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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_MOUSE             Reviewed;        1816 AA.
Q6PFD9; Q68G59;
03-APR-2013, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 2.
25-OCT-2017, entry version 107.
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;
Flags: Precursor;
Name=Nup98;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888 AND SER-1027, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653; THR-670 AND
SER-888, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-618;
SER-623; SER-653; SER-680; SER-888; SER-1027; SER-1059; SER-1063;
SER-1328 AND THR-1771, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 732-880 IN COMPLEX WITH
YEAST NUP82 AND NUP159, INTERACTION WITH NUP88, MUTAGENESIS OF
LYS-831, AND SUBUNIT.
PubMed=22480613; DOI=10.1016/j.jmb.2012.03.024;
Stuwe T., von Borzyskowski L.S., Davenport A.M., Hoelz A.;
"Molecular basis for the anchoring of proto-oncoprotein Nup98 to the
cytoplasmic face of the nuclear pore complex.";
J. Mol. Biol. 419:330-346(2012).
-!- 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 (By similarity). Interacts directly with NUP88 and NUP214,
subunits of the cytoplasmic filaments of the NPC
(PubMed:22480613). 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 (By
similarity). {ECO:0000250|UniProtKB:P52948,
ECO:0000269|PubMed:22480613}.
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000250|UniProtKB:P52948}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P52948}; Nucleoplasmic side
{ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear pore complex
{ECO:0000250|UniProtKB:P52948}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:P52948}. Note=Localized to the
nucleoplasmic side of the nuclear pore complex (NPC), at or near
the nucleoplasmic basket. Dissociates from the dissasembled NPC
structure early during prophase of mitosis. Colocalized with
NUP153 and TPR to the nuclear basket of NPC. Colocalized with DHX9
in diffuse and discrete intranuclear foci (GLFG-body). Remains
localized to the nuclear membrane after poliovirus (PV) infection.
{ECO:0000250|UniProtKB:P52948}.
-!- DOMAIN: Contains G-L-F-G repeats. The FG repeat domains have a
direct role in the transport (By similarity). {ECO:0000250}.
-!- PTM: 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}.
-!- SEQUENCE CAUTION:
Sequence=AAH50911.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH57608.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAI12913.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AC118592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050911; AAH50911.1; ALT_SEQ; mRNA.
EMBL; BC057608; AAH57608.1; ALT_SEQ; mRNA.
EMBL; BC078630; AAH78630.1; -; mRNA.
EMBL; BC112912; AAI12913.1; ALT_SEQ; mRNA.
CCDS; CCDS85358.1; -.
RefSeq; NP_001274093.1; NM_001287164.1.
RefSeq; NP_001274094.1; NM_001287165.1.
RefSeq; NP_075355.1; NM_022979.2.
UniGene; Mm.439800; -.
UniGene; Mm.486276; -.
PDB; 3TKN; X-ray; 3.40 A; C/F/I=732-880.
PDBsum; 3TKN; -.
ProteinModelPortal; Q6PFD9; -.
SMR; Q6PFD9; -.
BioGrid; 234738; 62.
IntAct; Q6PFD9; 59.
STRING; 10090.ENSMUSP00000068530; -.
MEROPS; S59.001; -.
iPTMnet; Q6PFD9; -.
PhosphoSitePlus; Q6PFD9; -.
EPD; Q6PFD9; -.
MaxQB; Q6PFD9; -.
PaxDb; Q6PFD9; -.
PeptideAtlas; Q6PFD9; -.
PRIDE; Q6PFD9; -.
GeneID; 269966; -.
KEGG; mmu:269966; -.
UCSC; uc009iqx.2; mouse.
CTD; 4928; -.
MGI; MGI:109404; Nup98.
eggNOG; KOG0845; Eukaryota.
eggNOG; ENOG410XPV4; LUCA.
HOGENOM; HOG000044579; -.
HOVERGEN; HBG052702; -.
InParanoid; Q6PFD9; -.
KO; K14297; -.
TreeFam; TF343335; -.
PRO; PR:Q6PFD9; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; ISO:MGI.
GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
GO; GO:0034399; C:nuclear periphery; ISO:MGI.
GO; GO:0005643; C:nuclear pore; ISO:MGI.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
GO; GO:0044615; C:nuclear pore nuclear basket; ISO:MGI.
GO; GO:0031080; C:nuclear pore outer ring; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003729; F:mRNA binding; ISO:MGI.
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; 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; ISO:MGI.
GO; GO:0006260; P:DNA replication; ISO:MGI.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0051292; P:nuclear pore complex assembly; ISO:MGI.
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; IBA:GO_Central.
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.
InterPro; IPR036903; Peptidase_S59_sf.
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; Autocatalytic cleavage; Complete proteome;
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_0000421837.
CHAIN 881 1816 Nuclear pore complex protein Nup96.
/FTId=PRO_0000421838.
