDLEQ
HMRKQHELFC CKLCAKHLKI FTHERKWYSR KELARHRMQG DPDDTSHRGH PLCKFCDDRY
LDNDELLKHL RRDHYFCHFC DSDGGQEYYS DYDYLREHFR EKHFLCEEGR CNTEQFTHAF
RTEIDYKAHK AAAHSKNRAE ARQNRHIDLQ FNYAPRHQRR NEGVVGGEDY EEVERFNRNL
RGARGGGRGG QQNLRGSWRY NREEEDREIA AAVRASVAAR RREEKRQAQE RELIKPKKEE
TVENEDFKNS RSLPKQSSDI PGKDVPAKTV NNNGPLRGED FPALGSATPC TNKLAEVKLK
EDDFPSLSST MVSGPMTPAY TAATRKQSAF LEDDFPALVS KIKPQKSLGN TCSAWLSSSN
KNVTNISRPV SSNSPISVYP TKTSTTALSI SSSSQQKKKT TSSKGNNRQN DREKSIPSSD
EDDGQVGKTT QEIRSVPTML DISSLLTEKS SVQSISKIGK RKKVGGEKQN TSALLTSVET
VKKVSQKENV PETKSQLLHF PQPINSTLVN EDNLIIEHLD NSIENKNPPI IREPPGLKKT
FSLGPNLLPD EDFPALLPKQ PPPGFSATFP LKNGPVNISP PPGYLAPASK PPPGFTGVPL
NINTSENANS IVGKSVSTTG MYTVPDNFQQ RNMELIQTIR NFLQNEESRF NEFKTYSRQF
RQGQMSATHY HKSCQELLGD NFKLVFNELL VLLPDTSKQQ ELLSAHKDIC LQENQGCNKP
KKNKINAWQS NSTSSNKNSL ELDCQVCPHC LQVLTEKDFV AHKIIHREDD DFPSLQAISK
IIS
//
