TOE1_HUMAN
ID TOE1_HUMAN Reviewed; 510 AA.
AC Q96GM8; B4DEM6; Q6IA35; Q8IWN5; Q9H846;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Target of EGR1 protein 1;
GN Name=TOE1;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, NUCLEAR
RP LOCALIZATION SIGNAL, AND FUNCTION.
RX PubMed=12562764; DOI=10.1074/jbc.m210502200;
RA De Belle I., Wu J.-X., Sperandio S., Mercola D., Adamson E.D.;
RT "In vivo cloning and characterization of a new growth suppressor protein
RT TOE1 as a direct target gene of Egr1.";
RL J. Biol. Chem. 278:14306-14312(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 2-56; 75-84; 96-106; 175-182; 239-249; 348-362 AND
RP 418-439, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP 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 IDENTIFICATION BY 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP 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-5, AND IDENTIFICATION BY MASS
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-358 AND SER-428, AND
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP 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 [17]
RP INVOLVEMENT IN PCH7, FUNCTION, INTERACTION WITH SNRNA, TISSUE SPECIFICITY,
RP VARIANTS PCH7 SER-73; THR-103; TYR-148; GLY-173; LYS-220; 231-TYR--SER-510
RP DEL; SER-239; TRP-253; GLN-319; TYR-319 AND PHE-496, AND CHARACTERIZATION
RP OF VARIANTS PCH7 THR-103; TYR-148; GLY-173 AND LYS-220.
RX PubMed=28092684; DOI=10.1038/ng.3762;
RA Lardelli R.M., Schaffer A.E., Eggens V.R., Zaki M.S., Grainger S.,
RA Sathe S., Van Nostrand E.L., Schlachetzki Z., Rosti B., Akizu N., Scott E.,
RA Silhavy J.L., Heckman L.D., Rosti R.O., Dikoglu E., Gregor A.,
RA Guemez-Gamboa A., Musaev D., Mande R., Widjaja A., Shaw T.L.,
RA Markmiller S., Marin-Valencia I., Davies J.H., de Meirleir L.,
RA Kayserili H., Altunoglu U., Freckmann M.L., Warwick L., Chitayat D.,
RA Blaser S., Caglayan A.O., Bilguvar K., Per H., Fagerberg C.,
RA Christesen H.T., Kibaek M., Aldinger K.A., Manchester D., Matsumoto N.,
RA Muramatsu K., Saitsu H., Shiina M., Ogata K., Foulds N., Dobyns W.B.,
RA Chi N.C., Traver D., Spaccini L., Bova S.M., Gabriel S.B., Gunel M.,
RA Valente E.M., Nassogne M.C., Bennett E.J., Yeo G.W., Baas F.,
RA Lykke-Andersen J., Gleeson J.G.;
RT "Biallelic mutations in the 3' exonuclease TOE1 cause pontocerebellar
RT hypoplasia and uncover a role in snRNA processing.";
RL Nat. Genet. 49:457-464(2017).
RN [18]
RP STRUCTURE BY NMR OF 285-321.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-CCCH domain of target of EGR1, member 1
RT (nuclear).";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Inhibits cell growth rate and cell cycle. Induces CDKN1A
CC expression as well as TGF-beta expression. Mediates the inhibitory
CC growth effect of EGR1. Involved in the maturation of snRNAs and snRNA
CC 3'-tail processing (PubMed:28092684). {ECO:0000269|PubMed:12562764,
CC ECO:0000269|PubMed:28092684}.
CC -!- SUBUNIT: Interacts with U1, U2, U4, U5 and U6 snRNAs.
CC {ECO:0000269|PubMed:28092684}.
CC -!- INTERACTION:
CC Q96GM8; P05067: APP; NbExp=3; IntAct=EBI-717460, EBI-77613;
CC Q96GM8; P04637: TP53; NbExp=3; IntAct=EBI-717460, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12562764}.
CC Nucleus speckle {ECO:0000269|PubMed:12562764}. Note=Localizes to
CC nuclear speckles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96GM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96GM8-2; Sequence=VSP_055529;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:28092684}.
