PUM1_HUMAN
ID PUM1_HUMAN Reviewed; 1186 AA.
AC Q14671; A8K6W4; B4DG92; D3DPN3; E9PCJ0; Q53HH5; Q5VXY7; Q9HAN1;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Pumilio homolog 1 {ECO:0000305};
DE Short=HsPUM;
DE Short=Pumilio-1;
GN Name=PUM1 {ECO:0000312|HGNC:HGNC:14957};
GN Synonyms=KIAA0099 {ECO:0000303|PubMed:7788527}, PUMH1;
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), AND TISSUE SPECIFICITY.
RX PubMed=12459267; DOI=10.1016/s0378-1119(02)01060-0;
RA Spassov D.S., Jurecic R.;
RT "Cloning and comparative sequence analysis of PUM1 and PUM2 genes, human
RT members of the Pumilio family of RNA-binding proteins.";
RL Gene 299:195-204(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Amygdala, 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 [6]
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 [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 INDUCTION.
RX PubMed=12771951; DOI=10.1038/sj.onc.1206537;
RA Dazard J.-E., Gal H., Amariglio N., Rechavi G., Domany E., Givol D.;
RT "Genome-wide comparison of human keratinocyte and squamous cell carcinoma
RT responses to UVB irradiation: implications for skin and epithelial
RT cancer.";
RL Oncogene 22:2993-3006(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, 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 IDENTIFICATION BY 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 [12]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=18776931; DOI=10.1371/journal.pone.0003164;
RA Galgano A., Forrer M., Jaskiewicz L., Kanitz A., Zavolan M., Gerber A.P.;
RT "Comparative analysis of mRNA targets for human PUF-family proteins
RT suggests extensive interaction with the miRNA regulatory system.";
RL PLoS ONE 3:E3164-E3164(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-75; SER-209 AND
RP SER-709, AND 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-209; SER-709 AND
RP SER-806, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, PHOSPHORYLATION AT SER-209 AND
RP SER-714, AND MUTAGENESIS OF SER-209 AND SER-714.
RX PubMed=20818387; DOI=10.1038/ncb2105;
RA Kedde M., van Kouwenhove M., Zwart W., Oude Vrielink J.A., Elkon R.,
RA Agami R.;
RT "A Pumilio-induced RNA structure switch in p27-3' UTR controls miR-221 and
RT miR-222 accessibility.";
RL Nat. Cell Biol. 12:1014-1020(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-106; SER-209 AND
RP SER-709, AND IDENTIFICATION 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 [17]
RP FUNCTION.
RX PubMed=20860814; DOI=10.1186/1758-907x-1-17;
RA Leibovich L., Mandel-Gutfreund Y., Yakhini Z.;
RT "A structural-based statistical approach suggests a cooperative activity of
RT PUM1 and miR-410 in human 3'-untranslated regions.";
RL Silence 1:17-17(2010).
RN [18]
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 [19]
RP DOMAIN, FUNCTION, AND MUTAGENESIS OF 863-SER--GLN-867; 899-ASN--GLN-903;
RP 935-CYS--GLN-939; 971-ASN--GLN-975; CYS-1007; 1007-CYS--GLN-1011;
RP 1043-ASN--GLN-1047; 1079-SER--GLU-1083 AND 1122-ASN--GLN-1126.
RX PubMed=21572425; DOI=10.1038/nchembio.577;
RA Filipovska A., Razif M.F., Nygaard K.K., Rackham O.;
RT "A universal code for RNA recognition by PUF proteins.";
RL Nat. Chem. Biol. 7:425-427(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-709, AND
RP IDENTIFICATION BY 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 [21]
RP FUNCTION.
RX PubMed=22345517; DOI=10.1101/gad.182568.111;
RA Miles W.O., Tschop K., Herr A., Ji J.Y., Dyson N.J.;
RT "Pumilio facilitates miRNA regulation of the E2F3 oncogene.";
RL Genes Dev. 26:356-368(2012).
RN [22]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH A DEADENYLASE COMPLEX.
RX PubMed=22955276; DOI=10.1074/jbc.m112.373522;
RA Van Etten J., Schagat T.L., Hrit J., Weidmann C.A., Brumbaugh J.,
RA Coon J.J., Goldstrohm A.C.;
RT "Human Pumilio proteins recruit multiple deadenylases to efficiently
RT repress messenger RNAs.";
RL J. Biol. Chem. 287:36370-36383(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-112; SER-124;
RP SER-159; SER-197; SER-209; SER-709; SER-806 AND SER-822, AND IDENTIFICATION
RP 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 [25]
RP INTERACTION WITH TRIM71.
