ID A0A9W3GPJ4_CAMBA Unreviewed; 900 AA.
AC A0A9W3GPJ4;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
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_010948187.1};
OS Camelus bactrianus (Bactrian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9837 {ECO:0000313|RefSeq:XP_010948187.1};
RN [1] {ECO:0000313|RefSeq:XP_010948187.1}
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_010948187.1; XM_010949885.2.
DR AlphaFoldDB; A0A9W3GPJ4; -.
DR KEGG; cbai:105064854; -.
DR CTD; 90850; -.
DR OrthoDB; 3838338at2759; -.
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 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 271..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..425
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..455
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..537
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..672
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 98718 MW; 22BAD497FAD44420 CRC64;
MAAVATAGPE GRRVVQEAAA AVPERGGGSC VLCCGDLEAT ALGRCDHPVC CRCSTKMRVL
CEQRYCAVCR EELRQVVFGR KLPAFATIPI HQLQHEKKYD IYFADGKVFA LYRQLLQHEC
PRCPELPPFG LFGDLEQHMR KQHELFCCKL CLKHLKIFTY ERKWYSRKDL ARHRMQGDPD
DTSHRGHPLC KFCDERYLDN DELLKHLRRD HYFCHFCDSD GAQDYYSDYA YLREHFREKH
FLCEEGRCST EQFTHAFRTE IDLKAHRTAC HSRSRAEARQ NRQIDLQFSY APRHSRRNEG
VVSGEDYEEL DRYNRQGRAG RASGRGAQQS RRGSWRYKRE EEDREEEQQQ QQQQQETRRS
EDQVEGTRPR KEEAVVRGPE GPRGPRRPPR TQGEGPGPKE SSTNGPVSQE AFPATGLAAG
TALPSTLPPP TSKLKDEDFP SLCASASSSS STAAALGPVG LPLAYAVPSR GRSTFQEDDF
PALVSSASKP TAAATSLISA WNSSGSKKVA HPTTGAQSAG GSSQPSRKAG KGGKGGKKGG
PPPVEEEEDG RTGLTAQELR SVPTTVTVSS LLALASTQTF TKVGKKKKVG SEKPGAASPP
PLPSDKDGSP GAEQAPTAPT GRAEGPVGVV VNGHTEGPVP ARSTPKEPPG LPRPQGPLPC
PTPQEDFPAL GGPCPPRMPP PPGFNTVVLL KGTPPPPPPG LVPPISKPPP GFSGLLPSPH
PACVPSTTTT TKAPRLTSMP RAYLVPENFR ERNLQLIQSI KDFLQSDEAR FNKFKSHSGE
FRQGVISAAQ YYKSCRDLLG ENFQKIFNEL LVLLPDTAKQ QELLSAHTDF RGQERPPGTK
AKKNKKNAWQ ASTRQTGLDC CVCPTCQQVL AHGDVRSHQA LHAARDDDFP SLQAIARILT
//
