Full text data of NUP50
NUP50
(NPAP60L)
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear pore complex protein Nup50 (50 kDa nucleoporin; Nuclear pore-associated protein 60 kDa-like; Nucleoporin Nup50)
Nuclear pore complex protein Nup50 (50 kDa nucleoporin; Nuclear pore-associated protein 60 kDa-like; Nucleoporin Nup50)
UniProt
Q9UKX7
ID NUP50_HUMAN Reviewed; 468 AA.
AC Q9UKX7; B1AHA4; B2RB15; O75644; Q8N6V5; Q9NPM9; Q9NPR6; Q9P1K5;
read moreDT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Nuclear pore complex protein Nup50;
DE AltName: Full=50 kDa nucleoporin;
DE AltName: Full=Nuclear pore-associated protein 60 kDa-like;
DE AltName: Full=Nucleoporin Nup50;
GN Name=NUP50; Synonyms=NPAP60L; ORFNames=PRO1146;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10449902;
RA Trichet V., Shkolny D., Dunham I., Beare D., McDermid H.E.;
RT "Mapping and complex expression pattern of the human NPAP60L
RT nucleoporin gene.";
RL Cytogenet. Cell Genet. 85:221-226(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-179 (ISOFORM 1).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP ABSENCE OF INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
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
RT periphery of the nuclear pore complex.";
RL Mol. Biol. Cell 14:1923-1940(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP SPECTROMETRY.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [15]
RP FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=20016008; DOI=10.1091/mbc.E09-05-0374;
RA Ogawa Y., Miyamoto Y., Asally M., Oka M., Yasuda Y., Yoneda Y.;
RT "Two isoforms of Npap60 (Nup50) differentially regulate nuclear
RT protein import.";
RL Mol. Biol. Cell 21:630-638(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; THR-246; THR-259
RP AND SER-296, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP STRUCTURE BY NMR OF 351-468.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RANBD1 domain from human nucleoporin 50
RT kDa.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Component of the nuclear pore complex that has a direct
CC role in nuclear protein import. Actively displaces NLSs from
CC importin-alpha, and facilitates disassembly of the importin-
CC alpha:beta-cargo complex and importin recycling. Interacts with
CC multiple transport receptor proteins including CDKN1B. This
CC interaction is required for correct intracellular transport and
CC degradation of CDKN1B.
CC -!- SUBUNIT: Interacts with Importin alpha-2, Importin beta, Importin
CC beta-2, NUP153, Ran binding protein 7, CDKN1B and itself (By
CC similarity). Does not interact with TPR.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus
CC membrane; Peripheral membrane protein; Nucleoplasmic side (By
CC similarity). Note=Localizes to the nucleoplasmic fibrils of the
CC nuclear pore complex (By similarity). Dissociates from the NPC
CC structure early during prophase of mitosis. Associates to the
CC newly formed nuclear membrane during telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Npap60L;
CC IsoId=Q9UKX7-1; Sequence=Displayed;
CC Name=2; Synonyms=Npap60S;
CC IsoId=Q9UKX7-2; Sequence=VSP_040633;
CC Note=Contrarily to Npap60L, Npap60S does not displaces NLSs, but
CC stabilizes their binding to importin-alpha;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in testis,
CC peripheral blood leukocytes and fetal liver.
CC -!- DOMAIN: Contains FG repeats.
CC -!- SIMILARITY: Contains 1 RanBD1 domain.
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DR EMBL; AF107840; AAD53401.1; -; mRNA.
DR EMBL; AF116624; AAF71047.1; -; mRNA.
DR EMBL; CR456533; CAG30419.1; -; mRNA.
DR EMBL; AK314454; BAG37062.1; -; mRNA.
DR EMBL; AL008718; CAI17944.1; -; Genomic_DNA.
DR EMBL; Z82243; CAI17944.1; JOINED; Genomic_DNA.
DR EMBL; Z82243; CAI17926.1; -; Genomic_DNA.
DR EMBL; AL008718; CAI17926.1; JOINED; Genomic_DNA.
