NUP98_CAEEL
ID NUP98_CAEEL Reviewed; 1678 AA.
AC G5EEH9; D1MN48; H2L014;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Nuclear pore complex protein Nup98-Nup96 {ECO:0000250|UniProtKB:P52948};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:P52948};
DE Contains:
DE RecName: Full=Nuclear pore complex protein Nup98 {ECO:0000250|UniProtKB:P52948};
DE AltName: Full=98 kDa nucleoporin {ECO:0000250|UniProtKB:P52948};
DE AltName: Full=Nucleoporin Nup98 {ECO:0000250|UniProtKB:P52948};
DE Short=CeNup98 {ECO:0000303|PubMed:20335358};
DE Contains:
DE RecName: Full=Nuclear pore complex protein Nup96 {ECO:0000250|UniProtKB:P52948};
DE AltName: Full=96 kDa nucleoporin {ECO:0000250|UniProtKB:P52948};
DE AltName: Full=Nucleoporin Nup96 {ECO:0000250|UniProtKB:P52948};
DE Short=CeNup96 {ECO:0000303|PubMed:20335358};
DE Flags: Precursor;
GN Name=npp-10 {ECO:0000312|WormBase:ZK328.5b}; ORFNames=ZK328.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ADF47155.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION,
RP PROTEOLYTIC CLEAVAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:ADF47155.1};
RX PubMed=20335358; DOI=10.1242/dev.047654;
RA Voronina E., Seydoux G.;
RT "The C. elegans homolog of nucleoporin Nup98 is required for the integrity
RT and function of germline P granules.";
RL Development 137:1441-1450(2010).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CCD70954.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD70955.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12937276; DOI=10.1091/mbc.e03-04-0237;
RA Galy V., Mattaj I.W., Askjaer P.;
RT "Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit
RT of nuclear pore complex size exclusion in vivo.";
RL Mol. Biol. Cell 14:5104-5115(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16950114; DOI=10.1016/j.cub.2006.06.067;
RA Galy V., Askjaer P., Franz C., Lopez-Iglesias C., Mattaj I.W.;
RT "MEL-28, a novel nuclear-envelope and kinetochore protein essential for
RT zygotic nuclear-envelope assembly in C. elegans.";
RL Curr. Biol. 16:1748-1756(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22238360; DOI=10.1091/mbc.e11-11-0927;
RA Rodenas E., Gonzalez-Aguilera C., Ayuso C., Askjaer P.;
RT "Dissection of the NUP107 nuclear pore subcomplex reveals a novel
RT interaction with spindle assembly checkpoint protein MAD1 in Caenorhabditis
RT elegans.";
RL Mol. Biol. Cell 23:930-944(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=28122936; DOI=10.1242/jcs.196709;
RA Ferreira J., Stear J.H., Saumweber H.;
RT "Nucleoporins NPP-10, NPP-13 and NPP-20 are required for HCP-4 nuclear
RT import to establish correct centromere assembly.";
RL J. Cell Sci. 130:963-974(2017).
CC -!- FUNCTION: Nup98 and Nup96 play a role in the bidirectional transport
CC across the nucleoporin complex (NPC) (PubMed:20335358,
CC PubMed:28122936). Required for the nuclear import of hcp-4 during
CC mitotic prophase, this step is essential for centrosome assembly and
CC resolution (PubMed:28122936). Regulates nucleoporin npp-5 localization
CC to the nuclear membrane during interphase and to kinetochores during
CC metaphase (PubMed:22238360). Has a role in P granule integrity; may
CC promote the 'liquid phase' of P granules by increasing the number of
CC interacting RNA-protein complexes (PubMed:20335358). Binds nos-2 mRNA,
CC probably indirectly, and promotes its accumulation in P granules
CC (PubMed:20335358). {ECO:0000269|PubMed:20335358,
CC ECO:0000269|PubMed:22238360, ECO:0000269|PubMed:28122936}.
CC -!- SUBUNIT: Part of the NPC. {ECO:0000250|UniProtKB:P52948}.
CC -!- SUBCELLULAR LOCATION: [Nuclear pore complex protein Nup98]: Cytoplasmic
CC granule {ECO:0000269|PubMed:20335358}. Nucleus membrane
CC {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:20335358,
CC ECO:0000269|PubMed:28122936}; Peripheral membrane protein
CC {ECO:0000269|PubMed:20335358}; Nucleoplasmic side
CC {ECO:0000269|PubMed:20335358}. Note=P granule localization dependent on
CC nucleoporins npp-7, npp-8 and npp-9 which are involved in P granule
CC integrity. {ECO:0000269|PubMed:20335358}.
CC -!- SUBCELLULAR LOCATION: [Nuclear pore complex protein Nup96]: Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:20335358}. Nucleus envelope
CC {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:20335358,
CC ECO:0000269|PubMed:22238360}. Chromosome {ECO:0000269|PubMed:16950114}.
