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 02-NOV-2016, entry version 133. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. III. RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by RT analysis of 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA 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., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA 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 RP 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP CHARACTERIZATION. RX PubMed=9348540; DOI=10.1091/mbc.8.10.2017; RA Grandi P., Dang T., Pane N., Shevchenko A., Mann M., Forbes D., RA 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 RT assembly."; RL Mol. Biol. Cell 8:2017-2038(1997). RN [6] RP ABSENCE 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 RT periphery of 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 RT and Tpr as the architectural element of the nuclear basket."; RL Mol. Biol. Cell 15:4261-4277(2004). RN [8] RP FUNCTION, INTERACTION WITH NUP53, AND IDENTIFICATION IN A COMPLEX WITH RP 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 RT for the 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 RT the 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome 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; RP SER-72; SER-75; SER-80; SER-430 AND SER-767, AND IDENTIFICATION BY RP MASS 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 RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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., RA Pabst W.L., Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M., RA Tan W., Schapiro D., Rao J., Choi W.I., Hermle T., Kemper M.J., RA Pohl M., Ozaltin F., Konrad M., Bogdanovic R., Buescher R., RA Helmchen U., Serdaroglu E., Lifton R.P., 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). CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly CC and/or maintenance. May anchor nucleoporins, but not NUP153 and CC TPR, to the NPC. During renal development, regulates podocyte CC migration and proliferation through SMAD4 signaling CC (PubMed:26878725). {ECO:0000269|PubMed:15229283, CC ECO:0000269|PubMed:15703211, ECO:0000269|PubMed:26878725}. CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). Component of the CC p62 complex, a complex composed of NUP62 and NUP54. Forms a CC complex with NUP53, NUP155, NUP205 and lamin B; the interaction CC with NUP53 is direct. Does not interact with TPR. Interacts with CC SMAD4 and IPO7; translocates SMAD4 to the nucleus through the NPC CC upon BMP7 stimulation resulting in activation of SMAD4 signaling CC (PubMed:26878725). {ECO:0000269|PubMed:15229283, CC ECO:0000269|PubMed:15703211, ECO:0000269|PubMed:26878725}. CC -!- SUBCELLULAR LOCATION: Nucleus membrane CC {ECO:0000250|UniProtKB:Q66HC5}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q66HC5}. Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283}. CC Nucleus envelope {ECO:0000269|PubMed:26878725}. Note=Localizes at CC the nuclear basket and at or near the nuclear entry to the gated CC channel of the pore. 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 Note=No experimental confirmation available.; CC -!- DISEASE: Nephrotic syndrome 12 (NPHS12) [MIM:616892]: A form of CC nephrotic syndrome, a renal disease clinically characterized by CC severe proteinuria, resulting in complications such as CC hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show CC non-specific histologic changes such as focal segmental CC glomerulosclerosis and diffuse mesangial proliferation. Some CC affected individuals have an inherited steroid-resistant form and CC progress to end-stage renal failure. NPHS12 inheritance is CC autosomal recessive. {ECO:0000269|PubMed:26878725}. Note=The CC disease is caused by mutations affecting the gene represented in CC 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=Translation N-terminally shortened.; 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_001242796.1. [Q8N1F7-2] DR RefSeq; NP_055484.3; NM_014669.4. [Q8N1F7-1] DR RefSeq; XP_005256320.1; XM_005256263.3. [Q8N1F7-1] DR UniGene; Hs.276878; -. 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 PDBsum; 5IJN; -. DR PDBsum; 5IJO; -. DR ProteinModelPortal; Q8N1F7; -. DR SMR; Q8N1F7; -. DR BioGrid; 115041; 75. DR DIP; DIP-44020N; -. DR IntAct; Q8N1F7; 33. DR MINT; MINT-3039167; -. DR STRING; 9606.ENSP00000310668; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR iPTMnet; Q8N1F7; -. DR PhosphoSitePlus; Q8N1F7; -. DR SwissPalm; Q8N1F7; -. DR BioMuta; NUP93; -. DR DMDM; 116242684; -. DR EPD; Q8N1F7; -. DR MaxQB; Q8N1F7; -. DR PaxDb; Q8N1F7; -. DR PeptideAtlas; Q8N1F7; -. DR PRIDE; Q8N1F7; -. DR Ensembl; ENST00000308159; ENSP00000310668; ENSG00000102900. [Q8N1F7-1] DR Ensembl; ENST00000542526; ENSP00000440235; ENSG00000102900. [Q8N1F7-2] DR Ensembl; ENST00000564887; ENSP00000458039; ENSG00000102900. [Q8N1F7-2] DR GeneID; 9688; -. DR KEGG; hsa:9688; -. DR UCSC; uc002eka.4; human. [Q8N1F7-1] DR CTD; 9688; -. DR GeneCards; NUP93; -. DR HGNC; HGNC:28958; NUP93. DR HPA; HPA017937; -. DR MIM; 614351; gene. DR MIM; 616892; phenotype. DR neXtProt; NX_Q8N1F7; -. DR OpenTargets; ENSG00000102900; -. DR PharmGKB; PA134912759; -. DR eggNOG; KOG2168; Eukaryota. DR eggNOG; ENOG410XPN3; LUCA. DR GeneTree; ENSGT00390000016353; -. DR HOGENOM; HOG000007350; -. DR HOVERGEN; HBG052701; -. DR InParanoid; Q8N1F7; -. DR KO; K14309; -. DR PhylomeDB; Q8N1F7; -. DR TreeFam; TF315118; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. 