ID NUP98_HUMAN Reviewed; 1817 AA. AC P52948; Q8IUT2; Q8WYB0; Q96E54; Q9H3Q4; Q9NT02; Q9UF57; Q9UHX0; Q9Y6J4; AC Q9Y6J5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 4. DT 27-MAR-2024, entry version 236. DE RecName: Full=Nuclear pore complex protein Nup98-Nup96 {ECO:0000305}; DE EC=3.4.21.- {ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282}; DE Contains: DE RecName: Full=Nuclear pore complex protein Nup98; DE AltName: Full=98 kDa nucleoporin; DE AltName: Full=Nucleoporin Nup98; DE Short=Nup98; DE Contains: DE RecName: Full=Nuclear pore complex protein Nup96; DE AltName: Full=96 kDa nucleoporin; DE AltName: Full=Nucleoporin Nup96; DE Short=Nup96; DE Flags: Precursor; GN Name=NUP98 {ECO:0000312|HGNC:HGNC:8068}; Synonyms=ADAR2; 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 4), AND CHROMOSOMAL TRANSLOCATION WITH RP HOXA9. RX PubMed=8563754; DOI=10.1038/ng0296-159; RA Borrow J., Shearman A.M., Stanton V.P., Becher R., Collins T., RA Williams A.J., Dube I., Katz F., Kwong Y.L., Morris C., Ohyashiki K., RA Toyama K., Rowley J., Housman D.E.; RT "The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the RT genes for nucleoporin NUP98 and class I homeoprotein HOXA9."; RL Nat. Genet. 12:159-167(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Arai Y., Kaneko Y., Kubo T., Arai K., Hosoda F., Ohki M.; RT "Molecular analysis of the chromosomal breakpoints and identification of RT the repetitive sequences near the breakpoints of NUP98 in therapy-related RT leukemia with inv(11)(p15q22)."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF RP 1648-1664, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF RP 863-PHE--TYR-883. RX PubMed=10087256; DOI=10.1083/jcb.144.6.1097; RA Fontoura B.M.A., Blobel G., Matunis M.J.; RT "A conserved biogenesis pathway for nucleoporins: proteolytic processing of RT a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, RT Nup96."; RL J. Cell Biol. 144:1097-1112(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RA Borrow J., Housman D.E.; RT "An alternative splice form of NUP98 encodes a 196kDa NUP196 isoform."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 963-1817 (ISOFORM 6). RC TISSUE=Lung carcinoma; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1176-1817 (ISOFORM 5). RC TISSUE=Liver; RA Xu Y.H., Guo B.C., Yu Y.L.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1212-1817 (ISOFORM 5). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1227-1817 (ISOFORM 5). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP CHROMOSOMAL TRANSLOCATION WITH TOP1. RX PubMed=10556215; RA Ahuja H.G., Felix C.A., Aplan P.D.; RT "The t(11;20)(p15;q11) chromosomal translocation associated with therapy- RT related myelodysplastic syndrome results in an NUP98-TOP1 fusion."; RL Blood 94:3258-3261(1999). RN [11] RP INTERACTION WITH RAE1. RX PubMed=10209021; DOI=10.1083/jcb.145.2.237; RA Pritchard C.E., Fornerod M., Kasper L.H., van Deursen J.M.; RT "RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 RT motif at the nuclear pore complex through multiple domains."; RL J. Cell Biol. 145:237-254(1999). RN [12] RP INTERACTION WITH VESICULAR STOMATITIS VIRUS PROTEIN M (MICROBIAL RP INFECTION), SUBCELLULAR LOCATION, AND SUBCELLULAR LOCATION (MICROBIAL RP INFECTION). RX PubMed=11106761; DOI=10.1016/s1097-2765(00)00120-9; RA von Kobbe C., van Deursen J.M., Rodrigues J.P., Sitterlin D., Bachi A., RA Wu X., Wilm M., Carmo-Fonseca M., Izaurralde E.; RT "Vesicular stomatitis virus matrix protein inhibits host cell gene RT expression by targeting the nucleoporin Nup98."; RL Mol. Cell 6:1243-1252(2000). RN [13] RP CHROMOSOMAL TRANSLOCATION WITH NSD1. RX PubMed=11493482; DOI=10.1182/blood.v98.4.1264; RA Jaju R.J., Fidler C., Haas O.A., Strickson A.J., Watkins F., Clark K., RA Cross N.C., Cheng J.F., Aplan P.D., Kearney L., Boultwood J., RA Wainscoat J.S.; RT "A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo RT childhood acute myeloid leukemia."; RL Blood 98:1264-1267(2001). RN [14] RP SUBUNIT. RX PubMed=11684705; DOI=10.1083/jcb.200108007; RA Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.; RT "Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA RT export."; RL J. Cell Biol. 155:339-354(2001). RN [15] RP CHROMOSOMAL TRANSLOCATION WITH WHSC1L1. RX PubMed=11986249; DOI=10.1182/blood.v99.10.3857; RA Rosati R., La Starza R., Veronese A., Aventin A., Schwienbacher C., RA Vallespi T., Negrini M., Martelli M.F., Mecucci C.; RT "NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with RT t(8;11)(p11.2;p15)."; RL Blood 99:3857-3860(2002). RN [16] RP SUBCELLULAR LOCATION. RX PubMed=11839768; DOI=10.1083/jcb.200106046; RA Frosst P., Guan T., Subauste C., Hahn K., Gerace L.; RT "Tpr is localized within the nuclear basket of the pore complex and has a RT role in nuclear protein export."; RL J. Cell Biol. 156:617-630(2002). RN [17] RP LACK OF INTERACTION WITH TPR, AND SUBCELLULAR LOCATION. RX PubMed=12802065; DOI=10.1091/mbc.e02-09-0620; RA Hase M.E., Cordes V.C.; RT "Direct interaction with nup153 mediates binding of Tpr to the periphery of RT the nuclear pore complex."; RL Mol. Biol. Cell 14:1923-1940(2003). RN [18] RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR RP LOCATION. RX PubMed=15229283; DOI=10.1091/mbc.e04-03-0165; RA Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.; RT "Nucleoporins as components of the nuclear pore complex core structure and RT Tpr as the architectural element of the nuclear basket."; RL Mol. Biol. Cell 15:4261-4277(2004). RN [19] RP CHROMOSOMAL TRANSLOCATION WITH NUP98, AND DISEASE. RX PubMed=16028218; DOI=10.1002/gcc.20233; RA Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., RA Harbott J.; RT "Characterization of 6q abnormalities in childhood acute myeloid leukemia RT and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98- RT C6orf80 fusion in a case of acute megakaryoblastic leukemia."; RL Genes Chromosomes Cancer 44:225-232(2005). RN [20] RP CHROMOSOMAL TRANSLOCATION WITH PSIP1/LEDGF. RX PubMed=15725483; DOI=10.1016/j.leukres.2004.09.002; RA Morerio C., Acquila M., Rosanda C., Rapella A., Tassano E., Micalizzi C., RA Panarello C.; RT "t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute myeloid RT leukemia."; RL Leuk. Res. 29:467-470(2005). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-839 AND RP SER-888, AND IDENTIFICATION BY 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 [22] RP CHROMOSOMAL TRANSLOCATION WITH LNP1. RX PubMed=16467868; DOI=10.1038/sj.leu.2404130; RA Romana S.P., Radford-Weiss I., Ben Abdelali R., Schluth C., Petit A., RA Dastugue N., Talmant P., Bilhou-Nabera C., Mugneret F., RA Lafage-Pochitaloff M., Mozziconacci M.-J., Andrieu J., Lai J.-L., Terre C., RA Rack K., Cornillet-Lefebvre P., Luquet I., Nadal N., Nguyen-Khac F., RA Perot C., Van den Akker J., Fert-Ferrer S., Cabrol C., Charrin C., RA Tigaud I., Poirel H., Vekemans M., Bernard O.A., Berger R.; RT "NUP98 rearrangements in hematopoietic malignancies: a study of the Groupe RT Francophone de Cytogenetique Hematologique."; RL Leukemia 20:696-706(2006). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623; RP SER-1028 AND SER-1060, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [24] RP CHROMOSOMAL TRANSLOCATION WITH PHF23. RC TISSUE=Peripheral blood; RX PubMed=17287853; DOI=10.1038/sj.leu.2404579; RA Reader J.C., Meekins J.S., Gojo I., Ning Y.; RT "A novel NUP98-PHF23 fusion resulting from a cryptic translocation RT t(11;17)(p15;p13) in acute myeloid leukemia."; RL Leukemia 21:842-844(2007). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 AND SER-612, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND IDENTIFICATION BY RP 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 [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-839; SER-888; RP SER-934; THR-1000; SER-1023; SER-1028; SER-1043; SER-1060 AND THR-1070, AND 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 [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-618; RP SER-623 AND SER-625, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [32] RP SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING. RX PubMed=20407419; DOI=10.1038/emboj.2010.54; RA Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., RA Thyberg J., Cordes V.C.; RT "Protein Tpr is required for establishing nuclear pore-associated zones of RT heterochromatin exclusion."; RL EMBO J. 29:1659-1673(2010). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-608; SER-612; RP SER-623; THR-670; SER-673; SER-681; SER-839; SER-888 AND SER-934, AND RP 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 [34] 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 [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-623; SER-683; RP SER-839 AND SER-888, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [36] RP CHROMOSOMAL TRANSLOCATION WITH NUP98. RX PubMed=22058212; DOI=10.3324/haematol.2011.047969; RA Petit A., Ragu C., Soler G., Ottolenghi C., Schluth C., Radford-Weiss I., RA Schneider-Maunoury S., Callebaut I., Dastugue N., Drabkin H.A., RA Bernard O.A., Romana S., Penard-Lacronique V.; RT "Functional analysis of the NUP98-CCDC28A fusion protein."; RL Haematologica 97:379-387(2012). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623; RP SER-681; SER-683; SER-839; SER-888; THR-1000; SER-1023; SER-1028; SER-1043 RP AND SER-1060, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [38] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 CAPSID PROTEIN RP P24 AND NUCLEOCAPSID PROTEIN P7 (MICROBIAL INFECTION). RX PubMed=23523133; DOI=10.1016/j.virol.2013.02.008; RA Di Nunzio F., Fricke T., Miccio A., Valle-Casuso J.C., Perez P., Souque P., RA Rizzi E., Severgnini M., Mavilio F., Charneau P., Diaz-Griffero F.; RT "Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of RT HIV-1 replication."; RL Virology 440:8-18(2013). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-888 AND SER-897, 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 [40] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [41] RP FUNCTION, INTERACTION WITH DHX9, AND SUBCELLULAR LOCATION. RX PubMed=28221134; DOI=10.7554/elife.18825; RA Capitanio J.S., Montpetit B., Wozniak R.W.; RT "Human Nup98 regulates the localization and activity of DExH/D-box helicase RT DHX9."; RL Elife 6:0-0(2017). RN [42] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-563; LYS-603 AND LYS-665, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [43] RP INTERACTION WITH NUP88. RX PubMed=30543681; DOI=10.1371/journal.pgen.1007845; RA Bonnin E., Cabochette P., Filosa A., Juehlen R., Komatsuzaki S., RA Hezwani M., Dickmanns A., Martinelli V., Vermeersch M., Supply L., RA Martins N., Pirenne L., Ravenscroft G., Lombard M., Port S., Spillner C., RA Janssens S., Roets E., Van Dorpe J., Lammens M., Kehlenbach R.H., RA Ficner R., Laing N.G., Hoffmann K., Vanhollebeke B., Fahrenkrog B.; RT "Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia RT deformation sequence."; RL PLoS Genet. 