ID A0A6J3H2S0_SAPAP Unreviewed; 722 AA.
AC A0A6J3H2S0;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=E3 ubiquitin-protein ligase ZNF598 isoform X4 {ECO:0000313|RefSeq:XP_032124092.1};
GN Name=ZNF598 {ECO:0000313|RefSeq:XP_032124092.1};
OS Sapajus apella (Brown-capped capuchin) (Cebus apella).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Sapajus.
OX NCBI_TaxID=9515 {ECO:0000313|Proteomes:UP000504640, ECO:0000313|RefSeq:XP_032124092.1};
RN [1] {ECO:0000313|RefSeq:XP_032124092.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_032124092.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_032124092.1; XM_032268201.1.
DR AlphaFoldDB; A0A6J3H2S0; -.
DR GeneID; 116542933; -.
DR CTD; 90850; -.
DR Proteomes; UP000504640; Unplaced.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR InterPro; IPR057634; PAH_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; PF23230; zf-C2H2_13; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000504640}.
FT DOMAIN 16..37
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 141..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..158
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..185
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..279
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..334
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..364
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 78219 MW; 7D04AE6786852598 CRC64;
MQGDPDDTSH RGHPLCKFCD ERYLDNDELL KHLRRDHYFC HFCDSDGAQD YYSDYAYLRE
HFREKHFLCE EGRCSTEQFT HAFRTEIDLK AHRTACHSRS RAEARQNRQI DLQFSYVPRH
SRRNEGVVGG DDYEEVDRYS RQGRAARAGT RGAQQSRRGS WRYKREEEDR EVAAAVRASV
AAQQQEEARR SEDREEGGRL KKEEAAVRGP EEPRGPRHPP RTQGEGPGPK ETSTNGPVSQ
ETFPVTGPAT PGPLPPPSPK LKDEDFPSLS ASTSSSCSTA ATLASVGLAL PYAIPARSRS
AFQEEDFPAL VSSAPKPGTT PTSLVSAWNS SSSSNKVARP PPSAQAASSG QPTRKAGKGN
RGGRKGGLPL PEEEESGSPA AQEPRSARPM GSVASALRPA STQPSKVGKK KKVGSETPST
ALPQPPPPSC PPGSAQALET PATRAEGPVA IVVNGHTEGP APARSVPKEP PGLPRPLGSF
PCPPEDFPAL GGPCPPRMPP PPGFSAVVLL KGTPPPPPPG LAPPVSKPPP PGFSGLLPSP
HPACVPSPAT TITKAPRPTP APRAYLVPEN FRERNLQLIQ SIRDFLQSDE ARFSEFKSHS
GEFRQGLISA AQYYKSCRDL LGENFQKVFN ELLVLLPDTA KQQELLSAHM DFCSREKPPS
TKSKKNKKSA WQATTEQAGL DCHVCPTCQQ VLAHGDVSSH QELHAARDDD FPSLQAIARI
IT
//
