ID NU214_HUMAN Reviewed; 2090 AA. AC P35658; A6NFQ0; Q15010; Q3KQZ0; Q5JUP7; Q75R47; Q86XD3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 27-MAR-2024, entry version 223. DE RecName: Full=Nuclear pore complex protein Nup214; DE AltName: Full=214 kDa nucleoporin; DE AltName: Full=Nucleoporin Nup214; DE AltName: Full=Protein CAN; GN Name=NUP214; Synonyms=CAIN, CAN, KIAA0023; 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 [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH DEK, RP AND VARIANT SER-574. RC TISSUE=Testis; RX PubMed=1549122; DOI=10.1128/mcb.12.4.1687-1697.1992; RA Von Lindern M., Fornerod M., Van Baal S., Jaegle M., De Wit T., Buijs A., RA Grosveld G.; RT "The translocation (6;9), associated with a specific subtype of acute RT myeloid leukemia, results in the fusion of two genes, dek and can, and the RT expression of a chimeric, leukemia-specific dek-can mRNA."; RL Mol. Cell. Biol. 12:1687-1697(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Nagase T., Kikuno R., Ohara O.; RT "Homo sapiens mRNA for KIAA0023 splice variant 1 protein."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT RP SER-574. RC TISSUE=Placenta, and Testis; 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 [6] RP CHROMOSOMAL TRANSLOCATION WITH SET. RX PubMed=1630450; DOI=10.1128/mcb.12.8.3346-3355.1992; RA von Lindern M., van Baal S., Wiegant J., Raap A., Hagemeijer A., RA Grosveld G.; RT "Can, a putative oncogene associated with myeloid leukemogenesis, may be RT activated by fusion of its 3' half to different genes: characterization of RT the set gene."; RL Mol. Cell. Biol. 12:3346-3355(1992). RN [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8108440; DOI=10.1073/pnas.91.4.1519; RA Kraemer D., Wozniak R.W., Blobel G., Radu A.; RT "The human CAN protein, a putative oncogene product associated with myeloid RT leukemogenesis, is a nuclear pore complex protein that faces the RT cytoplasm."; RL Proc. Natl. Acad. Sci. U.S.A. 91:1519-1523(1994). RN [8] RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND INTERACTION WITH RP NUP88 AND XPO1. RX PubMed=9049309; DOI=10.1093/emboj/16.4.807; RA Fornerod M., van Deursen J.M., van Baal S., Reynolds A., Davis D., RA Murti K.G., Fransen J., Grosveld G.; RT "The human homologue of yeast CRM1 is in a dynamic subcomplex with RT CAN/Nup214 and the novel nuclear pore component Nup88."; RL EMBO J. 16:807-816(1997). RN [9] RP INTERACTION WITH XPO5. RX PubMed=11777942; DOI=10.1083/jcb.200110082; RA Brownawell A.M., Macara I.G.; RT "Exportin-5, a novel karyopherin, mediates nuclear export of double- RT stranded RNA binding proteins."; RL J. Cell Biol. 156:53-64(2002). RN [10] RP INTERACTION WITH ZFP36. RX PubMed=14766228; DOI=10.1016/j.bbrc.2004.01.080; RA Carman J.A., Nadler S.G.; RT "Direct association of tristetraprolin with the nucleoporin CAN/Nup214."; RL Biochem. Biophys. Res. Commun. 315:445-449(2004). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430 AND THR-439, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; SER-940 AND SER-1181, RP AND 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; THR-434; THR-437; RP THR-439; SER-666; SER-970; SER-974; SER-1023 AND SER-1963, 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 [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP INTERACTION WITH HHV-1 PROTEIN UL25 (MICROBIAL INFECTION). RX PubMed=19386703; DOI=10.1128/jvi.02655-08; RA Pasdeloup D., Blondel D., Isidro A.L., Rixon F.J.; RT "Herpesvirus capsid association with the nuclear pore complex and viral DNA RT release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25."; RL J. Virol. 