14:E1007845-E1007845(2018). RN [44] RP INTERACTION WITH SARS-COV-2 ORF6 PROTEIN (MICROBIAL INFECTION), AND RP SUBCELLULAR LOCATION. RX PubMed=33097660; DOI=10.1073/pnas.2016650117; RA Miorin L., Kehrer T., Sanchez-Aparicio M.T., Zhang K., Cohen P., RA Patel R.S., Cupic A., Makio T., Mei M., Moreno E., Danziger O., White K.M., RA Rathnasinghe R., Uccellini M., Gao S., Aydillo T., Mena I., Yin X., RA Martin-Sancho L., Krogan N.J., Chanda S.K., Schotsaert M., Wozniak R.W., RA Ren Y., Rosenberg B.R., Fontoura B.M.A., Garcia-Sastre A.; RT "SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize RT interferon signaling."; RL Proc. Natl. Acad. Sci. U.S.A. 117:28344-28354(2020). RN [45] RP INTERACTION WITH SARS-COV-2 ORF6 PROTEIN (MICROBIAL INFECTION), AND RP SUBCELLULAR LOCATION. RX PubMed=33360543; DOI=10.1016/j.bbrc.2020.11.115; RA Kato K., Ikliptikawati D.K., Kobayashi A., Kondo H., Lim K., Hazawa M., RA Wong R.W.; RT "Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from RT the nuclear pore complex."; RL Biochem. Biophys. Res. Commun. 536:59-66(2021). RN [46] RP INTERACTION WITH SARS-COV-2 ORF6 PROTEIN (MICROBIAL INFECTION) AND SARS-COV RP ORF6 (MICROBIAL INFECTION). RX PubMed=33849972; DOI=10.1128/mbio.00065-21; RA Addetia A., Lieberman N.A.P., Phung Q., Hsiang T.Y., Xie H., RA Roychoudhury P., Shrestha L., Loprieno M.A., Huang M.L., Gale M. Jr., RA Jerome K.R., Greninger A.L.; RT "SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through RT Interactions with Rae1 and Nup98."; RL MBio 12:0-0(2021). RN [47] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, CATALYTIC RP ACTIVITY, INTERACTION WITH NUP96, SUBCELLULAR LOCATION, AUTOPROTEOLYTIC RP PROCESSING, ACTIVE SITE, AND MUTAGENESIS OF LYS-808; ASN-816; HIS-879; RP SER-881 AND LYS-882. RX PubMed=12191480; DOI=10.1016/s1097-2765(02)00589-0; RA Hodel A.E., Hodel M.R., Griffis E.R., Hennig K.A., Ratner G.A., Xu S., RA Powers M.A.; RT "The three-dimensional structure of the autoproteolytic, nuclear pore- RT targeting domain of the human nucleoporin Nup98."; RL Mol. Cell 10:347-358(2002). RN [48] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 733-887, CATALYTIC ACTIVITY, RP SUBUNIT, AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, AND MUTAGENESIS OF RP SER-881. RX PubMed=18287282; DOI=10.1110/ps.073311808; RA Sun Y., Guo H.C.; RT "Structural constraints on autoprocessing of the human nucleoporin Nup98."; RL Protein Sci. 17:494-505(2008). RN [49] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 158-213 IN COMPLEX WITH RAE1, AND RP INTERACTION WITH RAE1. RX PubMed=20498086; DOI=10.1073/pnas.1005389107; RA Ren Y., Seo H.S., Blobel G., Hoelz A.; RT "Structural and functional analysis of the interaction between the RT nucleoporin Nup98 and the mRNA export factor Rae1."; RL Proc. Natl. Acad. Sci. U.S.A. 107:10406-10411(2010). RN [50] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH HOXA9. RX PubMed=8563753; DOI=10.1038/ng0296-154; RA Nakamura T., Largaespada D.A., Lee M.P., Johnson L.A., Ohyashiki K., RA Toyama K., Chen S.J., Willman C.L., Chen I.M., Feinberg A.P., Jenkins N.A., RA Copeland N.G., Shaughnessy J.D. Jr.; RT "Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome RT translocation t(7;11)(p15;p15) in human myeloid leukaemia."; RL Nat. Genet. 12:154-158(1996). RN [51] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH RAP1GDS1. RX PubMed=10477737; RA Hussey D.J., Nicola M., Moore S., Peters G.B., Dobrovic A.; RT "The (4;11)(q21;p15) translocation fuses the NUP98 and RAP1GDS1 genes and RT is recurrent in T-cell acute lymphocytic leukemia."; RL Blood 94:2072-2079(1999). RN [52] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH RAP1GDS1. RX PubMed=10929031; DOI=10.1046/j.1365-2141.2000.02106.x; RA Mecucci C., La Starza R., Negrini M., Sabbioni S., Crescenzi B., Leoni P., RA Di Raimondo F., Krampera M., Cimino G., Tafuri A., Cuneo A., Vitale A., RA Foa R.; RT "t(4;11)(q21;p15) translocation involving NUP98 and RAP1GDS1 genes: RT characterization of a new subset of T acute lymphoblastic leukaemia."; RL Br. J. Haematol. 109:788-793(2000). RN [53] RP DISEASE, AND CHROMOSOMAL TRANSLOCATIONS WITH KDM5A AND RAP1GDS1. RX PubMed=16419055; DOI=10.1002/gcc.20308; RA van Zutven L.J., Onen E., Velthuizen S.C., van Drunen E., von Bergh A.R., RA van den Heuvel-Eibrink M.M., Veronese A., Mecucci C., Negrini M., RA de Greef G.E., Beverloo H.B.; RT "Identification of NUP98 abnormalities in acute leukemia: JARID1A (12p13) RT as a new partner gene."; RL Genes Chromosomes Cancer 45:437-446(2006). RN [54] RP VARIANT [LARGE SCALE ANALYSIS] VAL-1669. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [55] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH KDM5A. RX PubMed=23531517; DOI=10.1038/leu.2013.87; RA de Rooij J.D., Hollink I.H., Arentsen-Peters S.T., van Galen J.F., RA Berna Beverloo H., Baruchel A., Trka J., Reinhardt D., Sonneveld E., RA Zimmermann M., Alonzo T.A., Pieters R., Meshinchi S., RA van den Heuvel-Eibrink M.M., Zwaan C.M.; RT "NUP98/JARID1A is a novel recurrent abnormality in pediatric acute RT megakaryoblastic leukemia with a distinct HOX gene expression pattern."; RL Leukemia 27:2280-2288(2013). RN [56] RP CHARACTERIZATION OF CHROMOSOMAL TRANSLOCATION WITH HOXA9. RX PubMed=34163069; DOI=10.1038/s41586-021-03662-5; RA Ahn J.H., Davis E.S., Daugird T.A., Zhao S., Quiroga I.Y., Uryu H., Li J., RA Storey A.J., Tsai Y.H., Keeley D.P., Mackintosh S.G., Edmondson R.D., RA Byrum S.D., Cai L., Tackett A.J., Zheng D., Legant W.R., Phanstiel D.H., RA Wang G.G.; RT "Phase separation drives aberrant chromatin looping and cancer RT development."; RL Nature 595:591-595(2021). CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly CC and/or maintenance. NUP98 and NUP96 are involved in the bidirectional CC transport across the NPC (PubMed:33097660). May anchor NUP153 and TPR CC to the NPC. In cooperation with DHX9, plays a role in transcription and CC alternative splicing activation of a subset of genes (PubMed:28221134). CC Involved in the localization of DHX9 in discrete intranuclear foci CC (GLFG-body) (PubMed:28221134). {ECO:0000269|PubMed:15229283, CC ECO:0000269|PubMed:33097660}. CC -!