ID A0A8C6FEY9_MOSMO Unreviewed; 905 AA.
AC A0A8C6FEY9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-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|Ensembl:ENSMMSP00000001249.1};
OS Moschus moschiferus (Siberian musk deer) (Moschus sibiricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Moschidae;
OC Moschus.
OX NCBI_TaxID=68415 {ECO:0000313|Ensembl:ENSMMSP00000001249.1, ECO:0000313|Proteomes:UP000694544};
RN [1] {ECO:0000313|Ensembl:ENSMMSP00000001249.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMMSP00000001249.1}
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}.
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 AlphaFoldDB; A0A8C6FEY9; -.
DR Ensembl; ENSMMST00000001368.1; ENSMMSP00000001249.1; ENSMMSG00000000995.1.
DR GeneTree; ENSGT00390000014178; -.
DR Proteomes; UP000694544; 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:UP000694544};
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 29..69
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 280..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..392
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 493..504
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..535
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..545
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 98857 MW; 84687CE44A2F084E CRC64;
MAAAAGPEGQ RAAQEAAAAA APERGGGSCV LCCGDLEAMA LGRCDHPVCY RCSTKMRVLC
EQRYCAVCRE ELRQVVFGKA LPAFAAIPLH QLQHEKQHDI YFTDGRVFAL YRQLLQHECP
HCPERPPFSL FGDLEQHMRK QHELFCCKLC LRHLQIFTHE RKWYSRKDLA RHRVQGDPDD
TSHRGHPLCK FCDERYLDND ELLKHLRRDH YFCHFCDADG AQDYYSDYTY LREHFREKHF
LCEEGRCSTE QFTHAFRTEI DLKAHRTACH SRSRAEARQN RQIDLQFSYA PRHSRRSEGV
IGGEDYEELD RYNRQGRMGR ASGRGAQQSR RGSWRYKREE EDREVAAAIR ASVATQQQQQ
QQQETRRTED QEEGGRPKKE DAGLRGPEEA RGPRRQARTQ GEGPGPKEAS ANGPVSQEAF
STTGPAAGAT LPNALPAPTP KLKDEDFPSL CASASSLSPA AAAPGPVGLA LAYPVPARGR
TTFQEEDFPA LVSSASKPSS TPTSLISAWN SGASKKVAHP APGSQSTSGG SQPPRKSGKG
GKGGKKGGPL PMEEVEEDGR VGLTAQELRS VPTTVAVSSL LAGAATQTFT KVGKKKKVGS
EKSGAASPPP PDREGPPGAE LAPTAPPGRA EGPAAVIVNG HSEGPAPARS TPKEPPGLPR
PLGPPPCPTP QEDFPALCGP CPPRMPPPPG FNAVVLLKGT PPPPGLAPPI SKPPPGFSGL
PSSPHPACVP STTITTKAPR PTPVPRAYLV PENFRERNLQ LIQSIRDFLQ SDEARFSKFK
SYSGEFRQGV ISAAQYYKSC RDLLGENFEK IFNELLVLLP DTAKQQELLL AHTDFRGREK
PPSMKAKKNR KSVWQSSTRQ AGLDCCVCPT CQQVLAHGDV GSHQALHAAR DNDFPSLQAL
ARILT
//