83:6610-6623(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430 AND SER-989, AND 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657; THR-670; SER-678; RP SER-940; SER-1045; SER-1081; THR-1134; THR-1150; THR-1156; THR-1312 AND RP SER-1985, AND 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 [20] 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; THR-434; THR-437; RP SER-657; THR-670; SER-678 AND SER-940, AND IDENTIFICATION BY MASS RP 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 [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-416; SER-421; RP SER-430; SER-433; THR-434; THR-437; SER-651; SER-657; SER-666; THR-670; RP SER-678; SER-760; SER-940; THR-1021; SER-1023; SER-1045; SER-1056; RP SER-1081; THR-1156 AND SER-1353, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-433 AND SER-678, AND RP IDENTIFICATION 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., 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 [25] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HADV-5 PROTEIN L3, AND RP REGION. RX PubMed=25410864; DOI=10.1128/jvi.02639-14; RA Cassany A., Ragues J., Guan T., Begu D., Wodrich H., Kann M., Nemerow G.R., RA Gerace L.; RT "Nuclear import of adenovirus DNA involves direct interaction of hexon with RT an N-terminal domain of the nucleoporin Nup214."; RL J. Virol. 89:1719-1730(2015). RN [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1538, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [27] RP INTERACTION WITH NUP88. RX PubMed=30543681; DOI=10.1371/journal.pgen.1007845; RA Bonnin E., Cabochette P., Filosa A., Juehlen R., Komatsuzaki S., RA Hezwani M., Dickmanns A., Martinelli V., Vermeersch M., Supply L., RA Martins N., Pirenne L., Ravenscroft G., Lombard M., Port S., Spillner C., RA Janssens S., Roets E., Van Dorpe J., Lammens M., Kehlenbach R.H., RA Ficner R., Laing N.G., Hoffmann K., Vanhollebeke B., Fahrenkrog B.; RT "Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia RT deformation sequence."; RL PLoS Genet. 14:E1007845-E1007845(2018). RN [28] RP FUNCTION, INVOLVEMENT IN IIAE9, VARIANTS IIAE9 CYS-38 AND SER-387, AND RP CHARACTERIZATION OF VARIANT IIAE9 CYS-38. RX PubMed=31178128; DOI=10.1016/j.ajhg.2019.05.003; RA Fichtman B., Harel T., Biran N., Zagairy F., Applegate C.D., Salzberg Y., RA Gilboa T., Salah S., Shaag A., Simanovsky N., Ayoubieh H., Sobreira N., RA Punzi G., Pierri C.L., Hamosh A., Elpeleg O., Harel A., Edvardson S.; RT "Pathogenic variants in NUP214 cause 'plugged' nuclear pore channels and RT acute febrile encephalopathy."; RL Am. J. Hum. Genet. 105:48-64(2019). RN [29] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-434, AND BETA-PROPELLER DOMAIN. RX PubMed=17264208; DOI=10.1073/pnas.0610828104; RA Napetschnig J., Blobel G., Hoelz A.; RT "Crystal structure of the N-terminal domain of the human protooncogene RT Nup214/CAN."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1783-1788(2007). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-405 IN COMPLEX WITH DDX19B, AND RP MUTAGENESIS OF VAL-353 AND ASP-359. RX PubMed=19219046; DOI=10.1038/nsmb.1561; RA von Moeller H., Basquin C., Conti E.; RT "The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin RT NUP214 in a mutually exclusive manner."; RL Nat. Struct. Mol. Biol. 16:247-254(2009). RN [31] RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 1-450 IN COMPLEX WITH DDX19B, AND RP COILED-COIL DOMAIN. RX PubMed=19208808; DOI=10.1073/pnas.0813267106; RA Napetschnig J., Kassube S.A., Debler E.W., Wong R.W., Blobel G., Hoelz A.; RT "Structural and functional analysis of the interaction between the RT nucleoporin Nup214 and the DEAD-box helicase Ddx19."; RL Proc. Natl. Acad. Sci. U.S.A. 106:3089-3094(2009). RN [32] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH ABL1. RX PubMed=15361874; DOI=10.1038/ng1425; RA Graux C., Cools J., Melotte C., Quentmeier H., Ferrando A., Levine R., RA Vermeesch J.R., Stul M., Dutta B., Boeckx N., Bosly A., Heimann P., RA Uyttebroeck A., Mentens N., Somers R., MacLeod R.A., Drexler H.G., RA Look A.T., Gilliland D.G., Michaux L., Vandenberghe P., Wlodarska I., RA Marynen P., Hagemeijer A.; RT "Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute RT lymphoblastic leukemia."; RL Nat. Genet. 36:1084-1089(2004). RN [33] RP VARIANTS [LARGE SCALE ANALYSIS] ALA-424; LEU-1378 AND VAL-1392. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [34] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH SQSTM1. RX PubMed=20851865; DOI=10.3324/haematol.2010.029769; RA Gorello P., La Starza R., Di Giacomo D., Messina M., Puzzolo M.C., RA Crescenzi B., Santoro A., Chiaretti S., Mecucci C.; RT "SQSTM1-NUP214: a new gene fusion in adult T-cell acute lymphoblastic RT leukemia."; RL Haematologica 95:2161-2163(2010). RN [35] RP VARIANT IIAE9 GLY-154, AND INVOLVEMENT IN IIAE9. RX PubMed=30758658; DOI=10.1007/s00439-019-01979-w; RA Shamseldin H.E., Makhseed N., Ibrahim N., Al-Sheddi T., Alobeid E., RA Abdulwahab F., Alkuraya F.S.; RT "NUP214 deficiency causes severe encephalopathy and microcephaly in RT humans."; RL Hum. Genet. 138:221-229(2019). CC -!- FUNCTION: Part of the nuclear pore complex (PubMed:9049309). Has a CC critical role in nucleocytoplasmic transport (PubMed:31178128). May CC serve as a docking site in the receptor-mediated import of substrates CC across the nuclear pore complex (PubMed:31178128, PubMed:8108440). CC {ECO:0000269|PubMed:31178128, ECO:0000269|PubMed:9049309, CC ECO:0000303|PubMed:8108440}. CC -!- FUNCTION: (Microbial infection) Required for capsid disassembly of the CC human adenovirus 5 (HadV-5) leading to release of the viral genome to CC the nucleus (in vitro). {ECO:0000269|PubMed:25410864}. CC -!- SUBUNIT: Homodimer. Part of the nuclear pore complex (NPC) CC (PubMed:9049309). Interacts with NUP88 (PubMed:9049309, CC PubMed:30543681). Interacts with ZFP36; this interaction increases upon CC lipopolysaccharide (LPS) stimulation (PubMed:14766228). Interacts with CC DDX19 (PubMed:19219046, PubMed:19208808). Interacts with XPO1 CC (PubMed:9049309). Interacts with XPO5 (PubMed:11777942). CC {ECO:0000269|PubMed:11777942, ECO:0000269|PubMed:14766228, CC ECO:0000269|PubMed:19208808, ECO:0000269|PubMed:19219046, CC ECO:0000269|PubMed:30543681, ECO:0000269|PubMed:9049309}. CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 1 CC (HHV-1) protein UL25; this interaction might be essential to the capsid CC docking onto the host nuclear pore. {ECO:0000269|PubMed:19386703}. CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus) with human CC adenovirus 5 (HAdV-5) protein L3 (hexon); this interaction might be CC essential for the release of the virus genome to the nucleus. CC {ECO:0000269|PubMed:25410864}. CC -!- INTERACTION: CC P35658-1; Q9UMR2-1: DDX19B; NbExp=9; IntAct=EBI-15757000, EBI-5773937; CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:8108440}. Note=Cytoplasmic side of the nuclear pore CC complex. {ECO:0000269|PubMed:8108440}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P35658-1; Sequence=Displayed; CC Name=2; CC IsoId=P35658-2; Sequence=VSP_034896; CC Name=3; CC IsoId=P35658-3; Sequence=VSP_034897; CC Name=4; CC IsoId=P35658-4; Sequence=VSP_034896, VSP_034897; CC Name=5; CC IsoId=P35658-5; Sequence=VSP_034896, VSP_034898, VSP_034899; CC -!- TISSUE SPECIFICITY: Expressed in thymus, spleen, bone marrow, kidney, CC brain and testis, but hardly in all other tissues or in whole embryos CC during development. CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for CC karyopherins (importins, exportins) and form probably an affinity CC gradient, guiding the transport proteins unidirectionally with their CC cargo through the NPC. FG repeat regions are highly flexible and lack CC ordered secondary structure. The overall conservation of FG repeats CC regarding exact sequence, spacing, and repeat unit length is limited. CC {ECO:0000305}. CC -!- DOMAIN: The beta-propeller contains long interblade connector loops, CC and mediates interaction with DDX19B. CC -!- PTM: Probably glycosylated as it reacts with wheat germ agglutinin CC (WGA). CC -!- DISEASE: Note=A chromosomal aberration involving NUP214 is found in a CC subset of acute myeloid leukemia (AML); also known as acute non- CC lymphocytic leukemia. Translocation t(6;9)(p23;q34) with DEK. It CC results in the formation of a DEK-CAN fusion gene. CC {ECO:0000269|PubMed:1549122}. CC -!- DISEASE: Note=A chromosomal aberration involving NUP214 is found in CC some cases of acute undifferentiated leukemia (AUL). Translocation CC t(6;9)(q21;q34.1) with SET. {ECO:0000269|PubMed:1630450}. CC -!