ID SPN1_HUMAN Reviewed; 360 AA. AC O95149; A6NE34; A8K0B0; D3DW76; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=Snurportin-1; DE AltName: Full=RNA U transporter 1; GN Name=SNUPN; Synonyms=RNUT1, SPN1; 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], PROTEIN SEQUENCE OF 34-52; 54-69; 128-144; RP 211-221 AND 323-327, FUNCTION IN U SNRNP NUCLEAR IMPORT, INTERACTION WITH RP KPNB1, RNA-BINDING, AND SUBCELLULAR LOCATION. RC TISSUE=Brain; RX PubMed=9670026; DOI=10.1093/emboj/17.14.4114; RA Huber J., Cronshagen U., Kadokura M., Marshallsay C., Wada T., Sekine M., RA Luehrmann R.; RT "Snurportin1, an m3G-cap-specific nuclear import receptor with a novel RT domain structure."; RL EMBO J. 17:4114-4126(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 FUNCTION, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, INTERACTION RP WITH IPO7; KPNB1 AND XPO1, IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH RP XPO1 AND RAN, AND SUBCELLULAR LOCATION. RX PubMed=10209022; DOI=10.1083/jcb.145.2.255; RA Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., RA Hartmann E., Luehrmann R., Goerlich D.; RT "CRM1-mediated recycling of snurportin 1 to the cytoplasm."; RL J. Cell Biol. 145:255-264(1999). RN [7] RP IDENTIFICATION IN AN IMPORT SNRNP COMPLEX, INTERACTION WITH DDX20; SMN1 AND RP SNRPB, AND SUBCELLULAR LOCATION. RX PubMed=12095920; DOI=10.1093/hmg/11.15.1785; RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.; RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex RT with snurportin1 and importin beta."; RL Hum. Mol. Genet. 11:1785-1795(2002). RN [8] RP FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-27; TRP-107; 203-PHE--TRP-207 AND RP TRP-276, AND RNA-BINDING. RX PubMed=16030253; DOI=10.1091/mbc.e05-04-0316; RA Ospina J.K., Gonsalvez G.B., Bednenko J., Darzynkiewicz E., Gerace L., RA Matera A.G.; RT "Cross-talk between snurportin1 subdomains."; RL Mol. Biol. Cell 16:4660-4671(2005). 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 MET-1, 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 [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY RP 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 [14] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 97-300 IN COMPLEX WITH M3G-CAP, RP MUTAGENESIS OF TRP-107 AND TRP-276, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15920472; DOI=10.1038/sj.emboj.7600701; RA Strasser A., Dickmanns A., Luehrmann R., Ficner R.; RT "Structural basis for m3G-cap-mediated nuclear import of spliceosomal RT UsnRNPs by snurportin1."; RL EMBO J. 24:2235-2243(2005). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 25-64 IN COMPLEX WITH KPNB1, AND RP INTERACTION WITH KPNB1. RX PubMed=18187419; DOI=10.1074/jbc.m709093200; RA Mitrousis G., Olia A.S., Walker-Kopp N., Cingolani G.; RT "Molecular basis for the recognition of snurportin 1 by importin beta."; RL J. Biol. Chem. 283:7877-7884(2008). RN [16] RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 25-64 IN COMPLEX WITH KPNB1, AND RP INTERACTION WITH KPNB1. RX PubMed=20476751; DOI=10.1021/bi100292y; RA Bhardwaj A., Cingolani G.; RT "Conformational selection in the recognition of the snurportin importin RT beta binding domain by importin beta."; RL Biochemistry 49:5042-5047(2010). CC -!