RX PubMed=23125361; DOI=10.1093/nar/gks1032;
RA Loedige I., Gaidatzis D., Sack R., Meister G., Filipowicz W.;
RT "The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA
RT function.";
RL Nucleic Acids Res. 41:518-532(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-229, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-796, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [28]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DHX58.
RX PubMed=25340845; DOI=10.1371/journal.ppat.1004417;
RA Narita R., Takahasi K., Murakami E., Hirano E., Yamamoto S.P., Yoneyama M.,
RA Kato H., Fujita T.;
RT "A novel function of human Pumilio proteins in cytoplasmic sensing of viral
RT infection.";
RL PLoS Pathog. 10:E1004417-E1004417(2014).
RN [29]
RP FUNCTION.
RX PubMed=25768905; DOI=10.1016/j.cell.2015.02.012;
RA Gennarino V.A., Singh R.K., White J.J., De Maio A., Han K., Kim J.Y.,
RA Jafar-Nejad P., di Ronza A., Kang H., Sayegh L.S., Cooper T.A., Orr H.T.,
RA Sillitoe R.V., Zoghbi H.Y.;
RT "Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by
RT increasing wild-type Ataxin1 levels.";
RL Cell 160:1087-1098(2015).
RN [30]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=26724866; DOI=10.1016/j.cell.2015.12.017;
RA Lee S., Kopp F., Chang T.C., Sataluri A., Chen B., Sivakumar S., Yu H.,
RA Xie Y., Mendell J.T.;
RT "Noncoding RNA NORAD regulates genomic stability by sequestering PUMILIO
RT proteins.";
RL Cell 164:69-80(2016).
RN [31]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
RN [32]
RP FUNCTION, INVOLVEMENT IN SCA47, VARIANTS SCA47 SER-1033; TRP-1137 AND
RP TRP-1145, AND CHARACTERIZATION OF VARIANTS SCA47 SER-1033; TRP-1137 AND
RP TRP-1145.
RX PubMed=29474920; DOI=10.1016/j.cell.2018.02.006;
RA Gennarino V.A., Palmer E.E., McDonell L.M., Wang L., Adamski C.J.,
RA Koire A., See L., Chen C.A., Schaaf C.P., Rosenfeld J.A., Panzer J.A.,
RA Moog U., Hao S., Bye A., Kirk E.P., Stankiewicz P., Breman A.M.,
RA McBride A., Kandula T., Dubbs H.A., Macintosh R., Cardamone M., Zhu Y.,
RA Ying K., Dias K.R., Cho M.T., Henderson L.B., Baskin B., Morris P., Tao J.,
RA Cowley M.J., Dinger M.E., Roscioli T., Caluseriu O., Suchowersky O.,
RA Sachdev R.K., Lichtarge O., Tang J., Boycott K.M., Holder J.L. Jr.,
RA Zoghbi H.Y.;
RT "A mild PUM1 mutation is associated with adult-onset ataxia, whereas
RT haploinsufficiency causes developmental delay and seizures.";
RL Cell 172:924-936(2018).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 828-1166.
RX PubMed=11336708; DOI=10.1016/s1097-2765(01)00229-5;
RA Wang X., Zamore P.D., Hall T.M.T.;
RT "Crystal structure of a Pumilio homology domain.";
RL Mol. Cell 7:855-865(2001).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 828-1176 IN COMPLEX WITH RNA, AND
RP MUTAGENESIS OF 1043-ASN-TYR-1044 AND GLN-1047.
RX PubMed=12202039; DOI=10.1016/s0092-8674(02)00873-5;
RA Wang X., McLachlan J., Zamore P.D., Hall T.M.T.;
RT "Modular recognition of RNA by a human pumilio-homology domain.";
RL Cell 110:501-512(2002).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 828-1170 IN COMPLEX WITH
RP CONSENSUS MRNA, FUNCTION, RNA-BINDING, AND DOMAIN.