DR EMBL; Z82243; CAQ07372.1; -; Genomic_DNA.
DR EMBL; Z82243; CAQ07374.1; -; Genomic_DNA.
DR EMBL; AL008718; CAQ07374.1; JOINED; Genomic_DNA.
DR EMBL; AL008718; CAQ08670.1; -; Genomic_DNA.
DR EMBL; Z82243; CAQ08670.1; JOINED; Genomic_DNA.
DR EMBL; CH471138; EAW73370.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73372.1; -; Genomic_DNA.
DR EMBL; BC016055; AAH16055.1; -; mRNA.
DR EMBL; BC028125; AAH28125.1; -; mRNA.
DR EMBL; BC070133; AAH70133.1; -; mRNA.
DR EMBL; AL389949; CAB97527.1; -; mRNA.
DR EMBL; AL389950; CAB97528.1; -; mRNA.
DR RefSeq; NP_009103.2; NM_007172.3.
DR RefSeq; NP_705931.1; NM_153645.2.
DR RefSeq; XP_005261368.1; XM_005261311.1.
DR RefSeq; XP_005261369.1; XM_005261312.1.
DR RefSeq; XP_005261370.1; XM_005261313.1.
DR RefSeq; XP_005261371.1; XM_005261314.1.
DR UniGene; Hs.475103; -.
DR PDB; 2EC1; NMR; -; A=351-468.
DR PDB; 3TJ3; X-ray; 2.70 A; C/D=1-109.
DR PDBsum; 2EC1; -.
DR PDBsum; 3TJ3; -.
DR ProteinModelPortal; Q9UKX7; -.
DR SMR; Q9UKX7; 1-47, 351-468.
DR IntAct; Q9UKX7; 8.
DR MINT; MINT-3081797; -.
DR STRING; 9606.ENSP00000345895; -.
DR PhosphoSite; Q9UKX7; -.
DR DMDM; 20455193; -.
DR PaxDb; Q9UKX7; -.
DR PRIDE; Q9UKX7; -.
DR DNASU; 10762; -.
DR Ensembl; ENST00000347635; ENSP00000345895; ENSG00000093000.
DR Ensembl; ENST00000396096; ENSP00000379403; ENSG00000093000.
DR Ensembl; ENST00000407019; ENSP00000385555; ENSG00000093000.
DR GeneID; 10762; -.
DR KEGG; hsa:10762; -.
DR UCSC; uc003bfr.3; human.
DR CTD; 10762; -.
DR GeneCards; GC22P045559; -.
DR HGNC; HGNC:8065; NUP50.
DR HPA; HPA047162; -.
DR MIM; 604646; gene.
DR neXtProt; NX_Q9UKX7; -.
DR PharmGKB; PA31852; -.
DR eggNOG; NOG255247; -.
DR HOVERGEN; HBG052697; -.
DR InParanoid; Q9UKX7; -.
DR KO; K14295; -.
DR OMA; ECKGGDE; -.
DR OrthoDB; EOG7CRTR9; -.
DR PhylomeDB; Q9UKX7; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; NUP50; human.
DR EvolutionaryTrace; Q9UKX7; -.
DR GeneWiki; NUP50; -.
DR GenomeRNAi; 10762; -.
DR NextBio; 40867; -.
DR PMAP-CutDB; Q9UKX7; -.
DR PRO; PR:Q9UKX7; -.
DR ArrayExpress; Q9UKX7; -.
DR Bgee; Q9UKX7; -.
DR CleanEx; HS_NUP50; -.
DR Genevestigator; Q9UKX7; -.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0015758; P:glucose transport; TAS:Reactome.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010827; P:regulation of glucose transport; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR015007; NUP2/50/61.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR000156; Ran_bind_dom.
DR Pfam; PF08911; NUP50; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport.
FT CHAIN 1 468 Nuclear pore complex protein Nup50.
FT /FTId=PRO_0000204868.
FT REPEAT 76 77 1.
FT REPEAT 113 114 2.
FT REPEAT 225 226 3.
