ID A0A8C5KIE8_JACJA Unreviewed; 858 AA.
AC A0A8C5KIE8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 2.
DT 28-JAN-2026, entry version 19.
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:ENSJJAP00000008548.1};
OS Jaculus jaculus (Lesser Egyptian jerboa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Dipodoidea;
OC Dipodidae; Dipodinae; Jaculus.
OX NCBI_TaxID=51337 {ECO:0000313|Ensembl:ENSJJAP00000008548.1, ECO:0000313|Proteomes:UP000694385};
RN [1] {ECO:0000313|Ensembl:ENSJJAP00000008548.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSJJAP00000008548.1}
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A8C5KIE8; -.
DR Ensembl; ENSJJAT00000014979.1; ENSJJAP00000008548.1; ENSJJAG00000012668.1.
DR GeneTree; ENSGT00390000014178; -.
DR OMA; CEKKYDI; -.
DR Proteomes; UP000694385; 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; IPR056437; Znf-C2H2_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
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; PF23230; zf-C2H2_13; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
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:UP000694385};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 149..170
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 271..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..497
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..641
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 94561 MW; A071B1D35DCBAEBB CRC64;
MGRCDHPVCY RCSTKMRVLC EQRYCAVCRE ELRQVVFGKK LPAFATIPIH QLQHEKKYDI
YFADGKVFAL YRQLLQHECP QCPQLPPFGL FGDLEQHMRK QHELFCCKLC LKHLKIFTYE
RKWYSRKDLA RHRMQGDPDD TSHRGHPLCK FCDERYLDND ELLKHLRRDH YFCHFCDSDG
AQDYYSDYAY LREHFREKHF LCEEGRCSTE QFTHAFRTEI DLKAHKTACH SRSRAEARQN
RQIDLQFSFV PRHSRRSEGV VGGEDYEEVD RYNRQGRAGR ASGRGAQQSR RGSWRYKREE
EDREVAAAIR ASVAAQQQEE TRRTEDREEG GRPKKEETAA RGPEELRGPR RLPRTQGEGS
GPKEVLTNGP LSQEAFPATG SVAATPSTLL PPTPKLKDED FPSLCASTSS CCTTAATGSV
GLALAYPGPT KGKNTFQDED FPALVSSAPK PTAPSSLISA WNSSCSKKGA PPTSGALAAA
GGSQPSRKAG KGNRSSRKGG PPPVDEEEGG GLTVQELRSV PTTVAVSSLL GPVSTQSSTK
GNKKKKVGSE KPGATSSPLP PSDCTQKTPG ADQGPEASTS KAEVPAAIIV NGHSEGPALA
RSTPKEPPGL PRPLGPLPCP TPQEDFPALG GPCPPRMPPP PGFNTVVLLK GTPPPPPPGL
VPPVSKPPPG FSSFLPSSQP ACVPSSTTTM KTPRLPPTPR AYLVPENFRE RNLQLIQSIK
DFLQSDEARF SRFKSQSGEF RQGMISAAQY YKSCWDLLGE NFQKIFSELL VLLPDTAKQQ
ELLSAHTDFR GREKAPGAKS KKKKNVWQAS TQQAGLDCCV CPTCQQVLAH DDVSSHQALH
AARDDDFPSL QAIARIIT
//