- FUNCTION: Functions as an U snRNP-specific nuclear import adapter. CC Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import CC of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs. CC {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:15920472, CC ECO:0000269|PubMed:16030253, ECO:0000269|PubMed:9670026}. CC -!- SUBUNIT: Component of an import snRNP complex composed of KPNB1, SNUPN, CC SMN1 and ZNF259. Component of a nuclear export receptor complex CC composed of KPNB1, Ran, SNUPN and XPO1. Found in a trimeric export CC complex with SNUPN, Ran and XPO1. Interacts (via IBB domain) with CC KPNB1; the interaction is direct. Interacts with DDX20, IPO7, SMN1, CC SNRPB and XPO1. Interacts directly with XPO1. Its interaction with XPO1 CC and binding to m3G-cap U snRNPs appears to be mutually exclusive. CC {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:12095920, CC ECO:0000269|PubMed:15920472, ECO:0000269|PubMed:16030253, CC ECO:0000269|PubMed:18187419, ECO:0000269|PubMed:20476751, CC ECO:0000269|PubMed:9670026}. CC -!- INTERACTION: CC O95149; O14980: XPO1; NbExp=8; IntAct=EBI-714033, EBI-355867; CC O95149; Q6P5F9: Xpo1; Xeno; NbExp=2; IntAct=EBI-714033, EBI-2550236; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10209022, CC ECO:0000269|PubMed:15920472}. Cytoplasm {ECO:0000269|PubMed:12095920, CC ECO:0000269|PubMed:9670026, ECO:0000305|PubMed:10209022}. CC Note=Nucleoplasmic shuttling protein. Its nuclear import involves the CC nucleocytoplasmic transport receptor importin beta (PubMed:10209022, CC PubMed:12095920). It is re-exported to the cytoplasm by the XPO1- CC dependent nuclear export receptor pathway (PubMed:10209022). CC {ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:12095920}. CC -!- SIMILARITY: Belongs to the snurportin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF039029; AAC70906.1; -; mRNA. DR EMBL; CR456811; CAG33092.1; -; mRNA. DR EMBL; AK289475; BAF82164.1; -; mRNA. DR EMBL; CH471136; EAW99245.1; -; Genomic_DNA. DR EMBL; CH471136; EAW99246.1; -; Genomic_DNA. DR EMBL; BC004203; AAH04203.1; -; mRNA. DR CCDS; CCDS10281.1; -. DR RefSeq; NP_001036046.1; NM_001042581.1. DR RefSeq; NP_001036053.1; NM_001042588.1. DR RefSeq; NP_005692.1; NM_005701.3. DR PDB; 1XK5; X-ray; 2.40 A; A=97-300. DR PDB; 2P8Q; X-ray; 2.35 A; B=25-64. DR PDB; 2Q5D; X-ray; 3.20 A; C/D=25-64. DR PDB; 2QNA; X-ray; 2.84 A; B=1-66. DR PDB; 3GB8; X-ray; 2.90 A; B=1-328. DR PDB; 3GJX; X-ray; 2.50 A; B/E=1-360. DR PDB; 3LWW; X-ray; 3.15 A; B/D=25-64. DR PDB; 3NBY; X-ray; 3.42 A; B/E=15-360. DR PDB; 3NBZ; X-ray; 2.80 A; B/E=15-360. DR PDB; 3NC0; X-ray; 2.90 A; B/E=15-360. DR PDB; 5DIS; X-ray; 2.85 A; C=1-287. DR PDBsum; 1XK5; -. DR PDBsum; 2P8Q; -. DR PDBsum; 2Q5D; -. DR PDBsum; 2QNA; -. DR PDBsum; 3GB8; -. DR PDBsum; 3GJX; -. DR PDBsum; 3LWW; -. DR PDBsum; 3NBY; -. DR PDBsum; 3NBZ; -. DR PDBsum; 3NC0; -. DR PDBsum; 5DIS; -. DR AlphaFoldDB; O95149; -. DR SASBDB; O95149; -. DR SMR; O95149; -. DR BioGRID; 115384; 44. DR ComplexPortal; CPX-1032; Importin complex, Snurportin variant. DR CORUM; O95149; -. DR DIP; DIP-48513N; -. DR ELM; O95149; -. DR IntAct; O95149; 26. DR MINT; O95149; -. DR STRING; 9606.ENSP00000454852; -. DR ChEMBL; CHEMBL3885569; -. DR GlyCosmos; O95149; 1 site, 1 glycan. DR GlyGen; O95149; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O95149; -. DR