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-168276; NS1 Mediated Effects on Host Pathways. DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis. 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-3108214; SUMOylation of DNA damage response and repair 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-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-6784531; tRNA processing in the nucleus. DR ChiTaRS; NUP93; human. DR GeneWiki; NUP93; -. DR GenomeRNAi; 9688; -. DR PRO; PR:Q8N1F7; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000102900; -. DR CleanEx; HS_NUP93; -. DR ExpressionAtlas; Q8N1F7; baseline and differential. DR Genevisible; Q8N1F7; HS. DR GO; GO:0016020; C:membrane; IDA: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:0031047; P:gene silencing by RNA; TAS:Reactome. DR GO; GO:0072015; P:glomerular visceral epithelial cell development; IMP:UniProtKB. DR GO; GO:0090521; P:glomerular visceral epithelial cell migration; IMP:UniProtKB. DR GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome. DR GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome. DR GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome. DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; 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:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central. DR GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; IDA:UniProtKB. DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central. DR GO; GO:0016925; P:protein sumoylation; TAS:Reactome. DR GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome. DR GO; GO:0010827; P:regulation of glucose transport; TAS:Reactome. DR GO; GO:0072001; P:renal system development; ISS:UniProtKB. DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB. DR GO; GO:0006409; P:tRNA export from nucleus; TAS:Reactome. DR GO; GO:0016032; P:viral process; TAS:Reactome. DR GO; GO:0019083; P:viral transcription; TAS:Reactome. 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; Complete proteome; KW Disease mutation; Membrane; mRNA transport; Nuclear pore complex; KW Nucleus; Phosphoprotein; Polymorphism; Protein transport; KW Reference proteome; Translocation; Transport. FT CHAIN 1 819 Nuclear pore complex protein Nup93. FT /FTId=PRO_0000124782. FT MOD_RES 49 49 Phosphothreonine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 52 52 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 66 66 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 72 72 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 75 75 Phosphoserine. FT {ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 80 80 Phosphoserine. FT {ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 430 430 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 767 767 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT VAR_SEQ 1 123 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043117. FT VARIANT 388 388 R -> W (in NPHS12; doesnt affect nuclear FT envelope localization; impairs nuclear FT pore complex assembly; doesn't abrogate FT interaction with NUP205; doesn't affect FT SMAD4 interaction; doesn't affect IPO7 FT interaction; impairs SMAD4 protein import FT into nucleus; impairs SMAD4 protein FT signal transduction; dbSNP:rs145146218). FT {ECO:0000269|PubMed:26878725}. FT /FTId=VAR_076473. FT VARIANT 509 509 S -> R (in dbSNP:rs17853288). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_028160. FT VARIANT 591 591 G -> V (in NPHS12; doesnt affect nuclear FT envelope localization; doesn't affect FT nuclear pore complex assembly; doesn't FT abrogate interaction with NUP205; FT abrogates SMAD4 interaction; abrogates FT IPO7 interaction; impairs SMAD4 protein FT import into nucleus; impairs SMAD4 FT protein signal transduction; FT dbSNP:rs145473779). FT {ECO:0000269|PubMed:26878725}. FT /FTId=VAR_076474. FT VARIANT 629 629 Y -> C (in NPHS12; doesnt affect nuclear FT envelope localization; doesn't affect FT nuclear pore complex assembly; doesn't FT abrogate interaction with NUP205; FT abrogates SMAD4 interaction; abrogates FT IPO7 interaction; impairs SMAD4 protein FT import; impairs SMAD4 protein signal FT transduction into nucleus;; FT dbSNP:rs757674160). FT {ECO:0000269|PubMed:26878725}. FT /FTId=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 //