ID A0A9B0U1F0_CHRAS Unreviewed; 902 AA.
AC A0A9B0U1F0;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 15.
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_006874016.1};
OS Chrysochloris asiatica (Cape golden mole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Chrysochloridae; Chrysochlorinae; Chrysochloris.
OX NCBI_TaxID=185453 {ECO:0000313|Proteomes:UP000504623, ECO:0000313|RefSeq:XP_006874016.1};
RN [1] {ECO:0000313|RefSeq:XP_006874016.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_006874016.1};
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_006874016.1; XM_006873954.1.
DR AlphaFoldDB; A0A9B0U1F0; -.
DR GeneID; 102842066; -.
DR CTD; 90850; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000504623; 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; IPR056437; Znf-C2H2_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; PF23230; zf-C2H2_13; 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:UP000504623};
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 30..70
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..548
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..581
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 98563 MW; 2AA1063F1DC85AA9 CRC64;
MAAATAAAGG EGRRGTPETS VASERGGGSC VLCCGDLETT ALGRCDHPVC YRCSTKMRVL
CEQRYCAVCR EELRQVVFGK KLPAFATIPI HQLQHEPKYD IYFADEKVFA LYRQLLQHEC
PQCPALPPFS LFGDLEQHMR RQHELFCCKL CLKHLKIFTY ERKWYSRKDL ARHRMQGDPD
DTSHRGHPLC KFCDERYLDN DELLKHLRRD HYFCHFCDAD GAQDYYSDYT YLREHFREKH
FLCEEGRCST EQFTHAFRTE IDLKAHRTAC HSRSRAEARQ NRQIDLQFSY TPRHPRRGEG
VIGGEDYEEV DRYNRQGRVG RAGARGAQQS RRGSWRYKRE EEDRDTAVVI RALVATQQQD
EKRRVEDREG GPRAREEVAG RVSEELRSGQ RPPRAQGEGL GPKEVSTNGP MNQEPFPVPG
PAVGVCRLFL PWPSAPAPPV QKLKDEDFPS LSLSSLGAGS GPAGLALAYH VATRARGTFQ
DEDFPALVSS VGRPSTTPTS IISAWNSSRK VARPSSGAGA PAAGGGQSIR KASKGSGKGS
SKGSGKGGHT SPEHQGTSPE LCSLPTSAPS SSSQALAPSQ PVTKGNRKKK VGSEKPGAMS
PPPLDRTPKA PDKDGLGAEP VPSDPTSGTE GPAAMAINGH MEGLALAHSG APKEPPGLLR
PPPCLTPQED FPALGGPGAL RMPPPPGFNT VVLLKGAPPP PPPGLVPTVS KPPPGFSGLV
SSTQPVCVSS TNTKAPRLTP PPRAYLVPEN FRERNLKLIQ SIKNFLQSDE ACFSKFKNHS
GEFRQGVIPA VQYYKSCRDL LGESFQKIFP ELLVLLPDTA KQQELLAAHT DFCSHEQPSG
ARSKKSKKSV WQANTPTAGL DCCVCPTCQQ VLAHGDVSSH QALHAARDDD FPSLQAIARV
IT
//
