ID ZN598_HUMAN Reviewed; 904 AA. AC Q86UK7; Q8IW49; Q8N3D9; Q96FG3; Q9H7J3; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-JAN-2026, entry version 165. DE RecName: Full=E3 ubiquitin-protein ligase ZNF598 {ECO:0000305}; DE EC=2.3.2.27 {ECO:0000305|PubMed:28065601, ECO:0000305|PubMed:28132843, ECO:0000305|PubMed:28685749, ECO:0000305|PubMed:36302773}; DE AltName: Full=Zinc finger protein 598 {ECO:0000312|HGNC:HGNC:28079}; GN Name=ZNF598 {ECO:0000303|PubMed:28132843, GN ECO:0000312|HGNC:HGNC:28079}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS TYR-453; RP THR-608 AND MET-637. RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 236-904 (ISOFORM 2), AND VARIANTS TYR-453; THR-608 RP AND MET-637. RC TISSUE=Lung, and Skin; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-904 (ISOFORM 3), AND VARIANT RP SER-725. RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 (ISOFORM 2), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431 (ISOFORM 3), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP FUNCTION, AND IDENTIFICATION IN THE 4EHP-GYF2 COMPLEX. RX PubMed=22751931; DOI=10.1128/mcb.00455-12; RA Morita M., Ler L.W., Fabian M.R., Siddiqui N., Mullin M., Henderson V.C., RA Alain T., Fonseca B.D., Karashchuk G., Bennett C.F., Kabuta T., Higashi S., RA Larsson O., Topisirovic I., Smith R.J., Gingras A.C., Sonenberg N.; RT "A novel 4EHP-GIGYF2 translational repressor complex is essential for RT mammalian development."; RL Mol. Cell. Biol. 32:3585-3593(2012). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 (ISOFORM 2), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431 (ISOFORM 3), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=28065601; DOI=10.1016/j.molcel.2016.11.039; RA Juszkiewicz S., Hegde R.S.; RT "Initiation of quality control during poly(A) translation requires site- RT specific ribosome ubiquitination."; RL Mol. Cell 65:743-750(2016). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF CYS-29. RX PubMed=28132843; DOI=10.1016/j.molcel.2016.12.026; RA Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A., Bennett E.J.; RT "ZNF598 and RACK1 regulate mammalian ribosome-associated quality control RT function by mediating regulatory 40S ribosomal ubiquitylation."; RL Mol. Cell 65:751-760(2017). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=28757607; DOI=10.1038/s41467-017-00188-1; RA Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T., RA Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R., RA Inada T.; RT "Ubiquitination of stalled ribosome triggers ribosome-associated quality RT control."; RL Nat. Commun. 8:159-159(2017). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH UBE2D3. RX PubMed=28685749; DOI=10.1038/ncomms16056; RA Garzia A., Jafarnejad S.M., Meyer C., Chapat C., Gogakos T., Morozov P., RA Amiri M., Shapiro M., Molina H., Tuschl T., Sonenberg N.; RT "The E3 ubiquitin ligase and RNA-binding protein ZNF598 orchestrates RT ribosome quality control of premature polyadenylated mRNAs."; RL Nat. Commun. 8:16056-16056(2017). RN [14] RP FUNCTION, AND FUNCTION (MICROBIAL INFECTION). RX PubMed=29719242; DOI=10.1016/j.celrep.2018.03.132; RA DiGiuseppe S., Rollins M.G., Bartom E.T., Walsh D.; RT "ZNF598 plays distinct roles in interferon-stimulated gene expression and RT poxvirus protein synthesis."; RL Cell Rep. 23:1249-1258(2018). RN [15] RP FUNCTION. RX PubMed=30293783; DOI=10.1016/j.molcel.2018.08.037; RA Juszkiewicz S., Chandrasekaran V., Lin Z., Kraatz S., Ramakrishnan V., RA Hegde R.S.; RT "ZNF598 is a quality control sensor of collided ribosomes."; RL Mol. Cell 72:469-481(2018). RN [16] RP FUNCTION. RX PubMed=32579943; DOI=10.1016/j.molcel.2020.06.006; RA