NUP50_HUMAN
ID NUP50_HUMAN Reviewed; 468 AA.
AC Q9UKX7; B1AHA4; B2RB15; O75644; Q8N6V5; Q9NPM9; Q9NPR6; Q9P1K5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 189.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10449902; DOI=10.1159/000015297;
RA Trichet V., Shkolny D., Dunham I., Beare D., McDermid H.E.;
RT "Mapping and complex expression pattern of the human NPAP60L nucleoporin
RT 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 deduced by
RT 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., 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 [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., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., 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., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., 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., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 LACK 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 periphery of
RT the nuclear pore complex.";
RL Mol. Biol. Cell 14:1923-1940(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [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., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, AND IDENTIFICATION BY MASS
RP 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 [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 protein
RT import.";
RL Mol. Biol. Cell 21:630-638(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; THR-246; THR-259 AND
RP SER-296, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [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., 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP 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., 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-208; SER-221 AND
RP SER-270, AND IDENTIFICATION BY MASS 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
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 [23]
RP STRUCTURE BY NMR OF 351-468.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RANBD1 domain from human nucleoporin 50 kDa.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Component of the nuclear pore complex that has a direct role
CC in nuclear protein import (PubMed:20016008). Actively displaces NLSs
CC from importin-alpha, and facilitates disassembly of the importin-
CC alpha:beta-cargo complex and importin recycling (PubMed:20016008).
CC Interacts with regulatory proteins of cell cycle progression including
CC CDKN1B (By similarity). This interaction is required for correct
CC intracellular transport and degradation of CDKN1B (By similarity).
CC {ECO:0000250|UniProtKB:Q9JIH2, ECO:0000269|PubMed:20016008}.
CC -!- SUBUNIT: Interacts with Importin alpha-2, Importin beta, Importin beta-
CC 2, NUP153, Ran binding protein 7, CDKN1B and itself (By similarity).
CC Does not interact with TPR. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UKX7; Q14145: KEAP1; NbExp=3; IntAct=EBI-2371082, EBI-751001;
CC Q9UKX7; P52294: KPNA1; NbExp=8; IntAct=EBI-2371082, EBI-358383;
CC Q9UKX7; P52292: KPNA2; NbExp=9; IntAct=EBI-2371082, EBI-349938;
CC Q9UKX7; Q7Z726: KPNA2; NbExp=3; IntAct=EBI-2371082, EBI-10323362;
CC Q9UKX7; O00505: KPNA3; NbExp=6; IntAct=EBI-2371082, EBI-358297;
CC Q9UKX7; O00629: KPNA4; NbExp=6; IntAct=EBI-2371082, EBI-396343;
CC Q9UKX7; O15131: KPNA5; NbExp=4; IntAct=EBI-2371082, EBI-540602;
CC Q9UKX7; O60684: KPNA6; NbExp=6; IntAct=EBI-2371082, EBI-359923;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:12802065}. Nucleus membrane
CC {ECO:0000250|UniProtKB:O08587}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O08587}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:O08587}. Note=Localizes to the nucleoplasmic
CC fibrils of the nuclear pore complex (By similarity). Dissociates from
CC the NPC structure early during prophase of mitosis (PubMed:12802065).
CC Associates with the newly formed nuclear membrane during telophase
CC (PubMed:12802065). In the testis, the localization changes during germ
CC cell differentiation from the nuclear surface in spermatocytes to the
CC whole nucleus (interior) in spermatids and back to the nuclear surface
CC in spermatozoa (By similarity). {ECO:0000250|UniProtKB:O08587,
CC ECO:0000269|PubMed:12802065}.
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 -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in testis, peripheral
CC blood leukocytes and fetal liver.
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 -!- MISCELLANEOUS: [Isoform 2]: Contrarily to Npap60L, Npap60S does not
CC displaces NLSs, but stabilizes their binding to importin-alpha.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; 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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82243; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS14062.1; -. [Q9UKX7-1]
DR CCDS; CCDS14063.1; -. [Q9UKX7-2]
DR RefSeq; NP_009103.2; NM_007172.3. [Q9UKX7-1]
DR RefSeq; NP_705931.1; NM_153645.2. [Q9UKX7-2]
DR RefSeq; XP_005261369.1; XM_005261312.1. [Q9UKX7-2]
DR RefSeq; XP_005261371.1; XM_005261314.1. [Q9UKX7-2]
DR RefSeq; XP_006724166.1; XM_006724103.1. [Q9UKX7-1]
DR RefSeq; XP_006724167.1; XM_006724104.1. [Q9UKX7-2]
DR RefSeq; XP_011528135.1; XM_011529833.1. [Q9UKX7-1]
DR RefSeq; XP_016884026.1; XM_017028537.1. [Q9UKX7-2]
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 AlphaFoldDB; Q9UKX7; -.
