NU214_HUMAN
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 03-AUG-2022, entry version 214.
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="http://atlasgeneticsoncology.org/Genes/CANID29.html";
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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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 PDBsum; 2OIT; -.
DR PDBsum; 3FHC; -.
DR PDBsum; 3FMO; -.
DR PDBsum; 3FMP; -.
DR PDBsum; 5DIS; -.
DR AlphaFoldDB; P35658; -.
DR SMR; P35658; -.
DR BioGRID; 113717; 130.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR DIP; DIP-38367N; -.
DR IntAct; P35658; 80.
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-Linked glycan (4 sites).
DR GlyGen; P35658; 176 sites, 2 O-linked glycans (176 sites).
DR iPTMnet; P35658; -.
DR MetOSite; P35658; -.
DR PhosphoSitePlus; P35658; -.
DR BioMuta; NUP214; -.
DR DMDM; 205831380; -.
DR EPD; P35658; -.
DR jPOST; P35658; -.
DR MassIVE; P35658; -.
DR MaxQB; P35658; -.
DR PaxDb; P35658; -.
DR PeptideAtlas; P35658; -.
DR PRIDE; 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 Antibodypedia; 18059; 80 antibodies from 19 providers.
DR DNASU; 8021; -.
DR Ensembl; ENST00000359428.10; ENSP00000352400.5; ENSG00000126883.18. [P35658-1]
DR Ensembl; ENST00000411637.6; ENSP00000396576.2; ENSG00000126883.18. [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 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; 747759at2759; -.
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; 711 hits in 1080 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 162 other tissues.
DR ExpressionAtlas; P35658; baseline and differential.
DR Genevisible; P35658; HS.
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:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC: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; -; 1.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR041553; Nup214_FG.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR PANTHER; PTHR23193; PTHR23193; 1.
DR Pfam; PF18617; Nup214_FG; 1.
DR SMART; SM00320; WD40; 2.
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; unknown pathological 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