- FUNCTION: (Microbial infection) Interacts with HIV-1 capsid protein P24 CC and nucleocapsid protein P7 and may thereby promote the integration of CC the virus in the host nucleus (in vitro) (PubMed:23523133). Binding CC affinity to HIV-1 CA-NC complexes bearing the capsid change Asn-74-Asp CC is reduced (in vitro) (PubMed:23523133). {ECO:0000269|PubMed:23523133}. CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:15229283, CC PubMed:18287282). Interacts directly with NUP96 (PubMed:12191480). Part CC of the Nup160 subcomplex in the nuclear pore which is composed of CC NUP160, NUP133, NUP107 and NUP96; this complex plays a role in RNA CC export and in tethering NUP98 and NUP153 to the nucleus CC (PubMed:11684705). Interacts with RAE1 (PubMed:10209021, CC PubMed:20498086). Does not interact with TPR (PubMed:11684705). CC Interacts with NUP88 (PubMed:30543681). Interacts directly with NUP88 CC and NUP214, subunits of the cytoplasmic filaments of the NPC (By CC similarity). Interacts (via N-terminus) with DHX9 (via DRBM, OB-fold CC and RGG domains); this interaction occurs in a RNA-dependent manner and CC stimulates DHX9-mediated ATPase activity (PubMed:28221134). CC {ECO:0000250|UniProtKB:Q6PFD9, ECO:0000269|PubMed:10209021, CC ECO:0000269|PubMed:11684705, ECO:0000269|PubMed:12191480, CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:18287282, CC ECO:0000269|PubMed:20498086, ECO:0000269|PubMed:28221134, CC ECO:0000269|PubMed:30543681}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 capsid protein P24 CC and nucleocapsid protein P7 (in vitro); the interaction may promote the CC integration of the virus in the host nucleus (in vitro). CC {ECO:0000269|PubMed:23523133}. CC -!- SUBUNIT: (Microbial infection) Interacts with vesicular stomatitis CC virus protein M (PubMed:11106761). {ECO:0000269|PubMed:11106761}. CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS- CC CoV-2 ORF6 protein; the interaction blocks STAT1 nuclear translocation, CC antagonizes interferon signaling and blocks mRNA nuclear export (ex CC vivo). {ECO:0000269|PubMed:33097660, ECO:0000269|PubMed:33360543, CC ECO:0000269|PubMed:33849972}. CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus/SARS-CoV CC ORF6 protein. {ECO:0000269|PubMed:34163069}. CC -!- INTERACTION: CC P52948; P78406: RAE1; NbExp=11; IntAct=EBI-295727, EBI-724495; CC P52948; P0DTC6: 6; Xeno; NbExp=11; IntAct=EBI-295727, EBI-25475897; CC P52948; P59634: 6; Xeno; NbExp=6; IntAct=EBI-295727, EBI-25489038; CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:10087256, CC ECO:0000269|PubMed:11106761, ECO:0000269|PubMed:11839768, CC ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:12802065, CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:20407419, CC ECO:0000269|PubMed:28221134, ECO:0000269|PubMed:33360543}; Peripheral CC membrane protein; Nucleoplasmic side {ECO:0000269|PubMed:11839768}. CC Nucleus, nuclear pore complex {ECO:0000269|PubMed:11839768, CC ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283, CC ECO:0000269|PubMed:33097660}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:28221134}. CC Note=Localized to the nucleoplasmic side of the nuclear pore complex CC (NPC), at or near the nucleoplasmic basket (PubMed:11839768). CC Dissociates from the dissasembled NPC structure early during prophase CC of mitosis (PubMed:12802065). Colocalized with NUP153 and TPR to the CC nuclear basket of NPC (PubMed:11839768). Colocalized with DHX9 in CC diffuse and discrete intranuclear foci (GLFG-body) (PubMed:11839768, CC PubMed:28221134). {ECO:0000269|PubMed:11106761, CC ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065, CC ECO:0000269|PubMed:28221134}. CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:11106761}. CC Note=(Microbial infection) Remains localized to the nuclear membrane CC after poliovirus (PV) infection. {ECO:0000269|PubMed:11106761}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=Nup98-Nup96 precursor; CC IsoId=P52948-1; Sequence=Displayed; CC Name=2; Synonyms=Nup98-Nup96 precursor splice variant 1; CC IsoId=P52948-2; Sequence=VSP_003619, VSP_007944; CC Name=3; Synonyms=Nup98-specific 1; CC IsoId=P52948-3; Sequence=VSP_007942, VSP_007943; CC Name=4; CC IsoId=P52948-4; Sequence=VSP_003619, VSP_007942, VSP_007943; CC Name=5; Synonyms=Nup196, ADIR2; CC IsoId=P52948-5; Sequence=VSP_003619; CC Name=6; CC IsoId=P52948-6; Sequence=VSP_038328; CC -!- DOMAIN: Contains G-L-F-G repeats. The FG repeat domains in Nup98 have a CC direct role in the transport. CC -!