ID A0A8U0UVM8_MUSPF Unreviewed; 920 AA.
AC A0A8U0UVM8;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
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_044928061.1};
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_044928061.1};
RN [1] {ECO:0000313|RefSeq:XP_044928061.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044928061.1};
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_044928061.1; XM_045072126.1.
DR AlphaFoldDB; A0A8U0UVM8; -.
DR GeneID; 101678845; -.
DR CTD; 90850; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000000715; 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:UP000000715};
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 37..77
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 321..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..339
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..371
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..474
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..515
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..556
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..682
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 99769 MW; E0658D65A734EC6E CRC64;
MAAAAAAAAA VVAAAGAEGR RAALEAAATP ERGGGSCVLC CGDLEATALG RCDHPVCYRC
STKMRVLCEQ RYCAVCREEL RQVVFGKKLP AFATISLHQL QHEKKYDIYF ADGKVFALYR
QLLQHECPQC PALPPFGLFG DLEQHMRKQH ELFCCKLCLK HLKIFTYERK WYSRKDLARH
RMQGDPDDTS HRGHPLCKFC DERYLDNDEL LKHLRRDHYF CHFCDAEGAQ DYYSDYAYLR
EHFREKHFLC EEGRCSTEQF THAFRTEIDL KAHRTTCHSR SRAEARQNRQ IDLQFSYAPR
HSRRNEGVVG GEDYEEVDRY NRQGRAGRAS GRGAQQNRRG SWRYKREEED REVAAAIRAS
VAVQQQQQQQ QEARRSEDRE EGGRAKKDEA GVRGLEELRG PRRPPRTQGE GAGLKEASPN
GPVSPEGTPA TGPAPGAVLP STLPPPTSKL KDEDFPSLCA STSSSSSSCS AVAAPGPVGL
GLTYPVPARG RSTFQEDDFP ALVSSASKPS TAPTSLISAW NGSGSKKVAH PTAGAPAASG
SSQPARKAGK GGKGSKKAGP LPSEEEEEDG RTGLTAQELR SVPTTVAVSS LLALASTQTL
TKVGKKKKVG SEKPGAVSPP PLPPDKDGPL GAEQTPTTSA GRAEGPVALI VNGHTEGPAP
ARSTPKEPPG LPRPLGPLPC PTPQEDFPAL GVPCPPRMPP PPGFSAVVLL KGTPPPPPPG
LVPPISKPPP GFSGLLPGSH PACVPSTVTT TKAPRLTAAP QAYLVPENFR ERNLQLIQSI
RDFLQSDEAR FGKFKSHSGE FRQGVISAAQ YYKSCRDLLG ENFQKIFNEL LVLLPDTAKQ
QELLSAHTHF RGRERPPGTK AKKNKKSAWQ GSARPAGLDC CVCPTCQQVL AHGDVSSHQA
LHAAQDHDFP SLQAIARILT
//
