NU153_HUMAN
ID NU153_HUMAN Reviewed; 1475 AA.
AC P49790; B4DIK2; E7EPX5; F6QR24; Q4LE47; Q5T9I7; Q7Z743;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Nuclear pore complex protein Nup153;
DE AltName: Full=153 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup153;
GN Name=NUP153;
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).
RX PubMed=8110839; DOI=10.1016/0167-4781(94)90040-x;
RA McMorrow I., Bastos R., Horton H., Burke B.;
RT "Sequence analysis of a cDNA encoding a human nuclear pore complex protein,
RT hnup153.";
RL Biochim. Biophys. Acta 1217:219-223(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT THR-827.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Myeloma;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-90 AND
RP PHE-381.
RC TISSUE=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 PROTEIN SEQUENCE OF 2-17; 251-263; 295-309; 367-379; 706-718 AND 1046-1056,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11839768; DOI=10.1083/jcb.200106046;
RA Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
RT "Tpr is localized within the nuclear basket of the pore complex and has a
RT role in nuclear protein export.";
RL J. Cell Biol. 156:617-630(2002).
RN [9]
RP FUNCTION IN ANCHORING TPR, AND INTERACTION WITH TPR.
RX PubMed=12802065; DOI=10.1091/mbc.e02-09-0620;
RA Hase M.E., Cordes V.C.;
RT "Direct interaction with nup153 mediates binding of Tpr to the periphery of
RT the nuclear pore complex.";
RL Mol. Biol. Cell 14:1923-1940(2003).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15229283; DOI=10.1091/mbc.e04-03-0165;
RA Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.;
RT "Nucleoporins as components of the nuclear pore complex core structure and
RT Tpr as the architectural element of the nuclear basket.";
RL Mol. Biol. Cell 15:4261-4277(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 AND THR-588, AND
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-209; SER-338 AND SER-633, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP 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-209; SER-240; SER-257;
RP SER-330; SER-334; SER-338; SER-343; THR-369; SER-522; SER-529; SER-614;
RP SER-619; SER-1457 AND SER-1463, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 HIV INTEGRASE (MICROBIAL INFECTION).
RX PubMed=19369352; DOI=10.1128/jvi.02061-08;
RA Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.;
RT "Integrase interacts with nucleoporin NUP153 to mediate the nuclear import
RT of human immunodeficiency virus type 1.";
RL J. Virol. 83:6522-6533(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-338; SER-516;
RP SER-522 AND SER-1463, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-718 AND LYS-954, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP INTERACTION WITH MCM3AP.
RX PubMed=20005110; DOI=10.1016/j.cub.2009.10.078;
RA Wickramasinghe V.O., McMurtrie P.I., Mills A.D., Takei Y., Penrhyn-Lowe S.,
RA Amagase Y., Main S., Marr J., Stewart M., Laskey R.A.;
RT "mRNA export from mammalian cell nuclei is dependent on GANP.";
RL Curr. Biol. 20:25-31(2010).
RN [21]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=20407419; DOI=10.1038/emboj.2010.54;
RA Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H.,
RA Thyberg J., Cordes V.C.;
RT "Protein Tpr is required for establishing nuclear pore-associated zones of
RT heterochromatin exclusion.";
RL EMBO J. 29:1659-1673(2010).
RN [22]
RP INTERACTION WITH TPR.
RX PubMed=20133940; DOI=10.1074/jbc.m110.105890;
RA Nakano H., Funasaka T., Hashizume C., Wong R.W.;
RT "Nucleoporin translocated promoter region (Tpr) associates with dynein
RT complex, preventing chromosome lagging formation during mitosis.";
RL J. Biol. Chem. 285:10841-10849(2010).
RN [23]
RP INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN (MICROBIAL INFECTION).
RX PubMed=20126445; DOI=10.1371/journal.ppat.1000741;
RA Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J.,
RA Stoeber M., Pante N., Kann M.;
RT "Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in
RT the nuclear basket.";
RL PLoS Pathog. 6:E1000741-E1000741(2010).