RX PubMed=18328718; DOI=10.1016/j.str.2008.01.006;
RA Gupta Y.K., Nair D.T., Wharton R.P., Aggarwal A.K.;
RT "Structures of human Pumilio with noncognate RNAs reveal molecular
RT mechanisms for binding promiscuity.";
RL Structure 16:549-557(2008).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 828-1176, FUNCTION, RNA-BINDING,
RP AND DOMAIN.
RX PubMed=21653694; DOI=10.1074/jbc.m111.244889;
RA Dong S., Wang Y., Cassidy-Amstutz C., Lu G., Bigler R., Jezyk M.R., Li C.,
RA Hall T.M., Wang Z.;
RT "Specific and modular binding code for cytosine recognition in Pumilio/FBF
RT (PUF) RNA-binding domains.";
RL J. Biol. Chem. 286:26732-26742(2011).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 828-1176 IN COMPLEX WITH CONSENSUS
RP MRNA, FUNCTION, RNA-BINDING, AND DOMAIN.
RX PubMed=21397187; DOI=10.1016/j.str.2010.12.019;
RA Lu G., Hall T.M.;
RT "Alternate modes of cognate RNA recognition by human PUMILIO proteins.";
RL Structure 19:361-367(2011).
CC -!- FUNCTION: Sequence-specific RNA-binding protein that acts as a post-
CC transcriptional repressor by binding the 3'-UTR of mRNA targets. Binds
CC to an RNA consensus sequence, the Pumilio Response Element (PRE), 5'-
CC UGUANAUA-3', that is related to the Nanos Response Element (NRE)
CC (PubMed:21572425, PubMed:18328718, PubMed:21653694, PubMed:21397187).
CC Mediates post-transcriptional repression of transcripts via different
CC mechanisms: acts via direct recruitment of the CCR4-POP2-NOT
CC deadenylase leading to translational inhibition and mRNA degradation
CC (PubMed:22955276). Also mediates deadenylation-independent repression
CC by promoting accessibility of miRNAs (PubMed:18776931, PubMed:20818387,
CC PubMed:20860814, PubMed:22345517). Following growth factor stimulation,
CC phosphorylated and binds to the 3'-UTR of CDKN1B/p27 mRNA, inducing a
CC local conformational change that exposes miRNA-binding sites, promoting
CC association of miR-221 and miR-222, efficient suppression of CDKN1B/p27
CC expression, and rapid entry to the cell cycle (PubMed:20818387). Acts
CC as a post-transcriptional repressor of E2F3 mRNAs by binding to its 3'-
CC UTR and facilitating miRNA regulation (PubMed:22345517,
CC PubMed:29474920). Represses a program of genes necessary to maintain
CC genomic stability such as key mitotic, DNA repair and DNA replication
CC factors. Its ability to repress those target mRNAs is regulated by the
CC lncRNA NORAD (non-coding RNA activated by DNA damage) which, due to its
CC high abundance and multitude of PUMILIO binding sites, is able to
CC sequester a significant fraction of PUM1 and PUM2 in the cytoplasm
CC (PubMed:26724866). Involved in neuronal functions by regulating ATXN1
CC mRNA levels: acts by binding to the 3'-UTR of ATXN1 transcripts,
CC leading to their down-regulation independently of the miRNA machinery
CC (PubMed:25768905, PubMed:29474920). Plays a role in cytoplasmic sensing
CC of viral infection (PubMed:25340845). In testis, acts as a post-
CC transcriptional regulator of spermatogenesis by binding to the 3'-UTR
CC of mRNAs coding for regulators of p53/TP53. Involved in embryonic stem
CC cell renewal by facilitating the exit from the ground state: acts by
CC targeting mRNAs coding for naive pluripotency transcription factors and
CC accelerates their down-regulation at the onset of differentiation (By
CC similarity). Binds specifically to miRNA MIR199A precursor, with PUM2,
CC regulates miRNA MIR199A expression at a postranscriptional level
CC (PubMed:28431233). {ECO:0000250|UniProtKB:Q80U78,
CC ECO:0000269|PubMed:18328718, ECO:0000269|PubMed:18776931,
CC ECO:0000269|PubMed:20818387, ECO:0000269|PubMed:20860814,
CC ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:21572425,
CC ECO:0000269|PubMed:21653694, ECO:0000269|PubMed:22345517,
CC ECO:0000269|PubMed:22955276, ECO:0000269|PubMed:25340845,
CC ECO:0000269|PubMed:25768905, ECO:0000269|PubMed:26724866,
CC ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:29474920}.