- DISEASE: Encephalopathy, acute, infection-induced, 9 (IIAE9) CC [MIM:618426]: An autosomal recessive disorder characterized by infancy- CC onset of episodic neurodevelopmental regression in association with CC infection-induced febrile illness. Clinical features include poor CC overall growth, seizures, myoclonic jerks, microcephaly, ataxia, and CC cerebellar atrophy. {ECO:0000269|PubMed:30758658, CC ECO:0000269|PubMed:31178128}. Note=Disease susceptibility is associated CC with variants affecting the gene represented in this entry. CC -!- DISEASE: Note=Chromosomal aberrations involving NUP214 are found in CC acute lymphoblastic leukemia (PubMed:20851865, PubMed:15361874). CC Translocation t(9;9)(q34;q34) with ABL1 (PubMed:15361874). CC Translocation t(5;9)(q35;q34) with SQSTM1 (PubMed:20851865). CC {ECO:0000269|PubMed:15361874, ECO:0000269|PubMed:20851865}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD07398.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/29/CAN"; 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; X64228; CAA45535.1; -; mRNA. DR EMBL; AB159230; BAD07398.1; ALT_INIT; mRNA. DR EMBL; D14689; BAA03515.1; -; mRNA. DR EMBL; AL157938; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC045620; AAH45620.2; -; mRNA. DR EMBL; BC105998; AAI05999.1; -; mRNA. DR CCDS; CCDS6940.1; -. [P35658-1] DR CCDS; CCDS83429.1; -. [P35658-4] DR PIR; S26058; S26058. DR RefSeq; NP_001305253.1; NM_001318324.1. [P35658-4] DR RefSeq; NP_001305254.1; NM_001318325.1. DR RefSeq; NP_005076.3; NM_005085.3. [P35658-1] DR PDB; 2OIT; X-ray; 1.65 A; A=1-434. DR PDB; 3FHC; X-ray; 2.80 A; A=1-405. DR PDB; 3FMO; X-ray; 2.51 A; A=1-450. DR PDB; 3FMP; X-ray; 3.19 A; A/C=1-450. DR PDB; 5DIS; X-ray; 2.85 A; D=1916-2027. DR PDB; 7R5J; EM; 50.00 A; V0=1-2090. DR PDB; 7R5K; EM; 12.00 A; V0=1-2090. DR PDBsum; 2OIT; -. DR PDBsum; 3FHC; -. DR PDBsum; 3FMO; -. DR PDBsum; 3FMP; -. DR PDBsum; 5DIS; -. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR AlphaFoldDB; P35658; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; P35658; -. DR BioGRID; 113717; 183. DR ComplexPortal; CPX-873; Nuclear pore complex. DR DIP; DIP-38367N; -. DR IntAct; P35658; 81. DR MINT; P35658; -. DR STRING; 9606.ENSP00000352400; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyConnect; 2843; 1 O-GlcNAc glycan (4 sites). DR GlyCosmos; P35658; 176 sites, 2 glycans. DR GlyGen; P35658; 213 sites, 2 O-linked glycans (213 sites). DR iPTMnet; P35658; -. DR MetOSite; P35658; -. DR PhosphoSitePlus; P35658; -. DR SwissPalm; P35658; -. DR BioMuta; NUP214; -. DR DMDM; 205831380; -. DR EPD; P35658; -. DR jPOST; P35658; -. DR MassIVE; P35658; -. DR MaxQB; P35658; -. DR PaxDb; 9606-ENSP00000352400; -. DR PeptideAtlas; P35658; -. DR ProteomicsDB; 55122; -. [P35658-1] DR ProteomicsDB; 55123; -. [P35658-2] DR ProteomicsDB; 55124; -. [P35658-3] DR ProteomicsDB; 55125; -. [P35658-4] DR ProteomicsDB; 55126; -. [P35658-5] DR Pumba; P35658; -. DR Antibodypedia; 18059; 122 antibodies from 19 providers. DR DNASU; 8021; -. DR Ensembl; ENST00000359428.10; ENSP00000352400.5; ENSG00000126883.19. [P35658-1] DR Ensembl; ENST00000411637.6; ENSP00000396576.2; ENSG00000126883.19. [P35658-4] DR GeneID; 8021; -. DR KEGG; hsa:8021; -. DR MANE-Select; ENST00000359428.10; ENSP00000352400.5; NM_005085.4; NP_005076.3. DR UCSC; uc004cag.4; human. [P35658-1] DR AGR; HGNC:8064; -. DR CTD; 8021; -. DR DisGeNET; 8021; -. DR GeneCards; NUP214; -. DR HGNC; HGNC:8064; NUP214. DR HPA; ENSG00000126883; Tissue enhanced (testis). DR MalaCards; NUP214; -. DR MIM; 114350; gene. DR MIM; 618426; phenotype. DR neXtProt; NX_P35658; -. DR OpenTargets; ENSG00000126883; -. DR Orphanet; 402014; Acute myeloid leukemia with t(6;9)(p23;q34). DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia. DR PharmGKB; PA31851; -. DR VEuPathDB; HostDB:ENSG00000126883; -. DR eggNOG; KOG3630; Eukaryota. DR GeneTree; ENSGT00940000153253; -. DR HOGENOM; CLU_001606_0_0_1; -. DR InParanoid; P35658; -. DR OMA; WLSTFQF; -. DR OrthoDB; 2883156at2759; -. DR PhylomeDB; P35658; -. DR TreeFam; TF323517; -. DR PathwayCommons; P35658; -. 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-450520; HuR (ELAVL1) binds and stabilizes mRNA. 