RN [24]
RP GLYCOSYLATION AT SER-534; SER-544; SER-908; SER-909; SER-1113 AND THR-1156.
RX PubMed=20068230; DOI=10.1126/scisignal.2000526;
RA Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D.,
RA Shabanowitz J., Hunt D.F., Hart G.W.;
RT "Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates
RT cytokinesis.";
RL Sci. Signal. 3:RA2-RA2(2010).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-209; SER-240;
RP SER-338; SER-500; SER-614; SER-619; SER-633; SER-687 AND SER-1463, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-209 AND SER-687, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
RP INTERACTION WITH HIKESHI.
RX PubMed=22541429; DOI=10.1016/j.cell.2012.02.058;
RA Kose S., Furuta M., Imamoto N.;
RT "Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat
RT shock-induced nuclear damage.";
RL Cell 149:578-589(2012).
RN [29]
RP INTERACTION WITH EPSTEIN-BARR VIRUS BGLF4 (MICROBIAL INFECTION).
RX PubMed=22623767; DOI=10.1128/jvi.01058-12;
RA Chang C.W., Lee C.P., Huang Y.H., Yang P.W., Wang J.T., Chen M.R.;
RT "Epstein-Barr virus protein kinase BGLF4 targets the nucleus through
RT interaction with nucleoporins.";
RL J. Virol. 86:8072-8085(2012).
RN [30]
RP FUNCTION IN RNA EXPORT, INTERACTION WITH MAPK1, AND SUBCELLULAR LOCATION.
RX PubMed=22253824; DOI=10.1371/journal.pone.0029921;
RA Rajanala K., Nandicoori V.K.;
RT "Localization of nucleoporin Tpr to the nuclear pore complex is essential
RT for Tpr mediated regulation of the export of unspliced RNA.";
RL PLoS ONE 7:E29921-E29921(2012).
RN [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-185; SER-203;
RP SER-209; SER-240; SER-257; SER-297; SER-320; SER-330; SER-334; SER-338;
RP SER-343; THR-369; THR-388; SER-516; SER-522; SER-607; SER-614; SER-619;
RP SER-687; SER-891; SER-1461 AND SER-1463, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP INTERACTION WITH MCM3AP.
RX PubMed=23652018; DOI=10.1038/ncomms2823;
RA Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P.,
RA Goodman M.F., Sakaguchi N.;
RT "GANP regulates recruitment of AID to immunoglobulin variable regions by
RT modulating transcription and nucleosome occupancy.";
RL Nat. Commun. 4:1830-1830(2013).
RN [34]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HIV-1 CAPSID PROTEIN P24,
RP DOMAIN (MICROBIAL INFECTION), REGION (MICROBIAL INFECTION), AND MUTAGENESIS
RP OF PHE-1415.
RX PubMed=24130490; DOI=10.1371/journal.ppat.1003693;
RA Matreyek K.A., Yucel S.S., Li X., Engelman A.;
RT "Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding
RT pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.";
RL PLoS Pathog. 9:E1003693-E1003693(2013).
RN [35]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 CAPSID PROTEIN
RP P24.
RX PubMed=23523133; DOI=10.1016/j.virol.2013.02.008;
RA Di Nunzio F., Fricke T., Miccio A., Valle-Casuso J.C., Perez P., Souque P.,
RA Rizzi E., Severgnini M., Mavilio F., Charneau P., Diaz-Griffero F.;
RT "Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of
RT HIV-1 replication.";
RL Virology 440:8-18(2013).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102; SER-192; SER-333;
RP SER-338 AND SER-518, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-353, 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 [40]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-2 VPX.
RX PubMed=31913756; DOI=10.1091/mbc.e19-08-0438;
RA Singh S.P., Raja S., Mahalingam S.;
RT "Viral protein X unlocks the nuclear pore complex through a human Nup153-
RT dependent pathway to promote nuclear translocation of the lentiviral
RT genome.";
RL Mol. Biol. Cell 31:304-317(2020).
