ID A0A2K5PIJ0_CEBIM Unreviewed; 842 AA.
AC A0A2K5PIJ0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE SubName: Full=Zinc finger protein 598, E3 ubiquitin ligase {ECO:0000313|Ensembl:ENSCCAP00000003468.1};
GN Name=ZNF598 {ECO:0000313|Ensembl:ENSCCAP00000003468.1};
OS Cebus imitator (Panamanian white-faced capuchin) (Cebus capucinus
OS imitator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Cebus.
OX NCBI_TaxID=2715852 {ECO:0000313|Ensembl:ENSCCAP00000003468.1, ECO:0000313|Proteomes:UP000233040};
RN [1] {ECO:0000313|Ensembl:ENSCCAP00000003468.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCAP00000003468.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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DR AlphaFoldDB; A0A2K5PIJ0; -.
DR STRING; 9516.ENSCCAP00000003468; -.
DR Ensembl; ENSCCAT00000019851.1; ENSCCAP00000003468.1; ENSCCAG00000018310.1.
DR GeneTree; ENSGT00390000014178; -.
DR OMA; CEKKYDI; -.
DR Proteomes; UP000233040; Unassembled WGS sequence.
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:UP000233040}.
FT DOMAIN 134..155
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 217..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..604
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 388..399
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..454
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..484
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 92859 MW; B6BA9E714912B14A CRC64;
MRVLCEQRYC AVCREELRQV VFGKKLPAFA TIPIHQLQYE KKYDIYFADG KVYALYRQLL
QHECPRCPEL PPFSLFGDLE QHMRKQHELF CCRLCLQHLQ IFTYERKWYS RKDLARHRMQ
GDPDDTSHRG HPLCKFCDER YLDNDELLKH LRRDHYFCHF CDSDGAQDYY SDYAYLREHF
REKHFLCEEG RCSTEQFTHA FRTEIDLKAH RTACHSRSRA EARQNRQIDL QFSYAPRHSR
RNEGVVGGDD YEEVDRYSRQ GRAARAGTRG AQQSRRGSWR YKREEEDREV AAAVRASVAA
QQQEEARRSE DREEGGRPKK EEAAVRGPEE PRGPRHPPRT QGEGPGPKET STNGPVSQET
FPVTGPATPG CVPLPPPSPK LKDEDFPSLS ASTSSSCSTA ATLASVGLAL PYAIPARSRS
AFQEEDFPAL VSSAPKPGTT PTSLVSAWNS SSSSNKVARP PPSAQAASSG QPTRKAGKGN
RGGRKGGLPL PEEEESGSPA AQEPRSARPM GSVASALRPA STQPSKVGKK KKVGSETPST
ALPQPPPPSC PPGPAQAPET PATRAEGPVA IIVNGHTEGP APARSVPKEP PGLPRPLGSF
PCPPEDFPAL GGPCPPRMPP PPGFSAVVLL KGMPPPPPPG LAPPVSKPPP PGFSGLLPSP
HPACVPSPAT TITKAPRPTP APRAYLVPEN FRERNLQLIQ SIRDFLQSDE ARFSEFKSHS
GEFRQGLISA AQYYKSCRDL LGENFQKVFN ELLVLLPDTA KQQELLSAHM DFCSREKPPS
SKSKKNKKSA WQATTEQAGL DCRVCPTCQQ VLAHGDVSSH QELHAARDDD FPSLQAIARI
IT
//