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   24-JAN-2024, entry version 235.
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";
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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; 224.
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; 372 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   Genevisible; P52948; HS.
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.
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
//