ID A0A8C9C4P5_PHOSS Unreviewed; 910 AA.
AC A0A8C9C4P5;
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:ENSPSNP00000016126.1};
OS Phocoena sinus (Vaquita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Phocoenidae; Phocoena.
OX NCBI_TaxID=42100 {ECO:0000313|Ensembl:ENSPSNP00000016126.1, ECO:0000313|Proteomes:UP000694554};
RN [1] {ECO:0000313|Ensembl:ENSPSNP00000016126.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Morin P., Mountcastle J., Fungtammasan C., Rhie A., Rojas-Bracho L.,
RA Smith C.R., Taylor B.L., Gulland F.M.D., Musser W., Houck M., Haase B.,
RA Paez S., Howe K., Torrance J., Formenti G., Phillippy A., Ryder O.,
RA Jarvis E.D., Fedrigo O.;
RT "Phocoena sinus (Vaquita) genome, mPhoSin1, primary haplotype.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPSNP00000016126.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPSNP00000016126.1}
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 RefSeq; XP_032462736.1; XM_032606845.1.
DR AlphaFoldDB; A0A8C9C4P5; -.
DR Ensembl; ENSPSNT00000018199.1; ENSPSNP00000016126.1; ENSPSNG00000011838.1.
DR GeneID; 116740846; -.
DR KEGG; psiu:116740846; -.
DR CTD; 90850; -.
DR GeneTree; ENSGT00390000014178; -.
DR Proteomes; UP000694554; Chromosome 15.
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:UP000694554};
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 281..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..366
FT /note="Low complexity"
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 495..506
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..547
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..633
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..670
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 99330 MW; EAAD463894441746 CRC64;
MAAAAAADPE GRRAALEAAV AAPERGGGSC VLCCGDLEAT ALGRCDHPVC YRCSTKMRVL
CEQRYCAVCR EELRQVVFGK KLPTFATIPI HQLQHEKKYD IYFADGKVFA LYRQLLQHEC
PRCPELPPFG LFGDLEQHMR KQHELFCCKL CLKHLKIFTY ERKWYSRKDL ARHRMQGDPD
DTSHRGHPLC KFCDERYLDN DELLKHLRRD HYFCHFCDSD GAQDYYSDYA YLREHFREKH
FLCEEGRCST EQFTHAFRTE IDLKAHKMAC HSRSRAEARQ NRQIDLQFSY TPRHSRRNEG
VVGGEDYEEL DRYNRQGRTG RASGRGAQQS RRGSWRYKRE EEDREVAAAI RASVAAQQQQ
QQQQQQDTRR SEDQEEGSRP RKEEAGARGP EEPRGPRRLP RTQGEGPGSK EASINGPVSQ
EALPATGSAA GATFPSALPP PTSKLKDEDF PSLCASTSPC SAAAALGPVG LAVAYSVPAR
GRSTFQEEDF PALVSSASKP STAPTSLISA WNSSGSKKVA HPAPGAQSAS GGSQPPRKAG
KGGKGGKKSG LPCAEEEEEE DGRSSLTTQE VWGVPTTVAV SSLLAVASTQ TFTKVGKKKK
VGSEKSGASS PPPLPPDKDG PPGAEQAPAA PTGRAEGSAA VIVNGHTEGL VPARSIPKEP
PGLPRPLGPL PCPTPQEDFP ALCGPCPPRM PPPPGFNTVV LLKGAPPPPP PGLVPPVSKP
PPGFSGLLPS PHPACVPSTT TTTKAPTPVP RAYLIPENFR ERNLQLIQSI KDFLQSDEAC
FSKFKSHSGQ FRQGVISAAQ YYKSCRDLLG ENFQKIFNEL LVLLPDTAKQ QELLSAHTGF
RGRERPPGTK AKKSKKSAWQ ASTQQAGLDC CVCPTCQQVL AHGDVNSHQA LHAARDDDFP
SLQAIARILT
//