CC -!- SUBUNIT: Recruits the CCR4-POP2-NOT deadenylase leading to
CC translational inhibition and mRNA degradation (PubMed:22955276). In
CC case of viral infection, interacts with DHX58 (PubMed:25340845).
CC Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner
CC (PubMed:23125361). {ECO:0000269|PubMed:22955276,
CC ECO:0000269|PubMed:23125361, ECO:0000269|PubMed:25340845}.
CC -!- INTERACTION:
CC Q14671; O15354: GPR37; NbExp=3; IntAct=EBI-948453, EBI-15639515;
CC Q14671; P28799: GRN; NbExp=3; IntAct=EBI-948453, EBI-747754;
CC Q14671; P28799-2: GRN; NbExp=3; IntAct=EBI-948453, EBI-25860013;
CC Q14671; O76024: WFS1; NbExp=3; IntAct=EBI-948453, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:26724866}.
CC Cytoplasm, P-body {ECO:0000305|PubMed:20818387}. Cytoplasmic granule
CC {ECO:0000269|PubMed:25340845}. Note=Recruited to cytoplasmic stress
CC granules upon viral infection. {ECO:0000269|PubMed:25340845}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q14671-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14671-2; Sequence=VSP_017059, VSP_017060, VSP_017061;
CC Name=3;
CC IsoId=Q14671-3; Sequence=VSP_017061;
CC Name=4;
CC IsoId=Q14671-4; Sequence=VSP_053703, VSP_053704, VSP_017059;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, muscle,
CC intestine and stomach. Not expressed in cerebellum, corpus callosum,
CC caudate nucleus, hippocampus, medulla oblongata and putamen. Expressed
CC in all fetal tissues tested. {ECO:0000269|PubMed:12459267}.
CC -!- INDUCTION: Strongly down-regulated in keratinocytes upon UVB
CC irradiation. {ECO:0000269|PubMed:12771951}.
CC -!- DOMAIN: The pumilio repeats mediate the association with RNA by packing
CC together to form a right-handed superhelix that approximates a half
CC donut. RNA-binding occurs on the concave side of the surface
CC (PubMed:21397187). PUM1 is composed of 8 pumilio repeats of 36
CC residues; each repeat binds a single nucleotide in its RNA target.
CC Residues at positions 12 and 16 of the pumilio repeat bind each RNA
CC base via hydrogen bonding or van der Waals contacts with the Watson-
CC Crick edge, while the amino acid at position 13 makes a stacking
CC interaction. The recognition of RNA by pumilio repeats is base
CC specific: cysteine and glutamine at position 12 and 16, respectively,
CC bind adenine; asparagine and glutamine bind uracil; and serine and
CC glutamate bind guanine (PubMed:21572425. PubMed:18328718,
CC PubMed:21653694). {ECO:0000269|PubMed:18328718,
CC ECO:0000269|PubMed:21397187, ECO:0000269|PubMed:21572425,
CC ECO:0000269|PubMed:21653694}.
CC -!- PTM: Phosphorylation at Ser-714 promotes RNA-binding activity.
CC Following growth factor stimulation phosphorylated at Ser-714,
CC promoting binding to the 3'-UTR of CDKN1B/p27 mRNA.
CC {ECO:0000269|PubMed:20818387}.
CC -!- DISEASE: Spinocerebellar ataxia 47 (SCA47) [MIM:617931]: A form of
CC spinocerebellar ataxia, a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA47 is an autosomal dominant disease with
CC a highly variable phenotype and incomplete penetrance. Clinical
CC features include developmental disability, ataxia, and seizures.
CC {ECO:0000269|PubMed:29474920}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07895.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF315592; AAG31807.1; -; mRNA.
DR EMBL; D43951; BAA07895.3; ALT_INIT; mRNA.
DR EMBL; AL356320; CAH71203.1; -; Genomic_DNA.
DR EMBL; AL445235; CAH71203.1; JOINED; Genomic_DNA.
DR EMBL; AK291779; BAF84468.1; -; mRNA.
DR EMBL; AK294477; BAG57703.1; -; mRNA.
DR EMBL; AK222605; BAD96325.1; -; mRNA.
DR EMBL; AL445235; CAI22246.1; -; Genomic_DNA.
DR EMBL; AL356320; CAI22246.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX07633.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07634.1; -; Genomic_DNA.
