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Nuclear pore complex protein Nup93 (93 kDa nucleoporin) (Nucleoporin Nup93)

 NUP93_HUMAN             Reviewed;         819 AA.
Q8N1F7; B3KPQ8; Q14705;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
12-SEP-2018, entry version 152.
RecName: Full=Nuclear pore complex protein Nup93;
AltName: Full=93 kDa nucleoporin;
AltName: Full=Nucleoporin Nup93;
Name=NUP93; Synonyms=KIAA0095;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Amygdala, and Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-509.
TISSUE=Skin;
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).
[5]
FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, INTERACTION WITH
P62 COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=9348540; DOI=10.1091/mbc.8.10.2017;
Grandi P., Dang T., Pane N., Shevchenko A., Mann M., Forbes D.,
Hurt E.;
"Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a
novel 205-kDa protein and is required for correct nuclear pore
assembly.";
Mol. Biol. Cell 8:2017-2038(1997).
[6]
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).
[7]
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).
[8]
FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, INTERACTION WITH
NUP35, AND IDENTIFICATION IN A COMPLEX WITH NUP155; NUP205 AND LAMIN
B.
PubMed=15703211; DOI=10.1091/mbc.E04-10-0857;
Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.;
"Vertebrate Nup53 interacts with the nuclear lamina and is required
for the assembly of a Nup93-containing complex.";
Mol. Biol. Cell 16:2382-2394(2005).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-72, 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-72, 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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-52; SER-66;
SER-72; SER-75; SER-80; SER-430 AND SER-767, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, 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).
[17]
INVOLVEMENT IN NPHS12, VARIANTS NPHS12 TRP-388; VAL-591 AND CYS-629,
CHARACTERIZATION OF VARIANTS NPHS12 TRP-388; VAL-591 AND CYS-629,
INTERACTION WITH IPO7; SMAD4 AND NUP205, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=26878725; DOI=10.1038/ng.3512;
Braun D.A., Sadowski C.E., Kohl S., Lovric S., Astrinidis S.A.,
Pabst W.L., Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M.,
Tan W., Schapiro D., Rao J., Choi W.I., Hermle T., Kemper M.J.,
Pohl M., Ozaltin F., Konrad M., Bogdanovic R., Buescher R.,
Helmchen U., Serdaroglu E., Lifton R.P., Antonin W., Hildebrandt F.;
"Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid-
resistant nephrotic syndrome.";
Nat. Genet. 48:457-465(2016).
-!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
and/or maintenance (PubMed:9348540). May anchor nucleoporins, but
not NUP153 and TPR, to the NPC. During renal development,
regulates podocyte migration and proliferation through SMAD4
signaling (PubMed:26878725). {ECO:0000269|PubMed:15229283,
ECO:0000269|PubMed:15703211, ECO:0000269|PubMed:26878725,
ECO:0000269|PubMed:9348540}.
-!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:9348540,
PubMed:15229283, PubMed:15703211). Component of the p62 complex, a
complex composed of NUP62 and NUP54 (PubMed:9348540). Forms a
complex with NUP35, NUP155, NUP205 and lamin B; the interaction
with NUP35 is direct (PubMed:15703211). Does not interact with TPR
(PubMed:12802065, PubMed:15229283). Interacts with SMAD4 and IPO7;
translocates SMAD4 to the nucleus through the NPC upon BMP7
stimulation resulting in activation of SMAD4 signaling
(PubMed:26878725). {ECO:0000269|PubMed:12802065,
ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:15703211,
ECO:0000269|PubMed:26878725, ECO:0000269|PubMed:9348540}.
-!- SUBCELLULAR LOCATION: Nucleus membrane
{ECO:0000250|UniProtKB:Q66HC5}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q66HC5}. Nucleus, nuclear pore complex
{ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
ECO:0000269|PubMed:9348540}. Nucleus envelope
{ECO:0000269|PubMed:26878725, ECO:0000269|PubMed:9348540}.
Note=Localizes at the nuclear basket and at or near the nuclear
entry to the gated channel of the pore.
