ID A0A8M1G429_URSMA Unreviewed; 915 AA.
AC A0A8M1G429;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
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_040490386.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_040490386.1};
RN [1] {ECO:0000313|RefSeq:XP_040490386.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_040490386.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_040490386.1; XM_040634452.1.
DR AlphaFoldDB; A0A8M1G429; -.
DR GeneID; 103668776; -.
DR KEGG; umr:103668776; -.
DR CTD; 90850; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000261680; 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:UP000261680};
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 31..71
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 282..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..551
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_040490386.1"
SQ SEQUENCE 915 AA; 99750 MW; 74A022DE462D042B CRC64;
VDQAAAAAAG AEGRRAALEA AAAPERGGGS CVLCCGDLEA TALGRCDHPV CYRCSTKMRV
LCEQRYCAVC REELRQVVFG KKLPAFATIP LQQLQHEKKY DIYFADGKVF ALYRQLLQHE
CPQCPELPPF GLFGDLEQHM RKQHELFCCK LCLKHLKIFT YERKWYSRKD LARHRMQGDP
DDTSHRGHPL CKFCDERYLD NDELLKHLRR DHYFCHFCDS DGAQDYYSDY AYLREHFREK
HFLCEEGRCS TEQFTHAFRT EIDLKAHRTA CHSRSRAEAR QNRQIDLQFS YAPRHSRRNE
GVVGGEDYEE VDRYNRQGRT GRASGRGAQQ SRRGSWRYKR EEEDREVAAA IRASVAVQQQ
QQQQQQETRR SEDREEDGRA KKEEAGLRGL EEPRGPRRPP RTQGEGAGLK EASPNGPVSQ
EGLPAPGPAT GATLPSTLPP PTSKLKDEDF PSLCASTSSS SSSCSAATAL GPVGLALAYP
VPARGRSTFQ EDDFPALVSS ACKPSTAPTS LISAWNSSSS KKVAHPSTGA QAAGGSSQPP
RKAGKGGKGS KKGGLPPSEE EEEDGRAGLT AQELRSVPTT VAVSSLLALA STQTVTKVGK
KKKVGLEKPG AASPPPLPPD KDGPPGAEEA PTTTAGRAEG PIALIVNGHT EGPAPARSTP
KEPPGLPRPL GPLPCPTPQE DFPALGVPCP PRMPPPPGFN AVVLLKGTPP PPPPGLVPPV
SKPPPGFSGL LPSPHPACVP STATTTKAPR LTPTPQAYLV PENFRERNLQ LIQSIKDFLQ
SDEARFGKFK SHSGEFRQGV ISAAQYYKSC RDLLGENFQK IFNELLVLLP DTAKQQELLS
AHTHFRGRER PPGTKAKKNK KSAWQASTRP AGLDCCVCPT CQQVLAHGDV SSHQALHAAQ
DNDFPSLQAI ARILT
//