CC -!- DISEASE: Pontocerebellar hypoplasia 7 (PCH7) [MIM:614969]: A form of
CC pontocerebellar hypoplasia, a group of related disorders characterized
CC by underdevelopment of the pons and the cerebellum. Pontocerebellar
CC hypoplasia also causes impaired growth of other parts of the brain,
CC leading to an unusually small head size. PCH7 patients manifest delayed
CC psychomotor development, hypotonia, breathing abnormalities, and
CC gonadal abnormalities. {ECO:0000269|PubMed:28092684}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; AY169960; AAN75441.1; -; mRNA.
DR EMBL; AK024011; BAB14774.1; -; mRNA.
DR EMBL; AK293704; BAG57137.1; -; mRNA.
DR EMBL; CR457320; CAG33601.1; -; mRNA.
DR EMBL; AL359540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009364; AAH09364.1; -; mRNA.
DR CCDS; CCDS521.1; -. [Q96GM8-1]
DR RefSeq; NP_079353.3; NM_025077.3. [Q96GM8-1]
DR PDB; 2FC6; NMR; -; A=285-321.
DR PDBsum; 2FC6; -.
DR AlphaFoldDB; Q96GM8; -.
DR SMR; Q96GM8; -.
DR BioGRID; 125269; 129.
DR CORUM; Q96GM8; -.
DR IntAct; Q96GM8; 60.
DR MINT; Q96GM8; -.
DR STRING; 9606.ENSP00000361162; -.
DR GlyGen; Q96GM8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96GM8; -.
DR PhosphoSitePlus; Q96GM8; -.
DR BioMuta; TOE1; -.
DR DMDM; 74751888; -.
DR EPD; Q96GM8; -.
DR jPOST; Q96GM8; -.
DR MassIVE; Q96GM8; -.
DR MaxQB; Q96GM8; -.
DR PaxDb; Q96GM8; -.
DR PeptideAtlas; Q96GM8; -.
DR PRIDE; Q96GM8; -.
DR ProteomicsDB; 3971; -.
DR ProteomicsDB; 76647; -. [Q96GM8-1]
DR Antibodypedia; 18606; 191 antibodies from 28 providers.
DR DNASU; 114034; -.
DR Ensembl; ENST00000372090.6; ENSP00000361162.5; ENSG00000132773.12. [Q96GM8-1]
DR GeneID; 114034; -.
DR KEGG; hsa:114034; -.
DR MANE-Select; ENST00000372090.6; ENSP00000361162.5; NM_025077.4; NP_079353.3.
DR UCSC; uc009vxq.4; human. [Q96GM8-1]
DR CTD; 114034; -.
DR DisGeNET; 114034; -.
DR GeneCards; TOE1; -.
DR HGNC; HGNC:15954; TOE1.
DR HPA; ENSG00000132773; Low tissue specificity.
DR MalaCards; TOE1; -.
DR MIM; 613931; gene.
DR MIM; 614969; phenotype.
DR neXtProt; NX_Q96GM8; -.
DR OpenTargets; ENSG00000132773; -.
DR Orphanet; 284339; Pontocerebellar hypoplasia type 7.
DR PharmGKB; PA38064; -.
DR VEuPathDB; HostDB:ENSG00000132773; -.
DR eggNOG; KOG1990; Eukaryota.
DR GeneTree; ENSGT00940000153167; -.
DR HOGENOM; CLU_044804_1_0_1; -.
DR InParanoid; Q96GM8; -.
DR OMA; LLCTEDY; -.
DR OrthoDB; 1402758at2759; -.
DR PhylomeDB; Q96GM8; -.
DR TreeFam; TF314502; -.
DR PathwayCommons; Q96GM8; -.
DR SignaLink; Q96GM8; -.
DR BioGRID-ORCS; 114034; 397 hits in 1082 CRISPR screens.
DR ChiTaRS; TOE1; human.
DR EvolutionaryTrace; Q96GM8; -.
DR GeneWiki; TOE1; -.
DR GenomeRNAi; 114034; -.
DR Pharos; Q96GM8; Tbio.
DR PRO; PR:Q96GM8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96GM8; protein.
DR Bgee; ENSG00000132773; Expressed in olfactory bulb and 192 other tissues.
DR Genevisible; Q96GM8; HS.