RN [41]
RP STRUCTURE BY NMR OF 722-761 IN COMPLEX WITH ZINC, STRUCTURE BY NMR OF
RP 773-822 IN COMPLEX WITH ZINC, AND STRUCTURE BY NMR OF 851-890 IN COMPLEX
RP WITH ZINC.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second, third and fourth ZF-RanBP domains from
RT human nuclear pore complex protein NUP153.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [42] {ECO:0000312|PDB:5TSV, ECO:0000312|PDB:5TSX}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1407-1429, FUNCTION (MICROBIAL
RP INFECTION), INTERACTION WITH HIV-1 CAPSID PROTEIN P24, AND DOMAIN
RP (MICROBIAL INFECTION).
RX PubMed=29997211; DOI=10.1128/jvi.00648-18;
RA Buffone C., Martinez-Lopez A., Fricke T., Opp S., Severgnini M., Cifola I.,
RA Petiti L., Frabetti S., Skorupka K., Zadrozny K.K., Ganser-Pornillos B.K.,
RA Pornillos O., Di Nunzio F., Diaz-Griffero F.;
RT "Nup153 Unlocks the Nuclear Pore Complex for HIV-1 Nuclear Translocation in
RT Nondividing Cells.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), a complex
CC required for the trafficking across the nuclear envelope. Functions as
CC a scaffolding element in the nuclear phase of the NPC essential for
CC normal nucleocytoplasmic transport of proteins and mRNAs. Involved in
CC the quality control and retention of unspliced mRNAs in the nucleus; in
CC association with TPR, regulates the nuclear export of unspliced mRNA
CC species bearing constitutive transport element (CTE) in a NXF1- and
CC KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear
CC membrane at NPC. The repeat-containing domain may be involved in
CC anchoring other components of the NPC to the pore membrane. Possible
CC DNA-binding subunit of the nuclear pore complex (NPC).
CC {ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
CC ECO:0000269|PubMed:22253824}.
CC -!- FUNCTION: (Microbial infection) Interacts with HIV-1 caspid protein P24
CC and thereby promotes the integration of the virus in the nucleus of
CC non-dividing cells (in vitro). {ECO:0000269|PubMed:23523133,
CC ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:29997211}.
CC -!- FUNCTION: (Microbial infection) Binds HIV-2 protein vpx and thereby
CC promotes the nuclear translocation of the lentiviral genome (in vitro).
CC {ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:31913756}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds at least 4 zinc ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with RAN; the interaction occurs in a GTP- and GDP-
CC independent manner (By similarity). Part of the nuclear pore complex
CC (NPC). Interacts with TPR (via coiled coil region); the interaction is
CC direct and provides a link between the core structure and the TPR-
CC containing nuclear basket of the nuclear pore complex (NPC). Interacts
CC with HIKESHI, SENP2 and XPO5. Interacts with MCM3AP isoform GANP; this
CC interaction is required for GANP localization at the nuclear pore
CC complex (PubMed:20005110, PubMed:23652018). {ECO:0000250,
CC ECO:0000269|PubMed:11777942, ECO:0000269|PubMed:12802065,
CC ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:20005110,
CC ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:22253824,
CC ECO:0000269|PubMed:22541429, ECO:0000269|PubMed:23652018}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with HIV-1
CC capsid protein p24 (CA) (via N-terminus). {ECO:0000269|PubMed:23523133,
CC ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:29997211}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 integrase; this
CC interaction might play a role in nuclear import of HIV pre-integration
CC complex. {ECO:0000269|PubMed:19369352}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus capsid
CC protein; this interaction probably plays a role in nuclear import of
CC HBV genome. {ECO:0000269|PubMed:20126445}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-barr virus BGLF4;
CC this interaction allows BGLF4 nuclear entry.
CC {ECO:0000269|PubMed:22623767}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-2 virus protein vpx;
CC this interaction might promote vpx nuclear entry.
CC {ECO:0000269|PubMed:31913756}.
