ID ZCH18_HUMAN Reviewed; 953 AA. AC Q86VM9; Q96DG4; Q96MP7; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 2. DT 02-SEP-2026, entry version 170. DE RecName: Full=Zinc finger CCCH domain-containing protein 18 {ECO:0000305}; DE AltName: Full=Nuclear protein NHN1; GN Name=ZC3H18 {ECO:0000312|HGNC:HGNC:25091}; Synonyms=NHN1; 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]. RC TISSUE=Brain; 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 GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-440. RC TISSUE=Cervix, and Testis; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-78; SER-83; SER-868 RP AND SER-893, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND SER-534, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-868, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-67; SER-74; SER-78; RP THR-109; SER-110; SER-532 AND SER-534, AND IDENTIFICATION BY MASS RP 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY RP 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-74; SER-78; SER-83; RP THR-162; SER-534; SER-536; SER-842; SER-868 AND SER-893, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] 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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-6; SER-46; SER-78; SER-83; SER-173; SER-534; SER-536; RP SER-842; SER-868; SER-893 AND SER-896, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-46; SER-67; SER-74; RP SER-78; SER-83; SER-118; THR-162; SER-173; SER-179; SER-487; SER-532; RP SER-534; SER-536; SER-842 AND SER-868, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-46; SER-53; SER-534 RP AND SER-842, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-622 AND LYS-766, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-622 AND LYS-817, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [21] RP INTERACTION WITH ZFC3H1. RX PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025; RA Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D., RA Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A., RA Jensen T.H.; RT "Identification of a nuclear exosome decay pathway for processed RT transcripts."; RL Mol. Cell 64:520-533(2016). RN [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-510; LYS-622; LYS-661; LYS-766; RP LYS-817 AND LYS-908, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [23] RP METHYLATION AT HIS-242. RX PubMed=37612136; DOI=10.1101/gad.350755.123; RA Shimazu T., Yoshimoto R., Kotoshiba K., Suzuki T., Matoba S., Hirose M., RA Akakabe M., Sohtome Y., Sodeoka M., Ogura A., Dohmae N., Shinkai Y.; RT "Histidine N1-position-specific methyltransferase CARNMT1 targets C3H zinc RT finger proteins and modulates RNA metabolism."; RL Genes Dev. 37:724-742(2023). RN [24] RP METHYLATION AT HIS-242. RX PubMed=40473212; DOI=10.1016/j.jbc.2025.110335; RA Malecki J.M., Weirich S., Ramirez-Garrastacho M., Hagen L., Al-Egly J., RA Anonsen J.H., Schroer L., Herrera M.C., Davydova E., Slupphaug G., RA Jeltsch A., Falnes P.O.; RT "Identification of substrates and sequence requirements for CARNMT1- RT mediated histidine methylation of C3H zinc fingers."; RL J. Biol. Chem. 301:110335-110335(2025). CC -!- SUBUNIT: Interacts with ZFC3H1 in a RNase-insensitive manner. CC {ECO:0000269|PubMed:27871484}. CC -!- INTERACTION: CC Q86VM9; Q15554: TERF2; NbExp=2; IntAct=EBI-1045965, EBI-706637; CC Q86VM9; P0DTC4: E; Xeno; NbExp=3; IntAct=EBI-1045965, EBI-25475850; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB71237.1; Type=Miscellaneous discrepancy; Note=Non-canonical splice intron-exon junction.; 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; AK056632; BAB71237.1; ALT_SEQ; mRNA. DR EMBL; AC116552; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001584; AAH01584.1; -; mRNA. DR EMBL; BC050463; AAH50463.1; -; mRNA. DR CCDS; CCDS10967.1; -. DR RefSeq; NP_001281269.1; NM_001294340.2. DR RefSeq; NP_653205.3; NM_144604.4. DR PDB; 9T3X; EM; 2.10 A; C=101-135. DR AlphaFoldDB; Q86VM9; -. DR