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-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR SignaLink; P35658; -. DR SIGNOR; P35658; -. DR BioGRID-ORCS; 8021; 739 hits in 1160 CRISPR screens. DR ChiTaRS; NUP214; human. DR EvolutionaryTrace; P35658; -. DR GeneWiki; NUP214; -. DR GenomeRNAi; 8021; -. DR Pharos; P35658; Tbio. DR PRO; PR:P35658; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P35658; Protein. DR Bgee; ENSG00000126883; Expressed in left testis and 164 other cell types or tissues. DR ExpressionAtlas; P35658; baseline and differential. DR GO; GO:1990876; C:cytoplasmic side of nuclear pore; IDA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal. DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:GO_Central. DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central. DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central. DR GO; GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal. DR GO; GO:0006611; P:protein export from nucleus; IMP:MGI. DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central. DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl. DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:UniProtKB. DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR026054; Nucleoporin. DR InterPro; IPR041553; Nup214_FG. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR23193; NUCLEAR PORE COMPLEX PROTEIN NUP; 1. DR PANTHER; PTHR23193:SF21; NUCLEAR PORE COMPLEX PROTEIN NUP214; 1. DR Pfam; PF18617; Nup214_FG; 1. DR SMART; SM00320; WD40; 2. DR SUPFAM; SSF117289; Nucleoporin domain; 1. DR Genevisible; P35658; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement; KW Coiled coil; Disease variant; Glycoprotein; Host-virus interaction; KW Isopeptide bond; mRNA transport; Nuclear pore complex; Nucleus; KW Phosphoprotein; Protein transport; Proto-oncogene; Reference proteome; KW Repeat; Translocation; Transport; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..2090 FT /note="Nuclear pore complex protein Nup214" FT /id="PRO_0000204861" FT REPEAT 41..93 FT /note="Blade 1" FT REPEAT 94..150 FT /note="Blade 2" FT REPEAT 151..193 FT /note="Blade 3" FT REPEAT 194..239 FT /note="Blade 4" FT REPEAT 240..303 FT /note="Blade 5" FT REPEAT 304..359 FT /note="Blade 6" FT REPEAT 360..404 FT /note="Blade 7" FT REPEAT 484..485 FT /note="1" FT /evidence="ECO:0000305" FT REPEAT 548..549 FT /note="2" FT /evidence="ECO:0000305" FT REPEAT 1225..1226 FT /note="3" FT /evidence="ECO:0000305" FT REPEAT 1411..1412 FT /note="4" FT /evidence="ECO:0000305" FT REPEAT 1427..1428 FT /note="5" FT /evidence="ECO:0000305" FT REPEAT 1441..1442 FT /note="6" FT /evidence="ECO:0000305" FT REPEAT 1473..1474 FT /note="7" FT /evidence="ECO:0000305" FT REPEAT 1635..1636 FT /note="8" FT /evidence="ECO:0000305" FT REPEAT 1674..1675 FT /note="9" FT /evidence="ECO:0000305" FT REPEAT 1686..1687 FT /note="10" FT /evidence="ECO:0000305" FT REPEAT 1713..1714 FT /note="11" FT /evidence="ECO:0000305" FT REPEAT 1721..1722 FT /note="12" FT /evidence="ECO:0000305" FT REPEAT 1726..1727 FT /note="13" FT /evidence="ECO:0000305" FT REPEAT 1732..1733 FT /note="14" FT /evidence="ECO:0000305" FT REPEAT 1756..1757 FT /note="15" FT /evidence="ECO:0000305" FT REPEAT 1772..1773 FT /note="16" FT /evidence="ECO:0000305" FT REPEAT 1786..1787 FT /note="17" FT /evidence="ECO:0000305" FT REPEAT 1798..1799 FT /note="18" FT /evidence="ECO:0000305" FT REPEAT 1806..1807 FT /note="19" FT /evidence="ECO:0000305" FT REPEAT 1812..1813 FT /note="20" FT /evidence="ECO:0000305" FT REPEAT 1819..1820 FT /note="21" FT /evidence="ECO:0000305" FT REPEAT 1842..1843 FT /note="22" FT /evidence="ECO:0000305" FT REPEAT 1851..1852 FT /note="23" FT /evidence="ECO:0000305" FT REPEAT 1862..1863 FT /note="24" FT /evidence="ECO:0000305" FT REPEAT 1874..1875 FT /note="25" FT /evidence="ECO:0000305" FT REPEAT 1910..1911 FT /note="26" FT /evidence="ECO:0000305" FT REPEAT 1922..1923 FT /note="27" FT /evidence="ECO:0000305" FT REPEAT 1930..1931 FT /note="28" FT /evidence="ECO:0000305" FT REPEAT 1938..1939 FT /note="29" FT /evidence="ECO:0000305" FT REPEAT 