CC -!- INTERACTION:
CC P49790; P29323: EPHB2; NbExp=2; IntAct=EBI-286779, EBI-1059294;
CC P49790; Q14974: KPNB1; NbExp=8; IntAct=EBI-286779, EBI-286758;
CC P49790; Q16539-3: MAPK14; NbExp=2; IntAct=EBI-286779, EBI-6932370;
CC P49790; P49790: NUP153; NbExp=4; IntAct=EBI-286779, EBI-286779;
CC P49790; Q93009: USP7; NbExp=2; IntAct=EBI-286779, EBI-302474;
CC P49790; P70168: Kpnb1; Xeno; NbExp=2; IntAct=EBI-286779, EBI-540580;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus membrane. Nucleus, nuclear pore
CC complex. Note=Tightly associated with the nuclear membrane and lamina
CC (By similarity). Localized to the nucleoplasmic side of the nuclear
CC pore complex (NPC) core structure, forming a fibrous structure called
CC the nuclear basket. Dissociates from the NPC structure early during
CC prophase of mitosis. Integrated in the newly assembled nuclear envelope
CC of postmitotic cells early in G1. Colocalized with NUP98 and TPR to the
CC nuclear basket at the nucleoplasmic side of the NPC. Detected in
CC diffuse and discrete intranuclear foci. Remained localized to the
CC nuclear membrane after poliovirus (PV) infection. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P49790-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49790-2; Sequence=VSP_054265;
CC Name=3;
CC IsoId=P49790-3; Sequence=VSP_055134;
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: (Microbial infection) FG repeats mediates interaction with HIV-
CC 1 capsid protein p24 (CA). {ECO:0000269|PubMed:24130490,
CC ECO:0000269|PubMed:29997211}.
CC -!- PTM: Phosphorylated in interphase, hyperphosphorylated during mitosis.
CC May play a role in the reversible disassembly of the nuclear pore
CC complex during mitosis (By similarity). {ECO:0000250}.
CC -!- PTM: Proteolytically degraded after poliovirus (PV) infection;
CC degradation is partial and NCP- and TPR-binding domains withstand
CC degradation.
CC -!- PTM: O-glycosylated during cytokinesis at sites identical or close to
CC phosphorylation sites, this interferes with the phosphorylation status.
CC {ECO:0000269|PubMed:20068230}.
CC -!- SIMILARITY: Belongs to the NUP153 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06106.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z25535; CAA80982.1; -; mRNA.
DR EMBL; AK295644; BAG58514.1; -; mRNA.
DR EMBL; AB210024; BAE06106.1; ALT_INIT; mRNA.
DR EMBL; AL138824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052965; AAH52965.1; -; mRNA.
DR CCDS; CCDS4541.1; -. [P49790-1]
DR CCDS; CCDS64359.1; -. [P49790-3]
DR CCDS; CCDS75407.1; -. [P49790-2]
DR PIR; S42718; S42718.
DR RefSeq; NP_001265138.1; NM_001278209.1. [P49790-3]
DR RefSeq; NP_001265139.1; NM_001278210.1. [P49790-2]
DR RefSeq; NP_005115.2; NM_005124.3. [P49790-1]
DR PDB; 2EBQ; NMR; -; A=722-761.
DR PDB; 2EBR; NMR; -; A=851-890.
DR PDB; 2EBV; NMR; -; A=773-822.
DR PDB; 2GQE; NMR; -; A=722-750.
DR PDB; 4U0C; X-ray; 1.77 A; B=1407-1423.
DR PDB; 4U0D; X-ray; 3.00 A; M/N/O/P/Q/R=1407-1423.
DR PDB; 5TSV; X-ray; 2.50 A; D=1407-1429.
DR PDB; 5TSX; X-ray; 1.90 A; M/N/O/P/R/T=1407-1429.
DR PDB; 6AYA; X-ray; 2.40 A; B=1407-1423.
DR PDBsum; 2EBQ; -.
DR PDBsum; 2EBR; -.
DR PDBsum; 2EBV; -.
DR PDBsum; 2GQE; -.
DR PDBsum; 4U0C; -.
DR PDBsum; 4U0D; -.
DR PDBsum; 5TSV; -.
DR PDBsum; 5TSX; -.
DR PDBsum; 6AYA; -.
DR AlphaFoldDB; P49790; -.
