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Nuclear pore complex protein Nup50 (50 kDa nucleoporin) (Nuclear pore-associated protein 60 kDa-like) (Nucleoporin Nup50)

 NUP50_HUMAN             Reviewed;         468 AA.
Q9UKX7; B1AHA4; B2RB15; O75644; Q8N6V5; Q9NPM9; Q9NPR6; Q9P1K5;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 2.
18-JUL-2018, entry version 166.
RecName: Full=Nuclear pore complex protein Nup50;
AltName: Full=50 kDa nucleoporin;
AltName: Full=Nuclear pore-associated protein 60 kDa-like;
AltName: Full=Nucleoporin Nup50;
Name=NUP50; Synonyms=NPAP60L; ORFNames=PRO1146;
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=10449902;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
Liu M., He F.;
"Functional prediction of the coding sequences of 121 new genes
deduced by analysis of cDNA clones from human fetal liver.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-179 (ISOFORM 1).
The European IMAGE consortium;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[9]
LACK OF INTERACTION WITH TPR, AND SUBCELLULAR LOCATION.
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, 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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, 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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, 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).
[15]
FUNCTION, AND ALTERNATIVE SPLICING.
PubMed=20016008; DOI=10.1091/mbc.E09-05-0374;
Ogawa Y., Miyamoto Y., Asally M., Oka M., Yasuda Y., Yoneda Y.;
"Two isoforms of Npap60 (Nup50) differentially regulate nuclear
protein import.";
Mol. Biol. Cell 21:630-638(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; THR-246; THR-259
AND SER-296, 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).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, 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).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-208; SER-221 AND
SER-270, 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).
[21]
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).
[22]
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).
[23]
STRUCTURE BY NMR OF 351-468.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RANBD1 domain from human nucleoporin 50
kDa.";
Submitted (AUG-2007) to the PDB data bank.
-!- FUNCTION: Component of the nuclear pore complex that has a direct
role in nuclear protein import (PubMed:20016008). Actively
displaces NLSs from importin-alpha, and facilitates disassembly of
the importin-alpha:beta-cargo complex and importin recycling
(PubMed:20016008). Interacts with regulatory proteins of cell
cycle progression including CDKN1B (By similarity). This
interaction is required for correct intracellular transport and
degradation of CDKN1B (By similarity).
{ECO:0000250|UniProtKB:Q9JIH2, ECO:0000269|PubMed:20016008}.
-!- SUBUNIT: Interacts with Importin alpha-2, Importin beta, Importin
beta-2, NUP153, Ran binding protein 7, CDKN1B and itself (By
similarity). Does not interact with TPR. {ECO:0000250}.
-!- INTERACTION:
P52294:KPNA1; NbExp=6; IntAct=EBI-2371082, EBI-358383;
P52292:KPNA2; NbExp=8; IntAct=EBI-2371082, EBI-349938;
Q7Z726:KPNA2; NbExp=3; IntAct=EBI-2371082, EBI-10323362;
O00505:KPNA3; NbExp=5; IntAct=EBI-2371082, EBI-358297;
O00629:KPNA4; NbExp=5; IntAct=EBI-2371082, EBI-396343;
O15131:KPNA5; NbExp=3; IntAct=EBI-2371082, EBI-540602;
O60684:KPNA6; NbExp=5; IntAct=EBI-2371082, EBI-359923;
-!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
{ECO:0000269|PubMed:12802065}. Nucleus membrane
{ECO:0000250|UniProtKB:O08587}; Peripheral membrane protein
{ECO:0000250|UniProtKB:O08587}; Nucleoplasmic side
{ECO:0000250|UniProtKB:O08587}. Note=Localizes to the
nucleoplasmic fibrils of the nuclear pore complex (By similarity).
