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Nuclear pore complex protein Nup98-Nup96 (EC 3.4.21.-) [Cleaved into: Nuclear pore complex protein Nup98 (98 kDa nucleoporin) (Nucleoporin Nup98) (Nup98); Nuclear pore complex protein Nup96 (96 kDa nucleoporin) (Nucleoporin Nup96) (Nup96)]

 NUP98_HUMAN             Reviewed;        1817 AA.
P52948; Q8IUT2; Q8WYB0; Q96E54; Q9H3Q4; Q9NT02; Q9UF57; Q9UHX0;
Q9Y6J4; Q9Y6J5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
27-SEP-2017, entry version 193.
RecName: Full=Nuclear pore complex protein Nup98-Nup96;
EC=3.4.21.- {ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282};
Contains:
RecName: Full=Nuclear pore complex protein Nup98;
AltName: Full=98 kDa nucleoporin;
AltName: Full=Nucleoporin Nup98;
Short=Nup98;
Contains:
RecName: Full=Nuclear pore complex protein Nup96;
AltName: Full=96 kDa nucleoporin;
AltName: Full=Nucleoporin Nup96;
Short=Nup96;
Flags: Precursor;
Name=NUP98; Synonyms=ADAR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND CHROMOSOMAL TRANSLOCATION
WITH HOXA9.
PubMed=8563754; DOI=10.1038/ng0296-159;
Borrow J., Shearman A.M., Stanton V.P., Becher R., Collins T.,
Williams A.J., Dube I., Katz F., Kwong Y.L., Morris C., Ohyashiki K.,
Toyama K., Rowley J., Housman D.E.;
"The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses
the genes for nucleoporin NUP98 and class I homeoprotein HOXA9.";
Nat. Genet. 12:159-167(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Arai Y., Kaneko Y., Kubo T., Arai K., Hosoda F., Ohki M.;
"Molecular analysis of the chromosomal breakpoints and identification
of the repetitive sequences near the breakpoints of NUP98 in therapy-
related leukemia with inv(11)(p15q22).";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
1648-1664, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS
OF 863-PHE--TYR-883.
PubMed=10087256; DOI=10.1083/jcb.144.6.1097;
Fontoura B.M.A., Blobel G., Matunis M.J.;
"A conserved biogenesis pathway for nucleoporins: proteolytic
processing of a 186-kilodalton precursor generates Nup98 and the novel
nucleoporin, Nup96.";
J. Cell Biol. 144:1097-1112(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Borrow J., Housman D.E.;
"An alternative splice form of NUP98 encodes a 196kDa NUP196
isoform.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 963-1817 (ISOFORM 6).
TISSUE=Lung carcinoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1176-1817 (ISOFORM 5).
TISSUE=Liver;
Xu Y.H., Guo B.C., Yu Y.L.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1212-1817 (ISOFORM 5).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1227-1817 (ISOFORM 5).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
CHROMOSOMAL TRANSLOCATION WITH TOP1.
PubMed=10556215;
Ahuja H.G., Felix C.A., Aplan P.D.;
"The t(11;20)(p15;q11) chromosomal translocation associated with
therapy-related myelodysplastic syndrome results in an NUP98-TOP1
fusion.";
Blood 94:3258-3261(1999).
[11]
INTERACTION WITH RAE1.
PubMed=10209021; DOI=10.1083/jcb.145.2.237;
Pritchard C.E., Fornerod M., Kasper L.H., van Deursen J.M.;
"RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like
NUP98 motif at the nuclear pore complex through multiple domains.";
J. Cell Biol. 145:237-254(1999).
[12]
INTERACTION WITH VESICULAR STOMATITIS VIRUS PROTEIN M (MICROBIAL
INFECTION), AND SUBCELLULAR LOCATION.
PubMed=11106761; DOI=10.1016/S1097-2765(00)00120-9;
von Kobbe C., van Deursen J.M., Rodrigues J.P., Sitterlin D.,
Bachi A., Wu X., Wilm M., Carmo-Fonseca M., Izaurralde E.;
"Vesicular stomatitis virus matrix protein inhibits host cell gene
expression by targeting the nucleoporin Nup98.";
Mol. Cell 6:1243-1252(2000).
[13]
CHROMOSOMAL TRANSLOCATION WITH NSD1.