DR SASBDB; P49790; -.
DR SMR; P49790; -.
DR BioGRID; 115297; 174.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR DIP; DIP-38185N; -.
DR IntAct; P49790; 114.
DR MINT; P49790; -.
DR STRING; 9606.ENSP00000444029; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyConnect; 2878; 1 O-Linked glycan (8 sites).
DR GlyGen; P49790; 131 sites, 2 O-linked glycans (131 sites).
DR iPTMnet; P49790; -.
DR MetOSite; P49790; -.
DR PhosphoSitePlus; P49790; -.
DR SwissPalm; P49790; -.
DR BioMuta; NUP153; -.
DR DMDM; 206729891; -.
DR EPD; P49790; -.
DR jPOST; P49790; -.
DR MassIVE; P49790; -.
DR MaxQB; P49790; -.
DR PaxDb; P49790; -.
DR PeptideAtlas; P49790; -.
DR PRIDE; P49790; -.
DR ProteomicsDB; 27856; -.
DR ProteomicsDB; 56120; -. [P49790-1]
DR Antibodypedia; 10334; 179 antibodies from 35 providers.
DR DNASU; 9972; -.
DR Ensembl; ENST00000262077.3; ENSP00000262077.3; ENSG00000124789.12. [P49790-1]
DR Ensembl; ENST00000537253.5; ENSP00000444029.1; ENSG00000124789.12. [P49790-3]
DR Ensembl; ENST00000613258.4; ENSP00000478627.1; ENSG00000124789.12. [P49790-2]
DR GeneID; 9972; -.
DR KEGG; hsa:9972; -.
DR MANE-Select; ENST00000262077.3; ENSP00000262077.3; NM_005124.4; NP_005115.2.
DR UCSC; uc003ncd.3; human. [P49790-1]
DR CTD; 9972; -.
DR DisGeNET; 9972; -.
DR GeneCards; NUP153; -.
DR HGNC; HGNC:8062; NUP153.
DR HPA; ENSG00000124789; Low tissue specificity.
DR MIM; 603948; gene.
DR neXtProt; NX_P49790; -.
DR OpenTargets; ENSG00000124789; -.
DR PharmGKB; PA31848; -.
DR VEuPathDB; HostDB:ENSG00000124789; -.
DR eggNOG; KOG4719; Eukaryota.
DR GeneTree; ENSGT00940000153253; -.
DR HOGENOM; CLU_004629_1_0_1; -.
DR InParanoid; P49790; -.
DR OMA; SASEWEC; -.
DR OrthoDB; 141803at2759; -.
DR PhylomeDB; P49790; -.
DR TreeFam; TF323517; -.
DR PathwayCommons; P49790; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; P49790; -.
DR SIGNOR; P49790; -.
DR BioGRID-ORCS; 9972; 547 hits in 1098 CRISPR screens.
DR ChiTaRS; NUP153; human.
DR EvolutionaryTrace; P49790; -.
DR GeneWiki; NUP153; -.
DR GenomeRNAi; 9972; -.
DR Pharos; P49790; Tbio.
DR PRO; PR:P49790; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P49790; protein.
DR Bgee; ENSG00000124789; Expressed in secondary oocyte and 211 other tissues.
DR Genevisible; P49790; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0016020; C:membrane; IMP:CACAO.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IMP:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0046832; P:negative regulation of RNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR DisProt; DP01799; -.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR013913; Nup153_N.
DR InterPro; IPR018892; Retro-transposon_transp_CS.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23193; PTHR23193; 1.
DR Pfam; PF08604; Nup153; 1.
DR Pfam; PF10599; Nup_retrotrp_bd; 1.
DR Pfam; PF00641; zf-RanBP; 4.
DR SMART; SM00547; ZnF_RBZ; 4.
DR SUPFAM; SSF90209; SSF90209; 4.
DR PROSITE; PS01358; ZF_RANBP2_1; 4.