FT REPEAT 273 274 4.
FT REPEAT 303 304 5.
FT DOMAIN 335 468 RanBD1.
FT REGION 76 304 5 X 2 AA repeats of F-G.
FT REGION 144 206 Binding to CDKN1B (By similarity).
FT COMPBIAS 55 91 Gly-rich.
FT COMPBIAS 268 330 Ser-rich.
FT MOD_RES 83 83 N6-acetyllysine.
FT MOD_RES 221 221 Phosphoserine.
FT MOD_RES 246 246 Phosphothreonine.
FT MOD_RES 259 259 Phosphothreonine.
FT MOD_RES 296 296 Phosphoserine.
FT VAR_SEQ 1 28 Missing (in isoform 2).
FT /FTId=VSP_040633.
FT CONFLICT 235 235 T -> S (in Ref. 1; AAD53401).
FT TURN 12 14
FT STRAND 15 17
FT HELIX 32 37
FT STRAND 358 368
FT STRAND 370 385
FT STRAND 387 401
FT TURN 420 422
FT STRAND 423 428
FT STRAND 436 441
FT STRAND 443 448
FT HELIX 452 467
SQ SEQUENCE 468 AA; 50144 MW; 1F2775AE9AC8FAC4 CRC64;
MAKRNAEKEL TDRNWDQEDE AEEVGTFSMA SEEVLKNRAI KKAKRRNVGF ESDTGGAFKG
FKGLVVPSGG GRFSGFGSGA GGKPLEGLSN GNNITSAPPF ASAKAAADPK VAFGSLAANG
PTTLVDKVSN PKTNGDSQQP SSSGLASSKA CVGNAYHKQL AALNCSVRDW IVKHVNTNPL
CDLTPIFKDY EKYLANIEQQ HGNSGRNSES ESNKVAAETQ SPSLFGSTKL QQESTFLFHG
NKTEDTPDKK MEVASEKKTD PSSLGATSAS FNFGKKVDSS VLGSLSSVPL TGFSFSPGNS
SLFGKDTTQS KPVSSPFPTK PLEGQAEGDS GECKGGDEEE NDEPPKVVVT EVKEEDAFYS
KKCKLFYKKD NEFKEKGIGT LHLKPTANQK TQLLVRADTN LGNILLNVLI PPNMPCTRTG
KNNVLIVCVP NPPIDEKNAT MPVTMLIRVK TSEDADELHK ILLEKKDA
//
ID NUP50_HUMAN Reviewed; 468 AA.
AC Q9UKX7; B1AHA4; B2RB15; O75644; Q8N6V5; Q9NPM9; Q9NPR6; Q9P1K5;
read moreDT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Nuclear pore complex protein Nup50;
DE AltName: Full=50 kDa nucleoporin;
DE AltName: Full=Nuclear pore-associated protein 60 kDa-like;
DE AltName: Full=Nucleoporin Nup50;
GN Name=NUP50; Synonyms=NPAP60L; ORFNames=PRO1146;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10449902;
RA Trichet V., Shkolny D., Dunham I., Beare D., McDermid H.E.;
RT "Mapping and complex expression pattern of the human NPAP60L
RT nucleoporin gene.";
RL Cytogenet. Cell Genet. 85:221-226(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes
RT deduced by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-179 (ISOFORM 1).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP ABSENCE OF INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
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
RT periphery of the nuclear pore complex.";
RL Mol. Biol. Cell 14:1923-1940(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP SPECTROMETRY.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [15]
RP FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=20016008; DOI=10.1091/mbc.E09-05-0374;
RA Ogawa Y., Miyamoto Y., Asally M., Oka M., Yasuda Y., Yoneda Y.;
RT "Two isoforms of Npap60 (Nup50) differentially regulate nuclear
RT protein import.";
RL Mol. Biol. Cell 21:630-638(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; THR-246; THR-259
RP AND SER-296, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP STRUCTURE BY NMR OF 351-468.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RANBD1 domain from human nucleoporin 50
RT kDa.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Component of the nuclear pore complex that has a direct
CC role in nuclear protein import. Actively displaces NLSs from
CC importin-alpha, and facilitates disassembly of the importin-
CC alpha:beta-cargo complex and importin recycling. Interacts with
CC multiple transport receptor proteins including CDKN1B. This
CC interaction is required for correct intracellular transport and
CC degradation of CDKN1B.
