ID H0WXJ0_OTOGA Unreviewed; 898 AA.
AC H0WXJ0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 28-JAN-2026, entry version 65.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000007176.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000007176.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSOGAP00000007176.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; AAQR03078004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03078005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WXJ0; -.
DR FunCoup; H0WXJ0; 1320.
DR STRING; 30611.ENSOGAP00000007176; -.
DR Ensembl; ENSOGAT00000008025.2; ENSOGAP00000007176.2; ENSOGAG00000008022.2.
DR eggNOG; KOG2231; Eukaryota.
DR GeneTree; ENSGT00390000014178; -.
DR HOGENOM; CLU_015828_0_0_1; -.
DR InParanoid; H0WXJ0; -.
DR OMA; CEKKYDI; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
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:UP000005225};
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 27..67
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 315..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..539
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..580
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 99122 MW; 5B779480E9EB1294 CRC64;
AAAAGAEGRR TELEAVVTAP ERGGGSCVLC CGDLEATALG RCDHPVCYRC STKMRVLCEQ
RYCAVCREEL RQVVFGKKLP AFATIPLHQL QHEKKYDIYF ADGKVFALYR QLLQHECPRC
PELPPFSLFG DLEQHMRKQH ELFCCRLCLQ HLQIFTYERK WYSRKDLARH RMQGDPDDTS
HRGHPLCKFC DERYLDNDEL LKHLRRDHYF CHFCDADGAQ DYYSDYAYLR EHFREKHFLC
EEGRCSTEQF THAFRTEIDL KAHRTACHSR SRAEARQNRQ IDLQFIYAPR HSRRNEGVIG
GEDYEEVDRY SRMGRVGARG AQQSRRGSWR YKREEEDREV AAVIRASVAA QQQEETRRSE
DREEGSRPKK EETAARGSEE PRGPRRMLRT QGEGPSARET STNGPLSQET FATGASPMRY
VVGGQVTLPS PAPKLKDEDF PSLSASTSSS CSTATAPGPV GLALVYPIPR DRNTFQEEDF
PALVSSGSKP SAAAAPTSLI SAWNSNCSKK MVQPSPAAQA AGGGSQPTRK AGKGSRGKKG
GPPATEEEER GQELRSVHTI VSVSSPLGPA STQTSTQTSK IGKKKKVGSE KPSATSPQPL
PLSCTPKSLG AEQAPDIPTS RAEGPVGIVN GHAEGLSLAR STPKEPPGLP RPLGPLPCPT
PQDDFPALGG PCPPRMPPPP GFNTVVLVKP TPPPPPPGLA PPVSKPPPGF SGLLPSPHTA
CVPSPTNTTK APRLPPIPRA YLVPENFRER NLQLIQSIKD FLQSDEACFS KFKSHSGEFR
QGVISAAQYY KSCRDLLGEN FQKIFNELLV LLPDTAKQQE LLSAHTDFRS REKPPSTKSK
KNKKSAWQTD TRQVGLDCCV CPTCQQVLAH GDVSSHQALH AARDDDFPSL QAIARIIT
//