DR PROSITE; PS50199; ZF_RANBP2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW DNA-binding; Glycoprotein; Host-virus interaction; Isopeptide bond;
KW Membrane; Metal-binding; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport; Ubl conjugation;
KW Viral penetration into host nucleus; Virus entry into host cell; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1475
FT /note="Nuclear pore complex protein Nup153"
FT /id="PRO_0000204842"
FT REPEAT 236..237
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 652..653
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 715..716
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 786..787
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 905..906
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 926..927
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 961..962
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 983..984
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 1000..1001
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 1024..1025
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 1084..1085
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 1118..1119
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 1135..1136
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 1173..1174
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 1212..1213
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 1228..1229
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 1240..1241
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 1275..1276
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 1289..1290
FT /note="19"
FT /evidence="ECO:0000305"
FT REPEAT 1291..1292
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 1306..1307
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 1319..1320
FT /note="22"
FT /evidence="ECO:0000305"
FT REPEAT 1327..1328
FT /note="23"
FT /evidence="ECO:0000305"
FT REPEAT 1341..1342
FT /note="24"
FT /evidence="ECO:0000305"
FT REPEAT 1362..1363
FT /note="25"
FT /evidence="ECO:0000305"
FT REPEAT 1374..1375
FT /note="26"
FT /evidence="ECO:0000305"
FT REPEAT 1383..1384
FT /note="27"
FT /evidence="ECO:0000305"
FT REPEAT 1397..1398
FT /note="28"
FT /evidence="ECO:0000305"
FT REPEAT 1417..1418
FT /note="29"
FT /evidence="ECO:0000305"
FT ZN_FING 657..687
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 722..751
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 793..822
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 851..880
FT /note="RanBP2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..1418
FT /note="29 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 1128..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1475
FT /note="(Microbial infection) Interacts with HIV-1 capsid
FT protein p24 (CA)"
FT /evidence="ECO:0000269|PubMed:24130490"
FT REGION 1420..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 667
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P49791"
FT BINDING 728
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:2EBQ"
FT BINDING 731
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:2EBQ"
FT BINDING 742
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:2EBQ"
FT BINDING 745
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:2EBQ"
FT BINDING 799
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2EBV"
FT BINDING 802
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2EBV"
FT BINDING 813
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2EBV"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:2EBV"
FT BINDING 857
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:2EBR"
FT BINDING 860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:2EBR"
FT BINDING 871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:2EBR"
FT BINDING 874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:2EBR"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 369
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 384
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 388
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 718
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 954
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 534
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 544
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 908
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 909
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 1113
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 1156
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 465
FT /note="E -> ERQGLTVLPKLISSSCAQAIIPSWPLKVLRLQ (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055134"
FT VAR_SEQ 574..615
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054265"
FT VARIANT 90
FT /note="D -> N (in dbSNP:rs16879902)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_046554"
FT VARIANT 248
FT /note="I -> V (in dbSNP:rs2228375)"
FT /id="VAR_046555"
FT VARIANT 381
FT /note="V -> F (in dbSNP:rs17857419)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_070841"
FT VARIANT 402
FT /note="N -> K (in dbSNP:rs6906499)"
FT /id="VAR_046556"
FT VARIANT 821
FT /note="P -> L (in dbSNP:rs6905654)"
FT /id="VAR_046557"
FT VARIANT 827
FT /note="A -> T (in dbSNP:rs2274136)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_046558"
FT VARIANT 1388
FT /note="T -> A (in dbSNP:rs2228379)"
FT /id="VAR_046559"
FT MUTAGEN 1415
FT /note="F->A: Reduces binding to HIV-1 capsid protein p24
FT (CA)."
