NUP93_HUMAN
ID NUP93_HUMAN Reviewed; 819 AA.
AC Q8N1F7; B3KPQ8; Q14705;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Nuclear pore complex protein Nup93;
DE AltName: Full=93 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup93;
GN Name=NUP93; Synonyms=KIAA0095;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala, and Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-509.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, INTERACTION WITH P62
RP COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=9348540; DOI=10.1091/mbc.8.10.2017;
RA Grandi P., Dang T., Pane N., Shevchenko A., Mann M., Forbes D., Hurt E.;
RT "Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a
RT novel 205-kDa protein and is required for correct nuclear pore assembly.";
RL Mol. Biol. Cell 8:2017-2038(1997).
RN [6]
RP LACK OF INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
RX PubMed=12802065; DOI=10.1091/mbc.e02-09-0620;
RA Hase M.E., Cordes V.C.;
RT "Direct interaction with nup153 mediates binding of Tpr to the periphery of
RT the nuclear pore complex.";
RL Mol. Biol. Cell 14:1923-1940(2003).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15229283; DOI=10.1091/mbc.e04-03-0165;
RA Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.;
RT "Nucleoporins as components of the nuclear pore complex core structure and
RT Tpr as the architectural element of the nuclear basket.";
RL Mol. Biol. Cell 15:4261-4277(2004).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, INTERACTION WITH
RP NUP35, AND IDENTIFICATION IN A COMPLEX WITH NUP155; NUP205 AND LAMIN B.
RX PubMed=15703211; DOI=10.1091/mbc.e04-10-0857;
RA Hawryluk-Gara L.A., Shibuya E.K., Wozniak R.W.;
RT "Vertebrate Nup53 interacts with the nuclear lamina and is required for the
RT assembly of a Nup93-containing complex.";
RL Mol. Biol. Cell 16:2382-2394(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-72, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-72, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-75, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-52; SER-66; SER-72;
RP SER-75; SER-80; SER-430 AND SER-767, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP INVOLVEMENT IN NPHS12, VARIANTS NPHS12 TRP-388; VAL-591 AND CYS-629,
RP CHARACTERIZATION OF VARIANTS NPHS12 TRP-388; VAL-591 AND CYS-629,
RP INTERACTION WITH IPO7; SMAD4 AND NUP205, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=26878725; DOI=10.1038/ng.3512;
RA Braun D.A., Sadowski C.E., Kohl S., Lovric S., Astrinidis S.A., Pabst W.L.,
RA Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M., Tan W., Schapiro D.,
RA Rao J., Choi W.I., Hermle T., Kemper M.J., Pohl M., Ozaltin F., Konrad M.,
RA Bogdanovic R., Buescher R., Helmchen U., Serdaroglu E., Lifton R.P.,
RA Antonin W., Hildebrandt F.;
RT "Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid-
RT resistant nephrotic syndrome.";
RL Nat. Genet. 48:457-465(2016).
RN [18]
RP INTERACTION WITH HUMAN SARS-COV TRANSLATION INHIBITOR NSP1 (MICROBIAL
RP INFECTION).
RX PubMed=30943371; DOI=10.1139/bcb-2018-0394;
RA Gomez G.N., Abrar F., Dodhia M.P., Gonzalez F.G., Nag A.;
RT "SARS coronavirus protein nsp1 disrupts localization of Nup93 from the
RT nuclear pore complex.";
RL Biochem. Cell Biol. 97:758-766(2019).
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance (PubMed:9348540). May anchor nucleoporins, but not
CC NUP153 and TPR, to the NPC. During renal development, regulates
CC podocyte migration and proliferation through SMAD4 signaling
CC (PubMed:26878725). {ECO:0000269|PubMed:15229283,
CC ECO:0000269|PubMed:15703211, ECO:0000269|PubMed:26878725,
CC ECO:0000269|PubMed:9348540}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:9348540,
CC PubMed:15229283, PubMed:15703211). Component of the p62 complex, a
CC complex composed of NUP62 and NUP54 (PubMed:9348540). Forms a complex
CC with NUP35, NUP155, NUP205 and lamin B; the interaction with NUP35 is
CC direct (PubMed:15703211). Does not interact with TPR (PubMed:12802065,
CC PubMed:15229283). Interacts with SMAD4 and IPO7; translocates SMAD4 to
CC the nucleus through the NPC upon BMP7 stimulation resulting in
CC activation of SMAD4 signaling (PubMed:26878725).
