ID A0A8C4QG68_EPTBU Unreviewed; 892 AA.
AC A0A8C4QG68;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Eptatretus burgeri (Inshore hagfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC Myxiniformes; Myxinidae; Eptatretinae; Eptatretus.
OX NCBI_TaxID=7764 {ECO:0000313|Ensembl:ENSEBUP00000014902.1, ECO:0000313|Proteomes:UP000694388};
RN [1] {ECO:0000313|Ensembl:ENSEBUP00000014902.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSEBUP00000014902.1}
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 AlphaFoldDB; A0A8C4QG68; -.
DR Ensembl; ENSEBUT00000015478.1; ENSEBUP00000014902.1; ENSEBUG00000009389.1.
DR GeneTree; ENSGT00390000014178; -.
DR OMA; CEKKYDI; -.
DR Proteomes; UP000694388; 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 SUPFAM; SSF57850; RING/U-box; 1.
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:UP000694388};
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 60..100
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 24..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..544
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..642
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 98397 MW; 4683942F5810A1DA CRC64;
MASQSKIHGP TKSQLHDRFQ VRVQPQPRGR VQVHPGVGTV ASGGKKGEEV KGGSPGEGVC
VVCCQDMNVV AMGSCDHPVC LACSVKMRVL CGQPYCAVCR LHLDKVFITR TPTPFVSLDP
RTGISENEYG FSFCDGDLYA KFKALLSHTC PLCPKLQPFG TLGQLQAHMR RVHDLHACDL
CLKHLKIFTH ERRWYSRQDL AQHRRSGDTQ DRSHRGHPLC QFCSVRFLDN DELLRHLRQN
HYYCHFCDAD GSNEYYSDYE SLKDHFRRAH FLCEEGECAH EQFTHAFRSE IDLRAHRATV
HSRNRAEARH TRQLELAFSY PSRHVRCPDA RSFEEDFPSL QANSNVTFHT RTCSWKPSNV
PRTQGATQSA VQPKDCLTLT TILQPKAPTP AVARPGLTNS KTAPAASKTA QPSFAAEDFP
ALSRSSCHGA ATPTTSAWCG GAAVKLSSAA TISKASAKFS AAKVPIQPSL AIRPDGIAKN
DAGLKASALG KELVEKERLR IPKNQGTMDP MESSSSCSTK NDASSNAAQE MWSRKPGKKK
KKKGAGLAEV GNGLAKVDAP SKESEIVSVT EVKLKEDKTR DTKITKDEKK TKREQIHVEN
EDKKGQKHKN SDNGDDAPLE EEPSKWTETK GKKGKGKNKV KGVARGESES ATSADGKVDG
EENLESKTEK RGLTAPVLAN GHVDGLANGL TALQLKRSST CPPPPPPGLR KPDVPGISLE
DFPVPLVRGP YLQPENFSER NQALIKAIRA CLLDDKDRFN EFRRISGLFR QGTTSAEAYY
QQCRDLLGNS SFPSIFPELL ILLPDLGKQC ELLSVHGVWM ETHESCRTTK PVSKGSRRAK
RSVRASDDVE KTEKPLPGCS ICQRCGQVLG REDVTWHAER HMDTDFPQLG HA
//