PubMed=11493482; DOI=10.1182/blood.V98.4.1264;
Jaju R.J., Fidler C., Haas O.A., Strickson A.J., Watkins F., Clark K.,
Cross N.C., Cheng J.F., Aplan P.D., Kearney L., Boultwood J.,
Wainscoat J.S.;
"A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de
novo childhood acute myeloid leukemia.";
Blood 98:1264-1267(2001).
[14]
SUBUNIT.
PubMed=11684705; DOI=10.1083/jcb.200108007;
Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.;
"Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA
export.";
J. Cell Biol. 155:339-354(2001).
[15]
CHROMOSOMAL TRANSLOCATION WITH WHSC1L1.
PubMed=11986249; DOI=10.1182/blood.V99.10.3857;
Rosati R., La Starza R., Veronese A., Aventin A., Schwienbacher C.,
Vallespi T., Negrini M., Martelli M.F., Mecucci C.;
"NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated
with t(8;11)(p11.2;p15).";
Blood 99:3857-3860(2002).
[16]
SUBCELLULAR LOCATION.
PubMed=11839768; DOI=10.1083/jcb.200106046;
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
"Tpr is localized within the nuclear basket of the pore complex and
has a role in nuclear protein export.";
J. Cell Biol. 156:617-630(2002).
[17]
LACK OF INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
PubMed=12802065; DOI=10.1091/mbc.E02-09-0620;
Hase M.E., Cordes V.C.;
"Direct interaction with nup153 mediates binding of Tpr to the
periphery of the nuclear pore complex.";
Mol. Biol. Cell 14:1923-1940(2003).
[18]
FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=15229283; DOI=10.1091/mbc.E04-03-0165;
Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.;
"Nucleoporins as components of the nuclear pore complex core structure
and Tpr as the architectural element of the nuclear basket.";
Mol. Biol. Cell 15:4261-4277(2004).
[19]
CHROMOSOMAL TRANSLOCATION WITH NUP98, AND DISEASE.
PubMed=16028218; DOI=10.1002/gcc.20233;
Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J.,
Harbott J.;
"Characterization of 6q abnormalities in childhood acute myeloid
leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting
in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic
leukemia.";
Genes Chromosomes Cancer 44:225-232(2005).
[20]
CHROMOSOMAL TRANSLOCATION WITH PSIP1/LEDGF.
PubMed=15725483; DOI=10.1016/j.leukres.2004.09.002;
Morerio C., Acquila M., Rosanda C., Rapella A., Tassano E.,
Micalizzi C., Panarello C.;
"t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute
myeloid leukemia.";
Leuk. Res. 29:467-470(2005).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-839
AND SER-888, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[22]
CHROMOSOMAL TRANSLOCATION WITH LNP1.
PubMed=16467868; DOI=10.1038/sj.leu.2404130;
Romana S.P., Radford-Weiss I., Ben Abdelali R., Schluth C., Petit A.,
Dastugue N., Talmant P., Bilhou-Nabera C., Mugneret F.,
Lafage-Pochitaloff M., Mozziconacci M.-J., Andrieu J., Lai J.-L.,
Terre C., Rack K., Cornillet-Lefebvre P., Luquet I., Nadal N.,
Nguyen-Khac F., Perot C., Van den Akker J., Fert-Ferrer S., Cabrol C.,
Charrin C., Tigaud I., Poirel H., Vekemans M., Bernard O.A.,
Berger R.;
"NUP98 rearrangements in hematopoietic malignancies: a study of the
Groupe Francophone de Cytogenetique Hematologique.";
Leukemia 20:696-706(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623;
SER-1028 AND SER-1060, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[24]
CHROMOSOMAL TRANSLOCATION WITH PHF23.
TISSUE=Peripheral blood;
PubMed=17287853; DOI=10.1038/sj.leu.2404579;
Reader J.C., Meekins J.S., Gojo I., Ning Y.;
"A novel NUP98-PHF23 fusion resulting from a cryptic translocation
t(11;17)(p15;p13) in acute myeloid leukemia.";
Leukemia 21:842-844(2007).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 AND SER-612, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-839; SER-888;
SER-934; THR-1000; SER-1023; SER-1028; SER-1043; SER-1060 AND
THR-1070, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-618;
SER-623 AND SER-625, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[32]
SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
PubMed=20407419; DOI=10.1038/emboj.2010.54;
Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H.,
Thyberg J., Cordes V.C.;
"Protein Tpr is required for establishing nuclear pore-associated
zones of heterochromatin exclusion.";
EMBO J. 29:1659-1673(2010).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-608; SER-612;
SER-623; THR-670; SER-673; SER-681; SER-839; SER-888 AND SER-934, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-623; SER-683;
SER-839 AND SER-888, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[36]
CHROMOSOMAL TRANSLOCATION WITH NUP98.
