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 27-MAR-2024, entry version 186. 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}; 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; 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; 7MW0; X-ray; 2.00 A; A=174-819. DR PDB; 7MW1; X-ray; 3.40 A; A/B=174-819. DR PDB; 7PER; EM; 35.00 A; C/I/O/U=1-819. DR PDB; 7R5J; EM; 50.00 A; A0/A1/A2/A3/A4/A5/A6=1-819. DR PDB; 7R5K; EM; 12.00 A; A0/A1/A2/A3/A4/A5/A6=1-819. DR PDBsum; 5IJN; -. DR PDBsum; 5IJO; -. DR PDBsum; 7MW0; -. DR PDBsum; 7MW1; -. DR PDBsum; 7PER; -. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR AlphaFoldDB; Q8N1F7; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; Q8N1F7; -. DR BioGRID; 115041; 266. DR ComplexPortal; CPX-873; Nuclear pore complex. DR CORUM; Q8N1F7; -. DR DIP; DIP-44020N; -. DR IntAct; Q8N1F7; 93. DR MINT; Q8N1F7; -. DR STRING; 9606.ENSP00000310668; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyCosmos; Q8N1F7; 3 sites, 1 glycan. DR GlyGen; Q8N1F7; 6 sites, 1 O-linked glycan (6 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; 9606-ENSP00000310668; -. DR PeptideAtlas; Q8N1F7; -. DR ProteomicsDB; 71593; -. [Q8N1F7-1] DR ProteomicsDB; 71594; -. [Q8N1F7-2] DR Pumba; Q8N1F7; -. DR Antibodypedia; 14851; 156 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 AGR; HGNC:28958; -. 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; 5475244at2759; -. 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; 771 hits in 1168 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 191 other cell types or tissues. DR ExpressionAtlas; Q8N1F7; baseline and differential. 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; NAS: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 InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96. DR PANTHER; PTHR11225:SF4; NUCLEAR PORE COMPLEX PROTEIN NUP93; 1. DR PANTHER; PTHR11225; NUCLEAR PORE COMPLEX PROTEIN NUP93 NUCLEOPORIN NUP93 DEAD EYE PROTEIN; 1. DR Pfam; PF04097; Nic96; 1. DR Genevisible; Q8N1F7; HS. 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" FT HELIX 180..197 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 205..210 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 211..215 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 218..230 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 241..246 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 248..275 FT /evidence="ECO:0007829|PDB:7MW0" FT TURN 278..280 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 289..300 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 318..327 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 331..339 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 342..345 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 348..357 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 359..361 FT /evidence="ECO:0007829|PDB:7MW1" FT HELIX 365..377 FT /evidence="ECO:0007829|PDB:7MW0" FT TURN 378..381 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 385..394 FT /evidence="ECO:0007829|PDB:7MW0" FT TURN 404..406 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 410..420 FT /evidence="ECO:0007829|PDB:7MW0" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 437..445 FT /evidence="ECO:0007829|PDB:7MW0" FT TURN 446..448 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 449..452 FT /evidence="ECO:0007829|PDB:7MW0" FT TURN 455..457 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 459..468 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 472..481 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 483..485 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 486..498 FT /evidence="ECO:0007829|PDB:7MW0" FT STRAND 506..510 FT /evidence="ECO:0007829|PDB:7MW0" FT STRAND 512..514 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 528..536 FT /evidence="ECO:0007829|PDB:7MW0" FT TURN 537..542 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 544..551 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 552..554 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 565..577 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 580..584 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 597..601 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 606..618 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 622..631 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 635..646 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 647..649 FT /evidence="ECO:0007829|PDB:7MW0" FT STRAND 650..652 FT /evidence="ECO:0007829|PDB:7MW1" FT HELIX 659..677 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 683..703 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 707..717 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 724..726 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 727..734 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 739..742 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 745..761 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 781..797 FT /evidence="ECO:0007829|PDB:7MW0" FT HELIX 804..816 FT /evidence="ECO:0007829|PDB:7MW0" 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 //