- PTM: Isoform 1 to isoform 4 are autoproteolytically cleaved to yield CC Nup98 and Nup96 or Nup98 only, respectively (PubMed:10087256, CC PubMed:20407419, PubMed:12191480, PubMed:18287282). Cleaved Nup98 is CC necessary for the targeting of Nup98 to the nuclear pore and the CC interaction with Nup96 (PubMed:20407419, PubMed:12191480). CC {ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:12191480, CC ECO:0000269|PubMed:18287282, ECO:0000269|PubMed:20407419}. CC -!- PTM: Proteolytically degraded after poliovirus (PV) infection; CC degradation is partial and NCP- and TPR-binding domains withstand CC degradation. CC -!- DISEASE: Note=Chromosomal aberrations involving NUP98 have been found CC in acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9 CC (PubMed:8563753). The chimera includes NUP98 intrinsic disordered CC regions which contribute to aberrant liquid-liquid phase separation CC puncta of the chimera in the nucleus. This phase-separation enhances CC the chimera genomic targeting and induces organization of aberrant CC three-dimensional chromatin structures leading to tumorous CC transformation (PubMed:34163069). Translocation t(11;17)(p15;p13) with CC PHF23 (PubMed:17287853). {ECO:0000269|PubMed:17287853, CC ECO:0000269|PubMed:34163069, ECO:0000269|PubMed:8563753}. CC -!- DISEASE: Note=A chromosomal aberration involving NUP98 has been found CC in M0 type acute myeloid leukemia. Translocation t(4;11)(q23;p15) with CC RAP1GDS1. {ECO:0000269|PubMed:16419055}. CC -!- DISEASE: Note=A chromosomal aberration involving NUP98 has been found CC in T-cell acute lymphocytic leukemia. Translocation t(4;11)(q23;p15) CC with RAP1GDS1. {ECO:0000269|PubMed:10477737, CC ECO:0000269|PubMed:10929031}. CC -!- DISEASE: Note=A chromosomal aberration involving NUP98 has been found CC in M5 type acute myeloid leukemia. Translocation t(11;12)(p15;p13) with CC KDM5A. {ECO:0000269|PubMed:23531517}. CC -!- DISEASE: Note=Chromosomal aberrations involving NUP98 have been found CC in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) CC with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1. CC {ECO:0000269|PubMed:16028218}. CC -!- DISEASE: Note=Chromosomal aberrations involving NUP98 have been found CC in M7 type childhood acute myeloid leukemia. Translocation CC t(11;12)(p15;p13) with KDM5A. {ECO:0000269|PubMed:16419055, CC ECO:0000269|PubMed:23531517}. CC -!- DISEASE: Note=A chromosomal aberration involving NUP98 is found in a CC form of therapy-related myelodysplastic syndrome. Translocation CC t(11;20)(p15;q11) with TOP1. {ECO:0000269|PubMed:16028218}. CC -!- DISEASE: Note=A chromosomal aberration involving NUP98 is found in a CC form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation CC t(3;11)(q12.2;p15.4) with LNP1. {ECO:0000269|PubMed:16028218}. CC -!- DISEASE: Note=A chromosomal aberration involving NUP98 is associated CC with pediatric acute myeloid leukemia (AML) with intermediate CC characteristics between M2-M3 French-American-British (FAB) subtypes. CC Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric CC transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4. CC {ECO:0000269|PubMed:16028218}. CC -!- DISEASE: Note=A chromosomal aberration involving NUP98 has been CC identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5) with CC CCDC28A. The chimeric transcript is an in-frame fusion of NUP98 exon 13 CC to CCDC28A exon 2. Ectopic expression of NUP98-CCDC28A in mouse CC promotes the proliferative capacity and self-renewal potential of CC hematopoietic progenitors and rapidly induced fatal myeloproliferative CC neoplasms and defects in the differentiation of the erythro- CC megakaryocytic lineage. {ECO:0000269|PubMed:16028218}. CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD22395.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305}; CC Sequence=AAD22396.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305}; CC Sequence=AAF19342.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF19342.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/98/NUP"; 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; U41815; AAC50366.1; -; mRNA. DR EMBL; AB040538; BAB18537.1; -; mRNA. DR EMBL; AF071076; AAD22395.1; ALT_SEQ; mRNA. DR EMBL; AF071077; AAD22396.1; ALT_SEQ; mRNA. DR EMBL; AF231130; AAL56659.1; -; mRNA. DR EMBL; AC060812; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090587; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC041136; AAH41136.1; -; mRNA. DR EMBL; BC012906; AAH12906.2; -; mRNA. DR EMBL; AF116074; AAF19342.1; ALT_SEQ; mRNA. DR EMBL; BT007349; AAP36013.1; -; mRNA. DR EMBL; AL133601; CAB63736.1; -; mRNA. DR EMBL; AL137613; CAB70842.1; -; mRNA. DR CCDS; CCDS31347.1; -. [P52948-2] DR CCDS; CCDS41605.1; -. [P52948-3] DR CCDS; CCDS41606.1; -. [P52948-4] DR CCDS; CCDS7746.1; -. [P52948-5] DR CCDS; CCDS91412.1; -. [P52948-1] DR PIR; T43443; T43443. DR RefSeq; NP_005378.4; NM_005387.6. [P52948-3] DR RefSeq; NP_057404.2; NM_016320.4. [P52948-5] DR RefSeq; NP_624357.1; NM_139131.4. [P52948-4] DR RefSeq; NP_624358.2; NM_139132.3. [P52948-2] DR PDB; 1KO6; X-ray; 3.00 A; A/C=695-880, B/D=881-941. DR PDB; 2Q5X; X-ray; 1.90 A; A=733-887. DR PDB; 2Q5Y; X-ray; 2.30 A; A/C=729-880. DR PDB; 3MMY; X-ray; 1.65 A; B/D/F/H=158-213. DR PDB; 4OWR; X-ray; 3.15 A; B=157-213. DR PDB; 5A9Q; EM; 23.00 A; 5/E/N/W=881-1817. DR PDB; 6BZM; EM; 0.90 A; A/B=116-123. DR PDB; 7F60; X-ray; 2.85 A; C/D=1-1817. DR PDB; 7F90; X-ray; 2.39 A; B/D=1-1817. DR PDB; 7MNI; X-ray; 2.00 A; B/D=732-880. DR PDB; 7PEQ; EM; 35.00 A; AE/BE/CE/DE=881-1817. DR PDB; 7Q64; EM; 2.76 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=85-124. DR PDB; 7Q65; EM; 3.32 