ID A0A8U0RPT7_MUSPF Unreviewed; 775 AA.
AC A0A8U0RPT7;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=E3 ubiquitin-protein ligase ZNF598 isoform X2 {ECO:0000313|RefSeq:XP_044928062.1};
GN Name=ZNF598 {ECO:0000313|RefSeq:XP_044928062.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Proteomes:UP000000715, ECO:0000313|RefSeq:XP_044928062.1};
RN [1] {ECO:0000313|RefSeq:XP_044928062.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044928062.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
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DR RefSeq; XP_044928062.1; XM_045072127.1.
DR AlphaFoldDB; A0A8U0RPT7; -.
DR GeneID; 101678845; -.
DR CTD; 90850; -.
DR Proteomes; UP000000715; 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:UP000000715}.
FT DOMAIN 52..73
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 135..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..194
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..226
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..329
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..370
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..411
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..537
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 84128 MW; 02FDE6E03BFBD42C CRC64;
MRKQHELFCC KLCLKHLKIF TYERKWYSRK DLARHRMQGD PDDTSHRGHP LCKFCDERYL
DNDELLKHLR RDHYFCHFCD AEGAQDYYSD YAYLREHFRE KHFLCEEGRC STEQFTHAFR
TEIDLKAHRT TCHSRSRAEA RQNRQIDLQF SYAPRHSRRN EGVVGGEDYE EVDRYNRQGR
AGRASGRGAQ QNRRGSWRYK REEEDREVAA AIRASVAVQQ QQQQQQEARR SEDREEGGRA
KKDEAGVRGL EELRGPRRPP RTQGEGAGLK EASPNGPVSP EGTPATGPAP GAVLPSTLPP
PTSKLKDEDF PSLCASTSSS SSSCSAVAAP GPVGLGLTYP VPARGRSTFQ EDDFPALVSS
ASKPSTAPTS LISAWNGSGS KKVAHPTAGA PAASGSSQPA RKAGKGGKGS KKAGPLPSEE
EEEDGRTGLT AQELRSVPTT VAVSSLLALA STQTLTKVGK KKKVGSEKPG AVSPPPLPPD
KDGPLGAEQT PTTSAGRAEG PVALIVNGHT EGPAPARSTP KEPPGLPRPL GPLPCPTPQE
DFPALGVPCP PRMPPPPGFS AVVLLKGTPP PPPPGLVPPI SKPPPGFSGL LPGSHPACVP
STVTTTKAPR LTAAPQAYLV PENFRERNLQ LIQSIRDFLQ SDEARFGKFK SHSGEFRQGV
ISAAQYYKSC RDLLGENFQK IFNELLVLLP DTAKQQELLS AHTHFRGRER PPGTKAKKNK
KSAWQGSARP AGLDCCVCPT CQQVLAHGDV SSHQALHAAQ DHDFPSLQAI ARILT
//