CC -!- SUBUNIT: Interacts with Importin alpha-2, Importin beta, Importin
CC beta-2, NUP153, Ran binding protein 7, CDKN1B and itself (By
CC similarity). Does not interact with TPR.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus
CC membrane; Peripheral membrane protein; Nucleoplasmic side (By
CC similarity). Note=Localizes to the nucleoplasmic fibrils of the
CC nuclear pore complex (By similarity). Dissociates from the NPC
CC structure early during prophase of mitosis. Associates to the
CC newly formed nuclear membrane during telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Npap60L;
CC IsoId=Q9UKX7-1; Sequence=Displayed;
CC Name=2; Synonyms=Npap60S;
CC IsoId=Q9UKX7-2; Sequence=VSP_040633;
CC Note=Contrarily to Npap60L, Npap60S does not displaces NLSs, but
CC stabilizes their binding to importin-alpha;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in testis,
CC peripheral blood leukocytes and fetal liver.
CC -!- DOMAIN: Contains FG repeats.
CC -!- SIMILARITY: Contains 1 RanBD1 domain.
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DR EMBL; AF107840; AAD53401.1; -; mRNA.
DR EMBL; AF116624; AAF71047.1; -; mRNA.
DR EMBL; CR456533; CAG30419.1; -; mRNA.
DR EMBL; AK314454; BAG37062.1; -; mRNA.
DR EMBL; AL008718; CAI17944.1; -; Genomic_DNA.
DR EMBL; Z82243; CAI17944.1; JOINED; Genomic_DNA.
DR EMBL; Z82243; CAI17926.1; -; Genomic_DNA.
DR EMBL; AL008718; CAI17926.1; JOINED; Genomic_DNA.
DR EMBL; Z82243; CAQ07372.1; -; Genomic_DNA.
DR EMBL; Z82243; CAQ07374.1; -; Genomic_DNA.
DR EMBL; AL008718; CAQ07374.1; JOINED; Genomic_DNA.
DR EMBL; AL008718; CAQ08670.1; -; Genomic_DNA.
DR EMBL; Z82243; CAQ08670.1; JOINED; Genomic_DNA.
DR EMBL; CH471138; EAW73370.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73372.1; -; Genomic_DNA.
DR EMBL; BC016055; AAH16055.1; -; mRNA.
DR EMBL; BC028125; AAH28125.1; -; mRNA.
DR EMBL; BC070133; AAH70133.1; -; mRNA.
DR EMBL; AL389949; CAB97527.1; -; mRNA.
DR EMBL; AL389950; CAB97528.1; -; mRNA.
DR RefSeq; NP_009103.2; NM_007172.3.
DR RefSeq; NP_705931.1; NM_153645.2.
DR RefSeq; XP_005261368.1; XM_005261311.1.
DR RefSeq; XP_005261369.1; XM_005261312.1.
DR RefSeq; XP_005261370.1; XM_005261313.1.
DR RefSeq; XP_005261371.1; XM_005261314.1.
DR UniGene; Hs.475103; -.
DR PDB; 2EC1; NMR; -; A=351-468.
DR PDB; 3TJ3; X-ray; 2.70 A; C/D=1-109.
DR PDBsum; 2EC1; -.
DR PDBsum; 3TJ3; -.
DR ProteinModelPortal; Q9UKX7; -.
DR SMR; Q9UKX7; 1-47, 351-468.
DR IntAct; Q9UKX7; 8.
DR MINT; MINT-3081797; -.
DR STRING; 9606.ENSP00000345895; -.
DR PhosphoSite; Q9UKX7; -.
DR DMDM; 20455193; -.
DR PaxDb; Q9UKX7; -.
DR PRIDE; Q9UKX7; -.
