ID A0A2K6TY78_SAIBB Unreviewed; 844 AA.
AC A0A2K6TY78;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE SubName: Full=Zinc finger protein 598, E3 ubiquitin ligase {ECO:0000313|Ensembl:ENSSBOP00000024627.1};
GN Name=ZNF598 {ECO:0000313|Ensembl:ENSSBOP00000024627.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000024627.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000024627.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSBOP00000024627.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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DR AlphaFoldDB; A0A2K6TY78; -.
DR STRING; 39432.ENSSBOP00000024627; -.
DR Ensembl; ENSSBOT00000041487.1; ENSSBOP00000024627.1; ENSSBOG00000028788.1.
DR GeneTree; ENSGT00390000014178; -.
DR OMA; CEKKYDI; -.
DR Proteomes; UP000233220; 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; 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; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000233220}.
FT DOMAIN 134..155
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 216..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..276
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..303
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..476
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..488
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 93001 MW; CD08F413258F9A56 CRC64;
MRVLCEQRYC AVCREELRQV VFGKKLPAFA TIPIHQLQCE KKYDIYFADG KVYALYRQLL
QHECPRCPEL PPFSLFGDLE QHMRKQHELF CCRLCLQHLQ IFTYERKWYS RKDLARHRMQ
GDPDDTSHRG HPLCKFCDER YLDNDELLKH LRRDHYFCHF CDSDGAQDYY SDYAYLREHF
REKHFLCEEG RCSTEQFTHA FRTEIDLKAH RTACHSRSRA EARQNRQIDL QFSYAPRHSR
RNEGVVGGDD YEEVDRYSRQ GRAARAGTRG AQQSRRGSWR YKREEEDREL AAAVRASVAV
QQQEEARRSE DREEGGRPKK EEAAARGPEE PRGPRHPPRT QGEGPGPKET STNGPVSQET
FPVTGPATPG CVWVPGPLPP PSPKLKDEDF PSLSASTSSS CSTAATLASV GLALPYAIPA
RSRSAFQEED FPALVSSAPK PGTTPTSLVS AWNSSSSSKK VAQPPPSAQA ASSGQPTRKA
GKGNRGGRKG GLPLPEEEEG GSLAAQEPRS ARPMGSVSSA LRPASTQPSK VGKKKKVGSE
KPGTALPQPP PPSCPPGPPQ APEAPATRAE GPAAIIVNGH TEGPAPARSV PKEPPGLPKP
LGSFPCPQED FPALGGPCPP RMLPPPGFSA VVLLKGTPPP PPPGLVPPVS KPPPGFSGLP
SPHPACVPGP ATTTTKAPRP TPASRAYLVP ENFRERNLQL IQSIRDFLQS DEARFSEFKS
HSGEFRQGLI SAAQYYKSCR DLLGENFQKV FNELLVLLPD TAKQQELLSA HMDFCSREKP
PSTKSKKNKK SVWQATTQQA GLDCRVCPTC QQVLAHGDVS SHQELHAARD DDFPSLQAIA
RIIT
//