Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153)

 NU153_HUMAN             Reviewed;        1475 AA.
P49790; B4DIK2; E7EPX5; F6QR24; Q4LE47; Q5T9I7; Q7Z743;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 2.
25-OCT-2017, entry version 171.
RecName: Full=Nuclear pore complex protein Nup153;
AltName: Full=153 kDa nucleoporin;
AltName: Full=Nucleoporin Nup153;
Name=NUP153;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8110839; DOI=10.1016/0167-4781(94)90040-X;
McMorrow I., Bastos R., Horton H., Burke B.;
"Sequence analysis of a cDNA encoding a human nuclear pore complex
protein, hnup153.";
Biochim. Biophys. Acta 1217:219-223(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
THR-827.
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Myeloma;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ASN-90 AND PHE-381.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-17; 251-263; 295-309; 367-379; 706-718 AND
1046-1056, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
Submitted (MAR-2009) to UniProtKB.
[7]
INTERACTION WITH XPO5.
PubMed=11777942; DOI=10.1083/jcb.200110082;
Brownawell A.M., Macara I.G.;
"Exportin-5, a novel karyopherin, mediates nuclear export of double-
stranded RNA binding proteins.";
J. Cell Biol. 156:53-64(2002).
[8]
SUBCELLULAR LOCATION.
PubMed=11839768; DOI=10.1083/jcb.200106046;
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
"Tpr is localized within the nuclear basket of the pore complex and
has a role in nuclear protein export.";
J. Cell Biol. 156:617-630(2002).
[9]
FUNCTION IN ANCHORING TPR, AND INTERACTION WITH TPR.
PubMed=12802065; DOI=10.1091/mbc.E02-09-0620;
Hase M.E., Cordes V.C.;
"Direct interaction with nup153 mediates binding of Tpr to the
periphery of the nuclear pore complex.";
Mol. Biol. Cell 14:1923-1940(2003).
[10]
FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=15229283; DOI=10.1091/mbc.E04-03-0165;
Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.;
"Nucleoporins as components of the nuclear pore complex core structure
and Tpr as the architectural element of the nuclear basket.";
Mol. Biol. Cell 15:4261-4277(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338 AND THR-588, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-338 AND
SER-633, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-338, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-240; SER-257;
SER-330; SER-334; SER-338; SER-343; THR-369; SER-522; SER-529;
SER-614; SER-619; SER-1457 AND SER-1463, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
INTERACTION WITH HIV INTEGRASE.
PubMed=19369352; DOI=10.1128/JVI.02061-08;
Woodward C.L., Prakobwanakit S., Mosessian S., Chow S.A.;
"Integrase interacts with nucleoporin NUP153 to mediate the nuclear
import of human immunodeficiency virus type 1.";
J. Virol. 83:6522-6533(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-338; SER-516;
SER-522 AND SER-1463, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-718 AND LYS-954,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
PubMed=20407419; DOI=10.1038/emboj.2010.54;
Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H.,
Thyberg J., Cordes V.C.;
"Protein Tpr is required for establishing nuclear pore-associated
zones of heterochromatin exclusion.";
EMBO J. 29:1659-1673(2010).
[21]
INTERACTION WITH TPR.
PubMed=20133940; DOI=10.1074/jbc.M110.105890;
Nakano H., Funasaka T., Hashizume C., Wong R.W.;
"Nucleoporin translocated promoter region (Tpr) associates with dynein
complex, preventing chromosome lagging formation during mitosis.";
J. Biol. Chem. 285:10841-10849(2010).
[22]
INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN.
PubMed=20126445; DOI=10.1371/journal.ppat.1000741;
Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J.,
Stoeber M., Pante N., Kann M.;
"Nucleoporin 153 arrests the nuclear import of hepatitis B virus
capsids in the nuclear basket.";
PLoS Pathog. 6:E1000741-E1000741(2010).
[23]
GLYCOSYLATION AT SER-534; SER-544; SER-908; SER-909; SER-1113 AND
THR-1156.
