ZN598_DANRE
ID ZN598_DANRE Reviewed; 953 AA.
AC Q6PFK1; Q3S3B5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=E3 ubiquitin-protein ligase ZNF598 {ECO:0000250|UniProtKB:Q86UK7};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86UK7};
DE AltName: Full=Zinc finger protein 598 {ECO:0000250|UniProtKB:Q86UK7};
GN Name=znf598 {ECO:0000250|UniProtKB:Q86UK7};
GN Synonyms=zfp598 {ECO:0000250|UniProtKB:Q86UK7};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-360 (ISOFORM 1).
RA Tsai S.C., Kang C.K., Ho H.C.;
RT "Purification and characterization of zebrafish ZFP598.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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 a subset of 40S ribosomal subunits. Stalling
CC precludes synthesis of a long poly-lysine tail and initiates the RQC
CC pathway to degrade the potentially detrimental aberrant nascent
CC polypeptide. {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.
CC {ECO:0000250|UniProtKB:Q86UK7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PFK1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PFK1-2; Sequence=VSP_020668, VSP_020669;
CC -!- SIMILARITY: Belongs to the ZNF598 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57520.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABA00477.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC057520; AAH57520.1; ALT_INIT; mRNA.
DR EMBL; DQ173495; ABA00477.1; ALT_INIT; mRNA.
DR RefSeq; NP_001028890.1; NM_001033718.1.
DR AlphaFoldDB; Q6PFK1; -.
DR STRING; 7955.ENSDARP00000069243; -.
DR iPTMnet; Q6PFK1; -.
DR PaxDb; Q6PFK1; -.
DR PRIDE; Q6PFK1; -.
DR GeneID; 407728; -.
DR KEGG; dre:407728; -.
DR CTD; 90850; -.
DR ZFIN; ZDB-GENE-060602-3; znf598.
DR eggNOG; KOG2231; Eukaryota.
DR InParanoid; Q6PFK1; -.
DR OrthoDB; 1003372at2759; -.
DR PhylomeDB; Q6PFK1; -.
DR PRO; PR:Q6PFK1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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..953
FT /note="E3 ubiquitin-protein ligase ZNF598"
FT /id="PRO_0000250570"
FT ZN_FING 57..97
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 215..238
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT VAR_SEQ 349..360
FT /note="GPGGQQNLRSWR -> VMALWLVRTSLS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_020668"
FT VAR_SEQ 361..953
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_020669"
SQ SEQUENCE 953 AA; 106912 MW; 3E1A14813AA51516 CRC64;
MHCAERLRTE ERASPGLIAC TAVHKPSKST RIKPTKPHHT PSNSMESALK KDTESTCVLC
CQDIDLFAVG KCDHPVCYRC STKMRVLCEQ KYCAVCREQL DKVVFLRKPE AFATLNIHHY
QCEKKYDIYF GDGKVHAQFR KILLNECPHC PEPKVFSKFE ELEQHMRKQH ELFCCKLCLK
HLKIFSYERK WYSRKDLARH RMQGDPDDTS HRGHPLCKFC DDRYLDNDEL LKHLRRDHYF
CHFCDADGAQ EYYSDYQYLS EHFRESHYLC EEGRCSTEQF THAFRTEIDY KAHKAAAHSK
NRAEARQNRQ IDIQFNYAPR QQRRNDVGGD DYEEVDRFNR QGRPGRGRGP GGQQNLRSWR
YNREEEDREM AAAMRASMAS HQEERSHAQE RSMLKPRREE KLEPDETRNN RSTARPTNDT
QARSMKSNGS LAGQDFPVLG AGAPPAPVQS MIQKPSVSLK EDDFPSLSGS VVSSPMTPAY
TNQPRKHSSF QEEDFPALVS KIKPLKPQSS AASAWSQAGS KPVVAPNKPV VLPTKMTPMS
SSSILSSTDP LPSASVPQPL TASSSRRKKM LTLTESHKDP PKIRCPSSSD DEDPHSGKTA
QEIRTVPTML DISTLLTVKG SSPQANPKAS KKKKQTTASS LGSPSHTPET VSKMAHKENV
PEKKPPETGL NKAPTAPKTN SIVNGVAEKP AEALSCTSFP ENITSSKQPV TDQAPPSKEE
EFPALISKKP PPGFKSAFPL RNSQSALPPP PPPGLGPAVS KPPPGFTGVP LNSNVEDSSV
SAVNRPTPAI GSYLIPDHFQ QRNMDLIQSI KNFLQNDETK FNEFKNYSGQ FRQGALPAVQ
YYKSCQELLG ENFNRVFNEL LVLLPDTRKQ QELLTAHGDF KALEKQQQGS KPKKSKKKAW
QTGTSSSSSL DLDCQVCPTC KQVLALKDFN THKTLHIGDD DFPSLQAISK IIS