PubMed=22058212; DOI=10.3324/haematol.2011.047969;
Petit A., Ragu C., Soler G., Ottolenghi C., Schluth C.,
Radford-Weiss I., Schneider-Maunoury S., Callebaut I., Dastugue N.,
Drabkin H.A., Bernard O.A., Romana S., Penard-Lacronique V.;
"Functional analysis of the NUP98-CCDC28A fusion protein.";
Haematologica 97:379-387(2012).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623;
SER-681; SER-683; SER-839; SER-888; THR-1000; SER-1023; SER-1028;
SER-1043 AND SER-1060, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-888 AND
SER-897, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[40]
FUNCTION, INTERACTION WITH DHX9, AND SUBCELLULAR LOCATION.
PubMed=28221134; DOI=10.7554/eLife.18825;
Capitanio J.S., Montpetit B., Wozniak R.W.;
"Human Nup98 regulates the localization and activity of DExH/D-box
helicase DHX9.";
Elife 6:0-0(2017).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-563; LYS-603 AND LYS-665,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[42]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, CATALYTIC
ACTIVITY, INTERACTION WITH NUP96, SUBCELLULAR LOCATION,
AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, AND MUTAGENESIS OF LYS-808;
ASN-816; HIS-879; SER-881 AND LYS-882.
PubMed=12191480; DOI=10.1016/S1097-2765(02)00589-0;
Hodel A.E., Hodel M.R., Griffis E.R., Hennig K.A., Ratner G.A., Xu S.,
Powers M.A.;
"The three-dimensional structure of the autoproteolytic, nuclear pore-
targeting domain of the human nucleoporin Nup98.";
Mol. Cell 10:347-358(2002).
[43]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 733-887, CATALYTIC ACTIVITY,
SUBUNIT, AUTOPROTEOLYTIC PROCESSING, ACTIVE SITE, AND MUTAGENESIS OF
SER-881.
PubMed=18287282; DOI=10.1110/ps.073311808;
Sun Y., Guo H.C.;
"Structural constraints on autoprocessing of the human nucleoporin
Nup98.";
Protein Sci. 17:494-505(2008).
[44]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 158-213 IN COMPLEX WITH
RAE1.
PubMed=20498086; DOI=10.1073/pnas.1005389107;
Ren Y., Seo H.S., Blobel G., Hoelz A.;
"Structural and functional analysis of the interaction between the
nucleoporin Nup98 and the mRNA export factor Rae1.";
Proc. Natl. Acad. Sci. U.S.A. 107:10406-10411(2010).
[45]
VARIANT [LARGE SCALE ANALYSIS] VAL-1669.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
and/or maintenance. NUP98 and NUP96 are involved in the
bidirectional transport across the NPC. May anchor NUP153 and TPR
to the NPC. In cooperation with DHX9, plays a role in
transcription and alternative splicing activation of a subset of
genes (PubMed:28221134). Involved in the localization of DHX9 in
discrete intranuclear foci (GLFG-body) (PubMed:28221134).
{ECO:0000269|PubMed:15229283}.
-!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:15229283,
PubMed:18287282). Interacts directly with NUP96 (PubMed:12191480).
Part of the Nup160 subcomplex in the nuclear pore which is
composed of NUP160, NUP133, NUP107 and NUP96; this complex plays a
role in RNA export and in tethering NUP98 and NUP153 to the
nucleus (PubMed:11684705). Interacts with RAE1 (PubMed:10209021,
PubMed:20498086). Does not interact with TPR (PubMed:11684705).
Interacts directly with NUP88 and NUP214, subunits of the
cytoplasmic filaments of the NPC (By similarity). Interacts (via
N-terminus) with DHX9 (via DRBM, OB-fold and RGG domains); this
interaction occurs in a RNA-dependent manner and stimulates DHX9-
mediated ATPase activity (PubMed:28221134).