EMDB; EMD-55519; -. DR SMR; Q86VM9; -. DR BioGRID; 125858; 911. DR CORUM; Q86VM9; -. DR FunCoup; Q86VM9; 2665. DR IntAct; Q86VM9; 332. DR MINT; Q86VM9; -. DR NDEx; IQUERY-CP-ZC3H18; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000416951; -. DR BindingDB; Q86VM9; -. DR ChEMBL; CHEMBL5725041; -. DR GlyGen; Q86VM9; 6 sites, 3 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q86VM9; -. DR PhosphoSitePlus; Q86VM9; -. DR BioMuta; ZC3H18; -. DR DMDM; 269849528; -. DR jPOST; Q86VM9; -. DR MassIVE; Q86VM9; -. DR PaxDb; 9606-ENSP00000416951; -. DR PeptideAtlas; Q86VM9; -. DR Pumba; Q86VM9; -. DR Antibodypedia; 30727; 27 antibodies from 13 providers. DR DNASU; 124245; -. DR Ensembl; ENST00000301011.10; ENSP00000301011.5; ENSG00000158545.17. DR Ensembl; ENST00000867281.1; ENSP00000537340.1; ENSG00000158545.17. DR Ensembl; ENST00000929537.1; ENSP00000599596.1; ENSG00000158545.17. DR Ensembl; ENST00000967030.1; ENSP00000637089.1; ENSG00000158545.17. DR GeneID; 124245; -. DR KEGG; hsa:124245; -. DR MANE-Select; ENST00000301011.10; ENSP00000301011.5; NM_144604.4; NP_653205.3. DR UCSC; uc002fky.4; human. DR AGR; HGNC:25091; -. DR ClinPGx; PA162409533; -. DR CTD; 124245; -. DR DisGeNET; 124245; -. DR GeneCards; ZC3H18; -. DR HGNC; HGNC:25091; ZC3H18. DR HPA; ENSG00000158545; Low tissue specificity. DR OpenTargets; ENSG00000158545; -. DR VEuPathDB; HostDB:ENSG00000158545; -. DR eggNOG; ENOG502R7WP; Eukaryota. DR GeneTree; ENSGT00730000111190; -. DR HOGENOM; CLU_012901_0_0_1; -. DR InParanoid; Q86VM9; -. DR OMA; PYRNYRR; -. DR OrthoDB; 10072532at2759; -. DR PAN-GO; Q86VM9; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q86VM9; -. DR PathwayCommons; Q86VM9; -. DR Reactome; R-HSA-9930044; Nuclear RNA decay. DR SignaLink; Q86VM9; -. DR Agora; ENSG00000158545; -. DR BioGRID-ORCS; 124245; 482 hits in 1183 CRISPR screens. DR ChiTaRS; ZC3H18; human. DR GenomeRNAi; 124245; -. DR Pharos; Q86VM9; Tdark. DR PRO; PR:Q86VM9; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q86VM9; protein. DR Bgee; ENSG00000158545; Expressed in sural nerve and 167 other cell types or tissues. DR ExpressionAtlas; Q86VM9; baseline and differential. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0140262; F:mRNA cap binding complex binding; IDA:FlyBase. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:FlyBase. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0050779; P:RNA destabilization; IMP:FlyBase. DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1. DR InterPro; IPR052647; Zinc_finger_CCCH-type. DR InterPro; IPR041367; Znf-CCCH_4. DR InterPro; IPR000571; Znf_CCCH. DR InterPro; IPR036855; Znf_CCCH_sf. DR PANTHER; PTHR46582; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 18; 1. DR PANTHER; PTHR46582:SF1; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 18; 1. DR Pfam; PF18044; zf-CCCH_4; 1. DR SMART; SM00356; ZnF_C3H1; 1. DR SUPFAM; SSF90229; CCCH zinc finger; 1. DR PROSITE; PS50103; ZF_C3H1; 1. DR PDBsum; 9T3X; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Coiled coil; Isopeptide bond; Metal-binding; KW Methylation; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..953 FT /note="Zinc finger CCCH domain-containing protein 18" FT /id="PRO_0000311242" FT ZN_FING 219..245 FT /note="C3H1-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT REGION 1..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 391..928 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 105..134 FT /evidence="ECO:0000255" FT COILED 399..464 FT /evidence="ECO:0000255" FT COILED 921..950 FT /evidence="ECO:0000255" FT COMPBIAS 1..14 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..26 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 60..72 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 97..106 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 107..124 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 125..136 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 143..158 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 159..168 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 175..190 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..207 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 208..217 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 396..482 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 510..520 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 545..606 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 661..670 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 692..725 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 736..750 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 760..774 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 778..798 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 824..841 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 893..906 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 916..925 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 53 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 59 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6TQE1" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 74 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 78 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q0P678" FT MOD_RES 109 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 118 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 162 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 242 FT /note="Pros-methylhistidine" FT /evidence="ECO:0000269|PubMed:37612136, FT ECO:0000269|PubMed:40473212" FT MOD_RES 487 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 532 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 534 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 536 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 814 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q0P678" FT MOD_RES 842 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 852 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q0P678" FT MOD_RES 868 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 893 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 896 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CROSSLNK 510 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 622 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733" FT CROSSLNK 661 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 766 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 817 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 908 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 368 FT /note="A -> T (in dbSNP:rs34808360)" FT /id="VAR_037188" FT VARIANT 440 FT /note="R -> H (in dbSNP:rs17855686)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_037189" FT CONFLICT 251 FT /note="Y -> H (in Ref. 1; BAB71237)" FT /evidence="ECO:0000305" SQ SEQUENCE 953 AA; 106378 MW; F12E87B342E1F892 CRC64; MDVAESPERD PHSPEDEEQP QGLSDDDILR DSGSDQDLDG AGVRASDLED EESAARGPSQ EEEDNHSDEE DRASEPKSQD QDSEVNELSR GPTSSPCEEE GDEGEEDRTS DLRDEASSVT RELDEHELDY DEEVPEEPAP AVQEDEAEKA GAEDDEEKGE GTPREEGKAG VQSVGEKESL EAAKEKKKED DDGEIDDGEI DDDDLEEGEV KDPSDRKVRP RPTCRFFMKG NCTWGMNCRF IHPGVNDKGN YSLITKADPF PPNGAPPLGP HPLMPANPWG GPVVDEILPP PPPEPPTESA WERGLRHAKE VLKKATIRKE QEPDFEEKRF TVTIGEDERE FDKENEVFRD WNSRIPRDVR DTVLEPYADP YYDYEIERFW RGGQYENFRV QYTETEPYHN YRERERERER ENRQRERERE RERDRERERR QRERERERER ERDKERQRRK EEWERERAKR DEKDRQHRDR DREKEREKEK GKPKPRSPQP PSRQAEPPKK EAATTGPQVK RADEWKDPWR RSKSPKKKLG VSVSPSRARR RRKTSASSAS ASNSSRSSSR SSSYSGSGSS RSRSRSSSYS SYSSRSSRHS SFSGSRSRSR SFSSSPSPSP TPSPHRPSIR TKGEPAPPPG KAGEKSVKKP APPPAPPQAT KTTAPVPEPT KPGDPREARR KERPARTPPR RRTLSGSGSG SGSSYSGSSS RSRSLSVSSV SSVSSATSSS SSAHSVDSED MYADLASPVS SASSRSPAPA QTRKEKGKSK KEDGVKEEKR KRDSSTQPPK SAKPPAGGKS SQQPSTPQQA PPGQPQQGTF VAHKEIKLTL LNKAADKGSR KRYEPSDKDR QSPPPAKRPN TSPDRGSRDR KSGGRLGSPK PERQRGQNSK APAAPADRKR QLSPQSKSSS KVTSVPGKAS DPGAASTKSG KASTLSRREE LLKQLKAVED AIARKRAKIP GKA //