DR SMR; Q9UKX7; -.
DR BioGRID; 115982; 281.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR IntAct; Q9UKX7; 68.
DR MINT; Q9UKX7; -.
DR STRING; 9606.ENSP00000345895; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9UKX7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKX7; -.
DR PhosphoSitePlus; Q9UKX7; -.
DR SwissPalm; Q9UKX7; -.
DR BioMuta; NUP50; -.
DR DMDM; 20455193; -.
DR EPD; Q9UKX7; -.
DR jPOST; Q9UKX7; -.
DR MassIVE; Q9UKX7; -.
DR MaxQB; Q9UKX7; -.
DR PaxDb; Q9UKX7; -.
DR PeptideAtlas; Q9UKX7; -.
DR PRIDE; Q9UKX7; -.
DR ProteomicsDB; 84906; -. [Q9UKX7-1]
DR ProteomicsDB; 84907; -. [Q9UKX7-2]
DR Antibodypedia; 27795; 373 antibodies from 33 providers.
DR DNASU; 10762; -.
DR Ensembl; ENST00000347635.9; ENSP00000345895.3; ENSG00000093000.19. [Q9UKX7-1]
DR Ensembl; ENST00000396096.6; ENSP00000379403.2; ENSG00000093000.19. [Q9UKX7-2]
DR Ensembl; ENST00000407019.6; ENSP00000385555.2; ENSG00000093000.19. [Q9UKX7-2]
DR GeneID; 10762; -.
DR KEGG; hsa:10762; -.
DR MANE-Select; ENST00000347635.9; ENSP00000345895.3; NM_007172.4; NP_009103.2.
DR UCSC; uc003bfr.4; human. [Q9UKX7-1]
DR CTD; 10762; -.
DR DisGeNET; 10762; -.
DR GeneCards; NUP50; -.
DR HGNC; HGNC:8065; NUP50.
DR HPA; ENSG00000093000; Low tissue specificity.
DR MIM; 604646; gene.
DR neXtProt; NX_Q9UKX7; -.
DR OpenTargets; ENSG00000093000; -.
DR PharmGKB; PA31852; -.
DR VEuPathDB; HostDB:ENSG00000093000; -.
DR eggNOG; KOG2724; Eukaryota.
DR GeneTree; ENSGT00440000035348; -.
DR HOGENOM; CLU_032593_0_0_1; -.
DR InParanoid; Q9UKX7; -.
DR OMA; DTNPLCD; -.
DR OrthoDB; 793797at2759; -.
DR PhylomeDB; Q9UKX7; -.
DR TreeFam; TF106504; -.
DR PathwayCommons; Q9UKX7; -.
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; Q9UKX7; -.
DR SIGNOR; Q9UKX7; -.
DR BioGRID-ORCS; 10762; 293 hits in 1052 CRISPR screens.
DR ChiTaRS; NUP50; human.
DR EvolutionaryTrace; Q9UKX7; -.
DR GeneWiki; NUP50; -.
DR GenomeRNAi; 10762; -.
DR Pharos; Q9UKX7; Tbio.
DR PRO; PR:Q9UKX7; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UKX7; protein.
DR Bgee; ENSG00000093000; Expressed in epithelium of nasopharynx and 211 other tissues.
DR ExpressionAtlas; Q9UKX7; baseline and differential.
DR Genevisible; Q9UKX7; HS.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR DisProt; DP02455; -.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR015007; NUP2/50/61.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138; PTHR23138; 1.
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; Isopeptide bond; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport;
KW Ubl conjugation.
FT CHAIN 1..468
FT /note="Nuclear pore complex protein Nup50"
FT /id="PRO_0000204868"
FT REPEAT 76..77
FT /note="1"
FT REPEAT 113..114
FT /note="2"
FT REPEAT 225..226
FT /note="3"
FT REPEAT 273..274
FT /note="4"
FT REPEAT 303..304
FT /note="5"
FT DOMAIN 335..468
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..304
FT /note="5 X 2 AA repeats of F-G"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..206
FT /note="Binding to CDKN1B"
FT /evidence="ECO:0000250"
FT REGION 201..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH2"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH2"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH2"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 450
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH2"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040633"
FT CONFLICT 235
FT /note="T -> S (in Ref. 1; AAD53401)"
FT /evidence="ECO:0000305"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:3TJ3"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3TJ3"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:3TJ3"
FT STRAND 358..368
FT /evidence="ECO:0007829|PDB:2EC1"
FT STRAND 370..385
FT /evidence="ECO:0007829|PDB:2EC1"
FT STRAND 387..401
FT /evidence="ECO:0007829|PDB:2EC1"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:2EC1"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:2EC1"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:2EC1"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:2EC1"
FT HELIX 452..467
FT /evidence="ECO:0007829|PDB:2EC1"
FT INIT_MET Q9UKX7-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q9UKX7-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
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