PhosphoSitePlus; O95149; -. DR BioMuta; SNUPN; -. DR EPD; O95149; -. DR jPOST; O95149; -. DR MassIVE; O95149; -. DR MaxQB; O95149; -. DR PaxDb; 9606-ENSP00000454852; -. DR PeptideAtlas; O95149; -. DR ProteomicsDB; 50662; -. DR Pumba; O95149; -. DR Antibodypedia; 27339; 211 antibodies from 25 providers. DR DNASU; 10073; -. DR Ensembl; ENST00000308588.10; ENSP00000309831.5; ENSG00000169371.14. DR Ensembl; ENST00000564644.5; ENSP00000454852.1; ENSG00000169371.14. DR Ensembl; ENST00000564675.5; ENSP00000458053.1; ENSG00000169371.14. DR Ensembl; ENST00000567134.5; ENSP00000456224.1; ENSG00000169371.14. DR GeneID; 10073; -. DR KEGG; hsa:10073; -. DR MANE-Select; ENST00000308588.10; ENSP00000309831.5; NM_005701.4; NP_005692.1. DR UCSC; uc002ban.4; human. DR AGR; HGNC:14245; -. DR CTD; 10073; -. DR DisGeNET; 10073; -. DR GeneCards; SNUPN; -. DR HGNC; HGNC:14245; SNUPN. DR HPA; ENSG00000169371; Low tissue specificity. DR MIM; 607902; gene. DR neXtProt; NX_O95149; -. DR OpenTargets; ENSG00000169371; -. DR PharmGKB; PA34611; -. DR VEuPathDB; HostDB:ENSG00000169371; -. DR eggNOG; KOG3132; Eukaryota. DR GeneTree; ENSGT00510000047494; -. DR HOGENOM; CLU_056809_0_0_1; -. DR InParanoid; O95149; -. DR OMA; VQLSEWM; -. DR OrthoDB; 197726at2759; -. DR PhylomeDB; O95149; -. DR TreeFam; TF313108; -. DR PathwayCommons; O95149; -. DR Reactome; R-HSA-191859; snRNP Assembly. DR SignaLink; O95149; -. DR SIGNOR; O95149; -. DR BioGRID-ORCS; 10073; 717 hits in 1183 CRISPR screens. DR ChiTaRS; SNUPN; human. DR EvolutionaryTrace; O95149; -. DR GeneWiki; SNUPN; -. DR GenomeRNAi; 10073; -. DR Pharos; O95149; Tbio. DR PRO; PR:O95149; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; O95149; Protein. DR Bgee; ENSG00000169371; Expressed in left testis and 108 other cell types or tissues. DR ExpressionAtlas; O95149; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IPI:ComplexPortal. DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0061608; F:nuclear import signal receptor activity; IEA:InterPro. DR GO; GO:0000339; F:RNA cap binding; TAS:ProtInc. DR GO; GO:0006606; P:protein import into nucleus; IEA:InterPro. DR GO; GO:0006404; P:RNA import into nucleus; IDA:ComplexPortal. DR GO; GO:0061015; P:snRNA import into nucleus; IEA:InterPro. DR CDD; cd09232; Snurportin-1_C; 1. DR DisProt; DP01874; -. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR IDEAL; IID00115; -. DR InterPro; IPR002652; Importin-a_IBB. DR InterPro; IPR017336; Snurportin-1. DR InterPro; IPR024721; Snurportin-1_N. DR InterPro; IPR047857; Snurportin1_C. DR PANTHER; PTHR13403:SF6; SNURPORTIN-1; 1. DR PANTHER; PTHR13403; SNURPORTIN1 RNUT1 PROTEIN RNA, U TRANSPORTER 1; 1. DR Pfam; PF11538; Snurportin1; 1. DR PIRSF; PIRSF037955; Snurportin-1; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR PROSITE; PS51214; IBB; 1. DR Genevisible; O95149; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus; KW Phosphoprotein; Reference proteome; RNA-binding; Transport. FT CHAIN 1..360 FT /note="Snurportin-1" FT /id="PRO_0000191071" FT DOMAIN 11..73 FT /note="IBB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561" FT REGION 1..159 FT /note="Necessary for interaction with XPO1" FT /evidence="ECO:0000269|PubMed:10209022" FT REGION 1..65 FT /note="Necessary for interaction with KPNB1 and