Juszkiewicz S., Speldewinde S.H., Wan L., Svejstrup J.Q., Hegde R.S.; RT "The ASC-1 complex disassembles collided ribosomes."; RL Mol. Cell 79:603-614(2020). RN [17] RP FUNCTION, AND IDENTIFICATION IN THE 4EHP-GYF2 COMPLEX. RX PubMed=32726578; DOI=10.1016/j.molcel.2020.07.007; RA Hickey K.L., Dickson K., Cogan J.Z., Replogle J.M., Schoof M., RA D'Orazio K.N., Sinha N.K., Hussmann J.A., Jost M., Frost A., Green R., RA Weissman J.S., Kostova K.K.; RT "GIGYF2 and 4EHP Inhibit Translation Initiation of Defective Messenger RNAs RT to Assist Ribosome-Associated Quality Control."; RL Mol. Cell 79:950.e6-962.e6(2020). RN [18] RP FUNCTION. RX PubMed=32099016; DOI=10.1038/s41598-020-60241-w; RA Hashimoto S., Sugiyama T., Yamazaki R., Nobuta R., Inada T.; RT "Identification of a novel trigger complex that facilitates ribosome- RT associated quality control in mammalian cells."; RL Sci. Rep. 10:3422-3422(2020). RN [19] RP FUNCTION. RX PubMed=33581075; DOI=10.1016/j.molcel.2021.01.029; RA Goldman D.H., Livingston N.M., Movsik J., Wu B., Green R.; RT "Live-cell imaging reveals kinetic determinants of quality control RT triggered by ribosome stalling."; RL Mol. Cell 81:1830-1840(2021). RN [20] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=36302773; DOI=10.1038/s41467-022-34097-9; RA Narita M., Denk T., Matsuo Y., Sugiyama T., Kikuguchi C., Ito S., Sato N., RA Suzuki T., Hashimoto S., Machova I., Tesina P., Beckmann R., Inada T.; RT "A distinct mammalian disome collision interface harbors K63-linked RT polyubiquitination of uS10 to trigger hRQT-mediated subunit dissociation."; RL Nat. Commun. 13:6411-6411(2022). 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 (PubMed:28065601, PubMed:28132843, CC PubMed:28685749, PubMed:32099016, PubMed:32579943, PubMed:33581075). CC ZNF598 is activated when ribosomes are stalled within an mRNA following CC translation of prematurely polyadenylated mRNAs (PubMed:28065601, CC PubMed:28132843, PubMed:28685749). Acts as a ribosome collision sensor: CC specifically recognizes and binds collided di-ribosome, which arises CC when a trailing ribosome encounters a slower leading ribosome, leading CC to terminally arrest translation (PubMed:28065601, PubMed:28132843, CC PubMed:28685749, PubMed:30293783). Following binding to colliding CC ribosomes, mediates monoubiquitination of 40S ribosomal proteins CC RPS10/eS10 and RPS3/uS3, and 'Lys-63'-linked polyubiquitination of CC RPS20/uS10 (PubMed:28065601, PubMed:28132843, PubMed:28685749). 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 (PubMed:32099016, PubMed:32579943, PubMed:36302773). E3 CC ubiquitin-protein ligase activity is dependent on the E2 ubiquitin- CC conjugating enzyme UBE2D3 (PubMed:28685749). Also acts as an adapter CC that recruits the 4EHP-GYF2 complex to mRNAs (PubMed:22751931, CC PubMed:32726578). Independently of its role in RQC, may also act as a CC negative regulator of interferon-stimulated gene (ISG) expression CC (PubMed:29719242). {ECO:0000269|PubMed:22751931, CC ECO:0000269|PubMed:28065601, ECO:0000269|PubMed:28132843, CC ECO:0000269|PubMed:28685749, ECO:0000269|PubMed:29719242, CC ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:32099016, CC ECO:0000269|PubMed:32579943, ECO:0000269|PubMed:32726578, CC ECO:0000269|PubMed:33581075, ECO:0000269|PubMed:36302773}. CC -!- FUNCTION: (Microbial infection) Required for poxvirus protein synthesis CC by mediating ubiquitination of RPS10/eS10 and RPS20/uS10 CC (PubMed:29719242). Poxvirus encoding mRNAs contain unusual 5' poly(A) CC leaders and ZNF598 is required for their translational efficiency, CC possibly via its ability to suppress readthrough or sliding on shorter CC poly(A) tracts (PubMed:29719242). {ECO:0000269|PubMed:29719242}. 