ID A0A8C9AL68_PROSS Unreviewed; 875 AA.
AC A0A8C9AL68;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 17.
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:ENSPSMP00000035044.1};
OS Prolemur simus (Greater bamboo lemur) (Hapalemur simus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Lemuridae; Prolemur.
OX NCBI_TaxID=1328070 {ECO:0000313|Ensembl:ENSPSMP00000035044.1, ECO:0000313|Proteomes:UP000694414};
RN [1] {ECO:0000313|Ensembl:ENSPSMP00000035044.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPSMP00000035044.1}
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; A0A8C9AL68; -.
DR Ensembl; ENSPSMT00000040411.1; ENSPSMP00000035044.1; ENSPSMG00000024145.1.
DR GeneTree; ENSGT00390000014178; -.
DR Proteomes; UP000694414; 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:UP000694414};
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 12..52
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 298..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..335
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..442
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..512
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..527
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..658
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..681
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 96006 MW; ABDEE5396AC4ACB7 CRC64;
MAAAAGRGGG SCVLCCGDLE ATALGRCDHP VCYRCSTKMR VLCEQRYCAV CREELRQVVF
GKKLPAFATI PIHQLQHEKK YDIYFADGKV FALYRQLLQH ECPRCPELPP FSLFGDLEQH
MRKQHELFCC RLCLQHLQIF TYERKWYSRK DLARHRMQGD PDDTSHRGHP LCKFCDERYL
DNDELLKHLR RDHYFCHFCD ADGAQDYYSD YAYLREHFRE KHFLCEEGRC STEQFTHAFR
TEIDLKAHKT ACHSRSRAEA RQNRQIDLQF SYAPRHSRRN EGVVGGEDYE EVDRYSRASR
AGMRGTQQSR RGSWRYKREE EDRDVAAAVR ASVAAQHQEE TRRSEDREEG SRPKKEEAAA
RGPEEPRGPR RVPRAQGEGP GPKDTSANGP VGQETFAAMG PATGAAPLRC VGAGALPPST
PKLKDEDFPS LSASTSSSST AAALGPVGLA LAYPVPARGR GRNTFQEEDF PALVSSASKP
STAPTSLISA WNSSCSKKVA QPTPAAQAAV GGSQPTRKAG KGSRGKKGGP PAVEEEEGSQ
ELRSTRSTVS ASAQTSKVSR KKKVGSEKPS ATSPQPLPSS CPAKPLGAEQ VPEAPASRGE
GTIALINGHA EVPAPARGAP KEPPGLPRPL GPPPCPTPQE DFPALGGPCP PRMPPPPGFN
AVVLLKGTPP PPPPGLAPPV SKPPPGFSGL LPSPHPACVP GPTTTTKAPR LPPIPRTYLV
PENFRERNLQ LIQSIRDFLQ SDEARFSEFK SHSGEFRQGM ISAAQYYKSC RDLLGENFQK
IFNELLVLLP DTTKQQELLS AHADFHSREK PPGTKSRKNK KSAWQTDTRQ AGLDCCVCPT
CQQVLAHGDV SSHQGLHAAR DDDFPSLQAI ARIIT
//