DR EMBL; BC013398; AAH13398.1; -; mRNA.
DR CCDS; CCDS338.1; -. [Q14671-1]
DR CCDS; CCDS44099.1; -. [Q14671-3]
DR RefSeq; NP_001018494.1; NM_001020658.1. [Q14671-3]
DR RefSeq; NP_055491.1; NM_014676.2. [Q14671-1]
DR PDB; 1IB2; X-ray; 1.90 A; A=828-1176.
DR PDB; 1M8W; X-ray; 2.20 A; A/B=828-1176.
DR PDB; 1M8X; X-ray; 2.20 A; A/B=828-1176.
DR PDB; 1M8Y; X-ray; 2.60 A; A/B=828-1176.
DR PDB; 1M8Z; X-ray; 1.90 A; A=828-1176.
DR PDB; 2YJY; X-ray; 2.60 A; A/B=828-1176.
DR PDB; 3BSB; X-ray; 2.80 A; A/B=828-1170.
DR PDB; 3BSX; X-ray; 2.32 A; A/B=828-1170.
DR PDB; 3Q0L; X-ray; 2.50 A; A/B=828-1176.
DR PDB; 3Q0M; X-ray; 2.70 A; A/B=828-1176.
DR PDB; 3Q0N; X-ray; 2.40 A; A/B=828-1176.
DR PDB; 3Q0O; X-ray; 2.80 A; A/B=828-1176.
DR PDB; 3Q0P; X-ray; 2.60 A; A/B=828-1176.
DR PDB; 5YKH; X-ray; 2.46 A; A=898-1176.
DR PDB; 5YKI; X-ray; 2.25 A; A=898-1176.
DR PDBsum; 1IB2; -.
DR PDBsum; 1M8W; -.
DR PDBsum; 1M8X; -.
DR PDBsum; 1M8Y; -.
DR PDBsum; 1M8Z; -.
DR PDBsum; 2YJY; -.
DR PDBsum; 3BSB; -.
DR PDBsum; 3BSX; -.
DR PDBsum; 3Q0L; -.
DR PDBsum; 3Q0M; -.
DR PDBsum; 3Q0N; -.
DR PDBsum; 3Q0O; -.
DR PDBsum; 3Q0P; -.
DR PDBsum; 5YKH; -.
DR PDBsum; 5YKI; -.
DR AlphaFoldDB; Q14671; -.
DR SMR; Q14671; -.
DR BioGRID; 115050; 262.
DR DIP; DIP-29082N; -.
DR IntAct; Q14671; 48.
DR MINT; Q14671; -.
DR STRING; 9606.ENSP00000391723; -.
DR GlyGen; Q14671; 15 sites, 2 O-linked glycans (15 sites).
DR iPTMnet; Q14671; -.
DR MetOSite; Q14671; -.
DR PhosphoSitePlus; Q14671; -.
DR BioMuta; PUM1; -.
DR DMDM; 41688619; -.
DR UCD-2DPAGE; Q14671; -.
DR EPD; Q14671; -.
DR jPOST; Q14671; -.
DR MassIVE; Q14671; -.
DR MaxQB; Q14671; -.
DR PaxDb; Q14671; -.
DR PeptideAtlas; Q14671; -.
DR PRIDE; Q14671; -.
DR ProteomicsDB; 19456; -.
DR ProteomicsDB; 4116; -.
DR ProteomicsDB; 60101; -. [Q14671-1]
DR ProteomicsDB; 60102; -. [Q14671-2]
DR Antibodypedia; 16718; 280 antibodies from 33 providers.
DR DNASU; 9698; -.
DR Ensembl; ENST00000257075.9; ENSP00000257075.5; ENSG00000134644.16. [Q14671-1]
DR Ensembl; ENST00000373742.6; ENSP00000362847.2; ENSG00000134644.16. [Q14671-4]
DR Ensembl; ENST00000426105.7; ENSP00000391723.2; ENSG00000134644.16. [Q14671-3]
DR Ensembl; ENST00000440538.6; ENSP00000401777.2; ENSG00000134644.16. [Q14671-2]
DR GeneID; 9698; -.
DR KEGG; hsa:9698; -.
DR MANE-Select; ENST00000426105.7; ENSP00000391723.2; NM_001020658.2; NP_001018494.1. [Q14671-3]
DR UCSC; uc001bsh.2; human. [Q14671-1]
DR CTD; 9698; -.