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:0000305|PubMed:28065601, CC ECO:0000305|PubMed:28132843, ECO:0000305|PubMed:28685749, CC ECO:0000305|PubMed:36302773}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:28065601, ECO:0000269|PubMed:28132843, CC ECO:0000269|PubMed:28685749, ECO:0000269|PubMed:36302773}. CC -!- SUBUNIT: Interacts with the E2 ubiquitin-conjugating enzyme UBE2D3 CC (PubMed:28685749). Component of the 4EHP-GYF2 complex, at least CC composed of EIF4E2, GIGYF2 and ZNF598 (PubMed:22751931, CC PubMed:32726578). {ECO:0000269|PubMed:22751931, CC ECO:0000269|PubMed:28685749, ECO:0000269|PubMed:32726578}. CC -!- INTERACTION: CC Q86UK7; O75420: GIGYF1; NbExp=2; IntAct=EBI-719433, EBI-947774; CC Q86UK7; P62258: YWHAE; NbExp=3; IntAct=EBI-719433, EBI-356498; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28757607}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q86UK7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86UK7-2; Sequence=VSP_020661, VSP_020663, VSP_020664; CC Name=3; CC IsoId=Q86UK7-3; Sequence=VSP_020663; CC Name=4; CC IsoId=Q86UK7-4; Sequence=VSP_020660, VSP_020662, VSP_020664, CC VSP_020665; CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15777.1; 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; AK024487; BAB15777.1; ALT_INIT; mRNA. DR EMBL; BC010990; AAH10990.2; -; mRNA. DR EMBL; BC041015; AAH41015.1; -; mRNA. DR EMBL; BC050477; AAH50477.1; -; mRNA. DR EMBL; AL834428; CAD39089.1; -; mRNA. DR RefSeq; NP_835461.2; NM_178167.3. DR AlphaFoldDB; Q86UK7; -. DR BioGRID; 124771; 453. DR ComplexPortal; CPX-2332; 4EHP-GIGYF2 co-translational mRNA decay complex, ZNF598 variant. DR ComplexPortal; CPX-2336; 4EHP-GIGYF1 co-translational mRNA decay complex, ZNF598 variant. DR CORUM; Q86UK7; -. DR FunCoup; Q86UK7; 1356. DR IntAct; Q86UK7; 59. DR MINT; Q86UK7; -. DR STRING; 9606.ENSP00000455308; -. DR GlyGen; Q86UK7; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q86UK7; -. DR PhosphoSitePlus; Q86UK7; -. DR SwissPalm; Q86UK7; -. DR BioMuta; ZNF598; -. DR DMDM; 74727495; -. DR jPOST; Q86UK7; -. DR MassIVE; Q86UK7; -. DR PaxDb; 9606-ENSP00000411409; -. DR PeptideAtlas; Q86UK7; -. DR ProteomicsDB; 69826; -. [Q86UK7-1] DR ProteomicsDB; 69827; -. [Q86UK7-2] DR ProteomicsDB; 69828; -. [Q86UK7-3] DR ProteomicsDB; 69829; -. [Q86UK7-4] DR Pumba; Q86UK7; -. DR DNASU; 90850; -. DR GeneID; 90850; -. DR KEGG; hsa:90850; -. DR UCSC; uc002cof.3; human. [Q86UK7-1] DR AGR; HGNC:28079; -. DR ClinPGx; PA134944505; -. DR CTD; 90850; -. DR DisGeNET; 90850; -. DR GeneCards; ZNF598; -. DR HGNC; HGNC:28079; ZNF598. DR MIM; 617508; gene. DR eggNOG; KOG2231; Eukaryota. DR HOGENOM; CLU_015828_0_0_1; -. DR InParanoid; Q86UK7; -. DR OrthoDB; 3838338at2759; -. DR PAN-GO; Q86UK7; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q86UK7; -. DR PathwayCommons; Q86UK7; -. DR SignaLink; Q86UK7; -. DR SIGNOR; Q86UK7; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 90850; 35 hits in 408 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; ZNF598; human. DR GenomeRNAi; 90850; -. DR Pharos; Q86UK7; Tbio. DR PRO; PR:Q86UK7; -. DR Proteomes; UP000005640; Unplaced. DR RNAct; Q86UK7; protein. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. DR GO; GO:0140517; F:protein-RNA adaptor activity; IDA:UniProt. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0170011; F:stalled ribosome sensor activity; IDA:UniProt. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:UniProt. DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. 