DR DNASU; 10762; -.
DR Ensembl; ENST00000347635; ENSP00000345895; ENSG00000093000.
DR Ensembl; ENST00000396096; ENSP00000379403; ENSG00000093000.
DR Ensembl; ENST00000407019; ENSP00000385555; ENSG00000093000.
DR GeneID; 10762; -.
DR KEGG; hsa:10762; -.
DR UCSC; uc003bfr.3; human.
DR CTD; 10762; -.
DR GeneCards; GC22P045559; -.
DR HGNC; HGNC:8065; NUP50.
DR HPA; HPA047162; -.
DR MIM; 604646; gene.
DR neXtProt; NX_Q9UKX7; -.
DR PharmGKB; PA31852; -.
DR eggNOG; NOG255247; -.
DR HOVERGEN; HBG052697; -.
DR InParanoid; Q9UKX7; -.
DR KO; K14295; -.
DR OMA; ECKGGDE; -.
DR OrthoDB; EOG7CRTR9; -.
DR PhylomeDB; Q9UKX7; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; NUP50; human.
DR EvolutionaryTrace; Q9UKX7; -.
DR GeneWiki; NUP50; -.
DR GenomeRNAi; 10762; -.
DR NextBio; 40867; -.
DR PMAP-CutDB; Q9UKX7; -.
DR PRO; PR:Q9UKX7; -.
DR ArrayExpress; Q9UKX7; -.
DR Bgee; Q9UKX7; -.
DR CleanEx; HS_NUP50; -.
DR Genevestigator; Q9UKX7; -.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR GO; GO:0015758; P:glucose transport; TAS:Reactome.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010827; P:regulation of glucose transport; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR015007; NUP2/50/61.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR000156; Ran_bind_dom.
DR Pfam; PF08911; NUP50; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport.
FT CHAIN 1 468 Nuclear pore complex protein Nup50.
FT /FTId=PRO_0000204868.
FT REPEAT 76 77 1.
FT REPEAT 113 114 2.
FT REPEAT 225 226 3.
FT REPEAT 273 274 4.
FT REPEAT 303 304 5.
FT DOMAIN 335 468 RanBD1.
FT REGION 76 304 5 X 2 AA repeats of F-G.
FT REGION 144 206 Binding to CDKN1B (By similarity).
FT COMPBIAS 55 91 Gly-rich.
FT COMPBIAS 268 330 Ser-rich.
FT MOD_RES 83 83 N6-acetyllysine.
FT MOD_RES 221 221 Phosphoserine.
FT MOD_RES 246 246 Phosphothreonine.
FT MOD_RES 259 259 Phosphothreonine.
FT MOD_RES 296 296 Phosphoserine.
FT VAR_SEQ 1 28 Missing (in isoform 2).
FT /FTId=VSP_040633.
FT CONFLICT 235 235 T -> S (in Ref. 1; AAD53401).
FT TURN 12 14
FT STRAND 15 17
FT HELIX 32 37
FT STRAND 358 368
FT STRAND 370 385
FT STRAND 387 401
FT TURN 420 422
FT STRAND 423 428
FT STRAND 436 441
FT STRAND 443 448
FT HELIX 452 467
SQ SEQUENCE 468 AA; 50144 MW; 1F2775AE9AC8FAC4 CRC64;
MAKRNAEKEL TDRNWDQEDE AEEVGTFSMA SEEVLKNRAI KKAKRRNVGF ESDTGGAFKG
FKGLVVPSGG GRFSGFGSGA GGKPLEGLSN GNNITSAPPF ASAKAAADPK VAFGSLAANG
PTTLVDKVSN PKTNGDSQQP SSSGLASSKA CVGNAYHKQL AALNCSVRDW IVKHVNTNPL
CDLTPIFKDY EKYLANIEQQ HGNSGRNSES ESNKVAAETQ SPSLFGSTKL QQESTFLFHG
NKTEDTPDKK MEVASEKKTD PSSLGATSAS FNFGKKVDSS VLGSLSSVPL TGFSFSPGNS
SLFGKDTTQS KPVSSPFPTK PLEGQAEGDS GECKGGDEEE NDEPPKVVVT EVKEEDAFYS
KKCKLFYKKD NEFKEKGIGT LHLKPTANQK TQLLVRADTN LGNILLNVLI PPNMPCTRTG
KNNVLIVCVP NPPIDEKNAT MPVTMLIRVK TSEDADELHK ILLEKKDA
//
MIM
604646
*RECORD*
*FIELD* NO
604646
*FIELD* TI
*604646 NUCLEOPORIN, 50-KD; NUP50
;;NPAP60, RAT, HOMOLOG OF; NPAP60L
*FIELD* TX
DESCRIPTION
read more
The nuclear pore complex (NPC) allows the bidirectional transport of
macromolecules through the nuclear envelope. At least 50 to 100
different polypeptides, called nucleoporins, are associated with this
essential nuclear membrane structure.
