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 28-JAN-2026, entry version 103.
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, leading to degradation of
CC nascent peptide chains. ZNF598 is activated when ribosomes are stalled
CC within an mRNA following translation of prematurely polyadenylated
CC mRNAs. Acts as a ribosome collision sensor: specifically recognizes and
CC binds collided di-ribosome, which arises when a trailing ribosome
CC encounters a slower leading ribosome, leading to terminally arrest
CC translation. Following binding to colliding ribosomes, mediates
CC monoubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS3/uS3,
CC and 'Lys-63'-linked polyubiquitination of RPS20/uS10.
CC Polyubiquitination of RPS20/uS10 promotes recruitment of the RQT
CC (ribosome quality control trigger) complex, which drives the
CC disassembly of stalled ribosomes, followed by degradation of nascent
CC peptides. {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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q86UK7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
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/HEL2 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};
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 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 FunCoup; Q6PFK1; 1670.
DR STRING; 7955.ENSDARP00000069243; -.
DR GlyGen; Q6PFK1; 1 site.
DR iPTMnet; Q6PFK1; -.
DR PaxDb; 7955-ENSDARP00000069243; -.
DR GeneID; 407728; -.
DR KEGG; dre:407728; -.
DR AGR; ZFIN:ZDB-GENE-060602-3; -.
DR CTD; 90850; -.
DR ZFIN; ZDB-GENE-060602-3; znf598.
DR eggNOG; KOG2231; Eukaryota.
DR InParanoid; Q6PFK1; -.
DR OrthoDB; 3838338at2759; -.
DR PhylomeDB; Q6PFK1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6PFK1; -.
DR Proteomes; UP000000437; Chromosome 3.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; 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; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_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; 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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Translation regulation;
KW Ubl conjugation pathway; Zinc; 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 25..39
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..518
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..779
FT /note="Polar 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
//