1959..1960 FT /note="30" FT /evidence="ECO:0000305" FT REPEAT 1970..1971 FT /note="31" FT /evidence="ECO:0000305" FT REPEAT 1976..1977 FT /note="32" FT /evidence="ECO:0000305" FT REPEAT 1982..1983 FT /note="33" FT /evidence="ECO:0000305" FT REPEAT 1988..1989 FT /note="34" FT /evidence="ECO:0000305" FT REPEAT 1994..1995 FT /note="35" FT /evidence="ECO:0000305" FT REPEAT 2012..2013 FT /note="36" FT /evidence="ECO:0000305" FT REPEAT 2024..2025 FT /note="37" FT /evidence="ECO:0000305" FT REPEAT 2026..2027 FT /note="38" FT /evidence="ECO:0000305" FT REPEAT 2035..2036 FT /note="39" FT /evidence="ECO:0000305" FT REPEAT 2046..2047 FT /note="40" FT /evidence="ECO:0000305" FT REPEAT 2056..2057 FT /note="41" FT /evidence="ECO:0000305" FT REPEAT 2066..2067 FT /note="42" FT /evidence="ECO:0000305" FT REPEAT 2075..2076 FT /note="43" FT /evidence="ECO:0000305" FT REPEAT 2085..2086 FT /note="44" FT /evidence="ECO:0000305" FT REGION 41..404 FT /note="Seven-bladed beta propeller" FT REGION 236..1418 FT /note="44 X 2 AA repeats of F-G" FT /evidence="ECO:0000305" FT REGION 422..460 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 450..586 FT /note="(Microbial infection) Binds human adenovirus 5 FT (HAdV-5) protein L3 (hexon)" FT /evidence="ECO:0000269|PubMed:25410864" FT REGION 481..2076 FT /note="11 X 5 AA approximate repeats" FT REGION 489..536 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 597..700 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 740..768 FT /note="Leucine-zipper 1" FT REGION 861..882 FT /note="Leucine-zipper 2" FT REGION 987..1009 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1128..1152 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1168..1213 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1234..1316 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1337..1408 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1409..2084 FT /note="18 X 4 AA approximate repeats" FT REGION 1427..2085 FT /note="11 X 3 AA approximate repeats" FT REGION 1438..1467 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1479..1539 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1884..1903 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 680..1209 FT /evidence="ECO:0000269|PubMed:19208808" FT COMPBIAS 427..447 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 489..515 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 597..621 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 635..664 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1128..1149 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1234..1258 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1271..1313 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1339..1372 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1386..1408 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1479..1499 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1514..1539 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 444..445 FT /note="Breakpoint for translocation to form the NUP214-ABL1 FT fusion protein" FT /evidence="ECO:0000269|PubMed:15361874" FT SITE 812..813 FT /note="Breakpoint" FT SITE 1840..1841 FT /note="Breakpoint for translocation to form the NUP214-ABL1 FT fusion protein" FT /evidence="ECO:0000269|PubMed:15361874" FT SITE 1916..1917 FT /note="Breakpoint for translocation to form the NUP214-ABL1 FT fusion protein" FT /evidence="ECO:0000269|PubMed:15361874" FT SITE 1967..1968 FT /note="Breakpoint for translocation to form the NUP214-ABL1 FT fusion protein" FT /evidence="ECO:0000269|PubMed:15361874" FT SITE 1967..1968 FT /note="Breakpoint for translocation to form the NUP214- FT SQSTM1 fusion protein" FT /evidence="ECO:0000269|PubMed:20851865" FT SITE 2071..2072 FT /note="Breakpoint for translocation to form the NUP214-ABL1 FT fusion protein" FT /evidence="ECO:0000269|PubMed:15361874" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 416 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 430 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 433 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 434 