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=85-124. DR PDB; 7Q66; EM; 2.79 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=85-124. DR PDB; 7Q67; EM; 3.37 A; A/B/C/D/E/F/G/H/I/J/K=85-124. DR PDB; 7VPG; X-ray; 2.49 A; B/D/F/H=158-213. DR PDB; 7VPH; X-ray; 2.80 A; B/D/F/H=158-213. DR PDBsum; 1KO6; -. DR PDBsum; 2Q5X; -. DR PDBsum; 2Q5Y; -. DR PDBsum; 3MMY; -. DR PDBsum; 4OWR; -. DR PDBsum; 5A9Q; -. DR PDBsum; 6BZM; -. DR PDBsum; 7F60; -. DR PDBsum; 7F90; -. DR PDBsum; 7MNI; -. DR PDBsum; 7PEQ; -. DR PDBsum; 7Q64; -. DR PDBsum; 7Q65; -. DR PDBsum; 7Q66; -. DR PDBsum; 7Q67; -. DR PDBsum; 7VPG; -. DR PDBsum; 7VPH; -. DR AlphaFoldDB; P52948; -. DR EMDB; EMD-13851; -. DR EMDB; EMD-13852; -. DR EMDB; EMD-13853; -. DR EMDB; EMD-13854; -. DR SASBDB; P52948; -. DR SMR; P52948; -. DR BioGRID; 110982; 225. DR ComplexPortal; CPX-873; Nuclear pore complex. DR CORUM; P52948; -. DR DIP; DIP-32484N; -. DR IntAct; P52948; 87. DR MINT; P52948; -. DR STRING; 9606.ENSP00000316032; -. DR MEROPS; S59.001; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyConnect; 1578; 1 N-Linked glycan (1 site). DR GlyConnect; 2900; 1 O-GlcNAc glycan (3 sites). [P52948-4] DR GlyCosmos; P52948; 92 sites, 3 glycans. DR GlyGen; P52948; 107 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (106 sites). DR iPTMnet; P52948; -. DR MetOSite; P52948; -. DR PhosphoSitePlus; P52948; -. DR SwissPalm; P52948; -. DR BioMuta; NUP98; -. DR DMDM; 308153660; -. DR EPD; P52948; -. DR jPOST; P52948; -. DR MassIVE; P52948; -. DR MaxQB; P52948; -. DR PaxDb; 9606-ENSP00000316032; -. DR PeptideAtlas; P52948; -. DR ProteomicsDB; 56555; -. [P52948-1] DR ProteomicsDB; 56556; -. [P52948-2] DR ProteomicsDB; 56557; -. [P52948-3] DR ProteomicsDB; 56558; -. [P52948-4] DR ProteomicsDB; 56559; -. [P52948-5] DR ProteomicsDB; 56560; -. [P52948-6] DR Pumba; P52948; -. DR Antibodypedia; 23367; 373 antibodies from 33 providers. DR DNASU; 4928; -. DR Ensembl; ENST00000324932.12; ENSP00000316032.7; ENSG00000110713.18. [P52948-5] DR Ensembl; ENST00000355260.8; ENSP00000347404.3; ENSG00000110713.18. [P52948-2] DR Ensembl; ENST00000359171.8; ENSP00000352091.5; ENSG00000110713.18. [P52948-1] DR Ensembl; ENST00000397004.9; ENSP00000380199.4; ENSG00000110713.18. [P52948-4] DR Ensembl; ENST00000397007.10; ENSP00000380202.4; ENSG00000110713.18. [P52948-3] DR Ensembl; ENST00000700606.1; ENSP00000515094.1; ENSG00000110713.18. [P52948-4] DR GeneID; 4928; -. DR KEGG; hsa:4928; -. DR MANE-Select; ENST00000324932.12; ENSP00000316032.7; NM_016320.5; NP_057404.2. [P52948-5] DR UCSC; uc001lyh.3; human. [P52948-1] DR AGR; HGNC:8068; -. DR CTD; 4928; -. DR DisGeNET; 4928; -. DR GeneCards; NUP98; -. DR HGNC; HGNC:8068; NUP98. DR HPA; ENSG00000110713; Low tissue specificity. DR MalaCards; NUP98; -. DR MIM; 601021; gene. DR neXtProt; NX_P52948; -. DR OpenTargets; ENSG00000110713; -. DR PharmGKB; PA31856; -. DR VEuPathDB; HostDB:ENSG00000110713; -. DR eggNOG; KOG0845; Eukaryota. DR GeneTree; ENSGT00550000074799; -. DR HOGENOM; CLU_002330_1_0_1; -. DR InParanoid; P52948; -. DR OMA; PMGKGLN; -. DR OrthoDB; 1377152at2759; -. DR PhylomeDB; P52948; -. DR TreeFam; TF343335; -. DR PathwayCommons; P52948; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. [P52948-5] DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA. DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA. DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript. DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript. DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA. DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus. DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways. DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis. DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery. DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein. DR Reactome; R-HSA-180746; Nuclear import of Rev protein. DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs. DR Reactome; R-HSA-191859; snRNP Assembly. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. [P52948-5] DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. [P52948-5] DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins. DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins. DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC). DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. [P52948-5] DR Reactome; R-HSA-6784531; tRNA processing in the nucleus. DR Reactome; R-HSA-68877; Mitotic Prometaphase. [P52948-5] DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9610379; HCMV Late Events. DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation. [P52948-5] DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. [P52948-5] DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR SignaLink; P52948; -. DR SIGNOR; P52948; -. DR BioGRID-ORCS; 4928; 656 hits in 1172 CRISPR screens. DR ChiTaRS; NUP98; human. DR EvolutionaryTrace; P52948; -. DR GeneWiki; NUP98; -. DR GenomeRNAi; 4928; -. DR Pharos; P52948; Tbio. DR PRO; PR:P52948; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P52948; Protein. DR Bgee; ENSG00000110713; Expressed in left testis and 199 other cell types or tissues. DR ExpressionAtlas; P52948; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB. DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB. DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB. DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central. DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB. DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IMP:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IMP:UniProtKB. DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central. DR GO; GO:1990841; F:promoter-specific chromatin binding; IMP:UniProtKB. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB. DR GO; GO:0006999; P:nuclear pore organization; NAS:UniProtKB. DR GO; GO:0006913; P:nucleocytoplasmic transport; TAS:UniProtKB. DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central. DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central. DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IBA:GO_Central. DR DisProt; DP02123; -. DR Gene3D; 1.10.10.2360; -; 1. DR Gene3D; 1.25.40.690; -; 1. DR Gene3D; 3.30.1610.10; Peptidase S59, nucleoporin; 1. DR InterPro; IPR037665; Nucleoporin_S59-like. DR InterPro; IPR007230; Nup98_auto-Pept-S59_dom. DR InterPro; IPR036903; Nup98_auto-Pept-S59_dom_sf. DR InterPro; IPR021967; Nup98_C. DR PANTHER; PTHR23198:SF6; NUCLEAR PORE COMPLEX PROTEIN NUP98-NUP96; 1. DR PANTHER; PTHR23198; NUCLEOPORIN; 1. DR Pfam; PF04096; Nucleoporin2; 1. DR Pfam; PF12110; Nup96; 1. DR Pfam; PF21240; Nup98_GLEBS; 1. DR SUPFAM; SSF82215; C-terminal autoproteolytic domain of nucleoporin nup98; 1. DR PROSITE; PS51434; NUP_C; 1. DR Genevisible; P52948; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Autocatalytic cleavage; KW Chromosomal rearrangement; Direct protein sequencing; KW Host-virus interaction; Hydrolase; Isopeptide bond; Membrane; KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Protease; KW Protein transport; Reference proteome; Repeat; Serine protease; KW Translocation; Transport; Ubl conjugation. FT CHAIN 1..880 FT /note="Nuclear pore complex protein Nup98" FT /id="PRO_0000019929" FT CHAIN 881..1817 FT /note="Nuclear pore complex protein Nup96" FT /id="PRO_0000019930" FT DOMAIN 738..880 FT /note="Peptidase S59" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765" FT REGION 1..156 FT /note="FG repeats 1" FT REGION 157..213 FT /note="GLEBS; interaction with RAE1" FT /evidence="ECO:0000269|PubMed:10209021" FT REGION 214..480 FT /note="FG repeats 2" FT REGION 512..535 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 614..633 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 662..682 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 886..937 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 886..901 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 902..921 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 881 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:12191480, FT ECO:0000269|PubMed:18287282" FT SITE 391..392 FT /note="Breakpoint for translocation to form the NUP98- FT RAP1GDS1 fusion protein. Breakpoint for translocation to FT form the NUP98-RAP1GDS1 fusion protein" FT /evidence="ECO:0000269|PubMed:10477737, FT ECO:0000269|PubMed:16419055" FT SITE 486..487 FT /note="Breakpoint for translocation to form the NUP98-HOXA9 FT fusion protein. Breakpoint for translocation to form the FT NUP98-RAP1GDS1 fusion protein" FT /evidence="ECO:0000269|PubMed:10477737, FT ECO:0000269|PubMed:8563753" FT SITE 531..532 FT /note="Breakpoint for translocation to form NUP98-CCDC28A" FT SITE 531..532 FT /note="Breakpoint for translocation to form NUP98-PHF23 FT oncogene" FT SITE 531..532 FT /note="Breakpoint for translocation to form the NUP98-KDM5A FT fusion protein" FT /evidence="ECO:0000269|PubMed:16419055" FT SITE 880..881 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000269|PubMed:10087256, FT ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282" FT MOD_RES 524 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 603 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 608 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 612 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 618 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 623 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 625 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 653 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PFD9" FT MOD_RES 670 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 673 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 681 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 683 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 839 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 888 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 897 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 934 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 1000 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1023 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1028 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 1043 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1060 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 1064 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PFD9" FT MOD_RES 1070 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1329 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PFD9" FT MOD_RES 1772 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6PFD9" FT CROSSLNK 563 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 603 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 665 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 393..409 FT /note="Missing (in isoform 2, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:10087256, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:8563754, ECO:0000303|Ref.4, FT