PubMed=20068230; DOI=10.1126/scisignal.2000526;
Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K.,
Cheung W.D., Shabanowitz J., Hunt D.F., Hart G.W.;
"Extensive crosstalk between O-GlcNAcylation and phosphorylation
regulates cytokinesis.";
Sci. Signal. 3:RA2-RA2(2010).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-209; SER-240;
SER-338; SER-500; SER-614; SER-619; SER-633; SER-687 AND SER-1463, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-209 AND
SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
INTERACTION WITH HIKESHI.
PubMed=22541429; DOI=10.1016/j.cell.2012.02.058;
Kose S., Furuta M., Imamoto N.;
"Hikeshi, a nuclear import carrier for hsp70s, protects cells from
heat shock-induced nuclear damage.";
Cell 149:578-589(2012).
[28]
INTERACTION WITH EPSTEIN-BARR VIRUS BGLF4.
PubMed=22623767; DOI=10.1128/JVI.01058-12;
Chang C.W., Lee C.P., Huang Y.H., Yang P.W., Wang J.T., Chen M.R.;
"Epstein-Barr virus protein kinase BGLF4 targets the nucleus through
interaction with nucleoporins.";
J. Virol. 86:8072-8085(2012).
[29]
FUNCTION IN RNA EXPORT, INTERACTION WITH MAPK1, AND SUBCELLULAR
LOCATION.
PubMed=22253824; DOI=10.1371/journal.pone.0029921;
Rajanala K., Nandicoori V.K.;
"Localization of nucleoporin Tpr to the nuclear pore complex is
essential for Tpr mediated regulation of the export of unspliced
RNA.";
PLoS ONE 7:E29921-E29921(2012).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-185; SER-203;
SER-209; SER-240; SER-257; SER-297; SER-320; SER-330; SER-334;
SER-338; SER-343; THR-369; THR-388; SER-516; SER-522; SER-607;
SER-614; SER-619; SER-687; SER-891; SER-1461 AND SER-1463, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102; SER-192; SER-333;
SER-338 AND SER-518, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[36]
STRUCTURE BY NMR OF 722-761 IN COMPLEX WITH ZINC, STRUCTURE BY NMR OF
773-822 IN COMPLEX WITH ZINC, AND STRUCTURE BY NMR OF 851-890 IN
COMPLEX WITH ZINC.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the second, third and fourth ZF-RanBP domains
from human nuclear pore complex protein NUP153.";
Submitted (AUG-2007) to the PDB data bank.
-!- FUNCTION: Component of the nuclear pore complex (NPC), a complex
required for the trafficking across the nuclear envelope.
Functions as a scaffolding element in the nuclear phase of the NPC
essential for normal nucleocytoplasmic transport of proteins and
mRNAs. Involved in the quality control and retention of unspliced
mRNAs in the nucleus; in association with TPR, regulates the
nuclear export of unspliced mRNA species bearing constitutive
transport element (CTE) in a NXF1- and KHDRBS1-independent manner.
Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-
containing domain may be involved in anchoring other components of
the NPC to the pore membrane. Possible DNA-binding subunit of the
nuclear pore complex (NPC). {ECO:0000269|PubMed:12802065,
ECO:0000269|PubMed:15229283, ECO:0000269|PubMed:22253824}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds at least 4 zinc ions per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with RAN; the interaction occurs in a GTP- and
GDP-independent manner (By similarity). Part of the nuclear pore
complex (NPC). Interacts with TPR (via coiled coil region); the
interaction is direct and provides a link between the core
structure and the TPR-containing nuclear basket of the nuclear
pore complex (NPC). Interacts with HIV-1 integrase; this
interaction might play a role in nuclear import of HIV pre-
integration complex. Interacts with hepatitis B virus capsid
protein; this interaction probably plays a role in nuclear import
of HBV genome. Interacts with HIKESHI, SENP2 and XPO5. Interacts
with Epstein-barr virus BGLF4; this interaction allows BGLF4
nuclear entry. {ECO:0000250, ECO:0000269|PubMed:11777942,
ECO:0000269|PubMed:12802065, ECO:0000269|PubMed:15229283,
ECO:0000269|PubMed:19369352, ECO:0000269|PubMed:20126445,
ECO:0000269|PubMed:20133940, ECO:0000269|PubMed:22253824,
ECO:0000269|PubMed:22541429, ECO:0000269|PubMed:22623767}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-286779, EBI-286779;
P29323:EPHB2; NbExp=2; IntAct=EBI-286779, EBI-1059294;
P70168:Kpnb1 (xeno); NbExp=2; IntAct=EBI-286779, EBI-540580;
Q16539-3:MAPK14; NbExp=2; IntAct=EBI-286779, EBI-6932370;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus membrane. Nucleus, nuclear
pore complex. Note=Tightly associated with the nuclear membrane
and lamina (By similarity). Localized to the nucleoplasmic side of
the nuclear pore complex (NPC) core structure, forming a fibrous
structure called the nuclear basket. Dissociates from the NPC
structure early during prophase of mitosis. Integrated in the
newly assembled nuclear envelope of postmitotic cells early in G1.