m3G-cap U1 FT and U5 snRNP import receptor activity" FT /evidence="ECO:0000269|PubMed:18187419, FT ECO:0000269|PubMed:9670026" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 127..129 FT /note="Interaction with m3G-cap structure" FT /evidence="ECO:0000269|PubMed:15920472, FT ECO:0007744|PDB:1XK5" FT REGION 208..328 FT /note="Necessary for binding to the m3G-cap structure" FT /evidence="ECO:0000269|PubMed:9670026" FT REGION 339..360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 105 FT /note="Interaction with m3G-cap structure" FT /evidence="ECO:0000269|PubMed:15920472, FT ECO:0007744|PDB:1XK5" FT SITE 144 FT /note="Interaction with m3G-cap structure" FT /evidence="ECO:0000269|PubMed:15920472, FT ECO:0007744|PDB:1XK5" FT SITE 276 FT /note="Interaction with m3G-cap structure" FT /evidence="ECO:0000269|PubMed:15920472, FT ECO:0007744|PDB:1XK5" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 75 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 350 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MUTAGEN 27 FT /note="R->A: Abolishes interaction with KPNB1 and m3G-cap FT U1 snRNP import receptor activity." FT /evidence="ECO:0000269|PubMed:16030253" FT MUTAGEN 107 FT /note="W->A: Reduces binding to m3G-cap structure, FT interaction with XPO1 and snRNP import receptor activity." FT /evidence="ECO:0000269|PubMed:15920472, FT ECO:0000269|PubMed:16030253" FT MUTAGEN 203..207 FT /note="FRFYW->A: Reduces binding to m3G-cap structure." FT /evidence="ECO:0000269|PubMed:16030253" FT MUTAGEN 276 FT /note="W->A: Reduces binding to m3G-cap structure, FT interaction with XPO1 and snRNP import receptor activity." FT /evidence="ECO:0000269|PubMed:15920472, FT ECO:0000269|PubMed:16030253" FT HELIX 1..10 FT /evidence="ECO:0007829|PDB:3GJX" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:3NBY" FT HELIX 28..30 FT /evidence="ECO:0007829|PDB:2P8Q" FT HELIX 42..60 FT /evidence="ECO:0007829|PDB:2P8Q" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:2P8Q" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:3GJX" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:1XK5" FT HELIX 115..118 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 119..135 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:3NBY" FT STRAND 148..152 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 155..159 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:3NBZ" FT STRAND 170..177 FT /evidence="ECO:0007829|PDB:1XK5" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 182..191 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:5DIS" FT HELIX 201..211 FT /evidence="ECO:0007829|PDB:1XK5" FT TURN 212..214 FT /evidence="ECO:0007829|PDB:1XK5" FT TURN 216..219 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:1XK5" FT HELIX 239..246 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 254..263 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 268..277 FT /evidence="ECO:0007829|PDB:1XK5" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:1XK5" FT HELIX 282..286 FT /evidence="ECO:0007829|PDB:1XK5" FT STRAND 291..293 FT /evidence="ECO:0007829|PDB:3NBZ" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:1XK5" SQ SEQUENCE 360 AA; 41143 MW; 50B456D1C23B4BA1 CRC64; MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS TPKLKGSSHS PDHPGCLMEN //