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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_RAT               Reviewed;        1816 AA.
P49793; D3ZMW4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
08-MAR-2011, sequence version 2.
27-SEP-2017, entry version 139.
RecName: Full=Nuclear pore complex protein Nup98-Nup96;
EC=3.4.21.- {ECO:0000250|UniProtKB:P52948};
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;
Name=Nup98;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=7736573; DOI=10.1016/0092-8674(95)90331-3;
Radu A., Moore M.S., Blobel G.;
"The peptide repeat domain of nucleoporin Nup98 functions as a docking
site in transport across the nuclear pore complex.";
Cell 81:215-222(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
STRAIN=Brown Norway;
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
SUBCELLULAR LOCATION.
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]
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-653; SER-888
AND SER-934, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
and/or maintenance. Involved in the bidirectional transport across
the NPC. May anchor NUP153 and TPR to the NPC.
{ECO:0000250|UniProtKB:P52948}.
-!- 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. Involved in the localization of DHX9 in discrete
intranuclear foci (GLFG-body). {ECO:0000250|UniProtKB:P52948}.
-!- SUBUNIT: Part of the nuclear pore complex (NPC). Interacts
directly with NUP96. 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. Interacts with RAE1. Does not interact with
TPR. Interacts directly with NUP88 and NUP214, subunits of the
cytoplasmic filaments of the NPC. 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. {ECO:0000250|UniProtKB:P52948,
ECO:0000250|UniProtKB:Q6PFD9}.
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:11839768};
Peripheral membrane protein {ECO:0000269|PubMed:10087256};
Nucleoplasmic side {ECO:0000269|PubMed:10087256}. Nucleus, nuclear
pore complex {ECO:0000269|PubMed:10087256}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:10087256}. Note=Localized to the nucleoplasmic
side of the nuclear pore complex (NPC), at or near the
nucleoplasmic basket (PubMed:10087256). Dissociates from the
dissasembled NPC structure early during prophase of mitosis (By
similarity). Colocalizes with NUP153 to the nuclear basket of NPC
(By similarity). Colocalizes with TPR to the nuclear basket of NPC
(PubMed:10087256, PubMed:11839768). Colocalized with DHX9 in
diffuse and discrete intranuclear foci (GLFG-body) (By
similarity). Remains localized to the nuclear membrane after
poliovirus (PV) infection (By similarity).
{ECO:0000250|UniProtKB:P52948, ECO:0000269|PubMed:10087256,
ECO:0000269|PubMed:11839768}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Nup98-Nup96 precursor;
IsoId=P49793-1; Sequence=Displayed;
Name=2;
IsoId=P49793-2; Sequence=VSP_040702, VSP_040703;
-!- DOMAIN: Contains G-L-F-G repeats. The FG repeat domains have a
direct role in the transport (By similarity). {ECO:0000250}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Isoform 1 is autoproteolytically cleaved to yield Nup98 and
Nup96 or Nup98 only, respectively. Cleaved Nup98 is necessary for
the targeting of Nup98 to the nuclear pore and the interaction
with Nup96. {ECO:0000250|UniProtKB:P52948}.
-!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CH473956; EDM18207.1; -; Genomic_DNA.
EMBL; L39991; AAC42054.1; -; mRNA.
PIR; A56517; A56517.
RefSeq; NP_112336.2; NM_031074.2. [P49793-1]
RefSeq; XP_006229954.1; XM_006229892.3. [P49793-1]
RefSeq; XP_017445261.1; XM_017589772.1. [P49793-1]
UniGene; Rn.11324; -.
ProteinModelPortal; P49793; -.
SMR; P49793; -.
BioGrid; 249610; 1.
STRING; 10116.ENSRNOP00000027575; -.
MEROPS; S59.001; -.
iPTMnet; P49793; -.
PhosphoSitePlus; P49793; -.
PaxDb; P49793; -.
PRIDE; P49793; -.