Colocalized with NUP98 and TPR to the nuclear basket at the
nucleoplasmic side of the NPC. Detected in diffuse and discrete
intranuclear foci. Remained localized to the nuclear membrane
after poliovirus (PV) infection. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P49790-1; Sequence=Displayed;
Name=2;
IsoId=P49790-2; Sequence=VSP_054265;
Note=No experimental confirmation available.;
Name=3;
IsoId=P49790-3; Sequence=VSP_055134;
-!- DOMAIN: Contains F-X-F-G repeats.
-!- PTM: Phosphorylated in interphase, hyperphosphorylated during
mitosis. May play a role in the reversible disassembly of the
nuclear pore complex during mitosis (By similarity).
{ECO:0000250}.
-!- PTM: Proteolytically degraded after poliovirus (PV) infection;
degradation is partial and NCP- and TPR-binding domains withstand
degradation.
-!- PTM: O-glycosylated during cytokinesis at sites identical or close
to phosphorylation sites, this interferes with the phosphorylation
status. {ECO:0000269|PubMed:20068230}.
-!- SIMILARITY: Belongs to the NUP153 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE06106.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z25535; CAA80982.1; -; mRNA.
EMBL; AK295644; BAG58514.1; -; mRNA.
EMBL; AB210024; BAE06106.1; ALT_INIT; mRNA.
EMBL; AL138824; CAI12246.1; -; Genomic_DNA.
EMBL; AL138724; CAI12246.1; JOINED; Genomic_DNA.
EMBL; AL157776; CAI12246.1; JOINED; Genomic_DNA.
EMBL; AL157776; CAI16393.1; -; Genomic_DNA.
EMBL; AL138724; CAI16393.1; JOINED; Genomic_DNA.
EMBL; AL138824; CAI16393.1; JOINED; Genomic_DNA.
EMBL; AL138724; CAI40945.1; -; Genomic_DNA.
EMBL; AL138824; CAI40945.1; JOINED; Genomic_DNA.
EMBL; AL157776; CAI40945.1; JOINED; Genomic_DNA.
EMBL; BC052965; AAH52965.1; -; mRNA.
CCDS; CCDS4541.1; -. [P49790-1]
CCDS; CCDS64359.1; -. [P49790-3]
CCDS; CCDS75407.1; -. [P49790-2]
PIR; S42718; S42718.
RefSeq; NP_001265138.1; NM_001278209.1. [P49790-3]
RefSeq; NP_001265139.1; NM_001278210.1. [P49790-2]
RefSeq; NP_005115.2; NM_005124.3. [P49790-1]
UniGene; Hs.601591; -.
PDB; 2EBQ; NMR; -; A=722-761.
PDB; 2EBR; NMR; -; A=851-890.
PDB; 2EBV; NMR; -; A=773-822.
PDB; 2GQE; NMR; -; A=722-750.
PDB; 4U0C; X-ray; 1.77 A; B=1407-1423.
PDB; 4U0D; X-ray; 3.00 A; M/N/O/P/Q/R=1407-1423.
PDBsum; 2EBQ; -.
PDBsum; 2EBR; -.
PDBsum; 2EBV; -.
PDBsum; 2GQE; -.
PDBsum; 4U0C; -.
PDBsum; 4U0D; -.
ProteinModelPortal; P49790; -.
SMR; P49790; -.
