ID A0A6P6BQ03_PTEVA Unreviewed; 901 AA.
AC A0A6P6BQ03;
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_023377186.1};
OS Pteropus vampyrus (Large flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Pteropodinae; Pteropus.
OX NCBI_TaxID=132908 {ECO:0000313|Proteomes:UP000515202, ECO:0000313|RefSeq:XP_023377186.1};
RN [1] {ECO:0000313|RefSeq:XP_023377186.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_023377186.1};
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_023377186.1; XM_023521418.1.
DR AlphaFoldDB; A0A6P6BQ03; -.
DR GeneID; 105303331; -.
DR CTD; 90850; -.
DR Proteomes; UP000515202; 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:UP000515202};
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 28..68
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 281..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..327
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..495
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..537
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 901 AA; 98988 MW; 14618E914554AF31 CRC64;
MATAAGTDSR RAALEAAAAA PERGGGSCVL CCGDLEATAL GRCDHPVCYR CSTKMRVLCE
QRYCAVCREE LRQVVFGKKL PAFATIPIHQ LQHEKKYDIY FADGKVFALY RQLLHHECPR
CPELPPFGLF GDLEQHMRKQ HELFCCKLCL KHLKIFTYER KWYSRKDLAR HRMQGDPDDT
SHRGHPLCKF CDERYLDNDE LLKHLRRDHY FCHFCDSDGA QDYYSDYAYL REHFREKHFL
CEEGRCSTEQ FTHAFRTEID LKAHRTACHS RSRAEARQNR QIDLNFSYTP RHSRRNEGIV
SGEDYEEVDR YNRQGRASRA SGRGAQQNRR GSWREEEDRE VAAAIRASVV TQQQQEMHRS
EDREEGSRLK KEEAGVRGPE EPRGPRRLPR TQGEGPGPKE ASTNGPVSQE TFPTTSPASG
ATLPSTLLPP TLKLKDEDFP SLCTSASSCS AAAGLGPMGL ALAYPVPIRS RSTFQEDDFP
ALVSSTSKPS TAPTSLISAW NSSSSSKKVV QPTSGAQATS GGSQPPRKAG KGGKGSKKGG
LPVTEEEEEE DSRISLTAPE LRSGPTTVAV SSLLALASTQ TFTKVGKKKK VGSEKLGAAS
PPPLLPDKNG PPGAEQAPPV PIGRAEGPVA VIVNGHTEGS TPARSVAKEP PGLPRPLGPL
PCHTPQEDFP ALSSSCPPRM PPPPGFSTVV LLKGTPPPPP PGLVPSVSKP PPGFSGLLPS
PHPACVPSTT TTTKAPRLTP VPQAYLVPEN FRERNLQLIQ SIKDFLQSDE ARFSEFKSHS
GEFRQGVISA AQYYKSCRDL LGDNFQKIFN ELLVLLPDTA KQQELLSAHT DFQGRERPPG
TKAKKKKNAW QASTWQAGLD CCVCPTCQQV LAHCDVSSHQ ALHTARDDDF PSLQAVARTL
T
//