Ensembl; ENSRNOT00000027575; ENSRNOP00000027575; ENSRNOG00000020347. [P49793-1]
GeneID; 81738; -.
KEGG; rno:81738; -.
UCSC; RGD:71033; rat. [P49793-1]
CTD; 4928; -.
RGD; 71033; Nup98.
eggNOG; KOG0845; Eukaryota.
eggNOG; ENOG410XPV4; LUCA.
GeneTree; ENSGT00550000074799; -.
HOGENOM; HOG000044579; -.
HOVERGEN; HBG052702; -.
InParanoid; P49793; -.
KO; K14297; -.
OMA; KQHCITA; -.
OrthoDB; EOG091G00HN; -.
PhylomeDB; P49793; -.
TreeFam; TF343335; -.
Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
Reactome; R-RNO-191859; snRNP Assembly.
Reactome; R-RNO-2467813; Separation of Sister Chromatids.
Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
Reactome; R-RNO-68877; Mitotic Prometaphase.
PRO; PR:P49793; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000020347; -.
ExpressionAtlas; P49793; baseline and differential.
Genevisible; P49793; RN.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0000776; C:kinetochore; IEA:Ensembl.
GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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:RGD.
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; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:RGD.
GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
GO; GO:0008139; F:nuclear localization sequence binding; IDA:RGD.
GO; GO:0005487; F:nucleocytoplasmic transporter activity; IBA:GO_Central.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IBA:GO_Central.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; ISS:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
GO; GO:0006260; P:DNA replication; IEA:Ensembl.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS: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:RGD.
GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
GO; GO:0034398; P:telomere tethering at nuclear periphery; IBA:GO_Central.
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;
Acetylation; Alternative splicing; Autocatalytic cleavage;
Complete proteome; Direct protein sequencing; Hydrolase;
Isopeptide bond; Membrane; mRNA transport; Nuclear pore complex;
Nucleus; Phosphoprotein; Protease; Protein transport;
Reference proteome; Repeat; Serine protease; Translocation; Transport;
Ubl conjugation.
CHAIN 1 880 Nuclear pore complex protein Nup98.
/FTId=PRO_0000204890.
CHAIN 881 1816 Nuclear pore complex protein Nup96.
/FTId=PRO_0000405578.
DOMAIN 738 880 Peptidase S59. {ECO:0000255|PROSITE-
ProRule:PRU00765}.
REGION 1 156 FG repeats 1.
REGION 157 213 GLEBS; interaction with RAE1.
{ECO:0000250}.
REGION 214 480 FG repeats 2.
COMPBIAS 7 481 Gly/Thr-rich.
COMPBIAS 890 894 Poly-Glu.
ACT_SITE 881 881 Nucleophile.
{ECO:0000250|UniProtKB:P52948}.
SITE 880 881 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 603 603 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 618 618 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 625 625 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 670 670 Phosphothreonine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 673 673 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFD9}.
MOD_RES 681 681 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 839 839 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 888 888 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1027 1027 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 1059 1059 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 1063 1063 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFD9}.
MOD_RES 1069 1069 Phosphothreonine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFD9}.
MOD_RES 1771 1771 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6PFD9}.
CROSSLNK 563 563 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P52948}.
CROSSLNK 603 603 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P52948}.
CROSSLNK 665 665 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P52948}.
VAR_SEQ 930 938 PQSQSPEVE -> TSGREGQRM (in isoform 2).
{ECO:0000303|PubMed:7736573}.
/FTId=VSP_040702.
VAR_SEQ 939 1816 Missing (in isoform 2).
{ECO:0000303|PubMed:7736573}.
/FTId=VSP_040703.
CONFLICT 11 11 Missing (in Ref. 1; AAC42054).
{ECO:0000305}.
CONFLICT 46 46 N -> S (in Ref. 1; AAC42054).
{ECO:0000305}.
