ZN598_MOUSE
ID ZN598_MOUSE Reviewed; 908 AA.
AC Q80YR4; Q6KAT0; Q8R3S1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase ZNF598;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86UK7};
DE AltName: Full=Zinc finger protein 598 {ECO:0000312|MGI:MGI:2670965};
GN Name=Znf598 {ECO:0000250|UniProtKB:Q86UK7};
GN Synonyms=Zfp598 {ECO:0000312|MGI:MGI:2670965};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Natural killer cell;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 68-908 (ISOFORM 3).
RC STRAIN=Czech II; TISSUE=Embryo, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays a key role in the
CC ribosome quality control (RQC), a pathway that takes place when a
CC ribosome has stalled during translation. Required for ribosomes to
CC terminally stall during translation of poly(A) sequences by mediating
CC monoubiquitination of 40S ribosomal protein RPS10/eS10, RPS20/uS10 and
CC RPS3/uS3. Stalling precludes synthesis of a long poly-lysine tail and
CC initiates the RQC pathway to degrade the potentially detrimental
CC aberrant nascent polypeptide. Also acts as a component of the 4EHP-GYF2
CC complex, a multiprotein complex that acts as a repressor of translation
CC initiation. {ECO:0000250|UniProtKB:Q86UK7}.
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:0000250|UniProtKB:Q86UK7};
CC -!- SUBUNIT: Component of the 4EHP-GYF2 complex, at least composed of
CC EIF4E2, GIGYF2 and ZNF598. {ECO:0000250|UniProtKB:Q86UK7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80YR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YR4-2; Sequence=VSP_020667;
CC Name=3;
CC IsoId=Q80YR4-3; Sequence=VSP_020666;
CC -!- SIMILARITY: Belongs to the ZNF598 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK131127; BAD21377.1; ALT_INIT; mRNA.
DR EMBL; BC024690; AAH24690.1; -; mRNA.
DR EMBL; BC050859; AAH50859.1; -; mRNA.
DR CCDS; CCDS28490.1; -. [Q80YR4-1]
DR CCDS; CCDS89013.1; -. [Q80YR4-3]
DR RefSeq; NP_001335160.1; NM_001348231.1. [Q80YR4-3]
DR RefSeq; NP_898972.1; NM_183149.2. [Q80YR4-1]
DR RefSeq; XP_006524062.1; XM_006523999.1.
DR AlphaFoldDB; Q80YR4; -.
DR BioGRID; 229466; 5.
DR IntAct; Q80YR4; 1.
DR MINT; Q80YR4; -.
DR STRING; 10090.ENSMUSP00000038367; -.
DR iPTMnet; Q80YR4; -.
DR PhosphoSitePlus; Q80YR4; -.
DR EPD; Q80YR4; -.
DR MaxQB; Q80YR4; -.
DR PaxDb; Q80YR4; -.
DR PeptideAtlas; Q80YR4; -.
DR PRIDE; Q80YR4; -.
DR ProteomicsDB; 302131; -. [Q80YR4-1]
DR ProteomicsDB; 302132; -. [Q80YR4-2]
DR ProteomicsDB; 302133; -. [Q80YR4-3]
DR Antibodypedia; 23428; 146 antibodies from 23 providers.
DR DNASU; 213753; -.
DR Ensembl; ENSMUST00000047179; ENSMUSP00000038367; ENSMUSG00000041130. [Q80YR4-3]
DR Ensembl; ENSMUST00000234956; ENSMUSP00000157172; ENSMUSG00000041130. [Q80YR4-1]
DR GeneID; 213753; -.
DR KEGG; mmu:213753; -.
DR UCSC; uc008axn.1; mouse. [Q80YR4-1]
DR UCSC; uc008axo.1; mouse. [Q80YR4-2]
DR UCSC; uc008axp.1; mouse. [Q80YR4-3]
DR CTD; 213753; -.
DR MGI; MGI:2670965; Zfp598.
DR VEuPathDB; HostDB:ENSMUSG00000041130; -.
DR eggNOG; KOG2231; Eukaryota.
DR GeneTree; ENSGT00390000014178; -.
DR HOGENOM; CLU_015828_0_0_1; -.
DR InParanoid; Q80YR4; -.
DR OMA; NAWQTPA; -.
DR OrthoDB; 1003372at2759; -.
DR PhylomeDB; Q80YR4; -.
DR TreeFam; TF316196; -.
DR BioGRID-ORCS; 213753; 13 hits in 77 CRISPR screens.
DR ChiTaRS; Zfp598; mouse.
DR PRO; PR:Q80YR4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q80YR4; protein.
DR Bgee; ENSMUSG00000041130; Expressed in skin of snout and 259 other tissues.
DR Genevisible; Q80YR4; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR22938; PTHR22938; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Phosphoprotein; Reference proteome;
KW Transferase; Translation regulation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..908
FT /note="E3 ubiquitin-protein ligase ZNF598"
FT /id="PRO_0000250569"
FT ZN_FING 27..67
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 185..208
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 292..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q86UK7"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UK7"
FT VAR_SEQ 333..335
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020666"
FT VAR_SEQ 626..653
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15449545"
FT /id="VSP_020667"
FT CONFLICT 600
FT /note="L -> M (in Ref. 2; AAH24690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 99192 MW; 528DE75B72EDE40B CRC64;
MAAAAGAEGR RAALEAVAAP ERGGGSCVLC CGDLEATALG RCDHPVCYRC STKMRVLCEQ
RYCAVCREEL RQVVFGKKLP AFALIPIHQL QHEKKYDIYF ADGKVFALYR QLLQHECPRC
PHLPPFSLFG DLEQHMRKQH ELFCCKLCLK HLKIFTYERK WYSRKDLARH RMQGDPDDTS
HRGHPLCKFC DERYLDNDEL LKHLRRDHYF CHFCDSDGAQ DYYSDYAYLR EHFREKHFLC
EEGRCSTEQF THAFRTEIDL KAHKTACHSR SRAEARQNRQ IDLQFSFAPR HSRRSEGVVS
GEDYEEVDRY NRQGRAGRAS GRGAQQNRRG SWRYKREEED REVAAAIRAS VAAQQQEETQ
RVEDREEGSR PKKEEAAARV PEEPRGHRRL PRAQGEGSGS KEASANGPVS QEAFPATGPG
PVVALSNTLP PPSPELKEED FPSLCASTSS CCTAVTPGSV GLALAYPGPP RGKNTFQEED
FPALVSSAPK PSSAPSSLIS AWNSGCSKKG NLPTPGSQAV VGGSQPPRKA GKGSRGGRKG
GPAPVDEEDS GGLTVQGLRS VPTTVAVSSL LAPATNQSSA KVGKKKKVGS EKPGATSSPL
LPPDHTPKPS GAEQVLEAPL SKAEVPVTIV VNGHSEGSAL VRSAPKEPPG LPRPLGPLPC
PIPQEDFPAL GGPCPPRMPP PPGFSTVVLL KGTPPPPPPP PGLVPPISKP PPGFSSLLPS
SHSACAPSPT TTTTTTTTTK TPGLAPTPQA YLVPENFRER NLQLIQSIKD FLQSDEACFS
KFKSHSGEFR QGMISAAQYY KSCRDLLGES FQKIFSELLA LLPDTAKQQE LLSAHTDFCS
REKPPNSRSK RNKKNVWQTS TQQLGLDCCV CPTCQQVLAH GDVSSHQALH AARDDDFPSL
QAIARIIT