{ECO:0000250|UniProtKB:Q6PFD9, ECO:0000269|PubMed:10209021,
ECO:0000269|PubMed:11684705, ECO:0000269|PubMed:12191480,
ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:18287282,
ECO:0000269|PubMed:20498086, ECO:0000269|PubMed:28221134}.
-!- SUBUNIT: (Microbial infection) Interacts with vesicular stomatitis
virus protein M (PubMed:11106761). {ECO:0000269|PubMed:11106761}.
-!- INTERACTION:
Q9UBU9:NXF1; NbExp=2; IntAct=EBI-295727, EBI-398874;
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11106761,
ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12191480,
ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
ECO:0000269|PubMed:20407419, ECO:0000269|PubMed:28221134};
Peripheral membrane protein; Nucleoplasmic side
{ECO:0000269|PubMed:11839768}. Nucleus, nuclear pore complex
{ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065,
ECO:0000269|PubMed:15229283}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:28221134}.
Note=Localized to the nucleoplasmic side of the nuclear pore
complex (NPC), at or near the nucleoplasmic basket
(PubMed:11839768). Dissociates from the dissasembled NPC structure
early during prophase of mitosis (PubMed:12802065). Colocalized
with NUP153 and TPR to the nuclear basket of NPC
(PubMed:11839768). Colocalized with DHX9 in diffuse and discrete
intranuclear foci (GLFG-body) (PubMed:11839768, PubMed:28221134).
Remains localized to the nuclear membrane after poliovirus (PV)
infection (PubMed:11106761). {ECO:0000269|PubMed:11106761,
ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:12802065,
ECO:0000269|PubMed:28221134}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Nup98-Nup96 precursor;
IsoId=P52948-1; Sequence=Displayed;
Name=2; Synonyms=Nup98-Nup96 precursor splice variant 1;
IsoId=P52948-2; Sequence=VSP_003619, VSP_007944;
Name=3; Synonyms=Nup98-specific 1;
IsoId=P52948-3; Sequence=VSP_007942, VSP_007943;
Name=4;
IsoId=P52948-4; Sequence=VSP_003619, VSP_007942, VSP_007943;
Name=5; Synonyms=Nup196, ADIR2;
IsoId=P52948-5; Sequence=VSP_003619;
Name=6;
IsoId=P52948-6; Sequence=VSP_038328;
-!- DOMAIN: Contains G-L-F-G repeats. The FG repeat domains in Nup98
have a direct role in the transport.
-!- PTM: Isoform 1 to isoform 4 are autoproteolytically cleaved to
yield Nup98 and Nup96 or Nup98 only, respectively
(PubMed:10087256, PubMed:20407419, PubMed:12191480,
PubMed:18287282). Cleaved Nup98 is necessary for the targeting of
Nup98 to the nuclear pore and the interaction with Nup96
(PubMed:20407419, PubMed:12191480). {ECO:0000269|PubMed:10087256,
ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282,
ECO:0000269|PubMed:20407419}.
-!- PTM: Proteolytically degraded after poliovirus (PV) infection;
degradation is partial and NCP- and TPR-binding domains withstand
degradation.
-!- DISEASE: Note=A chromosomal aberration involving NUP98 is found in
a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15)
with HOXA9. Translocation t(11;17)(p15;p13) with PHF23.
{ECO:0000269|PubMed:16028218}.
-!- DISEASE: Note=A chromosomal aberration involving NUP98 is found in
childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5)
with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1.
{ECO:0000269|PubMed:16028218}.
-!- DISEASE: Note=A chromosomal aberration involving NUP98 is found in
a form of therapy-related myelodysplastic syndrome. Translocation
t(11;20)(p15;q11) with TOP1. {ECO:0000269|PubMed:16028218}.
-!- DISEASE: Note=A chromosomal aberration involving NUP98 is found in
a form of T-cell acute lymphoblastic leukemia (T-ALL).
Translocation t(3;11)(q12.2;p15.4) with LNP1.
{ECO:0000269|PubMed:16028218}.
-!- DISEASE: Note=A chromosomal aberration involving NUP98 is
associated with pediatric acute myeloid leukemia (AML) with
intermediate characteristics between M2-M3 French-American-British
(FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF.
The chimeric transcript is an in-frame fusion of NUP98 exon 8 to
PSIP1/LEDGF exon 4. {ECO:0000269|PubMed:16028218}.