CC {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
CC ECO:0000269|PubMed:15703211, ECO:0000269|PubMed:26878725,
CC ECO:0000269|PubMed:9348540}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV translation
CC inhibitor nsp1; this interaction may disrupt nuclear pore function.
CC {ECO:0000269|PubMed:30943371}.
CC -!- INTERACTION:
CC Q8N1F7; O43299: AP5Z1; NbExp=3; IntAct=EBI-1042703, EBI-740938;
CC Q8N1F7; Q15777: MPPED2; NbExp=3; IntAct=EBI-1042703, EBI-2350461;
CC Q8N1F7; Q14982: OPCML; NbExp=3; IntAct=EBI-1042703, EBI-6447201;
CC Q8N1F7; O60733: PLA2G6; NbExp=3; IntAct=EBI-1042703, EBI-12089905;
CC Q8N1F7; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-1042703, EBI-8644968;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q66HC5};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q66HC5}. Nucleus,
CC nuclear pore complex {ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:9348540}. Nucleus
CC envelope {ECO:0000269|PubMed:26878725, ECO:0000269|PubMed:9348540}.
CC Note=Localizes at the nuclear basket and at or near the nuclear entry
CC to the gated channel of the pore. {ECO:0000269|PubMed:9348540}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N1F7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N1F7-2; Sequence=VSP_043117;
CC -!- DISEASE: Nephrotic syndrome 12 (NPHS12) [MIM:616892]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form and progress to end-stage renal failure. NPHS12
CC inheritance is autosomal recessive. {ECO:0000269|PubMed:26878725}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07680.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D42085; BAA07680.2; ALT_INIT; mRNA.
DR EMBL; AK294176; BAH11689.1; -; mRNA.
DR EMBL; BC034346; AAH34346.1; -; mRNA.
DR EMBL; AC012181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK056637; BAG51770.1; -; mRNA.
DR CCDS; CCDS10769.1; -. [Q8N1F7-1]
DR CCDS; CCDS55996.1; -. [Q8N1F7-2]
DR RefSeq; NP_001229724.1; NM_001242795.1. [Q8N1F7-2]
DR RefSeq; NP_001229725.1; NM_001242796.2. [Q8N1F7-2]
DR RefSeq; NP_055484.3; NM_014669.4. [Q8N1F7-1]
DR RefSeq; XP_005256320.1; XM_005256263.3. [Q8N1F7-1]
DR PDB; 5IJN; EM; 21.40 A; C/I/O/U=1-819.
DR PDB; 5IJO; EM; 21.40 A; C/I/O/U=1-819.
DR PDB; 7PER; EM; 35.00 A; C/I/O/U=1-819.
DR PDBsum; 5IJN; -.
DR PDBsum; 5IJO; -.
DR PDBsum; 7PER; -.
DR AlphaFoldDB; Q8N1F7; -.
DR SMR; Q8N1F7; -.
DR BioGRID; 115041; 186.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; Q8N1F7; -.
DR DIP; DIP-44020N; -.
DR IntAct; Q8N1F7; 75.
DR MINT; Q8N1F7; -.
DR STRING; 9606.ENSP00000310668; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q8N1F7; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q8N1F7; -.
DR MetOSite; Q8N1F7; -.
DR PhosphoSitePlus; Q8N1F7; -.
DR SwissPalm; Q8N1F7; -.
DR BioMuta; NUP93; -.
DR DMDM; 116242684; -.
DR EPD; Q8N1F7; -.
DR jPOST; Q8N1F7; -.
DR MassIVE; Q8N1F7; -.
DR MaxQB; Q8N1F7; -.
DR PaxDb; Q8N1F7; -.
DR PeptideAtlas; Q8N1F7; -.
DR PRIDE; Q8N1F7; -.
DR ProteomicsDB; 71593; -. [Q8N1F7-1]
DR ProteomicsDB; 71594; -. [Q8N1F7-2]
DR Antibodypedia; 14851; 142 antibodies from 28 providers.
DR DNASU; 9688; -.
