ID A0A6P6E553_OCTDE Unreviewed; 937 AA.
AC A0A6P6E553;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
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_023567469.1};
OS Octodon degus (Degu) (Sciurus degus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Octodontidae;
OC Octodon.
OX NCBI_TaxID=10160 {ECO:0000313|Proteomes:UP000515203, ECO:0000313|RefSeq:XP_023567469.1};
RN [1] {ECO:0000313|RefSeq:XP_023567469.1}
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_023567469.1; XM_023711701.1.
DR AlphaFoldDB; A0A6P6E553; -.
DR FunCoup; A0A6P6E553; 1295.
DR GeneID; 101565450; -.
DR CTD; 90850; -.
DR InParanoid; A0A6P6E553; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000515203; 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:UP000515203};
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 29..69
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 351..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..369
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..468
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 102856 MW; 6263EA0EC13E585C CRC64;
MAAAVDAEGR PAVLEAVIAA PPERGGGSCV LCCGDLEATA LGRCDHPVCY RCSTKMRVLC
EQRYCAVCRE ELRQVVFGKK LPAFATIPIH QLQHEKKYDI YFADGKVFAL YRQLLQHECP
QCPQLPPFGL FGDLEQHMRK QHELFCCKLC LKHLKIFTYE RKWYSRKDLA RHRMQGDPDD
TSHRGHPLCK FCDERYLDND ELLKHLRRDH YFCHFCDSDG AQDYYSDYAY LREHFREKHF
LCEEGRCSTE QFTHAFRTEI DLKAHRMACH SRSRAEARQN RQIDLQFSFT PRHSRRTEGS
WLRTGEPLLQ YDLDGRPISP SALLGARTVT GCMLTTGVVS GEDYEEVDRY NRQGRAGRAS
GRGAQQSRRG SWRYKREEED REVAAAIRAS VATQQQDETR KSEDHEEGSR PKKEEGAARG
SEEPHGPRHL PRTQGEGPGP KEASGNGPVS QEASQGPGPA AAPLSTLLPP TPKLKDEDFP
SLHASTSSCC PVTASGPIGL ALVYPGATRG RNTFQEEDFP ALVSSVVKPS TTAPSLISAW
NSSCGKKGAV PTPGAQATSG GGQPPKKPGK GSKGCRKADS VPVEEEEGGG LTVQELRAIP
TTVAVSTLLG SASTYTSTKV SKKKKVGSDK PGAVPSPPVP PERTPNHPGA EQVLDISVSR
AEGPVPVING HTEGPASVRS TPKEPPGLPR PLGPLPYPTP QEDFPALGGP CPPRMPPPPG
FNTVVLLKGA PPPPPPGLMP PISKPPPGFS SFLPGPHPAC VPSPTTTTVK APRLTPIPRS
YIIPANFQDR NLKLIQSIMV FLHSDKARFS KFKSHSGEFR KGMISAAQYY RSCRDLLGEN
FQKIFSELVL LLPDIAKQHE LLSAHTDFCS REKPPVAKSK KNKKNAWQAN TQRMGLDCCV
CPTCQQVLGH DDVSSHQASH AREDDFPSLQ AIARIIT
//