{ECO:0000269|PubMed:9348540}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8N1F7-1; Sequence=Displayed;
Name=2;
IsoId=Q8N1F7-2; Sequence=VSP_043117;
Note=No experimental confirmation available.;
-!- DISEASE: Nephrotic syndrome 12 (NPHS12) [MIM:616892]: A form of
nephrotic syndrome, a renal disease clinically characterized by
severe proteinuria, resulting in complications such as
hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show
non-specific histologic changes such as focal segmental
glomerulosclerosis and diffuse mesangial proliferation. Some
affected individuals have an inherited steroid-resistant form and
progress to end-stage renal failure. NPHS12 inheritance is
autosomal recessive. {ECO:0000269|PubMed:26878725}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC)
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA07680.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D42085; BAA07680.2; ALT_INIT; mRNA.
EMBL; AK294176; BAH11689.1; -; mRNA.
EMBL; BC034346; AAH34346.1; -; mRNA.
EMBL; AC012181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC106779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK056637; BAG51770.1; -; mRNA.
CCDS; CCDS10769.1; -. [Q8N1F7-1]
CCDS; CCDS55996.1; -. [Q8N1F7-2]
RefSeq; NP_001229724.1; NM_001242795.1. [Q8N1F7-2]
RefSeq; NP_001229725.1; NM_001242796.2. [Q8N1F7-2]
RefSeq; NP_055484.3; NM_014669.4. [Q8N1F7-1]
RefSeq; XP_005256320.1; XM_005256263.3. [Q8N1F7-1]
UniGene; Hs.276878; -.
PDB; 5IJN; EM; 21.40 A; C/I/O/U=1-819.
PDB; 5IJO; EM; 21.40 A; C/I/O/U=1-819.
PDBsum; 5IJN; -.
PDBsum; 5IJO; -.
ProteinModelPortal; Q8N1F7; -.
SMR; Q8N1F7; -.
BioGrid; 115041; 82.
CORUM; Q8N1F7; -.
DIP; DIP-44020N; -.
IntAct; Q8N1F7; 55.
MINT; Q8N1F7; -.
STRING; 9606.ENSP00000310668; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q8N1F7; -.
PhosphoSitePlus; Q8N1F7; -.
SwissPalm; Q8N1F7; -.
BioMuta; NUP93; -.
DMDM; 116242684; -.
EPD; Q8N1F7; -.
MaxQB; Q8N1F7; -.
PaxDb; Q8N1F7; -.
PeptideAtlas; Q8N1F7; -.
PRIDE; Q8N1F7; -.
ProteomicsDB; 71593; -.
ProteomicsDB; 71594; -. [Q8N1F7-2]
Ensembl; ENST00000308159; ENSP00000310668; ENSG00000102900. [Q8N1F7-1]
Ensembl; ENST00000542526; ENSP00000440235; ENSG00000102900. [Q8N1F7-2]
Ensembl; ENST00000564887; ENSP00000458039; ENSG00000102900. [Q8N1F7-2]
GeneID; 9688; -.
KEGG; hsa:9688; -.
UCSC; uc002eka.4; human. [Q8N1F7-1]
CTD; 9688; -.
DisGeNET; 9688; -.
EuPathDB; HostDB:ENSG00000102900.12; -.
GeneCards; NUP93; -.
HGNC; HGNC:28958; NUP93.
HPA; HPA017937; -.
MalaCards; NUP93; -.
MIM; 614351; gene.
MIM; 616892; phenotype.
neXtProt; NX_Q8N1F7; -.
OpenTargets; ENSG00000102900; -.
PharmGKB; PA134912759; -.
eggNOG; KOG2168; Eukaryota.
eggNOG; ENOG410XPN3; LUCA.
GeneTree; ENSGT00390000016353; -.
HOGENOM; HOG000007350; -.
HOVERGEN; HBG052701; -.
InParanoid; Q8N1F7; -.
KO; K14309; -.
PhylomeDB; Q8N1F7; -.
TreeFam; TF315118; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
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-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
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-6784531; tRNA processing in the nucleus.
ChiTaRS; NUP93; human.
GeneWiki; NUP93; -.
GenomeRNAi; 9688; -.
PRO; PR:Q8N1F7; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000102900; Expressed in 214 organ(s), highest expression level in left lobe of thyroid gland.
CleanEx; HS_NUP93; -.
ExpressionAtlas; Q8N1F7; baseline and differential.
Genevisible; Q8N1F7; HS.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; 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:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
GO; GO:0072015; P:glomerular visceral epithelial cell development; IMP:UniProtKB.
GO; GO:0090521; P:glomerular visceral epithelial cell migration; IMP:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:UniProtKB.