CLONING
Using exon trapping and genomic sequence analysis to identify genes
within 22q13.3, Trichet et al. (1999) identified NUP50, a human homolog
of rat Npap60, is distantly related to the yeast Nup2 protein and
belongs to the FG (phe-gly) nucleoporin family. The authors isolated a
cDNA corresponding to the entire NUP50 coding sequence. The deduced
468-amino acid NUP50 protein contains 5 FG repeats. NUP50 shares 70%
sequence identity with rat Npap60. However, the C-terminal end of NUP50
is 87 amino acids longer than that of Npap60. Northern blot analysis of
various human tissues detected several NUP50 transcripts with different
tissue specificities: a 2-kb transcript expressed at low levels in all
tissues tested, but with considerably higher expression in testis,
peripheral blood leukocytes, and fetal liver; a 2.8-kb transcript
expressed in all tissues tested, but with highest expression in testis;
a 4-kb transcript expressed only in peripheral blood leukocytes; a 5-kb
transcript expressed at similar levels in all tissues tested; and an
8-kb transcript weakly expressed in spleen, testis, ovary, and blood
leukocytes. In addition, RT-PCR detected the 8-kb transcript in fetal
brain. Trichet et al. (1999) found that NUP50 transcripts use at least 3
alternative polyadenylation sites and possibly have alternative 5-prime
ends; they did not detect alternative splicing.
GENE FUNCTION
Many nuclear-targeted proteins are transported through the NPC by the
importin-alpha:importin-beta heterodimer (see 602738). Lindsay et al.
(2002) showed that NUP50, a protein previously believed to be a
structural component of the NPC, is a RAN (601179)-binding protein and a
cofactor for importin-alpha:importin-beta-mediated import. NUP50 is a
tristable switch that alternates between binding modes. The C terminus
binds importin-beta through RAN-GTP. The N terminus binds the C terminus
of importin-alpha, while a central domain binds importin-beta.
NUP50:importin-alpha:importin-beta binds cargo and can stimulate nuclear
import. Endogenous NUP50 can shuttle and is accessible from the
cytoplasmic side of the nuclear envelope. These findings identified
NUP50 as a cofactor for importin-alpha:importin-beta nuclear import and
as a subunit of the importin complex.
GENE STRUCTURE
Trichet et al. (1999) determined that the NUP50 gene contains 8 exons
spanning 20.7 kb.
MAPPING
Trichet et al. (1999) noted that the mouse Npap60 gene maps to
chromosome 15, in a region showing homology of synteny with human
22q13.3.
*FIELD* RF
1. Lindsay, M. E.; Plafker, K.; Smith, A. E.; Clurman, B. E.; Macara,
I. G.: Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated
nuclear protein import. Cell 110: 349-360, 2002.
2. Trichet, V.; Shkolny, D.; Dunham, I.; Beare, D.; McDermid, H. E.
: Mapping and complex expression pattern of the human NPAP60L nucleoporin
gene. Cytogenet. Cell Genet. 85: 221-226, 1999.