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 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Metal-binding; Phosphoprotein; KW Proteomics identification; Reference proteome; Transferase; KW Translation regulation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..904 FT /note="E3 ubiquitin-protein ligase ZNF598" FT /id="PRO_0000250568" FT ZN_FING 29..69 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 187..210 FT /note="C2H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 312..469 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 490..656 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 346..358 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 359..388 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 404..416 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 418..431 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 447..461 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 502..513 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 521..531 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 534..543 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 564..584 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 306 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 437 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..397 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020660" FT VAR_SEQ 335..337 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020661" FT VAR_SEQ 398..431 FT /note="EGPGPKETSTNGPVSQEAFSVTGPAAPGCVGVPG -> MVGGCGQPQVGAGR FT AGMEPRGLIAVDQLCFPAPS (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020662" FT VAR_SEQ 424..429 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005" FT /id="VSP_020663" FT VAR_SEQ 551 FT /note="Q -> QE (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_020664" FT VAR_SEQ 738..904 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020665" FT VARIANT 453 FT /note="S -> Y (in dbSNP:rs11556528)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_034470" FT VARIANT 608 FT /note="A -> T (in dbSNP:rs11248905)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_059818" FT VARIANT 637 FT /note="T -> M (in dbSNP:rs2286469)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_052147" FT VARIANT 725 FT /note="C -> S (in dbSNP:rs2286468)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_034471" FT MUTAGEN 29 FT /note="C->A: Abolishes E3 ubiquitin-protein ligase FT activity, leading to enhanced readthrough on the FT poly(A)-stall sequences." FT /evidence="ECO:0000269|PubMed:28132843" FT MOD_RES Q86UK7-2:428 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" FT MOD_RES Q86UK7-3:431 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" SQ SEQUENCE 904 AA; 98637 MW; 492F67EE4E334743 CRC64; MAAAGGAEGR RAALEAAAAA APERGGGSCV LCCGDLEATA LGRCDHPVCY RCSTKMRVLC EQRYCAVCRE ELRQVVFGKK LPAFATIPIH QLQHEKKYDI YFADGKVYAL YRQLLQHECP RCPELPPFSL FGDLEQHMRR QHELFCCRLC LQHLQIFTYE RKWYSRKDLA RHRMQGDPDD TSHRGHPLCK FCDERYLDND ELLKHLRRDH YFCHFCDSDG AQDYYSDYAY LREHFREKHF LCEEGRCSTE QFTHAFRTEI DLKAHRTACH SRSRAEARQN RHIDLQFSYA PRHSRRNEGV VGGEDYEEVD RYSRQGRVAR AGTRGAQQSR RGSWRYKREE EDREVAAAVR ASVAAQQQEE ARRSEDQEEG GRPKKEEAAA RGPEDPRGPR RSPRTQGEGP GPKETSTNGP VSQEAFSVTG PAAPGCVGVP GALPPPSPKL KDEDFPSLSA STSSSCSTAA TPGPVGLALP YAIPARGRSA FQEEDFPALV SSVPKPGTAP TSLVSAWNSS SSSKKVAQPP LSAQATGSGQ PTRKAGKGSR GGRKGGPPFT QEEEEDGGPA LQELLSTRPT GSVSSTLGLA SIQPSKVGKK KKVGSEKPGT TLPQPPPATC PPGALQAPEA PASRAEGPVA VVVNGHTEGP APARSAPKEP PGLPRPLGSF PCPTPQEDFP ALGGPCPPRM PPPPGFSAVV LLKGTPPPPP PGLVPPISKP PPGFSGLLPS PHPACVPSPA TTTTTKAPRL LPAPRAYLVP ENFRERNLQL IQSIRDFLQS DEARFSEFKS HSGEFRQGLI SAAQYYKSCR DLLGENFQKV FNELLVLLPD TAKQQELLSA HTDFCNREKP LSTKSKKNKK SAWQATTQQA GLDCRVCPTC QQVLAHGDAS SHQALHAARD DDFPSLQAIA RIIT //