DR Ensembl; ENST00000308159.10; ENSP00000310668.5; ENSG00000102900.13. [Q8N1F7-1]
DR Ensembl; ENST00000542526.5; ENSP00000440235.1; ENSG00000102900.13. [Q8N1F7-2]
DR Ensembl; ENST00000564887.5; ENSP00000458039.1; ENSG00000102900.13. [Q8N1F7-2]
DR GeneID; 9688; -.
DR KEGG; hsa:9688; -.
DR MANE-Select; ENST00000308159.10; ENSP00000310668.5; NM_014669.5; NP_055484.3.
DR UCSC; uc002eka.4; human. [Q8N1F7-1]
DR CTD; 9688; -.
DR DisGeNET; 9688; -.
DR GeneCards; NUP93; -.
DR HGNC; HGNC:28958; NUP93.
DR HPA; ENSG00000102900; Low tissue specificity.
DR MalaCards; NUP93; -.
DR MIM; 614351; gene.
DR MIM; 616892; phenotype.
DR neXtProt; NX_Q8N1F7; -.
DR OpenTargets; ENSG00000102900; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA134912759; -.
DR VEuPathDB; HostDB:ENSG00000102900; -.
DR eggNOG; KOG2168; Eukaryota.
DR GeneTree; ENSGT00390000016353; -.
DR HOGENOM; CLU_011846_1_0_1; -.
DR InParanoid; Q8N1F7; -.
DR OMA; LLMCGQF; -.
DR OrthoDB; 187731at2759; -.
DR PhylomeDB; Q8N1F7; -.
DR TreeFam; TF315118; -.
DR PathwayCommons; Q8N1F7; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q8N1F7; -.
DR SIGNOR; Q8N1F7; -.
DR BioGRID-ORCS; 9688; 742 hits in 1085 CRISPR screens.
DR ChiTaRS; NUP93; human.
DR GeneWiki; NUP93; -.
DR GenomeRNAi; 9688; -.
DR Pharos; Q8N1F7; Tbio.
DR PRO; PR:Q8N1F7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8N1F7; protein.
DR Bgee; ENSG00000102900; Expressed in ventricular zone and 189 other tissues.
DR ExpressionAtlas; Q8N1F7; baseline and differential.
DR Genevisible; Q8N1F7; HS.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; IDA:UniProtKB.
DR GO; GO:0051292; P:nuclear pore complex assembly; IDA:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
DR InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96.
DR PANTHER; PTHR11225; PTHR11225; 1.
DR Pfam; PF04097; Nic96; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..819
FT /note="Nuclear pore complex protein Nup93"
FT /id="PRO_0000124782"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043117"
FT VARIANT 388
FT /note="R -> W (in NPHS12; doesnt affect nuclear envelope
FT localization; impairs nuclear pore complex assembly;
FT doesn't abrogate interaction with NUP205; doesn't affect
FT SMAD4 interaction; doesn't affect IPO7 interaction; impairs
FT SMAD4 protein import into nucleus; impairs SMAD4 protein
FT signal transduction; dbSNP:rs145146218)"
FT /evidence="ECO:0000269|PubMed:26878725"
FT /id="VAR_076473"
FT VARIANT 509
FT /note="S -> R (in dbSNP:rs17853288)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028160"
FT VARIANT 591
FT /note="G -> V (in NPHS12; doesnt affect nuclear envelope
FT localization; doesn't affect nuclear pore complex assembly;
FT doesn't abrogate interaction with NUP205; abrogates SMAD4
FT interaction; abrogates IPO7 interaction; impairs SMAD4
FT protein import into nucleus; impairs SMAD4 protein signal
FT transduction; dbSNP:rs145473779)"
FT /evidence="ECO:0000269|PubMed:26878725"
FT /id="VAR_076474"
FT VARIANT 629
FT /note="Y -> C (in NPHS12; doesnt affect nuclear envelope
FT localization; doesn't affect nuclear pore complex assembly;
FT doesn't abrogate interaction with NUP205; abrogates SMAD4
FT interaction; abrogates IPO7 interaction; impairs SMAD4
FT protein import; impairs SMAD4 protein signal transduction
FT into nucleus;; dbSNP:rs757674160)"
FT /evidence="ECO:0000269|PubMed:26878725"
FT /id="VAR_076475"
SQ 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