DR GO; GO:0015030; C:Cajal body; IDA:HGNC.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:HGNC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IDA:HGNC.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; IDA:UniProtKB.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:HGNC.
DR GO; GO:0034472; P:snRNA 3'-end processing; IMP:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF04857; CAF1; 2.
DR Pfam; PF00642; zf-CCCH; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; Metal-binding; Neurodegeneration; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330"
FT CHAIN 2..510
FT /note="Target of EGR1 protein 1"
FT /id="PRO_0000270833"
FT ZN_FING 294..322
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 335..347
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12562764"
FT COMPBIAS 366..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 19..111
FT /note="GVSKSTTSGEELVVQVPVVDVQSNNFKEMWPSLLLAIKTANFVAVDTELSGL
FT GDRKSLLNQCIEERYKAVCHAARTRSILSLGLACFKRQPDK -> AEWAWGQEEFAEP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055529"
FT VARIANT 73
FT /note="R -> S (in PCH7; dbSNP:rs774056037)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078850"
FT VARIANT 103
FT /note="A -> T (in PCH7; reduced protein levels; decreased
FT function in snRNA 3'-end processing; dbSNP:rs371848318)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078851"
FT VARIANT 148
FT /note="F -> Y (in PCH7; reduced protein levels; decreased
FT function in snRNA 3'-end processing; dbSNP:rs148067486)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078852"
FT VARIANT 173
FT /note="V -> G (in PCH7; reduced protein levels;
FT dbSNP:rs777030573)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078853"
FT VARIANT 220
FT /note="E -> K (in PCH7; reduced protein levels; decreased
FT function in snRNA 3'-end processing; dbSNP:rs1570621473)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078809"
FT VARIANT 231..510
FT /note="Missing (in PCH7)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078854"
FT VARIANT 239
FT /note="F -> S (in PCH7; dbSNP:rs778263701)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078855"
FT VARIANT 253
FT /note="R -> W (in PCH7; dbSNP:rs368182654)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078856"
FT VARIANT 319
FT /note="H -> Q (in PCH7; dbSNP:rs758153898)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078857"
FT VARIANT 319
FT /note="H -> Y (in PCH7; dbSNP:rs750266350)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078858"
FT VARIANT 341
FT /note="R -> H (in dbSNP:rs9429157)"
FT /id="VAR_048752"
FT VARIANT 381
FT /note="E -> K (in dbSNP:rs61323219)"
FT /id="VAR_061109"
FT VARIANT 496
FT /note="S -> F (in PCH7; dbSNP:rs1570626350)"
FT /evidence="ECO:0000269|PubMed:28092684"
FT /id="VAR_078859"
FT CONFLICT 12
FT /note="A -> T (in Ref. 3; CAG33601)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="H -> R (in Ref. 2; BAB14774)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="D -> G (in Ref. 1; AAN75441)"
FT /evidence="ECO:0000305"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:2FC6"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2FC6"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2FC6"
SQ SEQUENCE 510 AA; 56548 MW; 5E4616F650E12929 CRC64;
MAADSDDGAV SAPAASDGGV SKSTTSGEEL VVQVPVVDVQ SNNFKEMWPS LLLAIKTANF
VAVDTELSGL GDRKSLLNQC IEERYKAVCH AARTRSILSL GLACFKRQPD KGEHSYLAQV
FNLTLLCMEE YVIEPKSVQF LIQHGFNFNQ QYAQGIPYHK GNDKGDESQS QSVRTLFLEL
IRARRPLVLH NGLIDLVFLY QNFYAHLPES LGTFTADLCE MFPAGIYDTK YAAEFHARFV
ASYLEYAFRK CERENGKQRA AGSPHLTLEF CNYPSSMRDH IDYRCCLPPA THRPHPTSIC
DNFSAYGWCP LGPQCPQSHD IDLIIDTDEA AAEDKRRRRR RREKRKRALL NLPGTQTSGE
AKDGPPKKQV CGDSIKPEET EQEVAADETR NLPHSKQGNK NDLEMGIKAA RPEIADRATS
EVPGSQASPN PVPGDGLHRA GFDAFMTGYV MAYVEVSQGP QPCSSGPWLP ECHNKVYLSG
KAVPLTVAKS QFSRSSKAHN QKMKLTWGSS