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 437 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 439 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:23186163" FT MOD_RES 657 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 666 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 670 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 678 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 760 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 940 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 970 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 974 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 989 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1021 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1023 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1045 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1056 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1081 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1134 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1150 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1156 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1181 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 1312 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1353 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1963 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1985 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT CROSSLNK 1538 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 590..601 FT /note="KFTAAATSTPVS -> N (in isoform 2, isoform 4 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7584026" FT /id="VSP_034896" FT VAR_SEQ 648 FT /note="S -> SA (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_034897" FT VAR_SEQ 1139..1148 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:7584026" FT /id="VSP_034898" FT VAR_SEQ 2026..2090 FT /note="FGSSSNTTSFGTLASQNAPTFGSLSQQTSGFGTQSSGFSGFGSGTGGFSFGS FT NNSSVQGFGGWRS -> SLAMSLSPTLKGRLLLMRPKAGGGREQAAPGRKSNESRSLGH FT LCMERALTSPLKVWEQQQHHILRHARESECPHFRITVPTDFWFWDPE (in isoform FT 5)" FT /evidence="ECO:0000303|PubMed:7584026" FT /id="VSP_034899" FT VARIANT 38 FT /note="R -> C (in IIAE9; decreased nuclear transport in FT patient cells; decreased protein levels in patient cells; FT dbSNP:rs143595616)" FT /evidence="ECO:0000269|PubMed:31178128" FT /id="VAR_082629" FT VARIANT 154 FT /note="D -> G (in IIAE9; uncertain significance; FT dbSNP:rs1564175808)" FT /evidence="ECO:0000269|PubMed:30758658" FT /id="VAR_082630" FT VARIANT 387 FT /note="P -> S (in IIAE9; dbSNP:rs563025075)" FT /evidence="ECO:0000269|PubMed:31178128" FT /id="VAR_082631" FT VARIANT 424 FT /note="G -> A (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035856" FT VARIANT 574 FT /note="P -> S (in dbSNP:rs103612)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:1549122" FT /id="VAR_045691" FT VARIANT 1378 FT /note="P -> L (in a breast cancer sample; somatic mutation; FT dbSNP:rs777822003)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035857" FT VARIANT 1392 FT /note="A -> V (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035858" FT VARIANT 1592 FT /note="G -> A (in dbSNP:rs28594669)" FT /id="VAR_061533" FT MUTAGEN 353 FT /note="V->A: Reduced binding to DDX19B." FT /evidence="ECO:0000269|PubMed:19219046" FT MUTAGEN 359 FT /note="D->R: Impairs interaction with DDX19B." FT /evidence="ECO:0000269|PubMed:19219046" FT CONFLICT 149 FT /note="G -> A (in Ref. 1; CAA45535)" FT /evidence="ECO:0000305" FT CONFLICT 175 FT /note="A -> D (in Ref. 1; CAA45535)" FT /evidence="ECO:0000305" FT CONFLICT 1091..1092 FT /note="AA -> QL (in Ref. 1; CAA45535)" FT /evidence="ECO:0000305" FT CONFLICT 1872 FT /note="S -> N (in Ref. 5; AAH45620)" FT /evidence="ECO:0000305" FT STRAND 4..7 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 11..21 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:2OIT" FT TURN 46..49 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 58..63 FT /evidence="ECO:0007829|PDB:2OIT" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 95..100 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 