ID A0A9F5J7Z1_PYTBI Unreviewed; 886 AA.
AC A0A9F5J7Z1;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
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_007438818.1,
GN ECO:0000313|RefSeq:XP_025029298.1, ECO:0000313|RefSeq:XP_025029299.1,
GN ECO:0000313|RefSeq:XP_025029300.1};
OS Python bivittatus (Burmese python) (Python molurus bivittatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Henophidia; Pythonidae; Python.
OX NCBI_TaxID=176946 {ECO:0000313|Proteomes:UP000695026, ECO:0000313|RefSeq:XP_025029298.1};
RN [1] {ECO:0000313|RefSeq:XP_007438818.1, ECO:0000313|RefSeq:XP_025029298.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_007438818.1,
RC ECO:0000313|RefSeq:XP_025029298.1};
RG RefSeq;
RL Submitted (APR-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_007438818.1; XM_007438756.2.
DR RefSeq; XP_025029298.1; XM_025173530.1.
DR RefSeq; XP_025029299.1; XM_025173531.1.
DR RefSeq; XP_025029300.1; XM_025173532.1.
DR AlphaFoldDB; A0A9F5J7Z1; -.
DR GeneID; 103052783; -.
DR KEGG; pbi:103052783; -.
DR CTD; 90850; -.
DR OMA; CEKKYDI; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000695026; 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; 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:UP000695026};
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 18..58
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 279..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..344
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..396
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..517
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 98156 MW; E3979B252C29CE31 CRC64;
MAASPPLESR SADGPGSCVL CCGELEVVAL GRCEHPICYR CSVRMRALCG VRYCAVCREE
LAQVVFGKKL PPFSTIILSQ LQHEKKYDIY FTDGKVYALY RKLLQHECPL CLESRAFPTI
VDLEQHMRKQ HELFCCKLCV KHLKIFTYER KWYSRKDLAR HRIHGDPDDT SHRGHPLCKF
CDERYLDNDE LLKHLRRDHY FCHFCDSDGA QEYYSDYEYL REHFREKHFL CEEGRCSTEQ
FTHAFRTEID YKAHKTACHS KNRAEARQNR QIDLQFNYAP RHQRRSEGVV SGEDYEEVDR
YNRQVRGGRS GPRGGQQNRR GSWRYKREEE DRDIAAAVRA SVAAKRQEEK KRVEDKEDNS
RAKKEDAKDP DATNSKRGLK PSSEAPVPKE AVPKAALSQD DFPAIGSPAV NSVQSSSQLA
SVKLDEEDFP SLSISSAPPV VSAAMPLSYT ATAQKTAFQE EDFPALVSKV RPGSKMVSTL
ASAWSGGSSK NMARAITATA SSASQPTRKG ASAGSSKASK KSKVMLSNDT QDSGGSITTQ
EIRSVPTMVD VSSLLAASNS QTFVKVGKKK KVGTEKLRTA SPPTLQEMPA SLPSAEKAAD
AEHPSTVAAS PNLPSASAAL VNGHSEKSML LCNASKEPPG LKKPPVGGQC LLPQEDFPAL
GNAGPPRMPP PPGFNSVVLL SSPPPPPGLS MPPSKPPPGF TPIPATSISE NAPAPVKEPK
LCQGPYLILE NFQQRNIQLI QSIKEFLQED ESQFNKFKTY SGQFRQGLIS AAQYYKSCQE
LLGENFKKIF NELLVLLPDT AKQQELLSAY NDLKVKAPAG SSPSSLSRSK KNRKMVWQTE
PASDLDCCVC PTCQQVLTQQ DLVSHQALHL EEDEFPSLQA ISRIIS
//