BioGrid; 115297; 119.
DIP; DIP-38185N; -.
IntAct; P49790; 90.
MINT; MINT-121422; -.
STRING; 9606.ENSP00000262077; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P49790; -.
PhosphoSitePlus; P49790; -.
DMDM; 206729891; -.
EPD; P49790; -.
MaxQB; P49790; -.
PaxDb; P49790; -.
PeptideAtlas; P49790; -.
PRIDE; P49790; -.
Ensembl; ENST00000262077; ENSP00000262077; ENSG00000124789. [P49790-1]
Ensembl; ENST00000537253; ENSP00000444029; ENSG00000124789. [P49790-3]
Ensembl; ENST00000613258; ENSP00000478627; ENSG00000124789. [P49790-2]
GeneID; 9972; -.
KEGG; hsa:9972; -.
UCSC; uc003ncd.3; human. [P49790-1]
CTD; 9972; -.
DisGeNET; 9972; -.
EuPathDB; HostDB:ENSG00000124789.11; -.
GeneCards; NUP153; -.
H-InvDB; HIX0032892; -.
H-InvDB; HIX0200901; -.
HGNC; HGNC:8062; NUP153.
HPA; HPA027896; -.
HPA; HPA027897; -.
HPA; HPA027898; -.
MIM; 603948; gene.
neXtProt; NX_P49790; -.
OpenTargets; ENSG00000124789; -.
PharmGKB; PA31848; -.
eggNOG; KOG4719; Eukaryota.
eggNOG; ENOG41107SV; LUCA.
GeneTree; ENSGT00700000104544; -.
HOGENOM; HOG000088610; -.
HOVERGEN; HBG052679; -.
InParanoid; P49790; -.
KO; K14296; -.
OMA; EEPKCQP; -.
OrthoDB; EOG091G015X; -.
PhylomeDB; P49790; -.
TreeFam; TF323517; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
SignaLink; P49790; -.
SIGNOR; P49790; -.
ChiTaRS; NUP153; human.
EvolutionaryTrace; P49790; -.
GeneWiki; NUP153; -.
GenomeRNAi; 9972; -.
PMAP-CutDB; P49790; -.
PRO; PR:P49790; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124789; -.
CleanEx; HS_NUP153; -.
Genevisible; P49790; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
GO; GO:0005487; F:nucleocytoplasmic transporter activity; IDA:UniProtKB.
GO; GO:0043495; F:protein membrane anchor; IMP:UniProtKB.
GO; GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0046832; P:negative regulation of RNA export from nucleus; IDA:UniProtKB.
GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0006110; P:regulation of glycolytic process; TAS:Reactome.
GO; GO:0006409; P:tRNA export from nucleus; TAS:Reactome.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
InterPro; IPR026054; Nucleoporin.
InterPro; IPR013913; Nup153_N.
InterPro; IPR018892; Retro-transposon_transp_CS.
InterPro; IPR001876; Znf_RanBP2.
InterPro; IPR036443; Znf_RanBP2_sf.
PANTHER; PTHR23193; PTHR23193; 1.
Pfam; PF08604; Nup153; 1.
Pfam; PF10599; Nup_retrotrp_bd; 1.
Pfam; PF00641; zf-RanBP; 4.
SMART; SM00547; ZnF_RBZ; 4.
SUPFAM; SSF90209; SSF90209; 4.
PROSITE; PS01358; ZF_RANBP2_1; 4.
PROSITE; PS50199; ZF_RANBP2_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; DNA-binding; Glycoprotein;
Host-virus interaction; Isopeptide bond; Membrane; Metal-binding;
mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat;
Translocation; Transport; Ubl conjugation;
Viral penetration into host nucleus; Virus entry into host cell; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
CHAIN 2 1475 Nuclear pore complex protein Nup153.
/FTId=PRO_0000204842.
ZN_FING 657 687 RanBP2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 722 751 RanBP2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 793 822 RanBP2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 851 880 RanBP2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
COMPBIAS 4 14 Gly-rich.
COMPBIAS 443 447 Poly-Gly.
METAL 664 664 Zinc 1. {ECO:0000250|UniProtKB:P49791}.
