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

 NUP98_DROME             Reviewed;        1960 AA.
Q9VCH5; B8A421; Q6NP55;
28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 3.
10-OCT-2018, entry version 146.
RecName: Full=Nuclear pore complex protein Nup98-Nup96 {ECO:0000312|FlyBase:FBgn0039120};
EC=3.4.21.- {ECO:0000250|UniProtKB:P52948};
Contains:
RecName: Full=Nuclear pore complex protein Nup98 {ECO:0000303|PubMed:21949861};
AltName: Full=Nucleoporin Nup98 {ECO:0000303|PubMed:25310983};
Short=Nup98 {ECO:0000303|PubMed:25310983};
Contains:
RecName: Full=Nuclear pore complex protein Nup96 {ECO:0000303|PubMed:25310983};
AltName: Full=Nucleoporin Nup96 {ECO:0000303|PubMed:25310983};
Short=Nup96 {ECO:0000303|PubMed:25310983};
Flags: Precursor;
Name=Nup98-96 {ECO:0000312|FlyBase:FBgn0039120};
Synonyms=Nup145 {ECO:0000303|PubMed:20547758},
Nup98 {ECO:0000312|FlyBase:FBgn0039120};
ORFNames=CG10198 {ECO:0000312|FlyBase:FBgn0039120};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
[1] {ECO:0000312|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000312|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000312|EMBL:AAR82742.1, ECO:0000312|EMBL:ACL68760.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND NUCLEOTIDE SEQUENCE [MRNA]
OF 770-1960 (ISOFORM A).
STRAIN=Berkeley {ECO:0000312|EMBL:AAR82742.1,
ECO:0000312|EMBL:ACL68760.1};
TISSUE=Embryo {ECO:0000312|EMBL:AAR82742.1,
ECO:0000312|EMBL:ACL68760.1};
Stapleton M., Brokstein P., Booth B., Hong L., Agbayani A.,
Carlson J., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D.,
Frise E., George R., Gonzalez M., Guarin H., Kronmiller B., Li P.,
Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V.,
Park S., Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
Rubin G.M., Celniker S.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20144760; DOI=10.1016/j.cell.2010.01.011;
Kalverda B., Pickersgill H., Shloma V.V., Fornerod M.;
"Nucleoporins directly stimulate expression of developmental and cell-
cycle genes inside the nucleoplasm.";
Cell 140:360-371(2010).
[5] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=20144761; DOI=10.1016/j.cell.2009.12.054;
Capelson M., Liang Y., Schulte R., Mair W., Wagner U., Hetzer M.W.;
"Chromatin-bound nuclear pore components regulate gene expression in
higher eukaryotes.";
Cell 140:372-383(2010).
[6] {ECO:0000305}
FUNCTION.
PubMed=20547758; DOI=10.1128/MCB.00124-10;
Chen X., Xu L.;
"Specific nucleoporin requirement for Smad nuclear translocation.";
Mol. Cell. Biol. 30:4022-4034(2010).
[7] {ECO:0000305}
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RAE1, AND TISSUE
SPECIFICITY.
PubMed=21874015; DOI=10.1038/nn.2922;
Tian X., Li J., Valakh V., DiAntonio A., Wu C.;
"Drosophila Rae1 controls the abundance of the ubiquitin ligase
Highwire in post-mitotic neurons.";
Nat. Neurosci. 14:1267-1275(2011).
[8] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21949861; DOI=10.1371/journal.pone.0025087;
Parrott B.B., Chiang Y., Hudson A., Sarkar A., Guichet A., Schulz C.;
"Nucleoporin98-96 function is required for transit amplification
divisions in the germ line of Drosophila melanogaster.";
PLoS ONE 6:E25087-E25087(2011).
[9] {ECO:0000305}
FUNCTION, INTERACTION WITH TRX; WDS; MBD-R2; PZG AND CHRO, SUBCELLULAR
LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=25310983; DOI=10.1016/j.celrep.2014.09.002;
Pascual-Garcia P., Jeong J., Capelson M.;
"Nucleoporin Nup98 associates with Trx/MLL and NSL histone-modifying
complexes and regulates Hox gene expression.";
Cell Rep. 9:433-442(2014).
