ID NUP93_HUMAN Reviewed; 819 AA. AC Q8N1F7; Q14705; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 18-APR-2012, entry version 85. 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]. RC TISSUE=Bone marrow; RX MEDLINE=95308325; 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], 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP CHARACTERIZATION. RX PubMed=9348540; 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 [4] 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-767, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, AND MASS RP SPECTROMETRY. 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-72, AND MASS RP SPECTROMETRY. 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] 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). CC -!- FUNCTION: Part of the nucleoporin complex; required for correct CC nuclear pore assembly. CC -!- SUBUNIT: Component of the p62 complex, a complex composed of NUP62 CC and NUP54. Forms a complex with NUP53, NUP155, NUP205 and lamin B; CC the interaction with NUP53 is direct. CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus CC membrane; Peripheral membrane protein (By similarity). CC Note=Localizes at the nuclear basket and at or near the nuclear CC entry to the gated channel of the pore. CC -!- SIMILARITY: Belongs to the nucleoporin interacting component (NIC) CC family. CC -!- SEQUENCE CAUTION: CC Sequence=BAA07680.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; 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; BC034346; AAH34346.1; -; mRNA. DR IPI; IPI00397904; -. DR RefSeq; NP_055484.3; NM_014669.4. DR UniGene; Hs.276878; -. DR ProteinModelPortal; Q8N1F7; -. DR SMR; Q8N1F7; 177-814. DR DIP; DIP-44020N; -. DR IntAct; Q8N1F7; 9. DR MINT; MINT-3039167; -. DR STRING; Q8N1F7; -. DR PhosphoSite; Q8N1F7; -. DR DMDM; 116242684; -. DR PRIDE; Q8N1F7; -. DR Ensembl; ENST00000308159; ENSP00000310668; ENSG00000102900. DR GeneID; 9688; -. DR KEGG; hsa:9688; -. DR UCSC; uc002eka.3; human. DR CTD; 9688; -. DR GeneCards; GC16P056764; -. DR H-InvDB; HIX0202270; -. DR HGNC; HGNC:28958; NUP93. DR HPA; HPA017937; -. DR MIM; 614351; gene. DR neXtProt; NX_Q8N1F7; -. DR PharmGKB; PA134912759; -. DR eggNOG; NOG312233; -. DR GeneTree; ENSGT00390000016353; -. DR HOGENOM; HBG314379; -. DR HOVERGEN; HBG052701; -. DR InParanoid; Q8N1F7; -. DR KO; K14309; -. DR OMA; FQVLFLT; -. DR OrthoDB; EOG4BRWK4; -. DR PhylomeDB; Q8N1F7; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR Reactome; REACT_6900; Immune System. DR NextBio; 36387; -. DR ArrayExpress; Q8N1F7; -. DR Bgee; Q8N1F7; -. DR CleanEx; HS_NUP93; -. DR Genevestigator; Q8N1F7; -. DR GermOnline; ENSG00000102900; Homo sapiens. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0015758; P:glucose transport; TAS:Reactome. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0010827; P:regulation of glucose transport; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0016032; P:viral reproduction; TAS:Reactome. DR InterPro; IPR007231; Nucleoporin_int_Nup93/Nic96. DR PANTHER; PTHR11225; NIC; 1. DR Pfam; PF04097; Nic96; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Membrane; mRNA transport; KW Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; KW Protein transport; Reference proteome; Translocation; Transport. FT CHAIN 1 819 Nuclear pore complex protein Nup93. FT /FTId=PRO_0000124782. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 52 52 Phosphoserine. FT MOD_RES 72 72 Phosphoserine. FT MOD_RES 430 430 Phosphoserine. FT MOD_RES 767 767 Phosphoserine. FT VARIANT 509 509 S -> R (in dbSNP:rs17853288). FT /FTId=VAR_028160. 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 //