ID A0A8J0Q3K0_XENLA Unreviewed; 902 AA.
AC A0A8J0Q3K0;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
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.S {ECO:0000313|RefSeq:NP_001089231.2,
GN ECO:0000313|Xenbase:XB-GENE-999294};
GN Synonyms=znf598 {ECO:0000313|RefSeq:NP_001089231.2};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:NP_001089231.2};
RN [1] {ECO:0000313|RefSeq:NP_001089231.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|RefSeq:NP_001089231.2}
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; NP_001089231.2; NM_001095762.1.
DR AlphaFoldDB; A0A8J0Q3K0; -.
DR GeneID; 734278; -.
DR KEGG; xla:734278; -.
DR AGR; Xenbase:XB-GENE-999294; -.
DR CTD; 734278; -.
DR Xenbase; XB-GENE-999294; znf598.S.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; 4.
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:UP000186698};
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 7..47
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 297..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..310
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 101064 MW; A31CA6115C702F2C CRC64;
MESEKSCVVC CQDMDLYAVG KCDHPVCYRC STKMRVLCEQ KYCAVCREEL DKVVFVNKLA
PFTSLPFQQM QYEKKYDIYF EDGKLFSQFR KLLQHECTLC PSMRPFHAFA DLEQHMRKHH
ELFCCKLCVR HLKNFTYERT WYSRRDLARH RIHGDPEDTS HRGHPLCKFC DERYLDNDEL
LKHLRRDHYF CHFCDSEGAQ EYYSDYTFLK EHFRESHFLC EEGRCNTEQF THAFPTEIDY
KAHKTACHSK NRAEARQNRQ IDIQFSYAPR HNRRAEGSSG VVGGEDYEEV DRYNRQARSA
RGAARGAQQQ NKRGSWRYKR EEEDRVVAAA VRASVAARRQ EEMGRKPAPE IPETTKSRQE
HSRDLEEGSK GKASSKPTTD LVGAEMLMKS VSLGPQENGK PQNATNGVLN TDDFPAIGSA
PLLSSRKPAA AKPKEEDFPS LSSVISSSSS SSVPAFSAGL SYTASARSSN KFQEEDFPAL
VSKINTNKPL SSVGSAWATA SSKSAPKAAG SSIAPPNKAV KKYPPPGNGK AAGKKISKPS
SISDDEDDGI GMTAQEFRSA PTMFDISKLL SSPTAQSCGK VSKKKRVGSE KQHQSSATQP
VYDKPPSSNS SLKENASEIE RTPTPPANSI LSDKSNTVAN GLPEKKLLDK SNTFKETTEL
KKGPVSVPQC PLPEEEFPAL MKSSMLRMPP PGFIPVVTVA PLAPPPGLSS SVGKPPPGFN
NLPPTALPSE PQNKTAKQPP FCSRTYLVPE NFQQRNMHLI NSIKDFLDSD ESKFNEFKSL
SGKFRQGLIS AAEYYQSCRQ LLRENFKLIF NELLVLLPDT TKQQELLSAH KESHVEEKPS
SNKPKKNKKT AWLMDSKSLD LDYSVCPSCG QVLAPRDHSS HKKLHLEDND FPSLQATRRI
IS
//