DR DisGeNET; 9698; -.
DR GeneCards; PUM1; -.
DR HGNC; HGNC:14957; PUM1.
DR HPA; ENSG00000134644; Low tissue specificity.
DR MalaCards; PUM1; -.
DR MIM; 607204; gene.
DR MIM; 617931; phenotype.
DR neXtProt; NX_Q14671; -.
DR OpenTargets; ENSG00000134644; -.
DR Orphanet; 589515; PUM1-associated developmental disability-ataxia-seizure syndrome.
DR PharmGKB; PA34042; -.
DR VEuPathDB; HostDB:ENSG00000134644; -.
DR eggNOG; KOG1488; Eukaryota.
DR GeneTree; ENSGT00940000158079; -.
DR InParanoid; Q14671; -.
DR OrthoDB; 207351at2759; -.
DR PhylomeDB; Q14671; -.
DR TreeFam; TF318160; -.
DR PathwayCommons; Q14671; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q14671; -.
DR SIGNOR; Q14671; -.
DR BioGRID-ORCS; 9698; 98 hits in 1072 CRISPR screens.
DR ChiTaRS; PUM1; human.
DR EvolutionaryTrace; Q14671; -.
DR GeneWiki; PUM1; -.
DR GenomeRNAi; 9698; -.
DR Pharos; Q14671; Tbio.
DR PRO; PR:Q14671; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q14671; protein.
DR Bgee; ENSG00000134644; Expressed in dorsal motor nucleus of vagus nerve and 208 other tissues.
DR ExpressionAtlas; Q14671; baseline and differential.
DR Genevisible; Q14671; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB.
DR GO; GO:0035196; P:miRNA processing; IMP:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IDA:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IDA:UniProtKB.
DR GO; GO:0016441; P:post-transcriptional gene silencing; ISS:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; IDA:UniProtKB.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; TAS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR CDD; cd07920; Pumilio; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR033712; Pumilio_RNA-bd.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR Pfam; PF00806; PUF; 8.
DR SMART; SM00025; Pumilio; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50302; PUM; 8.
DR PROSITE; PS50303; PUM_HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Differentiation; Disease variant; Methylation; Neurodegeneration;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spermatogenesis;
KW Spinocerebellar ataxia; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1186
FT /note="Pumilio homolog 1"
FT /id="PRO_0000075917"
FT DOMAIN 828..1168
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 848..883
FT /note="Pumilio 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 884..919
FT /note="Pumilio 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 920..955
FT /note="Pumilio 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 956..991
FT /note="Pumilio 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 992..1027
FT /note="Pumilio 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 1028..1063
FT /note="Pumilio 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 1064..1099
FT /note="Pumilio 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REPEAT 1103..1142
FT /note="Pumilio 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00317,
FT ECO:0000269|PubMed:21397187"
FT REGION 22..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..867
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000269|PubMed:18328718"
FT REGION 899..903
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000269|PubMed:18328718"
FT REGION 935..939
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000269|PubMed:18328718"
FT REGION 971..975
FT /note="Non-specific-nucleotide binding in RNA target"
FT /evidence="ECO:0000269|PubMed:18328718"
FT REGION 1007..1011
FT /note="Adenine-nucleotide binding in RNA target"
FT /evidence="ECO:0000269|PubMed:18328718"
FT REGION 1043..1047
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000269|PubMed:18328718,
FT ECO:0000269|PubMed:21397187, ECO:0007744|PDB:3BSB"
FT REGION 1079..1083
FT /note="Guanine-nucleotide binding in RNA target"
FT /evidence="ECO:0000269|PubMed:18328718,
FT ECO:0000269|PubMed:21397187, ECO:0007744|PDB:3BSB"