-!- DISEASE: Note=A chromosomal aberration involving NUP98 has been
identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5)
with CCDC28A. The chimeric transcript is an in-frame fusion of
NUP98 exon 13 to CCDC28A exon 2. Ectopic expression of NUP98-
CCDC28A in mouse promotes the proliferative capacity and self-
renewal potential of hematopoietic progenitors and rapidly induced
fatal myeloproliferative neoplasms and defects in the
differentiation of the erythro-megakaryocytic lineage.
{ECO:0000269|PubMed:16028218}.
-!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD22395.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
Sequence=AAD22396.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
Sequence=AAF19342.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAF19342.1; Type=Frameshift; Positions=1551; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NUPID98.html";
-----------------------------------------------------------------------
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EMBL; U41815; AAC50366.1; -; mRNA.
EMBL; AB040538; BAB18537.1; -; mRNA.
EMBL; AF071076; AAD22395.1; ALT_SEQ; mRNA.
EMBL; AF071077; AAD22396.1; ALT_SEQ; mRNA.
EMBL; AF231130; AAL56659.1; -; mRNA.
EMBL; AC060812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC041136; AAH41136.1; -; mRNA.
EMBL; BC012906; AAH12906.2; -; mRNA.
EMBL; AF116074; AAF19342.1; ALT_SEQ; mRNA.
EMBL; BT007349; AAP36013.1; -; mRNA.
EMBL; AL133601; CAB63736.1; -; mRNA.
EMBL; AL137613; CAB70842.1; -; mRNA.
CCDS; CCDS31347.1; -. [P52948-2]
CCDS; CCDS41605.1; -. [P52948-3]
CCDS; CCDS41606.1; -. [P52948-4]
CCDS; CCDS7746.1; -. [P52948-5]
PIR; T43443; T43443.
RefSeq; NP_005378.4; NM_005387.6. [P52948-3]
RefSeq; NP_057404.2; NM_016320.4. [P52948-5]
RefSeq; NP_624357.1; NM_139131.4. [P52948-4]
RefSeq; NP_624358.2; NM_139132.3. [P52948-2]
UniGene; Hs.524750; -.
PDB; 1KO6; X-ray; 3.00 A; A/C=695-880, B/D=881-941.
PDB; 2Q5X; X-ray; 1.90 A; A=733-887.
PDB; 2Q5Y; X-ray; 2.30 A; A/C=729-880.
PDB; 3MMY; X-ray; 1.65 A; B/D/F/H=158-213.
PDB; 4OWR; X-ray; 3.15 A; B=157-213.
PDB; 5A9Q; EM; 23.00 A; 5/E/N/W=881-1817.
PDBsum; 1KO6; -.
PDBsum; 2Q5X; -.
PDBsum; 2Q5Y; -.
PDBsum; 3MMY; -.
PDBsum; 4OWR; -.
PDBsum; 5A9Q; -.
ProteinModelPortal; P52948; -.
SMR; P52948; -.
BioGrid; 110982; 92.
CORUM; P52948; -.
DIP; DIP-32484N; -.
IntAct; P52948; 48.
MINT; MINT-121544; -.
STRING; 9606.ENSP00000316032; -.
MEROPS; S59.001; -.
iPTMnet; P52948; -.
PhosphoSitePlus; P52948; -.
BioMuta; NUP98; -.
DMDM; 308153660; -.
EPD; P52948; -.
MaxQB; P52948; -.
PaxDb; P52948; -.
PeptideAtlas; P52948; -.
PRIDE; P52948; -.
DNASU; 4928; -.
Ensembl; ENST00000324932; ENSP00000316032; ENSG00000110713. [P52948-5]
Ensembl; ENST00000355260; ENSP00000347404; ENSG00000110713. [P52948-2]
Ensembl; ENST00000359171; ENSP00000352091; ENSG00000110713. [P52948-1]
Ensembl; ENST00000397004; ENSP00000380199; ENSG00000110713. [P52948-4]
Ensembl; ENST00000397007; ENSP00000380202; ENSG00000110713. [P52948-3]
GeneID; 4928; -.
KEGG; hsa:4928; -.
UCSC; uc001lyh.3; human. [P52948-1]
CTD; 4928; -.
DisGeNET; 4928; -.
EuPathDB; HostDB:ENSG00000110713.15; -.
GeneCards; NUP98; -.