106..113 FT /evidence="ECO:0007829|PDB:2OIT" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 117..124 FT /evidence="ECO:0007829|PDB:2OIT" FT HELIX 125..129 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:2OIT" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 151..157 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 174..189 FT /evidence="ECO:0007829|PDB:2OIT" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 195..200 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 207..211 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 225..229 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:3FMO" FT STRAND 241..250 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 253..260 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 270..275 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 286..289 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 305..310 FT /evidence="ECO:0007829|PDB:2OIT" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 315..320 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:3FMO" FT STRAND 327..331 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 338..343 FT /evidence="ECO:0007829|PDB:2OIT" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:3FMP" FT STRAND 362..368 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 375..378 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 381..383 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:2OIT" FT STRAND 396..405 FT /evidence="ECO:0007829|PDB:2OIT" FT HELIX 1925..1929 FT /evidence="ECO:0007829|PDB:5DIS" FT STRAND 1937..1941 FT /evidence="ECO:0007829|PDB:5DIS" FT TURN 1943..1945 FT /evidence="ECO:0007829|PDB:5DIS" FT HELIX 2016..2019 FT /evidence="ECO:0007829|PDB:5DIS" SQ SEQUENCE 2090 AA; 213620 MW; EE6F0F3DE3D522C6 CRC64; MGDEMDAMIP EREMKDFQFR ALKKVRIFDS PEELPKERSS LLAVSNKYGL VFAGGASGLQ IFPTKNLLIQ NKPGDDPNKI VDKVQGLLVP MKFPIHHLAL SCDNLTLSAC MMSSEYGSII AFFDVRTFSN EAKQQKRPFA YHKLLKDAGG MVIDMKWNPT VPSMVAVCLA DGSIAVLQVT ETVKVCATLP STVAVTSVCW SPKGKQLAVG KQNGTVVQYL PTLQEKKVIP CPPFYESDHP VRVLDVLWIG TYVFAIVYAA ADGTLETSPD VVMALLPKKE EKHPEIFVNF MEPCYGSCTE RQHHYYLSYI EEWDLVLAAS AASTEVSILA RQSDQINWES WLLEDSSRAE LPVTDKSDDS LPMGVVVDYT NQVEITISDE KTLPPAPVLM LLSTDGVLCP FYMINQNPGV KSLIKTPERL SLEGERQPKS PGSTPTTPTS SQAPQKLDAS AAAAPASLPP SSPAAPIATF SLLPAGGAPT VFSFGSSSLK SSATVTGEPP SYSSGSDSSK AAPGPGPSTF SFVPPSKASL APTPAASPVA PSAASFSFGS SGFKPTLEST PVPSVSAPNI AMKPSFPPST SAVKVNLSEK FTAAATSTPV SSSQSAPPMS PFSSASKPAA SGPLSHPTPL SAPPSSVPLK SSVLPSPSGR SAQGSSSPVP SMVQKSPRIT PPAAKPGSPQ AKSLQPAVAE KQGHQWKDSD PVMAGIGEEI AHFQKELEEL KARTSKACFQ VGTSEEMKML RTESDDLHTF LLEIKETTES LHGDISSLKT TLLEGFAGVE EAREQNERNR DSGYLHLLYK RPLDPKSEAQ LQEIRRLHQY VKFAVQDVND VLDLEWDQHL EQKKKQRHLL VPERETLFNT LANNREIINQ QRKRLNHLVD SLQQLRLYKQ TSLWSLSSAV PSQSSIHSFD SDLESLCNAL LKTTIESHTK SLPKVPAKLS PMKQAQLRNF LAKRKTPPVR STAPASLSRS AFLSQRYYED LDEVSSTSSV SQSLESEDAR TSCKDDEAVV QAPRHAPVVR TPSIQPSLLP HAAPFAKSHL VHGSSPGVMG TSVATSASKI IPQGADSTML ATKTVKHGAP SPSHPISAPQ AAAAAALRRQ MASQAPAVNT LTESTLKNVP QVVNVQELKN NPATPSTAMG SSVPYSTAKT PHPVLTPVAA NQAKQGSLIN SLKPSGPTPA SGQLSSGDKA SGTAKIETAV TSTPSASGQF SKPFSFSPSG TGFNFGIITP TPSSNFTAAQ GATPSTKESS QPDAFSSGGG SKPSYEAIPE SSPPSGITSA SNTTPGEPAA SSSRPVAPSG TALSTTSSKL ETPPSKLGEL LFPSSLAGET LGSFSGLRVG QADDSTKPTN KASSTSLTST QPTKTSGVPS GFNFTAPPVL GKHTEPPVTS SATTTSVAPP AATSTSSTAV FGSLPVTSAG SSGVISFGGT SLSAGKTSFS FGSQQTNSTV PPSAPPPTTA ATPLPTSFPT LSFGSLLSSA TTPSLPMSAG RSTEEATSSA LPEKPGDSEV SASAASLLEE QQSAQLPQAP PQTSDSVKKE PVLAQPAVSN SGTAASSTSL VALSAEATPA TTGVPDARTE AVPPASSFSV PGQTAVTAAA ISSAGPVAVE TSSTPIASST TSIVAPGPSA EAAAFGTVTS GSSVFAQPPA ASSSSAFNQL TNNTATAPSA TPVFGQVAAS TAPSLFGQQT GSTASTAAAT PQVSSSGFSS PAFGTTAPGV FGQTTFGQAS VFGQSASSAA SVFSFSQPGF SSVPAFGQPA SSTPTSTSGS VFGAASSTSS SSSFSFGQSS PNTGGGLFGQ SNAPAFGQSP GFGQGGSVFG GTSAATTTAA TSGFSFCQAS GFGSSNTGSV FGQAASTGGI VFGQQSSSSS GSVFGSGNTG RGGGFFSGLG GKPSQDAANK NPFSSASGGF GSTATSNTSN LFGNSGAKTF GGFASSSFGE QKPTGTFSSG GGSVASQGFG FSSPNKTGGF GAAPVFGSPP TFGGSPGFGG VPAFGSAPAF TSPLGSTGGK VFGEGTAAAS AGGFGFGSSS NTTSFGTLAS QNAPTFGSLS QQTSGFGTQS SGFSGFGSGT GGFSFGSNNS SVQGFGGWRS //