CONFLICT 68 68 F -> L (in Ref. 1; AAC42054).
{ECO:0000305}.
SEQUENCE 1816 AA; 197283 MW; 70A7D8E23D542B42 CRC64;
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG LFGNSQTKPG
GLFGTSSFSQ PATSTSTGFG FGTSTGTSNS LFGTANTGTS LFSSQNNAFA QNKPTGFGNF
GTSTSSGGLF GTTNTTSNPF GNTSGSLFGP SSFTAAPTGT TIKFNPPTGT DTMVKAGVST
NISTKHQCIT AMKEYESKSL EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL
FSSSTTNSAF SYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTPNTGF
SFGNTSTLGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF GQPNTGFGAV
GSTLFGNNKL TTFGTSTTSA PSFGTTSGGL FGNKPTLTLG TNTNTSNFGF GTNNSGSSIF
GSKPAAGTLG TGLGTGFGTA LGAGQASLFG NNQPKIGGPL GTGAFGAPGF NTSTAILGFG
APQAPVALTD PNASAAQQAV LQQHLNSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA
QKALTTPTHY KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL
VLKNLNNSNL FSPVNHDSED LASPSEYPEN GERFSFLSKP VDENHQQDGD DDSLVSRFYT
NPIAKPIPQT PESAGNKNNS SSNVEDTFIA LNMRAALRNG LEGSSEETSF HDESLQDDRD
EIENSAFQIH PAGIVLTKVG YYTIPSMDDL AKITNEKGEC IVSDFTIGRK GYGSIYFEGD
VNLTNLNLDD IVHIRRKEVI VYVDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP
DRLADINYEG RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPPKTT
SKKLKTAPLP PAGQATTFQM TLNGKPAPPP QSQSPEVEQL GRVVELDSDM VDITQEPVPD
SVLEESVPED QEPVSASTQI ASSLGINPHV LQIMKASLLV DEEDVDAMEQ RFGHFPSRGD
TAQEICSPRL PISASHSSKS RSIVGGLLQS KFASGTFLSP SASVQECRTP RTSSLMNVPS
TSPWSVPLPL ATVFTVPSPA PEVPLKTVGI RRQPGLVPLE KSITYGKGKL LMDMALFMGR
SFRVGWGPNW TLANSGEQLH GSHELENHQV AESMEYGFLP NPVAVKSLSE SPFKVHLEKL
GLRQRKLDED LQLYQTPLEL KLKHSTVHVD ELCPLIVPNP GVSVIHGYAD WVKKSPRDLL
ELPIVKHWSL TWTLCEALWG HLKELDSQLD EPSEYIQTLE RRRAFSRWLS HTAAPQIEEE
VSLTRRDSPI EAVFSYLTGS RISEACCLAQ QSGDHRLALL LSQLVGSQSV RELLTMQLAD
WHQLQADSFI HDERLRIFAL LAGKPVWQLS EQKQINVCSQ LDWKRTLAIH LWYLLPPTAS
ISRALSMYEE AFQNTCEGDK YACPPLPSYL EGSGCVVEEE KDPQRPLQDV CFHLLKLYSD
RHYGLNQLLE PRSITADPLD YRLSWHLWEV LRALNYTHLS EQCEGVLQAS YAGQLESEGL
WEWAIFVFLH IDNSGMREKA VRELLTRHCQ LSETPESWAK ETFLTQKLCV PAEWIHEAKA
VRAHMESNKH LEALYLFKAG HWNRCHKLVV RHLASDAIIN ENYDYLKGFL EDLAPPERSS
LIQDWETSGL VYLDYIRVIE MLHRIQQVDC SGYELEHLHT KVTSLCNRIE QIPCYNAKDR
LAQSDMAKRV ANLLRVVLSL QHTPDATSNS TPDPQRVPLR LLAPHIGRLP MPEDYALEEL
RGLTQSYLRE LTVGSQ


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