METAL 667 667 Zinc 1. {ECO:0000250|UniProtKB:P49791}.
METAL 678 678 Zinc 1. {ECO:0000250|UniProtKB:P49791}.
METAL 681 681 Zinc 1. {ECO:0000250|UniProtKB:P49791}.
METAL 728 728 Zinc 2. {ECO:0000244|PDB:2EBQ}.
METAL 731 731 Zinc 2. {ECO:0000244|PDB:2EBQ}.
METAL 742 742 Zinc 2. {ECO:0000244|PDB:2EBQ}.
METAL 745 745 Zinc 2. {ECO:0000244|PDB:2EBQ}.
METAL 799 799 Zinc 3. {ECO:0000244|PDB:2EBV}.
METAL 802 802 Zinc 3. {ECO:0000244|PDB:2EBV}.
METAL 813 813 Zinc 3. {ECO:0000244|PDB:2EBV}.
METAL 816 816 Zinc 3. {ECO:0000244|PDB:2EBV}.
METAL 857 857 Zinc 4. {ECO:0000244|PDB:2EBR}.
METAL 860 860 Zinc 4. {ECO:0000244|PDB:2EBR}.
METAL 871 871 Zinc 4. {ECO:0000244|PDB:2EBR}.
METAL 874 874 Zinc 4. {ECO:0000244|PDB:2EBR}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 102 102 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 209 209 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 334 334 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 369 369 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 384 384 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 388 388 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 516 516 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 588 588 Phosphothreonine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 619 619 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 718 718 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 891 891 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 954 954 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1457 1457 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1461 1461 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1463 1463 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CARBOHYD 534 534 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:20068230}.
CARBOHYD 544 544 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:20068230}.
CARBOHYD 908 908 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:20068230}.
CARBOHYD 909 909 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:20068230}.
CARBOHYD 1113 1113 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:20068230}.
CARBOHYD 1156 1156 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:20068230}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 465 465 E -> ERQGLTVLPKLISSSCAQAIIPSWPLKVLRLQ (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055134.
VAR_SEQ 574 615 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_054265.
VARIANT 90 90 D -> N (in dbSNP:rs16879902).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_046554.
VARIANT 248 248 I -> V (in dbSNP:rs2228375).
/FTId=VAR_046555.
VARIANT 381 381 V -> F (in dbSNP:rs17857419).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_070841.
VARIANT 402 402 N -> K (in dbSNP:rs6906499).
/FTId=VAR_046556.
VARIANT 821 821 P -> L (in dbSNP:rs6905654).
/FTId=VAR_046557.
VARIANT 827 827 A -> T (in dbSNP:rs2274136).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_046558.
VARIANT 1388 1388 T -> A (in dbSNP:rs45475293).
/FTId=VAR_046559.
CONFLICT 111 111 E -> G (in Ref. 2; BAG58514).
{ECO:0000305}.
CONFLICT 454 455 TR -> HA (in Ref. 1; CAA80982).
{ECO:0000305}.
CONFLICT 813 813 C -> S (in Ref. 2; BAG58514).
{ECO:0000305}.
CONFLICT 836 836 S -> C (in Ref. 2; BAG58514).
{ECO:0000305}.
STRAND 723 727 {ECO:0000244|PDB:2EBQ}.
STRAND 729 731 {ECO:0000244|PDB:2EBQ}.
STRAND 743 745 {ECO:0000244|PDB:2EBQ}.
HELIX 755 757 {ECO:0000244|PDB:2EBQ}.
STRAND 794 796 {ECO:0000244|PDB:2EBV}.
STRAND 800 802 {ECO:0000244|PDB:2EBV}.
STRAND 814 816 {ECO:0000244|PDB:2EBV}.
STRAND 858 860 {ECO:0000244|PDB:2EBR}.
STRAND 872 874 {ECO:0000244|PDB:2EBR}.