CC Note=Requires mel-28 for chromatin association during early steps of
CC nuclear pore complex assembly. {ECO:0000269|PubMed:16950114}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000269|PubMed:20335358};
CC IsoId=G5EEH9-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=G5EEH9-2; Sequence=VSP_043739, VSP_043740;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=G5EEH9-3; Sequence=VSP_043738, VSP_043739, VSP_043740;
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level).
CC {ECO:0000269|PubMed:12937276, ECO:0000269|PubMed:22238360}.
CC -!- PTM: The Nup98 and Nup96 chains are autoproteolytically processed from
CC a single precursor protein. {ECO:0000269|PubMed:20335358}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC lethality (PubMed:12937276, PubMed:28122936). Two-cell embryos appear
CC to lack nuclei and pronuclei (PubMed:12937276). Also causes severe
CC defects in mitosis (PubMed:22238360, PubMed:28122936). Chromosome
CC condensation is severely impaired during prophase (PubMed:28122936).
CC Centrosome assembly during prophase and prometaphase and their
CC subsequent resolution are impaired which results from impaired nuclear
CC import of hcp-4 (PubMed:28122936). Impaired sister chromatin
CC segregation (PubMed:28122936). Loss of nucleoporin npp-5 localization
CC to the nuclear membrane during interphase and to kinetochores during
CC metaphase (PubMed:22238360). Irregular nuclear membrane distribution of
CC nucleoporin npp-13 (PubMed:28122936). Mutants display P granule
CC dispersion (PubMed:20335358). {ECO:0000269|PubMed:12937276,
CC ECO:0000269|PubMed:20335358, ECO:0000269|PubMed:22238360,
CC ECO:0000269|PubMed:28122936}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU174496; ADF47155.1; -; mRNA.
DR EMBL; FO081350; CCD70954.1; -; Genomic_DNA.
DR EMBL; FO081350; CCD70955.1; -; Genomic_DNA.
DR EMBL; FO081350; CCD70956.1; -; Genomic_DNA.
DR RefSeq; NP_001254934.1; NM_001268005.1. [G5EEH9-3]
DR RefSeq; NP_498309.3; NM_065908.3.
DR RefSeq; NP_498310.3; NM_065909.3. [G5EEH9-2]
DR AlphaFoldDB; G5EEH9; -.
DR SMR; G5EEH9; -.
DR BioGRID; 41073; 42.
DR IntAct; G5EEH9; 8.
DR STRING; 6239.ZK328.5b; -.
DR MEROPS; S59.A06; -.
DR EPD; G5EEH9; -.
DR PaxDb; G5EEH9; -.
DR PeptideAtlas; G5EEH9; -.
DR EnsemblMetazoa; ZK328.5a.1; ZK328.5a.1; WBGene00003796. [G5EEH9-2]
DR EnsemblMetazoa; ZK328.5b.1; ZK328.5b.1; WBGene00003796. [G5EEH9-1]
DR EnsemblMetazoa; ZK328.5c.1; ZK328.5c.1; WBGene00003796. [G5EEH9-3]
DR GeneID; 175852; -.
DR CTD; 175852; -.
DR WormBase; ZK328.5a; CE44281; WBGene00003796; npp-10. [G5EEH9-2]
DR WormBase; ZK328.5b; CE44292; WBGene00003796; npp-10. [G5EEH9-1]
DR WormBase; ZK328.5c; CE44327; WBGene00003796; npp-10. [G5EEH9-3]
DR eggNOG; KOG0845; Eukaryota.
DR GeneTree; ENSGT00550000074799; -.
DR HOGENOM; CLU_002330_1_0_1; -.
DR InParanoid; G5EEH9; -.
DR OMA; YESSRFI; -.
DR OrthoDB; 93359at2759; -.
DR PhylomeDB; G5EEH9; -.
DR Reactome; R-CEL-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-CEL-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-CEL-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-191859; snRNP Assembly.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-CEL-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:G5EEH9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003796; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0000776; C:kinetochore; IMP:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:1990893; P:mitotic chromosome centromere condensation; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; NAS:UniProtKB.
DR GO; GO:0051664; P:nuclear pore localization; IMP:UniProtKB.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0030719; P:P granule organization; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1610.10; -; 1.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR037665; Nucleoporin_S59-like.
DR InterPro; IPR037637; NUP98-NUP96.
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; PTHR23198; 2.
DR PANTHER; PTHR23198:SF17; PTHR23198:SF17; 2.
DR Pfam; PF04096; Nucleoporin2; 1.
DR Pfam; PF13634; Nucleoporin_FG; 3.
DR Pfam; PF12110; Nup96; 1.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autocatalytic cleavage; Cell cycle; Cell division;
KW Chromosome; Hydrolase; Membrane; Mitosis; mRNA transport;
KW Nuclear pore complex; Nucleus; Protease; Protein transport;
KW Reference proteome; RNA-binding; Serine protease; Translocation; Transport.