FT REGION 1122..1126
FT /note="Uracil-nucleotide binding in RNA target"
FT /evidence="ECO:0000269|PubMed:18328718,
FT ECO:0000269|PubMed:21397187, ECO:0007744|PDB:1M8W,
FT ECO:0007744|PDB:1M8X, ECO:0007744|PDB:3BSB,
FT ECO:0007744|PDB:3BSX, ECO:0007744|PDB:3Q0L,
FT ECO:0007744|PDB:3Q0M, ECO:0007744|PDB:3Q0N,
FT ECO:0007744|PDB:3Q0O, ECO:0007744|PDB:3Q0P"
FT COMPBIAS 33..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20818387,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TB72"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20818387"
FT MOD_RES 796
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MPLPPPGPGPEPIPGCTAPTQSPVGRHVVGVKGVGGM (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053703"
FT VAR_SEQ 145..240
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053704"
FT VAR_SEQ 417
FT /note="I -> IA (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:7788527"
FT /id="VSP_017059"
FT VAR_SEQ 597..623
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7788527"
FT /id="VSP_017060"
FT VAR_SEQ 950
FT /note="Q -> QVI (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:7788527, ECO:0000303|Ref.4"
FT /id="VSP_017061"
FT VARIANT 1033
FT /note="T -> S (in SCA47; results in reduced PUM1 protein
FT levels and decreased post-transcriptional repression of
FT E2F3 and ATXN1; dbSNP:rs771145682)"
FT /evidence="ECO:0000269|PubMed:29474920"
FT /id="VAR_080784"
FT VARIANT 1137
FT /note="R -> W (in SCA47; decreased post-transcriptional
FT repression of E2F3 and ATXN1; dbSNP:rs1557541619)"
FT /evidence="ECO:0000269|PubMed:29474920"
FT /id="VAR_080785"
FT VARIANT 1145
FT /note="R -> W (in SCA47; results in reduced PUM1 protein
FT levels and decreased post-transcriptional repression of
FT E2F3 and ATXN1; dbSNP:rs1557539450)"
FT /evidence="ECO:0000269|PubMed:29474920"
FT /id="VAR_080786"
FT MUTAGEN 209
FT /note="S->A: Does not affect RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:20818387"
FT MUTAGEN 714
FT /note="S->A: Decreased RNA-binding activity."
FT /evidence="ECO:0000269|PubMed:20818387"
FT MUTAGEN 714
FT /note="S->E: Phospho-mimic mutant; persistent RNA-binding
FT activity in quiescent cells."
FT /evidence="ECO:0000269|PubMed:20818387"
FT MUTAGEN 863..867
FT /note="SRFIQ->GRFIR: B and inds cytosine-nucleotide in RNA
FT target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 899..903
FT /note="NYVIQ->GYVIR: Specifically binds cytosine-nucleotide
FT in RNA target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 935..939
FT /note="CRVIQ->GRVIR: Specifically binds cytosine-nucleotide
FT in RNA target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 971..975
FT /note="NHVVQ->GHVVR: Specifically binds cytosine-nucleotide
FT in RNA target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 1007..1011
FT /note="CRVIQ->GRVIR,ARVIR,SRVIR,TRVIR,CRVIR: Specifically
FT binds cytosine-nucleotide in RNA target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 1007..1011
FT /note="CRVIQ->SRVIE: Specifically binds guanine-nucleotide
FT in RNA target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 1007
FT /note="C->N: Specifically binds uracil-nucleotide in RNA
FT target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 1043..1047
FT /note="NYVIQ->GYVIR: Specifically binds cytosine-nucleotide
FT in RNA target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 1043..1044
FT /note="NY->SN: Changes the specificity for RNA; when
FT associated with E-1047."
FT /evidence="ECO:0000269|PubMed:12202039"
FT MUTAGEN 1047
FT /note="Q->E: Changes the specificity for RNA; when
FT associated with 1043-SN-1044."
FT /evidence="ECO:0000269|PubMed:12202039"
FT MUTAGEN 1079..1083
FT /note="SNVVE->GNVVR: Specifically binds cytosine-nucleotide
FT in RNA target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT MUTAGEN 1122..1126
FT /note="NYVVQ->GYVVR: Specifically binds cytosine-nucleotide
FT in RNA target."