[10] {ECO:0000305}
FUNCTION.
PubMed=25201876; DOI=10.7554/eLife.03626;
Mondal B.C., Shim J., Evans C.J., Banerjee U.;
"Pvr expression regulators in equilibrium signal control and
maintenance of Drosophila blood progenitors.";
Elife 3:E03626-E03626(2014).
[11] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=25197089; DOI=10.1073/pnas.1410087111;
Panda D., Pascual-Garcia P., Dunagin M., Tudor M., Hopkins K.C.,
Xu J., Gold B., Raj A., Capelson M., Cherry S.;
"Nup98 promotes antiviral gene expression to restrict RNA viral
infection in Drosophila.";
Proc. Natl. Acad. Sci. U.S.A. 111:E3890-E3899(2014).
[12] {ECO:0000305}
FUNCTION.
PubMed=25852164; DOI=10.1128/mBio.02509-14;
Panda D., Gold B., Tartell M.A., Rausch K., Casas-Tinto S., Cherry S.;
"The transcription factor FoxK participates with Nup98 to regulate
antiviral gene expression.";
MBio 6:E02509-E02514(2015).
[13] {ECO:0000305}
FUNCTION, AND INTERACTION WITH RAE1.
PubMed=28554770; DOI=10.1016/j.bbamcr.2017.05.020;
Kristo I., Bajusz C., Borsos B.N., Pankotai T., Dopie J.,
Jankovics F., Vartiainen M.K., Erdelyi M., Vilmos P.;
"The actin binding cytoskeletal protein Moesin is involved in nuclear
mRNA export.";
Biochim. Biophys. Acta 1864:1589-1604(2017).
[14] {ECO:0000305}
FUNCTION, INTERACTION WITH MTOR; ECR; CP190; TRL; SU(HW) AND CTCF,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=28366641; DOI=10.1016/j.molcel.2017.02.020;
Pascual-Garcia P., Debo B., Aleman J.R., Talamas J.A., Lan Y.,
Nguyen N.H., Won K.J., Capelson M.;
"Metazoan nuclear pores provide a scaffold for poised genes and
mediate induced enhancer-promoter contacts.";
Mol. Cell 66:63-76(2017).
-!- FUNCTION: Part of the nuclear pore complex (NPC)
(PubMed:25197089). Required for MAD import as part of the Nup107-
160 complex and required for nuclear export of Moe probably via
its association with Rae1 (PubMed:20547758, PubMed:28554770).
Plays a role in nuclear mRNA export (PubMed:28554770). Promotes
cell antiviral response by upregulating FoxK-dependent antiviral
gene transcription (PubMed:25197089, PubMed:25852164). In germline
stem cells, involved in their maintenance and division together
with the TGF-Beta and EGFR signaling pathways (PubMed:21949861).
In larval lymph glands, has a role in the maintenance of
hematopoiesis by regulating Pvr expression (PubMed:25201876).
{ECO:0000269|PubMed:20547758, ECO:0000269|PubMed:21949861,
ECO:0000269|PubMed:25197089, ECO:0000269|PubMed:25201876,
ECO:0000269|PubMed:25852164, ECO:0000269|PubMed:28554770}.
-!- FUNCTION: Nuclear pore complex protein Nup98: Part of the nuclear
pore complex (NPC) (PubMed:25310983). In the nucleoplasm, binds to
transcriptionally active chromatin with a preference for
regulatory regions; co-localizes with RNA polymerase II in a RNA-
independent manner and before transition into transcription
elongation (PubMed:20144760, PubMed:20144761, PubMed:28366641).
Plays a role in the transcriptional memory process by stabilizing
enhancer-promoter loops and by mediating anchoring of chromatin to
the nuclear pore complex region (PubMed:28366641). During larval
development, interacts with trx and MBD-R2 and regulates
transcription of developmental genes including ecdysone-responsive
genes such as Eip74 and E23 (PubMed:20144761, PubMed:25310983,
PubMed:28366641). {ECO:0000269|PubMed:20144760,
ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:25310983,
ECO:0000269|PubMed:28366641}.
-!- FUNCTION: Nuclear pore complex protein Nup96: Part of the nuclear
pore complex (NPC). {ECO:0000269|PubMed:25310983}.
-!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:25310983).
Interacts with Rae1 (PubMed:21874015, PubMed:28554770). Nuclear
pore complex protein Nup98: Interacts with pzg and Chro
(PubMed:25310983). Interacts with MBD-R2; the interaction allows
Nup98 recruitment to chromatin (PubMed:25310983). Interacts with
Trx (PubMed:25310983). Interacts with Wds (PubMed:25310983).
Interacts with Mtor and Cp190 (PubMed:28366641). Upon ecdysone
stimulation, interacts with EcR, CTCF, su(Hw) and Trl
(PubMed:28366641). {ECO:0000269|PubMed:21874015,
ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:28366641,
ECO:0000269|PubMed:28554770}.
-!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:20144761}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:20144760}. Nucleus
membrane {ECO:0000269|PubMed:20144761,
ECO:0000269|PubMed:25197089}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P52948}; Nucleoplasmic side
{ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear pore complex
{ECO:0000269|PubMed:25310983}. Nucleus
{ECO:0000269|PubMed:28366641}. Note=Associates with
transcriptionally active chromatin. {ECO:0000269|PubMed:20144760,
ECO:0000269|PubMed:20144761, ECO:0000269|PubMed:28366641}.
-!- SUBCELLULAR LOCATION: Nuclear pore complex protein Nup98: Nucleus,
nuclear pore complex {ECO:0000269|PubMed:25310983}.
-!- SUBCELLULAR LOCATION: Nuclear pore complex protein Nup96: Nucleus,
nuclear pore complex {ECO:0000269|PubMed:25310983}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A {ECO:0000312|FlyBase:FBgn0039120};
IsoId=Q9VCH5-1; Sequence=Displayed;
Name=C {ECO:0000312|FlyBase:FBgn0039120};
IsoId=Q9VCH5-2; Sequence=VSP_059347, VSP_059348;
-!- TISSUE SPECIFICITY: Expressed in brain.
{ECO:0000269|PubMed:21874015}.
-!- DEVELOPMENTAL STAGE: Expressed during larval development
(PubMed:20144761). Expressed in brain in third instar larvae (at
protein level) (PubMed:28366641). {ECO:0000269|PubMed:20144761,
ECO:0000269|PubMed:28366641}.
-!- INDUCTION: Up-regulated upon Drosophila C virus (DCV) or Sindbis
virus (SINV) infection. {ECO:0000269|PubMed:25197089}.
-!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
karyopherins (importins, exportins) and form probably an affinity
gradient, guiding the transport proteins unidirectionally with
their cargo through the NPC. FG repeat regions are highly flexible
and lack ordered secondary structure. The overall conservation of
FG repeats regarding exact sequence, spacing, and repeat unit
length is limited. {ECO:0000305}.
-!- PTM: Isoform A and isoform C are autoproteolytically cleaved to
yield Nup98 and Nup96 or Nup98 only, respectively.
{ECO:0000250|UniProtKB:P52948}.
-!- DISRUPTION PHENOTYPE: Defective germline population maintenance
and differentiation when both Nup98 and Nup96 are disrupted
(PubMed:21949861). RNAi-mediated knockdown in the larval salivary
glands results in reduced transcription of developmental genes
Eip74EF and Eip75B and compromised transcriptional recovery after
heat shock (PubMed:20144761). RNAi-mediated knockdown in the larva
results in reduced expression of Hox genes such as Ubx and Antp
(PubMed:25310983). RNA-mediated knockdown in the adult fly
increases viral replication of Sindbis virus (SINV), vesicular
stomatitis virus (VSV) and Drosophila C virus (DCV)
(PubMed:25197089). {ECO:0000269|PubMed:20144761,
ECO:0000269|PubMed:21949861, ECO:0000269|PubMed:25197089,
ECO:0000269|PubMed:25310983}.
-!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
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EMBL; AE014297; AAF56190.3; -; Genomic_DNA.
EMBL; AE014297; AGB96265.1; -; Genomic_DNA.
EMBL; AE014297; AFH06584.1; -; Genomic_DNA.
EMBL; BT056313; ACL68760.1; -; mRNA.
EMBL; BT011076; AAR82742.1; -; mRNA.
RefSeq; NP_001247266.1; NM_001260337.1. [Q9VCH5-2]
RefSeq; NP_001262885.1; NM_001275956.1. [Q9VCH5-1]
RefSeq; NP_651187.2; NM_142930.3. [Q9VCH5-1]
UniGene; Dm.14811; -.
ProteinModelPortal; Q9VCH5; -.
SMR; Q9VCH5; -.
IntAct; Q9VCH5; 4.
MINT; Q9VCH5; -.
STRING; 7227.FBpp0083851; -.
MEROPS; S59.A04; -.
PaxDb; Q9VCH5; -.
PRIDE; Q9VCH5; -.
EnsemblMetazoa; FBtr0084460; FBpp0083851; FBgn0039120. [Q9VCH5-1]
EnsemblMetazoa; FBtr0304567; FBpp0293109; FBgn0039120. [Q9VCH5-2]
EnsemblMetazoa; FBtr0334894; FBpp0306915; FBgn0039120. [Q9VCH5-1]
GeneID; 42816; -.
KEGG; dme:Dmel_CG10198; -.
UCSC; CG10198-RA; d. melanogaster. [Q9VCH5-1]
CTD; 42816; -.
FlyBase; FBgn0039120; Nup98-96.
eggNOG; KOG0845; Eukaryota.
eggNOG; ENOG410XPV4; LUCA.
GeneTree; ENSGT00550000074799; -.
InParanoid; Q9VCH5; -.
KO; K14297; -.
OMA; TLQYQSI; -.
OrthoDB; EOG091G00HN; -.
PhylomeDB; Q9VCH5; -.
Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-DME-191859; snRNP Assembly.
Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
ChiTaRS; Mhc; fly.
GenomeRNAi; 42816; -.
PRO; PR:Q9VCH5; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0039120; Expressed in 29 organ(s), highest expression level in embryo.
ExpressionAtlas; Q9VCH5; baseline and differential.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0044613; C:nuclear pore central transport channel; ISS:FlyBase.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
GO; GO:0005704; C:polytene chromosome band; IDA:UniProtKB.
GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0017056; F:structural constituent of nuclear pore; ISS:FlyBase.
GO; GO:0071390; P:cellular response to ecdysone; IDA:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
GO; GO:0035080; P:heat shock-mediated polytene chromosome puffing; IDA:UniProtKB.
GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
GO; GO:0036098; P:male germ-line stem cell population maintenance; IGI:UniProtKB.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0043922; P:negative regulation by host of viral transcription; IMP:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IGI:FlyBase.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; 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; IMP:FlyBase.
GO; GO:0035075; P:response to ecdysone; IDA:UniProtKB.
GO; GO:0006405; P:RNA export from nucleus; IMP:UniProtKB.
GO; GO:0034398; P:telomere tethering at nuclear periphery; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; IMP:UniProtKB.
Gene3D; 3.30.1610.10; -; 1.
InterPro; IPR025574; Nucleoporin_FG_rpt.
InterPro; IPR037665; Nucleoporin_S59-like.
InterPro; IPR021967; Nup96.
InterPro; IPR037637; NUP98-NUP96.
InterPro; IPR007230; Peptidase_S59.
InterPro; IPR036903; Peptidase_S59_sf.
PANTHER; PTHR23198; PTHR23198; 2.
PANTHER; PTHR23198:SF6; PTHR23198:SF6; 2.
Pfam; PF04096; Nucleoporin2; 1.
Pfam; PF13634; Nucleoporin_FG; 5.
Pfam; PF12110; Nup96; 1.
SUPFAM; SSF82215; SSF82215; 1.
PROSITE; PS51434; NUP_C; 1.
1: Evidence at protein level;
Alternative splicing; Autocatalytic cleavage; Chromosome;
Complete proteome; Hydrolase; Membrane; mRNA transport;
Nuclear pore complex; Nucleus; Protease; Protein transport;
Reference proteome; Repeat; Serine protease; Transcription;
Transcription regulation; Translocation; Transport.
CHAIN 1 1028 Nuclear pore complex protein Nup98.
{ECO:0000305}.
/FTId=PRO_0000443442.
CHAIN 1029 1960 Nuclear pore complex protein Nup96.
{ECO:0000305}.