*FIELD* CN
Stylianos E. Antonarakis - updated: 09/09/2002
*FIELD* CD
Patti M. Sherman: 3/2/2000
*FIELD* ED
mgross: 09/09/2002
carol: 2/16/2002
mgross: 3/13/2000
mgross: 3/10/2000
psherman: 3/3/2000
*RECORD*
*FIELD* NO
604646
*FIELD* TI
*604646 NUCLEOPORIN, 50-KD; NUP50
;;NPAP60, RAT, HOMOLOG OF; NPAP60L
*FIELD* TX
DESCRIPTION
read more
The nuclear pore complex (NPC) allows the bidirectional transport of
macromolecules through the nuclear envelope. At least 50 to 100
different polypeptides, called nucleoporins, are associated with this
essential nuclear membrane structure.
CLONING
Using exon trapping and genomic sequence analysis to identify genes
within 22q13.3, Trichet et al. (1999) identified NUP50, a human homolog
of rat Npap60, is distantly related to the yeast Nup2 protein and
belongs to the FG (phe-gly) nucleoporin family. The authors isolated a
cDNA corresponding to the entire NUP50 coding sequence. The deduced
468-amino acid NUP50 protein contains 5 FG repeats. NUP50 shares 70%
sequence identity with rat Npap60. However, the C-terminal end of NUP50
is 87 amino acids longer than that of Npap60. Northern blot analysis of
various human tissues detected several NUP50 transcripts with different
tissue specificities: a 2-kb transcript expressed at low levels in all
tissues tested, but with considerably higher expression in testis,
peripheral blood leukocytes, and fetal liver; a 2.8-kb transcript
expressed in all tissues tested, but with highest expression in testis;
a 4-kb transcript expressed only in peripheral blood leukocytes; a 5-kb
transcript expressed at similar levels in all tissues tested; and an
8-kb transcript weakly expressed in spleen, testis, ovary, and blood
leukocytes. In addition, RT-PCR detected the 8-kb transcript in fetal
brain. Trichet et al. (1999) found that NUP50 transcripts use at least 3
alternative polyadenylation sites and possibly have alternative 5-prime
ends; they did not detect alternative splicing.
GENE FUNCTION
Many nuclear-targeted proteins are transported through the NPC by the
importin-alpha:importin-beta heterodimer (see 602738). Lindsay et al.
(2002) showed that NUP50, a protein previously believed to be a
structural component of the NPC, is a RAN (601179)-binding protein and a
cofactor for importin-alpha:importin-beta-mediated import. NUP50 is a
tristable switch that alternates between binding modes. The C terminus
binds importin-beta through RAN-GTP. The N terminus binds the C terminus
of importin-alpha, while a central domain binds importin-beta.
NUP50:importin-alpha:importin-beta binds cargo and can stimulate nuclear
import. Endogenous NUP50 can shuttle and is accessible from the
cytoplasmic side of the nuclear envelope. These findings identified
NUP50 as a cofactor for importin-alpha:importin-beta nuclear import and
as a subunit of the importin complex.
GENE STRUCTURE
Trichet et al. (1999) determined that the NUP50 gene contains 8 exons
spanning 20.7 kb.
MAPPING
Trichet et al. (1999) noted that the mouse Npap60 gene maps to
chromosome 15, in a region showing homology of synteny with human
22q13.3.
*FIELD* RF
1. Lindsay, M. E.; Plafker, K.; Smith, A. E.; Clurman, B. E.; Macara,
I. G.: Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated
nuclear protein import. Cell 110: 349-360, 2002.
2. Trichet, V.; Shkolny, D.; Dunham, I.; Beare, D.; McDermid, H. E.
: Mapping and complex expression pattern of the human NPAP60L nucleoporin
gene. Cytogenet. Cell Genet. 85: 221-226, 1999.
*FIELD* CN
Stylianos E. Antonarakis - updated: 09/09/2002
*FIELD* CD
Patti M. Sherman: 3/2/2000
*FIELD* ED
mgross: 09/09/2002
carol: 2/16/2002
mgross: 3/13/2000
mgross: 3/10/2000
psherman: 3/3/2000