HGNC; HGNC:8068; NUP98.
HPA; HPA074810; -.
MIM; 601021; gene.
neXtProt; NX_P52948; -.
OpenTargets; ENSG00000110713; -.
PharmGKB; PA31856; -.
eggNOG; KOG0845; Eukaryota.
eggNOG; ENOG410XPV4; LUCA.
GeneTree; ENSGT00550000074799; -.
HOVERGEN; HBG052702; -.
InParanoid; P52948; -.
KO; K14297; -.
OMA; KQHCITA; -.
OrthoDB; EOG091G00HN; -.
PhylomeDB; P52948; -.
TreeFam; TF343335; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SIGNOR; P52948; -.
ChiTaRS; NUP98; human.
EvolutionaryTrace; P52948; -.
GeneWiki; NUP98; -.
GenomeRNAi; 4928; -.
PMAP-CutDB; P52948; -.
PRO; PR:P52948; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110713; -.
ExpressionAtlas; P52948; baseline and differential.
Genevisible; P52948; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IMP:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IMP:UniProtKB.
GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
GO; GO:0005487; F:nucleocytoplasmic transporter activity; IBA:GO_Central.
GO; GO:1990841; F:promoter-specific chromatin binding; IMP:UniProtKB.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IMP:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
GO; GO:0006999; P:nuclear pore organization; NAS:UniProtKB.
GO; GO:0006913; P:nucleocytoplasmic transport; TAS:UniProtKB.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0000973; P:posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0006110; P:regulation of glycolytic process; TAS:Reactome.
GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0034398; P:telomere tethering at nuclear periphery; IBA:GO_Central.
GO; GO:0006409; P:tRNA export from nucleus; TAS:Reactome.
GO; GO:0016032; P:viral process; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
Gene3D; 3.30.1610.10; -; 1.
InterPro; IPR021967; Nup96.
InterPro; IPR007230; Peptidase_S59.
Pfam; PF04096; Nucleoporin2; 1.
Pfam; PF12110; Nup96; 1.
SUPFAM; SSF82215; SSF82215; 1.
PROSITE; PS51434; NUP_C; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Autocatalytic cleavage; Chromosomal rearrangement; Complete proteome;
Direct protein sequencing; Host-virus interaction; Hydrolase;
Isopeptide bond; Membrane; mRNA transport; Nuclear pore complex;
Nucleus; Phosphoprotein; Polymorphism; Protease; Protein transport;
Reference proteome; Repeat; Serine protease; Translocation; Transport;
Ubl conjugation.
CHAIN 1 880 Nuclear pore complex protein Nup98.
/FTId=PRO_0000019929.
CHAIN 881 1817 Nuclear pore complex protein Nup96.
/FTId=PRO_0000019930.
DOMAIN 738 880 Peptidase S59. {ECO:0000255|PROSITE-
ProRule:PRU00765}.
REGION 1 156 FG repeats 1.
REGION 157 213 GLEBS; interaction with RAE1.
{ECO:0000269|PubMed:10209021}.
REGION 214 480 FG repeats 2.
COMPBIAS 7 480 Gly/Thr-rich.
COMPBIAS 890 894 Poly-Glu.
ACT_SITE 881 881 Nucleophile.
{ECO:0000269|PubMed:12191480,
ECO:0000269|PubMed:18287282}.
SITE 531 532 Breakpoint for translocation to form
NUP98-CCDC28A.
SITE 531 532 Breakpoint for translocation to form
NUP98-PHF23 oncogene.
SITE 880 881 Cleavage; by autolysis.
{ECO:0000269|PubMed:10087256,
ECO:0000269|PubMed:12191480,
ECO:0000269|PubMed:18287282}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 603 603 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 618 618 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 625 625 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFD9}.
MOD_RES 670 670 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 673 673 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 681 681 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 839 839 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 888 888 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 897 897 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1000 1000 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1023 1023 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1043 1043 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1060 1060 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFD9}.
MOD_RES 1070 1070 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1329 1329 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFD9}.
MOD_RES 1772 1772 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6PFD9}.
CROSSLNK 563 563 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 603 603 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 665 665 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 393 409 Missing (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:10087256,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:8563754,
ECO:0000303|Ref.4, ECO:0000303|Ref.7,
ECO:0000303|Ref.8}.
/FTId=VSP_003619.