/FTId=PRO_0000443443.
REPEAT 2 3 1. {ECO:0000305}.
REPEAT 9 10 2. {ECO:0000305}.
REPEAT 18 19 3. {ECO:0000305}.
REPEAT 30 31 4. {ECO:0000305}.
REPEAT 35 36 5. {ECO:0000305}.
REPEAT 43 44 6. {ECO:0000305}.
REPEAT 59 60 7. {ECO:0000305}.
REPEAT 73 74 8. {ECO:0000305}.
REPEAT 81 82 9. {ECO:0000305}.
REPEAT 92 93 10. {ECO:0000305}.
REPEAT 105 106 11. {ECO:0000305}.
REPEAT 117 118 12. {ECO:0000305}.
REPEAT 125 126 13. {ECO:0000305}.
REPEAT 135 136 14. {ECO:0000305}.
REPEAT 148 149 15. {ECO:0000305}.
REPEAT 160 161 16. {ECO:0000305}.
REPEAT 163 164 17. {ECO:0000305}.
REPEAT 174 175 18. {ECO:0000305}.
REPEAT 264 265 19. {ECO:0000305}.
REPEAT 266 267 20. {ECO:0000305}.
REPEAT 282 283 21. {ECO:0000305}.
REPEAT 293 294 22. {ECO:0000305}.
REPEAT 304 305 23. {ECO:0000305}.
REPEAT 309 310 24. {ECO:0000305}.
REPEAT 319 320 25. {ECO:0000305}.
REPEAT 333 334 26. {ECO:0000305}.
REPEAT 352 353 27. {ECO:0000305}.
REPEAT 358 359 28. {ECO:0000305}.
REPEAT 365 366 29. {ECO:0000305}.
REPEAT 377 378 30. {ECO:0000305}.
REPEAT 384 385 31. {ECO:0000305}.
REPEAT 387 388 32. {ECO:0000305}.
REPEAT 400 401 33. {ECO:0000305}.
REPEAT 413 414 34. {ECO:0000305}.
REPEAT 426 427 35. {ECO:0000305}.
REPEAT 428 429 36. {ECO:0000305}.
REPEAT 441 442 37. {ECO:0000305}.
REPEAT 454 455 38. {ECO:0000305}.
REPEAT 467 468 39. {ECO:0000305}.
REPEAT 493 494 40. {ECO:0000305}.
REPEAT 496 497 41. {ECO:0000305}.
REPEAT 516 517 42. {ECO:0000305}.
REPEAT 527 528 43. {ECO:0000305}.
REPEAT 546 547 44. {ECO:0000305}.
REPEAT 553 554 45. {ECO:0000305}.
REPEAT 565 566 46. {ECO:0000305}.
DOMAIN 886 1028 Peptidase S59. {ECO:0000255|PROSITE-
ProRule:PRU00765}.
REGION 2 566 46 X 2 AA repeats of F-G. {ECO:0000305}.
COMPBIAS 359 579 Gly-rich. {ECO:0000255|PROSITE-
ProRule:PRU00008}.
ACT_SITE 1029 1029 Nucleophile.
{ECO:0000250|UniProtKB:P52948}.
SITE 1028 1029 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P52948}.
VAR_SEQ 1174 1179 ETTGRL -> GRWIIS (in isoform C).
/FTId=VSP_059347.
VAR_SEQ 1180 1960 Missing (in isoform C).
/FTId=VSP_059348.
CONFLICT 860 860 Q -> R (in Ref. 3; AAR82742).
{ECO:0000305}.