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


Related products :

Catalog number Product name Quantity
EIAAB28092 153 kDa nucleoporin,Homo sapiens,Human,Nuclear pore complex protein Nup153,Nucleoporin Nup153,NUP153
EIAAB28091 153 kDa nucleoporin,Nuclear pore complex protein Nup153,Nucleoporin Nup153,Nup153,Rat,Rattus norvegicus
CSB-EL016190HU Human Nuclear pore complex protein Nup153(NUP153) ELISA kit 96T
CSB-EL016190RA Rat Nuclear pore complex protein Nup153(NUP153) ELISA kit SpeciesRat 96T
CSB-EL016190RA Rat Nuclear pore complex protein Nup153(NUP153) ELISA kit 96T
CSB-EL016190HU Human Nuclear pore complex protein Nup153(NUP153) ELISA kit SpeciesHuman 96T
NU153_RAT ELISA Kit FOR Nuclear pore complex protein Nup153; organism: Rat; gene name: Nup153 96T
EIAAB28281 50 kDa nucleoporin,Homo sapiens,Human,NPAP60L,Nuclear pore complex protein Nup50,Nuclear pore-associated protein 60 kDa-like,Nucleoporin Nup50,NUP50,PRO1146
EIAAB28283 35 kDa nucleoporin,Homo sapiens,Human,Mitotic phosphoprotein 44,MP44,MP-44,Nuclear pore complex protein Nup53,Nucleoporin Nup35,Nucleoporin NUP53,NUP35,NUP53
EIAAB28295 85 kDa nucleoporin,FROUNT,Homo sapiens,Human,Nuclear pore complex protein Nup85,Nucleoporin Nup75,Nucleoporin Nup85,NUP75,NUP85,PCNT1,Pericentrin-1
EIAAB28285 35 kDa nucleoporin,Mitotic phosphoprotein 44,Mouse,Mp44,MP-44,Mus musculus,Nuclear pore complex protein Nup53,Nucleoporin Nup35,Nucleoporin NUP53,Nup35,Nup53
NU153_RAT Rat ELISA Kit FOR Nuclear pore complex protein Nup153 96T
EIAAB28282 50 kDa nucleoporin,Mouse,Mus musculus,Npap60,Nuclear pore complex protein Nup50,Nuclear pore-associated protein 60 kDa-like,Nucleoporin Nup50,Nup50
EIAAB28280 50 kDa nucleoporin,Npap60,Nuclear pore complex protein Nup50,Nuclear pore-associated protein 60 kDa-like,Nucleoporin Nup50,Nup50,Rat,Rattus norvegicus
EIAAB28284 35 kDa nucleoporin,Nuclear pore complex protein Nup53,Nucleoporin Nup35,Nucleoporin NUP53,Nup35,Nup53,Rat,Rattus norvegicus
EIAAB28298 88 kDa nucleoporin,Nuclear pore complex protein Nup88,Nucleoporin Nup84,Nucleoporin Nup88,Nup84,Nup88,Rat,Rattus norvegicus
abx108567 Polyclonal Rabbit Nuclear pore complex protein Nup153 Antibody (HRP) 100 μg
abx109340 Polyclonal Rabbit Nuclear pore complex protein Nup153 Antibody 100 μg
abx107146 Polyclonal Rabbit Nuclear pore complex protein Nup153 Antibody (FITC) 100 μg
abx105728 Polyclonal Rabbit Nuclear pore complex protein Nup153 Antibody (Biotin) 100 μg
EIAAB28097 160 kDa nucleoporin,Homo sapiens,Human,KIAA0197,Nuclear pore complex protein Nup160,Nucleoporin Nup160,NUP120,NUP160
EIAAB28292 85 kDa nucleoporin,FROUNT,Mouse,Mus musculus,Nuclear pore complex protein Nup85,Nucleoporin Nup85,Nup85,Pcnt1,Pericentrin-1
EIAAB28108 205 kDa nucleoporin,C7orf14,Homo sapiens,Human,KIAA0225,Nuclear pore complex protein Nup205,Nucleoporin Nup205,NUP205
EIAAB28093 155 kDa nucleoporin,Homo sapiens,Human,KIAA0791,Nuclear pore complex protein Nup155,Nucleoporin Nup155,NUP155
EIAAB28302 93 kDa nucleoporin,Homo sapiens,Human,KIAA0095,Nuclear pore complex protein Nup93,Nucleoporin Nup93,NUP93


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur