ZC3HF_HUMAN
ID ZC3HF_HUMAN Reviewed; 426 AA.
AC Q8WU90; B4DMW2; D3DPG7; Q5QTQ4; Q8WZ06; Q9NUZ3; Q9NZ37; Q9P079;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger CCCH domain-containing protein 15;
DE AltName: Full=DRG family-regulatory protein 1;
DE AltName: Full=Likely ortholog of mouse immediate early response erythropoietin 4;
GN Name=ZC3H15; Synonyms=DFRP1, LEREPO4;
GN ORFNames=HSPC303, HT010, MSTP012, PP730;
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 1).
RC TISSUE=Aorta;
RA Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W., Liu S.,
RA Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [9]
RP INTERACTION WITH DRG1, AND SUBCELLULAR LOCATION.
RX PubMed=15676025; DOI=10.1111/j.1365-2443.2005.00825.x;
RA Ishikawa K., Azuma S., Ikawa S., Semba K., Inoue J.;
RT "Identification of DRG family regulatory proteins (DFRPs): specific
RT regulation of DRG1 and DRG2.";
RL Genes Cells 10:139-150(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [11]
RP INTERACTION WITH DRG1 IN THE DRG1-ZC3H15/DFRP1 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19819225; DOI=10.1016/j.bbrc.2009.10.003;
RA Ishikawa K., Akiyama T., Ito K., Semba K., Inoue J.;
RT "Independent stabilizations of polysomal Drg1/Dfrp1 complex and non-
RT polysomal Drg2/Dfrp2 complex in mammalian cells.";
RL Biochem. Biophys. Res. Commun. 390:552-556(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP MASS 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 [16]
RP FUNCTION, AND INTERACTION WITH DRG1.
RX PubMed=23711155; DOI=10.1111/febs.12356;
RA Perez-Arellano I., Spinola-Amilibia M., Bravo J.;
RT "Human Drg1 is a potassium-dependent GTPase enhanced by Lerepo4.";
RL FEBS J. 280:3647-3657(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-351; SER-360 AND
RP SER-381, AND IDENTIFICATION BY MASS 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 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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP INTERACTION WITH MICROTUBULES.
RX PubMed=28855639; DOI=10.1038/s41598-017-10088-5;
RA Schellhaus A.K., Moreno-Andres D., Chugh M., Yokoyama H., Moschopoulou A.,
RA De S., Bono F., Hipp K., Schaeffer E., Antonin W.;
RT "Developmentally Regulated GTP binding protein 1 (DRG1) controls
RT microtubule dynamics.";
RL Sci. Rep. 7:9996-9996(2017).
CC -!- FUNCTION: Protects DRG1 from proteolytic degradation (PubMed:19819225).
CC Stimulates DRG1 GTPase activity likely by increasing the affinity for
CC the potassium ions (PubMed:23711155). {ECO:0000269|PubMed:19819225,
CC ECO:0000269|PubMed:23711155}.
CC -!- SUBUNIT: Interacts with DRG1; this interaction prevents DRG1 poly-
CC ubiquitination and degradation by proteasome. DRG1-ZC3H15/DFRP1 complex
CC co-sediments with polysomes. Associates with microtubules.
CC {ECO:0000269|PubMed:15676025, ECO:0000269|PubMed:19819225,
CC ECO:0000269|PubMed:23711155, ECO:0000269|PubMed:28855639}.
CC -!- INTERACTION:
CC Q8WU90; Q9Y295: DRG1; NbExp=9; IntAct=EBI-1042636, EBI-719554;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15676025,
CC ECO:0000269|PubMed:19819225}. Nucleus {ECO:0000250}. Note=The DRG1-
CC DFRP2/ZC3H15 complex associates with polysomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WU90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WU90-2; Sequence=VSP_055992, VSP_055993, VSP_055994;
CC -!- SIMILARITY: Belongs to the ZC3H15/TMA46 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28981.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF67649.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL55770.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ13514.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF109366; AAQ13514.1; ALT_FRAME; mRNA.
DR EMBL; AF161421; AAF28981.1; ALT_FRAME; mRNA.
DR EMBL; AF220184; AAF67649.1; ALT_FRAME; mRNA.
DR EMBL; AK001901; BAA91968.1; -; mRNA.
DR EMBL; AK297658; BAG60024.1; -; mRNA.
DR EMBL; AF289586; AAL55770.1; ALT_FRAME; mRNA.
DR EMBL; AC018867; AAX88885.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10935.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10936.1; -; Genomic_DNA.
DR EMBL; BC021102; AAH21102.1; -; mRNA.
DR CCDS; CCDS42791.1; -. [Q8WU90-1]
DR RefSeq; NP_060941.2; NM_018471.2. [Q8WU90-1]
DR AlphaFoldDB; Q8WU90; -.
DR SMR; Q8WU90; -.
DR BioGRID; 120956; 81.
DR IntAct; Q8WU90; 26.
DR MINT; Q8WU90; -.
DR STRING; 9606.ENSP00000338788; -.
DR GlyGen; Q8WU90; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WU90; -.
DR MetOSite; Q8WU90; -.
DR PhosphoSitePlus; Q8WU90; -.
DR SwissPalm; Q8WU90; -.
DR BioMuta; ZC3H15; -.
DR DMDM; 74730681; -.
DR EPD; Q8WU90; -.
DR jPOST; Q8WU90; -.
DR MassIVE; Q8WU90; -.
DR MaxQB; Q8WU90; -.
DR PaxDb; Q8WU90; -.
DR PeptideAtlas; Q8WU90; -.
DR PRIDE; Q8WU90; -.
DR ProteomicsDB; 4648; -.
DR ProteomicsDB; 74645; -. [Q8WU90-1]
DR Antibodypedia; 34002; 129 antibodies from 23 providers.
DR DNASU; 55854; -.
DR Ensembl; ENST00000337859.11; ENSP00000338788.6; ENSG00000065548.18. [Q8WU90-1]
DR GeneID; 55854; -.
DR KEGG; hsa:55854; -.
DR MANE-Select; ENST00000337859.11; ENSP00000338788.6; NM_018471.3; NP_060941.2.
DR UCSC; uc002upo.4; human. [Q8WU90-1]
DR CTD; 55854; -.
DR DisGeNET; 55854; -.
DR GeneCards; ZC3H15; -.
DR HGNC; HGNC:29528; ZC3H15.
DR HPA; ENSG00000065548; Low tissue specificity.
DR MIM; 619704; gene.
DR neXtProt; NX_Q8WU90; -.
DR OpenTargets; ENSG00000065548; -.
DR PharmGKB; PA162409508; -.
DR VEuPathDB; HostDB:ENSG00000065548; -.
DR eggNOG; KOG1763; Eukaryota.
DR GeneTree; ENSGT00390000015818; -.
DR HOGENOM; CLU_042870_3_0_1; -.
DR InParanoid; Q8WU90; -.
DR OMA; DGPMEEG; -.
DR OrthoDB; 1358374at2759; -.
DR PhylomeDB; Q8WU90; -.
DR TreeFam; TF300892; -.
DR PathwayCommons; Q8WU90; -.
DR SignaLink; Q8WU90; -.
DR BioGRID-ORCS; 55854; 21 hits in 1099 CRISPR screens.
DR ChiTaRS; ZC3H15; human.
DR GenomeRNAi; 55854; -.
DR Pharos; Q8WU90; Tbio.
DR PRO; PR:Q8WU90; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WU90; protein.
DR Bgee; ENSG00000065548; Expressed in sperm and 215 other tissues.
DR ExpressionAtlas; Q8WU90; baseline and differential.
DR Genevisible; Q8WU90; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR InterPro; IPR032378; ZC3H15/TMA46_C.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF16543; DFRP_C; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..426
FT /note="Zinc finger CCCH domain-containing protein 15"
FT /id="PRO_0000324642"
FT ZN_FING 99..126
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 174..212
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..260
FT /note="Required for interaction with DRG1"
FT /evidence="ECO:0000250"
FT REGION 299..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..86
FT /evidence="ECO:0000255"
FT COILED 218..285
FT /evidence="ECO:0000255"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..205
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055992"
FT VAR_SEQ 324..367
FT /note="DDSVSVNDIDLSLYIPRDVDETGITVASLERFSTYTSDKDENKL -> RGSF
FT VPHLLMLIERNNRKYHNMVKSHQHQSHSAWVQILTPTMGN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055993"
FT VAR_SEQ 368..426
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055994"
FT VARIANT 342
FT /note="V -> E (in dbSNP:rs11555006)"
FT /id="VAR_039867"
FT VARIANT 408
FT /note="T -> P (in dbSNP:rs1043497)"
FT /id="VAR_052969"
FT CONFLICT 10
FT /note="G -> R (in Ref. 5; AAL55770)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..17
FT /note="EQ -> DE (in Ref. 3; AAF67649)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="Q -> T (in Ref. 2; AAF28981)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="D -> G (in Ref. 5; AAL55770)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="A -> T (in Ref. 5; AAL55770)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="E -> D (in Ref. 2; AAF28981 and 3; AAF67649)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="Q -> R (in Ref. 4; BAA91968)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="V -> A (in Ref. 2; AAF28981)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="N -> T (in Ref. 2; AAF28981)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="D -> V (in Ref. 1; AAQ13514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 48602 MW; 4A80B7FDC3376181 CRC64;
MPPKKQAQAG GSKKAEQKKK EKIIEDKTFG LKNKKGAKQQ KFIKAVTHQV KFGQQNPRQV
AQSEAEKKLK KDDKKKELQE LNELFKPVVA AQKISKGADP KSVVCAFFKQ GQCTKGDKCK
FSHDLTLERK CEKRSVYIDA RDEELEKDTM DNWDEKKLEE VVNKKHGEAE KKKPKTQIVC
KHFLEAIENN KYGWFWVCPG GGDICMYRHA LPPGFVLKKD KKKEEKEDEI SLEDLIERER
SALGPNVTKI TLESFLAWKK RKRQEKIDKL EQDMERRKAD FKAGKALVIS GREVFEFRPE
LVNDDDEEAD DTRYTQGTGG DEVDDSVSVN DIDLSLYIPR DVDETGITVA SLERFSTYTS
DKDENKLSEA SGGRAENGER SDLEEDNERE GTENGAIDAV PVDENLFTGE DLDELEEELN
TLDLEE
