ID A0A4X2KPI6_VOMUR Unreviewed; 900 AA.
AC A0A4X2KPI6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
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|Ensembl:ENSVURP00010014074.1};
OS Vombatus ursinus (Common wombat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010014074.1, ECO:0000313|Proteomes:UP000314987};
RN [1] {ECO:0000313|Proteomes:UP000314987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yazar S.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSVURP00010014074.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSVURP00010014074.1}
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 RefSeq; XP_027718889.1; XM_027863088.1.
DR AlphaFoldDB; A0A4X2KPI6; -.
DR STRING; 29139.ENSVURP00010014074; -.
DR Ensembl; ENSVURT00010016021.1; ENSVURP00010014074.1; ENSVURG00010010805.1.
DR GeneID; 114043863; -.
DR CTD; 90850; -.
DR GeneTree; ENSGT00390000014178; -.
DR OMA; CEKKYDI; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000314987; 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; 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; 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:UP000314987};
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 32..72
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..358
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..408
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..433
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..457
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 100168 MW; E35A755AE7617350 CRC64;
MAASAGSAAP GRPGRPRAAP AAAPPERGGG SCVLCCGDLE ATALGRCDHP VCFRCSTKMR
VLCEQRYCAV CREELRQVVF GKKLPAFATI PIHQLQYEKK YDIYFADGKV YALYRKLLQH
ECPLCPEQRP FSLFVDLEQH MRKQHELFCC KLCVKHLKIF TYERKWYSRK DLARHRIHGD
PDDTSHRGHP LCKFCDERYL DNDELLKHLR RDHYFCHFCD SDGAQEYYSD YEYLREHFRE
KHFLCEEGRC NTEQFTHAFR TEIDYKAHKT SCHSKSRAEA RQNRQIDLQF SYAPRHARRG
EGVVGGDDYE EVDRHNRQSR ANRPGGRGAQ QNRRGSWRYK REEEDRDVAA AVRASVAARR
QEEKKWVEDK EDGGKVKKDE GKDSEETRSS RRAPKPSAEA PAPKEATANG PASQEDFVSF
SSSAGGALQS SLQPASVKLK EEDFPSLSSS SAPTVSSGMS LTYTVTAKKT SAFQEEDFPA
LVSKMRPSKA VSSITSAWNN NSSKSVVRPV APVQATSSQL TKKPSLITKG SGKASKKNNK
ALVSDDEDDS IGLTTQEIRN APTMFDVSSL LAASSSQPFI KVSKKKKTGA EKQNSASPPP
QPPMLEATAK PAWREKAPSP EHAPAPAFTA NGSEKPVAIV NGHSEKAAHV GSVPREPPGL
TKPPVTNQCP LPQEDFPALC SAGPPRMQPP PGFNSVVLLK SPPPPPGLSP PISKPPPGFT
IIPSNSISEP ITTSMKEQGP CQGTYLIPEN FQQRNMQLIQ SIKELLQSDE SRFNKFKSHS
GQFRQGRISA AQYYKSCREL LGENFRKIFS ELLVLLPDTA KQQELLSAHN DFRVQEKQGA
PKSRKNKKSA WPASTPSELD CCICPICHQV LTQDDLGTHR ALHIEDEEFP SLQAISRIIS
//