FT CHAIN 1..919
FT /note="Nuclear pore complex protein Nup98"
FT /evidence="ECO:0000305|PubMed:20335358"
FT /id="PRO_0000417448"
FT CHAIN 920..1678
FT /note="Nuclear pore complex protein Nup96"
FT /evidence="ECO:0000305|PubMed:20335358"
FT /id="PRO_0000417449"
FT DOMAIN 777..919
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 920
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT SITE 919..920
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT VAR_SEQ 140
FT /note="S -> SAS (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_043738"
FT VAR_SEQ 978..980
FT /note="IIL -> VRF (in isoform a and isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_043739"
FT VAR_SEQ 982..1678
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_043740"
SQ SEQUENCE 1678 AA; 180454 MW; 8F5F71E161392E98 CRC64;
MFGQNKSFGS SSFGGGSSGS GLFGQNNQNN QNKGLFGQPA NNSGTTGLFG AAQNKPAGSI
FGAASNTSSI FGSPQQPQNN QSSLFGGGQN NANRSIFGST SSAAPASSSL FGNNANNTGT
SSIFGSNNNA PSGGGLFGAS TVSGTTVKFE PPISSDTMMR NGTTQTISTK HMCISAMSKY
DGKSIEELRV EDYIANRKAP GTGTTSTGGG LFGASNTTNQ AGSSGLFGSS NAQQKTSLFG
GASTSSPFGG NTSTANTGSS LFGNNNANTS AASGSLFGAK PAGSSLFGST ATTGASTFGQ
TTGSSLFGNQ QPQTNTGGSL FGNTQNQNQS GSLFGNTGTT GTGLFGQAQQ QPQQQSSGFS
FGGAPAATNA FGQPAAANTG GSLFGNTSTA NTGSSLFGAK PATSTGFTFG ATQPTTTNAF
GSTNTGGGLF GNNAAKPGGL FGNTTNTGTG GGLFGSQPQA SSGGLFGSNT QATQPLNTGF
GNLAQPQIVM QQQVAPVPVI GVTADVLQMQ ANMKSLKSQL TNAPYGDSPL LKYNANPEID
GKSSPASTQR QLRFLAAKKG ALSSSSDAQD SSFIIPPISK VMSDLSPAVT RSADVTKDLN
YTSKEAPPSL ARGLRNSTFN PNMSLTNRSV HESSALDKTI DSALDASMNG TSNRLGVRGS
VRRSNLKQLD MSLLADSSRV GRESRVADPD ALPRISESER RQDVVTSTPA VDPVQAVIQR
HNDRNRDPPS LNLDTTCDEH TGLEPVSAAT SSAASVVSTP SEETVNVNSA AGVKLTKPDY
FSLPTINEMK NMIKNGRVVL EDGLTVGRSS YGSVYWPGRV ELKDVALDEI VVFRHREVTV
YPNEEEKAPE GQELNRPAEV TLERVWYTDK KTKKEVRDVV KLSEIGWREH LERQTIRMGA
AFKDFRAETG SWVFRVDHFS KYGLADDDEP MDGSPPQQAL QASSPLQVID MNTSARDVNN
QVQRKKVHKA TDAHHQEIIL ERVPAPAALG DVVPIIRRVN RKGLGGGTLD DSREESCIGN
MTTEFNESGH DSIIEEGQQP EKKPKLELLA DLEYESSRFI RNLQELKVMP KANDPAHRFH
GGGHSAKMIG YGKSKLIDIG IVKGRSSHVG WSETGCLVWS AQPRHNQVLF GTIDRTSDVN
ENTLISMLDV NVHVSETSRK GPSSQSNSVK SSLTSNFVTY SDSYSSMFAK YIDVAQAGGY
DGHVSVWKLI SALFPYERRE GWSFERGEEI GEWLRTEAVK SVPDDRSADT SSNGVWNQLC
LGDIDKAFQI AIDNNQPQLA TMLQTSAVCP EATVHCFKAQ LDNWKKCETL HLIPKETLKC
YVLMSGLSHY EWDQDGKNHS INCLDGLNWI QALGLHVWYL RAWTGLEESY DAYQKDVNAG
RAASNRGDLP GELIKLACES QHSVEVVLDC AAGENPNDYF LQWHVWSLLY SVGYRTMSKT
SETRLHRNYS SQLEASSLSK YALFVLQHID DDEERSTAVR SLLDRIARFT DNDMFDSISE
QFDIPSEWIA DAQFSIAKSV DDSTQLFELA VAAKNYLEIC RLFVDDIAPT AVVAGDHDAL
KAACAMVRPF ENQIPEWGAT GMVYTDYCRL INLIENDAEE ELLQDVLESL ETRLHAPTIS
KNSLQKLSLQ TIGRVLFEYR ADKNTLPEWT KLLGHRQMFK IFRDRSSWGI ERFTIEFD