FT /evidence="ECO:0000269|PubMed:24130490"
FT CONFLICT 111
FT /note="E -> G (in Ref. 2; BAG58514)"
FT /evidence="ECO:0000305"
FT CONFLICT 454..455
FT /note="TR -> HA (in Ref. 1; CAA80982)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="C -> S (in Ref. 2; BAG58514)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="S -> C (in Ref. 2; BAG58514)"
FT /evidence="ECO:0000305"
FT STRAND 723..727
FT /evidence="ECO:0007829|PDB:2EBQ"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:2EBQ"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:2EBQ"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:2EBQ"
FT STRAND 794..796
FT /evidence="ECO:0007829|PDB:2EBV"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:2EBV"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:2EBV"
FT STRAND 858..860
FT /evidence="ECO:0007829|PDB:2EBR"
FT STRAND 872..874
FT /evidence="ECO:0007829|PDB:2EBR"
SQ SEQUENCE 1475 AA; 153938 MW; D07455A691F7CD1F CRC64;
MASGAGGVGG GGGGKIRTRR CHQGPIKPYQ QGRQQHQGIL SRVTESVKNI VPGWLQRYFN
KNEDVCSCST DTSEVPRWPE NKEDHLVYAD EESSNITDGR ITPEPAVSNT EEPSTTSTAS
NYPDVLTRPS LHRSHLNFSM LESPALHCQP STSSAFPIGS SGFSLVKEIK DSTSQHDDDN
ISTTSGFSSR ASDKDITVSK NTSLPPLWSP EAERSHSLSQ HTATSSKKPA FNLSAFGTLS
PSLGNSSILK TSQLGDSPFY PGKTTYGGAA AAVRQSKLRN TPYQAPVRRQ MKAKQLSAQS
YGVTSSTARR ILQSLEKMSS PLADAKRIPS IVSSPLNSPL DRSGIDITDF QAKREKVDSQ
YPPVQRLMTP KPVSIATNRS VYFKPSLTPS GEFRKTNQRI DNKCSTGYEK NMTPGQNREQ
RESGFSYPNF SLPAANGLSS GVGGGGGKMR RERTRFVASK PLEEEEMEVP VLPKISLPIT
SSSLPTFNFS SPEITTSSPS PINSSQALTN KVQMTSPSST GSPMFKFSSP IVKSTEANVL
PPSSIGFTFS VPVAKTAELS GSSSTLEPII SSSAHHVTTV NSTNCKKTPP EDCEGPFRPA
EILKEGSVLD ILKSPGFASP KIDSVAAQPT ATSPVVYTRP AISSFSSSGI GFGESLKAGS
SWQCDTCLLQ NKVTDNKCIA CQAAKLSPRD TAKQTGIETP NKSGKTTLSA SGTGFGDKFK
PVIGTWDCDT CLVQNKPEAI KCVACETPKP GTCVKRALTL TVVSESAETM TASSSSCTVT
TGTLGFGDKF KRPIGSWECS VCCVSNNAED NKCVSCMSEK PGSSVPASSS STVPVSLPSG
GSLGLEKFKK PEGSWDCELC LVQNKADSTK CLACESAKPG TKSGFKGFDT SSSSSNSAAS
SSFKFGVSSS SSGPSQTLTS TGNFKFGDQG GFKIGVSSDS GSINPMSEGF KFSKPIGDFK
FGVSSESKPE EVKKDSKNDN FKFGLSSGLS NPVSLTPFQF GVSNLGQEEK KEELPKSSSA
GFSFGTGVIN STPAPANTIV TSENKSSFNL GTIETKSASV APFTCKTSEA KKEEMPATKG
GFSFGNVEPA SLPSASVFVL GRTEEKQQEP VTSTSLVFGK KADNEEPKCQ PVFSFGNSEQ
TKDENSSKST FSFSMTKPSE KESEQPAKAT FAFGAQTSTT ADQGAAKPVF SFLNNSSSSS
STPATSAGGG IFGSSTSSSN PPVATFVFGQ SSNPVSSSAF GNTAESSTSQ SLLFSQDSKL
ATTSSTGTAV TPFVFGPGAS SNNTTTSGFG FGATTTSSSA GSSFVFGTGP SAPSASPAFG
ANQTPTFGQS QGASQPNPPG FGSISSSTAL FPTGSQPAPP TFGTVSSSSQ PPVFGQQPSQ
SAFGSGTTPN SSSAFQFGSS TTNFNFTNNS PSGVFTFGAN SSTPAASAQP SGSGGFPFNQ
SPAAFTVGSN GKNVFSSSGT SFSGRKIKTA VRRRK