GO; GO:0006998; P:nuclear envelope organization; IDA:UniProtKB.
GO; GO:0051292; P:nuclear pore complex assembly; IDA:UniProtKB.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0072001; P:renal system development; ISS:UniProtKB.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
GO; GO:0016032; P:viral process; TAS:Reactome.
InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96.
PANTHER; PTHR11225; PTHR11225; 1.
Pfam; PF04097; Nic96; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Membrane; mRNA transport; Nuclear pore complex;
Nucleus; Phosphoprotein; Polymorphism; Protein transport;
Reference proteome; Translocation; Transport.
CHAIN 1 819 Nuclear pore complex protein Nup93.
/FTId=PRO_0000124782.
MOD_RES 49 49 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 767 767 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 123 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043117.
VARIANT 388 388 R -> W (in NPHS12; doesnt affect nuclear
envelope localization; impairs nuclear
pore complex assembly; doesn't abrogate
interaction with NUP205; doesn't affect
SMAD4 interaction; doesn't affect IPO7
interaction; impairs SMAD4 protein import
into nucleus; impairs SMAD4 protein
signal transduction; dbSNP:rs145146218).
{ECO:0000269|PubMed:26878725}.
/FTId=VAR_076473.
VARIANT 509 509 S -> R (in dbSNP:rs17853288).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_028160.
VARIANT 591 591 G -> V (in NPHS12; doesnt affect nuclear
envelope localization; doesn't affect
nuclear pore complex assembly; doesn't
abrogate interaction with NUP205;
abrogates SMAD4 interaction; abrogates
IPO7 interaction; impairs SMAD4 protein
import into nucleus; impairs SMAD4
protein signal transduction;
dbSNP:rs145473779).
{ECO:0000269|PubMed:26878725}.
/FTId=VAR_076474.
VARIANT 629 629 Y -> C (in NPHS12; doesnt affect nuclear
envelope localization; doesn't affect
nuclear pore complex assembly; doesn't
abrogate interaction with NUP205;
abrogates SMAD4 interaction; abrogates
IPO7 interaction; impairs SMAD4 protein
import; impairs SMAD4 protein signal
transduction into nucleus;;
dbSNP:rs757674160).
{ECO:0000269|PubMed:26878725}.
/FTId=VAR_076475.
SEQUENCE 819 AA; 93488 MW; 7A611FABE964FE98 CRC64;
MDTEGFGELL QQAEQLAAET EGISELPHVE RNLQEIQQAG ERLRSRTLTR TSQETADVKA
SVLLGSRGLD ISHISQRLES LSAATTFEPL EPVKDTDIQG FLKNEKDNAL LSAIEESRKR
TFGMAEEYHR ESMLVEWEQV KQRILHTLLA SGEDALDFTQ ESEPSYISDV GPPGRSSLDN
IEMAYARQIY IYNEKIVNGH LQPNLVDLCA SVAELDDKSI SDMWTMVKQM TDVLLTPATD
ALKNRSSVEV RMEFVRQALA YLEQSYKNYT LVTVFGNLHQ AQLGGVPGTY QLVRSFLNIK
LPAPLPGLQD GEVEGHPVWA LIYYCMRCGD LLAASQVVNR AQHQLGEFKT WFQEYMNSKD
RRLSPATENK LRLHYRRALR NNTDPYKRAV YCIIGRCDVT DNQSEVADKT EDYLWLKLNQ
VCFDDDGTSS PQDRLTLSQF QKQLLEDYGE SHFTVNQQPF LYFQVLFLTA QFEAAVAFLF
RMERLRCHAV HVALVLFELK LLLKSSGQSA QLLSHEPGDP PCLRRLNFVR LLMLYTRKFE
STDPREALQY FYFLRDEKDS QGENMFLRCV SELVIESREF DMILGKLEND GSRKPGVIDK
FTSDTKPIIN KVASVAENKG LFEEAAKLYD LAKNADKVLE LMNKLLSPVV PQISAPQSNK
ERLKNMALSI AERYRAQGIS ANKFVDSTFY LLLDLITFFD EYHSGHIDRA FDIIERLKLV
PLNQESVEER VAAFRNFSDE IRHNLSEVLL ATMNILFTQF KRLKGTSPSS SSRPQRVIED
RDSQLRSQAR TLITFAGMIP YRTSGDTNAR LVQMEVLMN


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