ID A0A8B7RYT1_HIPAR Unreviewed; 907 AA.
AC A0A8B7RYT1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
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_019504375.1};
OS Hipposideros armiger (Great Himalayan leaf-nosed bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Rhinolophoidea;
OC Hipposideridae; Hipposideros.
OX NCBI_TaxID=186990 {ECO:0000313|Proteomes:UP000694851, ECO:0000313|RefSeq:XP_019504375.1};
RN [1] {ECO:0000313|RefSeq:XP_019504375.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_019504375.1};
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_019504375.1; XM_019648830.1.
DR AlphaFoldDB; A0A8B7RYT1; -.
DR GeneID; 109385983; -.
DR KEGG; hai:109385983; -.
DR CTD; 90850; -.
DR OrthoDB; 3838338at2759; -.
DR Proteomes; UP000694851; 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:UP000694851};
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 30..70
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 315..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..361
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..544
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 907 AA; 99396 MW; 4DDAD592CEBE1305 CRC64;
MAAAAASADS RRAVLEAAAA AAPERGGGSC VLCCGDLEAT ALGRCDHPVC YRCSTKMRVL
CEQRYCAVCR EELRQVVFGK KLPAFATIPL HLLQHEKKYD IYFADGKVYA LYRQLLHHEC
PRCPELPPFG LFGDLEQHMR KQHELFCCKL CLKHLKIFTY ERKWYSRKDL ARHRMQGDPD
DTSHRGHPLC KFCDERYLDN DELLKHLRRD HYFCHFCDSD GAQDYYSDYA YLREHFREKH
FLCEEGRCST EQFTHAFRTE IDLKAHKTAC HSRSRAEARQ NRQIDLQFNY APRHSRRNEG
IVGGEDYEEV DRYNRQGRAG RASGRGAQQS RRGSWRYKRE EEDREVAAAI RASVAAQQQQ
QETHRSEDRE DGSRLKKEEA GMWGPEEPRG PRRLPRTQGE GQGPKEASTN GSVSQEAFPA
TSPAAGATLQ STLPPPTSKL KDEDFPSLCT SASSSCSAAA ALGPVGLALA YTVSTRGRST
FQEDDFPALV SSISKPSTAP TSLISAWNSS SSSKKVVQPT PGAQAAGGGS QPTRKVGKGG
KGSRKGGLPP TEEEEEEDSR IGLTAQELRS VPTTVAVSSL LALASSQTFT KVGKKKKMGS
EKLGAASPPP LPPDKNGSPG AEQAPMGRAE GPVAVIVNGH AEGSASARSI PKEPPGLPRP
LGPLPCPTPQ EDFPALGGPC PPRMPPPPGF STVVLLKGTP PPPPPGLVPP PVSKPPPGFS
GLLPSSHPAC VSSTTTTTKA PRLTPAPQAY LVPENFRERN LQLIQSIKDF LQSDEARFSE
FKNHSGEFRQ GVISAAQYYK SCRDLLGESF QKIFNELLVL LPDTAKQQEL LSAHRDFRGR
ERPPGTKAKK NKKNAWQANT WQVGLDCCVC PTCQQVLAHG DVSSHQALHA AQDDDFPSLQ
AVARTLT
//