ECO:0000303|Ref.7, ECO:0000303|Ref.8" FT /id="VSP_003619" FT VAR_SEQ 932..937 FT /note="SQSPEV -> VEKKGQ (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8563754, ECO:0000303|Ref.2" FT /id="VSP_007942" FT VAR_SEQ 938..1817 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8563754, ECO:0000303|Ref.2" FT /id="VSP_007943" FT VAR_SEQ 1085..1188 FT /note="WSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPREKSVTYGKGKLLMDMA FT LFMGRSFRVGWGPNWTLANSGEQLNGSHELENHQIADSMEFGFLPNPVAVKP -> C FT (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_038328" FT VAR_SEQ 1502..1576 FT /note="RHYDLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSAQCEGVLQASYA FT GQLESEGLWEWAIFVLLHIDNSG -> S (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10087256" FT /id="VSP_007944" FT VARIANT 1669 FT /note="G -> V (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035859" FT MUTAGEN 808 FT /note="K->A: No effect on autoprocessing. Severe loss of FT autoprocessing; when associated with A-879." FT /evidence="ECO:0000269|PubMed:12191480" FT MUTAGEN 816 FT /note="N->A: Slight reduction in autoprocessing." FT /evidence="ECO:0000269|PubMed:12191480" FT MUTAGEN 879 FT /note="H->A,Q: Moderate reduction in autoprocessing." FT /evidence="ECO:0000269|PubMed:12191480" FT MUTAGEN 880..883 FT /note="FSKY->SSKR: Loss of processing. Loss of nuclear FT membrane localization." FT /evidence="ECO:0000269|PubMed:10087256" FT MUTAGEN 881 FT /note="S->A: Loss of autoprocessing. Loss of nuclear FT membrane localization." FT /evidence="ECO:0000269|PubMed:12191480, FT ECO:0000269|PubMed:18287282" FT MUTAGEN 882 FT /note="K->A: No effect in autoprocessing." FT /evidence="ECO:0000269|PubMed:12191480" FT CONFLICT 318 FT /note="L -> S (in Ref. 6; AAH41136)" FT /evidence="ECO:0000305" FT CONFLICT 376 FT /note="S -> G (in Ref. 6; AAH41136)" FT /evidence="ECO:0000305" FT CONFLICT 756..757 FT /note="EK -> VF (in Ref. 3; AAD22395/AAD22396)" FT /evidence="ECO:0000305" FT CONFLICT 1281 FT /note="G -> A (in Ref. 3; AAD22395/AAD22396 and 4; FT AAL56659)" FT /evidence="ECO:0000305" FT CONFLICT 1534..1536 FT /note="ALN -> DLK (in Ref. 3; AAD22395)" FT /evidence="ECO:0000305" FT CONFLICT 1594 FT /note="E -> D (in Ref. 7; AAF19342)" FT /evidence="ECO:0000305" FT CONFLICT 1598 FT /note="S -> T (in Ref. 4; AAL56659)" FT /evidence="ECO:0000305" FT CONFLICT 1639 FT /note="K -> N (in Ref. 7; AAF19342)" FT /evidence="ECO:0000305" FT CONFLICT 1680 FT /note="S -> T (in Ref. 7; AAF19342)" FT /evidence="ECO:0000305" FT STRAND 91..96 FT /evidence="ECO:0007829|PDB:7Q64" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:7Q64" FT STRAND 105..113 FT /evidence="ECO:0007829|PDB:7Q66" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:7Q64" FT STRAND 168..172 FT /evidence="ECO:0007829|PDB:3MMY" FT STRAND 181..186 FT /evidence="ECO:0007829|PDB:3MMY" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:3MMY" FT TURN 193..197 FT /evidence="ECO:0007829|PDB:3MMY" FT HELIX 200..209 FT /evidence="ECO:0007829|PDB:3MMY" FT STRAND 741..745 FT /evidence="ECO:0007829|PDB:2Q5X" FT HELIX 747..753 FT /evidence="ECO:0007829|PDB:2Q5X" FT STRAND 761..769 FT /evidence="ECO:0007829|PDB:2Q5X" FT TURN 770..772 FT /evidence="ECO:0007829|PDB:2Q5X" FT STRAND 773..782 FT /evidence="ECO:0007829|PDB:2Q5X" FT HELIX 788..791 FT /evidence="ECO:0007829|PDB:2Q5X" FT STRAND 792..795 FT /evidence="ECO:0007829|PDB:2Q5X" FT STRAND 798..801 FT /evidence="ECO:0007829|PDB:2Q5X" FT HELIX 805..807 FT /evidence="ECO:0007829|PDB:2Q5Y" FT STRAND 819..823 FT /evidence="ECO:0007829|PDB:2Q5X" FT TURN 831..833 FT /evidence="ECO:0007829|PDB:2Q5X" FT HELIX 840..845 FT /evidence="ECO:0007829|PDB:2Q5X" FT HELIX 848..858 FT /evidence="ECO:0007829|PDB:2Q5X" FT STRAND 862..867 FT /evidence="ECO:0007829|PDB:2Q5X" FT TURN 868..871 FT /evidence="ECO:0007829|PDB:2Q5X" FT STRAND 872..879 FT /evidence="ECO:0007829|PDB:2Q5X" SQ SEQUENCE 1817 AA; 197579 MW; BC60E5456B936C79 CRC64; MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG TNTNTSNFGF GTNTSGNSIF GSKPAPGTLG TGLGAGFGTA LGAGQASLFG NNQPKIGGPL GTGAFGAPGF NTTTATLGFG APQAPVALTD PNASAAQQAV LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA QKALTTPTHY KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD EDSLVSHFYT NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG LEGSSEETSF HDESLQDDRE EIENNSYHMH PAGIILTKVG YYTIPSMDDL AKITNEKGEC IVSDFTIGRK GYGSIYFEGD VNLTNLNLDD IVHIRRKEVV VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP DRLADINYEG RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QSQSPEVEQL GRVVELDSDM VDITQEPVLD TMLEESMPED QEPVSASTHI ASSLGINPHV LQIMKASLLT DEEDVDMALD QRFSRLPSKA DTSQEICSPR LPISASHSSK TRSLVGGLLQ SKFTSGAFLS PSVSVQECRT PRAASLMNIP STSSWSVPPP LTSVFTMPSP APEVPLKTVG TRRQLGLVPR EKSVTYGKGK LLMDMALFMG RSFRVGWGPN WTLANSGEQL NGSHELENHQ IADSMEFGFL PNPVAVKPLT ESPFKVHLEK LSLRQRKPDE DMKLYQTPLE LKLKHSTVHV DELCPLIVPN LGVAVIHDYA DWVKEASGDL PEAQIVKHWS LTWTLCEALW GHLKELDSQL NEPREYIQIL ERRRAFSRWL SCTATPQIEE EVSLTQKNSP VEAVFSYLTG KRISEACSLA QQSGDHRLAL LLSQFVGSQS VRELLTMQLV DWHQLQADSF IQDERLRIFA LLAGKPVWQL SEKKQINVCS QLDWKRSLAI HLWYLLPPTA SISRALSMYE EAFQNTSDSD RYACSPLPSY LEGSGCVIAE EQNSQTPLRD VCFHLLKLYS DRHYDLNQLL EPRSITADPL DYRLSWHLWE VLRALNYTHL SAQCEGVLQA SYAGQLESEG LWEWAIFVLL HIDNSGIREK AVRELLTRHC QLLETPESWA KETFLTQKLR VPAKWIHEAK AVRAHMESDK HLEALCLFKA EHWNRCHKLI IRHLASDAII NENYDYLKGF LEDLAPPERS SLIQDWETSG LVYLDYIRVI EMLRHIQQVD CSGNDLEQLH IKVTSLCSRI EQIQCYSAKD RLAQSDMAKR VANLLRVVLS LHHPPDRTSD STPDPQRVPL RLLAPHIGRL PMPEDYAMDE LRSLTQSYLR ELAVGSL //