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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
 
 
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