VAR_SEQ 932 937 SQSPEV -> VEKKGQ (in isoform 3 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8563754,
ECO:0000303|Ref.2}.
/FTId=VSP_007942.
VAR_SEQ 938 1817 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8563754,
ECO:0000303|Ref.2}.
/FTId=VSP_007943.
VAR_SEQ 1085 1188 WSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPREKSVT
YGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLNGSHEL
ENHQIADSMEFGFLPNPVAVKP -> C (in isoform
6). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_038328.
VAR_SEQ 1502 1576 RHYDLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSA
QCEGVLQASYAGQLESEGLWEWAIFVLLHIDNSG -> S
(in isoform 2).
{ECO:0000303|PubMed:10087256}.
/FTId=VSP_007944.
VARIANT 1669 1669 G -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035859.
MUTAGEN 808 808 K->A: No effect on autoprocessing. Severe
loss of autoprocessing; when associated
with A-879.
{ECO:0000269|PubMed:12191480}.
MUTAGEN 816 816 N->A: Slight reduction in autoprocessing.
{ECO:0000269|PubMed:12191480}.
MUTAGEN 879 879 H->A,Q: Moderate reduction in
autoprocessing.
{ECO:0000269|PubMed:12191480}.
MUTAGEN 880 883 FSKY->SSKR: Loss of processing. Loss of
nuclear membrane localization.
{ECO:0000269|PubMed:10087256}.
MUTAGEN 881 881 S->A: Loss of autoprocessing. Loss of
nuclear membrane localization.
{ECO:0000269|PubMed:12191480,
ECO:0000269|PubMed:18287282}.
MUTAGEN 882 882 K->A: No effect in autoprocessing.
{ECO:0000269|PubMed:12191480}.
CONFLICT 318 318 L -> S (in Ref. 6; AAH41136).
{ECO:0000305}.
CONFLICT 376 376 S -> G (in Ref. 6; AAH41136).
{ECO:0000305}.
CONFLICT 756 757 EK -> VF (in Ref. 3; AAD22395/AAD22396).
{ECO:0000305}.
CONFLICT 1281 1281 G -> A (in Ref. 3; AAD22395/AAD22396 and
4; AAL56659). {ECO:0000305}.
CONFLICT 1534 1536 ALN -> DLK (in Ref. 3; AAD22395).
{ECO:0000305}.
CONFLICT 1594 1594 E -> D (in Ref. 7; AAF19342).
{ECO:0000305}.
CONFLICT 1598 1598 S -> T (in Ref. 4; AAL56659).
{ECO:0000305}.
CONFLICT 1639 1639 K -> N (in Ref. 7; AAF19342).
{ECO:0000305}.
CONFLICT 1680 1680 S -> T (in Ref. 7; AAF19342).
{ECO:0000305}.
STRAND 168 172 {ECO:0000244|PDB:3MMY}.
STRAND 181 186 {ECO:0000244|PDB:3MMY}.
HELIX 189 191 {ECO:0000244|PDB:3MMY}.
TURN 193 197 {ECO:0000244|PDB:3MMY}.
HELIX 200 209 {ECO:0000244|PDB:3MMY}.
STRAND 741 745 {ECO:0000244|PDB:2Q5X}.
HELIX 747 753 {ECO:0000244|PDB:2Q5X}.
STRAND 761 769 {ECO:0000244|PDB:2Q5X}.
TURN 770 772 {ECO:0000244|PDB:2Q5X}.
STRAND 773 782 {ECO:0000244|PDB:2Q5X}.
HELIX 788 791 {ECO:0000244|PDB:2Q5X}.
STRAND 792 795 {ECO:0000244|PDB:2Q5X}.
STRAND 798 801 {ECO:0000244|PDB:2Q5X}.
HELIX 805 807 {ECO:0000244|PDB:2Q5Y}.
STRAND 819 823 {ECO:0000244|PDB:2Q5X}.
TURN 831 833 {ECO:0000244|PDB:2Q5X}.
HELIX 840 845 {ECO:0000244|PDB:2Q5X}.
HELIX 848 858 {ECO:0000244|PDB:2Q5X}.
STRAND 862 867 {ECO:0000244|PDB:2Q5X}.
TURN 868 871 {ECO:0000244|PDB:2Q5X}.
STRAND 872 879 {ECO:0000244|PDB:2Q5X}.
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


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