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:0000244|PubMed:21183079}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 618 618 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 625 625 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 670 670 Phosphothreonine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 673 673 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
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:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 934 934 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 1027 1027 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 1059 1059 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1063 1063 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1069 1069 Phosphothreonine.
{ECO:0000250|UniProtKB:P52948}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1771 1771 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
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}.
MUTAGEN 831 831 K->A: Reduces interaction with NUP88.
{ECO:0000269|PubMed:22480613}.
STRAND 741 745 {ECO:0000244|PDB:3TKN}.
HELIX 749 752 {ECO:0000244|PDB:3TKN}.
STRAND 763 769 {ECO:0000244|PDB:3TKN}.
TURN 770 772 {ECO:0000244|PDB:3TKN}.
STRAND 773 780 {ECO:0000244|PDB:3TKN}.
HELIX 788 790 {ECO:0000244|PDB:3TKN}.
STRAND 792 795 {ECO:0000244|PDB:3TKN}.
STRAND 798 807 {ECO:0000244|PDB:3TKN}.
STRAND 813 815 {ECO:0000244|PDB:3TKN}.
STRAND 819 823 {ECO:0000244|PDB:3TKN}.
TURN 831 833 {ECO:0000244|PDB:3TKN}.
HELIX 840 845 {ECO:0000244|PDB:3TKN}.
HELIX 848 857 {ECO:0000244|PDB:3TKN}.
TURN 858 860 {ECO:0000244|PDB:3TKN}.
STRAND 862 867 {ECO:0000244|PDB:3TKN}.
TURN 868 871 {ECO:0000244|PDB:3TKN}.
STRAND 872 878 {ECO:0000244|PDB:3TKN}.
SEQUENCE 1816 AA; 197241 MW; CEB86B4A447E9750 CRC64;
MFNKSFGTPF GGSTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG LFGNSQTKPG
GLFGTSSFSQ PATSTSTGFG FGTSTGTSNS LFGTASTGTS LFSSQNNAFA QNKPTGFGNF
GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP SSFTAAPTGT TIKFNPPTGT DTMVKAGVST
NISTKHQCIT AMKEYESKSL EELRLEDYQA NRKGPQNQVG GGTTAGLFGS 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 VDENNQQDGE DDSLVSRFYT
NPIAKPIPQT PESVGNKNNS SSNVEDTIVA LNMRAALRNG LEGSSEETSF HDESLQDDRE
EIENNAYHIH PAGIVLTKVG YYTIPSMDDL AKITNEKGEC IVSDFTIGRK GYGSIYFEGD
VNLTNLNLDD IVHIRRKEVI VYVDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP
DRLADINYEG RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPPKTT
SKKLKTAPLP PAGQATTFQM TLNGKPAPPP QSQSPEVEQL GRVVELDSDM VDITQEPVPD
SVLEESVPED QEPVSASTHI ASSLGINPHV LQIMKASLLV DEEDVDAMDQ RFGHIPSKGE
TVQEICSPRL PISASHSSKS RSIVGGLLQS KFASGTFLSP SASVQECRTP RTSSRMNIPS
TSPWSVPLPL ATVFTVPSPA PEVQLKTVGI RRQPGLVPLE KSITYGKGKL LMDMALFMGR
SFRVGWGPNW TLANSGEQLH GSHELENHQV ADSMEYGFLP NPVAVKSLSE SPFKVHLEKL
GLRQRKLDED LQLYQTPLEL KLKHSTVHVD ELCPLIVPNP GVSVIHDYAD WVKDSPGDFL
ELPIVKHWSL TWTLCEALWG HLKELDGQLD EPSEYIQTLE RRRAFSRWLS HTAAPQIEEE
VSLTRRDSPV EAVFSYLTGS RISGACCLAQ QSGDHRLALL LSQLVGSQSV RELLTMQLAD
WHQLQADSFI HDERLRIFAL LAGKPVWQLS EQKQINVCSQ LDWKRTLAIH LWYLLPPTAS
ISRALSMYEE AFQNTPEGDK YACSPLPSYL EGCGCMVEEE KDSRRPLQDV CFHLLKLYSD
RHYELNQLLE PRSITADPLD YRLSWHLWEV LRALNYTHLS EQCEGVLQAS YAGQLESEGL
WEWAIFVFLH IDNSGMREKA VRELLTRHCQ LSETPESWAK EAFLTQKLCV PAEWIHEAKA
VRAHMESNKH LEALYLFKAG HWNRCHKLVI RHLASDAIIN ENYDYLKGFL EDLAPPERSS
LIQDWETSGL VYLDYIRVIE MLHRIQQVDC SGYELEHLHT KVTSLCNRIE QIPCYNAKDR
LAQSDMAKRV ANLLRVVLSL QHAPDATSNS TPDPQRVPLR LLAPHIGRLP MPEDYALEEL
RGLTQSYLRE LTVGSQ


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