SEQUENCE 1960 AA; 210139 MW; 00A94D1CCC25CBFC CRC64;
MFGGAKPSFG ATPAATSFGG FSGTTTTTPF GQSAFGKPAA PAFGNTSTFA AQPAQQSLFG
AAATPAQPAG GLFGANTSTG FGSTATAQPT AFGAFSQPQQ TSNIFGSTQT AASTSLFGQS
TLPAFGAAKP TMTAFGQTAA AQPTGSLFGQ PAAATSTTGF GGFGTSAPTT TNVFGSGTAS
AFAQPQATAV GASGVNTGTA VAKYQPTIGT DTLMKSGQAN SVNTKQHCIT AMKEFEGKSL
EELRLEDYMC GRKGPQAGNA PGAFGFGAQV TQPAQPASGG LFGSTAQPST GLFGQTVTEN
KSMFGTTAFG QQPATNNAFG AATQQNNFLQ KPFGATTTTP FAAPAADASN PFGAKPAFGQ
GGSLFGQAPA TSAAPAFGQT NTGFGGFGTT AGATQQSTLF GATPAADPNK SAFGLGTAAS
AATTGFGFGA PATSTAGGGL FGNKPATSFA APTFGATSTA STPFSNFGLN TSTAATGGGL
FNSGLNKPAT SGFGGFGATS AAPLNFNAGN TGGSLFGNTA KPGGGLFGGG TTTLGGTGAA
PTGGLFGGGT TSFGGVGGSL GGGGFGMGTN NSLTGGIMGA QPTLGIMTPS HQPIHQQILA
RVTSPYGDSP IFKDLKLSSE ADATRATNPA AQQAVLDLTS NQYKISTSNN PAPMKVKALG
STLNRKSLFD GLEEFDASVE GFNLKPSAKR LVIKPKVKSV EGGNPSSSIG SAPNTPQSRP
KGATPNKERE SFSGAIPSEP LPPAGNSPGA TNGRESQDNG RRESWLHPNN LEKVRQHNIQ
TGMDQGSPHN STLNELVPRK PLDTYRPSST VRLSVSTIPE NPFEDQSSTI ARRETFTSQQ
ANESVLSNRS NEAEDSAANQ SRLAIEAAAA EAADDESHPT GIVLRRVGYY TIPSLDDLRS
YLAEDGSCVV PNFTVGREGY GNVFFGKEMD VAGLNLDEIV HFRNKEIIIY PDDENKPPIG
QGLNRDAQVT LDQVWPLDKT KHEAIKDPQR LLEMDWEGKL RRVCDKNDTR FIEYRPETGS
WVFRVKHFSK YGLGDSDEED ELPTDPKKAK IATLEAQQRA NAEKMTLNSL RQAQKISEDA
ARNLDPKALV AGVASGFRPM DDTAEFLLMD KTQFFQAGGN SDFSMFDPPR QRPTITSPTA
VLAQEMVGNE AHKMQLMKSS FFVEDNAPED EPMETTGRLL RHRKFFNVEP LVWKDGASES
SSQYDFEHPS PALPISSSVS EASLMCDAHY EETSSMATGS IVAAVKETKF EMPVTKAFKF
VCKPKVAPIK LRATTVPLPR SIAYEMRDNW IADLGFYKGR SFKLSFGPQN SLVLPSTYNN
MQNLKEFTGP SLPVSMVFAP RSATDLSPSV MQLVEFNMVK GNEGFRESII PHLEVQLNDC
LSVNVEGSEC PCIHPDSGTK LVSKHFSESL KQRNAGLKED YSVSVWSLLF ALWGDHDELV
DLEKNSHYMV MCRRNLLSEW LENTLLGKDL LSKKVSTHSY LEHMLDLLSC HRVNEACELA
FSYDDANLAL VLSQLSSGAV FRLLMEEQLF AWQQSKSDKY IDLERLKMYM LAAGAPMMQS
SHGAINLLEN KNWLTALALQ LWYFTAPTSS ITDALNAYND AFQAEECYAE PPKPSYRDAP
TDTKKPVYDL RYHLLQLHSK RMHSLEETLN PITHTADAMD FRLSWLLLQT LRALGYRHCS
PLTEARLSVD FASQLENEGL WQWGIFVLLH IKQQTQRERA VQQMLQRNVS VSAKVALYAE
ERFIVEELGI PMSWVDYAKA VKAGASGKHH LQAKYLLKAK HFATAHDVIF QHIAPDAIIN
GKMKYLHSLL IQFEDTEGSS IRVPNWANQG QIFLDFIDIS AKFKQIRSVT NIADINARWE
NLKPQLSELC SRISLLPCPT SKHRLCQSEI SQSLSCLVHG MCIVCPEMES STVLKVALER
LPLPQEFASK ELRIWLEELL DKIQNEPPFS ERQQPTMMEI


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