FT /evidence="ECO:0000269|PubMed:21572425"
FT CONFLICT 216
FT /note="G -> E (in Ref. 4; BAD96325)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="Y -> N (in Ref. 4; BAD96325)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="M -> N (in Ref. 2; BAA07895)"
FT /evidence="ECO:0000305"
FT HELIX 831..837
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 846..849
FT /evidence="ECO:0007829|PDB:1IB2"
FT TURN 850..852
FT /evidence="ECO:0007829|PDB:2YJY"
FT HELIX 853..857
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 860..872
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 875..885
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 886..888
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 889..893
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 898..908
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 911..921
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 925..929
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 934..944
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 947..954
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 955..957
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 958..960
FT /evidence="ECO:0007829|PDB:5YKH"
FT HELIX 961..966
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 970..980
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 983..986
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 987..992
FT /evidence="ECO:0007829|PDB:1IB2"
FT TURN 993..996
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 997..1001
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1006..1016
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1019..1031
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1033..1036
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1042..1052
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1055..1065
FT /evidence="ECO:0007829|PDB:1IB2"
FT TURN 1066..1068
FT /evidence="ECO:0007829|PDB:3Q0M"
FT HELIX 1069..1073
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1078..1088
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1091..1103
FT /evidence="ECO:0007829|PDB:1IB2"
FT STRAND 1104..1106
FT /evidence="ECO:0007829|PDB:3Q0N"
FT STRAND 1107..1109
FT /evidence="ECO:0007829|PDB:3Q0M"
FT HELIX 1111..1116
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1121..1131
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1134..1142
FT /evidence="ECO:0007829|PDB:1IB2"
FT HELIX 1145..1147
FT /evidence="ECO:0007829|PDB:1M8Z"
FT HELIX 1148..1151
FT /evidence="ECO:0007829|PDB:1M8Z"
FT STRAND 1153..1155
FT /evidence="ECO:0007829|PDB:3BSB"
FT HELIX 1157..1164
FT /evidence="ECO:0007829|PDB:1M8Z"
FT TURN 1165..1169
FT /evidence="ECO:0007829|PDB:5YKH"
SQ SEQUENCE 1186 AA; 126473 MW; E1E0D8B3B0181308 CRC64;
MSVACVLKRK AVLWQDSFSP HLKHHPQEPA NPNMPVVLTS GTGSQAQPQP AANQALAAGT
HSSPVPGSIG VAGRSQDDAM VDYFFQRQHG EQLGGGGSGG GGYNNSKHRW PTGDNIHAEH
QVRSMDELNH DFQALALEGR AMGEQLLPGK KFWETDESSK DGPKGIFLGD QWRDSAWGTS
DHSVSQPIMV QRRPGQSFHV NSEVNSVLSP RSESGGLGVS MVEYVLSSSP GDSCLRKGGF
GPRDADSDEN DKGEKKNKGT FDGDKLGDLK EEGDVMDKTN GLPVQNGIDA DVKDFSRTPG
NCQNSANEVD LLGPNQNGSE GLAQLTSTNG AKPVEDFSNM ESQSVPLDPM EHVGMEPLQF
DYSGTQVPVD SAAATVGLFD YNSQQQLFQR PNALAVQQLT AAQQQQYALA AAHQPHIGLA
PAAFVPNPYI ISAAPPGTDP YTAGLAAAAT LGPAVVPHQY YGVTPWGVYP ASLFQQQAAA
AAAATNSANQ QTTPQAQQGQ QQVLRGGASQ RPLTPNQNQQ GQQTDPLVAA AAVNSALAFG
QGLAAGMPGY PVLAPAAYYD QTGALVVNAG ARNGLGAPVR LVAPAPVIIS SSAAQAAVAA
AAASANGAAG GLAGTTNGPF RPLGTQQPQP QPQQQPNNNL ASSSFYGNNS LNSNSQSSSL
FSQGSAQPAN TSLGFGSSSS LGATLGSALG GFGTAVANSN TGSGSRRDSL TGSSDLYKRT
SSSLTPIGHS FYNGLSFSSS PGPVGMPLPS QGPGHSQTPP PSLSSHGSSS SLNLGGLTNG
SGRYISAAPG AEAKYRSASS ASSLFSPSST LFSSSRLRYG MSDVMPSGRS RLLEDFRNNR
YPNLQLREIA GHIMEFSQDQ HGSRFIQLKL ERATPAERQL VFNEILQAAY QLMVDVFGNY
VIQKFFEFGS LEQKLALAER IRGHVLSLAL QMYGCRVIQK ALEFIPSDQQ NEMVRELDGH
VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFAL STHPYGCRVI QRILEHCLPD
QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVAEIRGNVL VLSQHKFASN
VVEKCVTHAS RTERAVLIDE VCTMNDGPHS ALYTMMKDQY ANYVVQKMID VAEPGQRKIV
MHKIRPHIAT LRKYTYGKHI LAKLEKYYMK NGVDLGPICG PPNGII