Dissociates from the NPC structure early during prophase of
mitosis (PubMed:12802065). Associates with the newly formed
nuclear membrane during telophase (PubMed:12802065). In the
testis, the localization changes during germ cell differentiation
from the nuclear surface in spermatocytes to the whole nucleus
(interior) in spermatids and back to the nuclear surface in
spermatozoa (By similarity). {ECO:0000250|UniProtKB:O08587,
ECO:0000269|PubMed:12802065}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Npap60L;
IsoId=Q9UKX7-1; Sequence=Displayed;
Name=2; Synonyms=Npap60S;
IsoId=Q9UKX7-2; Sequence=VSP_040633;
Note=Contrarily to Npap60L, Npap60S does not displaces NLSs, but
stabilizes their binding to importin-alpha. Initiator Met-1 is
removed. Contains a N-acetylalanine at position 2.
{ECO:0000244|PubMed:22814378};
-!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in testis,
peripheral blood leukocytes and fetal liver.
-!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
karyopherins (importins, exportins) and form probably an affinity
gradient, guiding the transport proteins unidirectionally with
their cargo through the NPC. FG repeat regions are highly flexible
and lack ordered secondary structure. The overall conservation of
FG repeats regarding exact sequence, spacing, and repeat unit
length is limited. {ECO:0000305}.
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EMBL; AF107840; AAD53401.1; -; mRNA.
EMBL; AF116624; AAF71047.1; -; mRNA.
EMBL; CR456533; CAG30419.1; -; mRNA.
EMBL; AK314454; BAG37062.1; -; mRNA.
EMBL; AL008718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z82243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471138; EAW73370.1; -; Genomic_DNA.
EMBL; CH471138; EAW73372.1; -; Genomic_DNA.
EMBL; BC016055; AAH16055.1; -; mRNA.
EMBL; BC028125; AAH28125.1; -; mRNA.
EMBL; BC070133; AAH70133.1; -; mRNA.
EMBL; AL389949; CAB97527.1; -; mRNA.
EMBL; AL389950; CAB97528.1; -; mRNA.
CCDS; CCDS14062.1; -. [Q9UKX7-1]
CCDS; CCDS14063.1; -. [Q9UKX7-2]
RefSeq; NP_009103.2; NM_007172.3. [Q9UKX7-1]
RefSeq; NP_705931.1; NM_153645.2. [Q9UKX7-2]
RefSeq; XP_005261369.1; XM_005261312.1. [Q9UKX7-2]
RefSeq; XP_005261371.1; XM_005261314.1. [Q9UKX7-2]
RefSeq; XP_006724166.1; XM_006724103.1. [Q9UKX7-1]
RefSeq; XP_006724167.1; XM_006724104.1. [Q9UKX7-2]
RefSeq; XP_011528135.1; XM_011529833.1. [Q9UKX7-1]
RefSeq; XP_016884026.1; XM_017028537.1. [Q9UKX7-2]
UniGene; Hs.475103; -.
PDB; 2EC1; NMR; -; A=351-468.
PDB; 3TJ3; X-ray; 2.70 A; C/D=1-109.
PDBsum; 2EC1; -.
PDBsum; 3TJ3; -.
ProteinModelPortal; Q9UKX7; -.
SMR; Q9UKX7; -.
BioGrid; 115982; 101.
IntAct; Q9UKX7; 35.
MINT; Q9UKX7; -.
STRING; 9606.ENSP00000345895; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q9UKX7; -.
PhosphoSitePlus; Q9UKX7; -.
BioMuta; NUP50; -.
DMDM; 20455193; -.
EPD; Q9UKX7; -.
PaxDb; Q9UKX7; -.
PeptideAtlas; Q9UKX7; -.
PRIDE; Q9UKX7; -.
ProteomicsDB; 84906; -.
ProteomicsDB; 84907; -. [Q9UKX7-2]
DNASU; 10762; -.
Ensembl; ENST00000347635; ENSP00000345895; ENSG00000093000. [Q9UKX7-1]
Ensembl; ENST00000396096; ENSP00000379403; ENSG00000093000. [Q9UKX7-2]
Ensembl; ENST00000407019; ENSP00000385555; ENSG00000093000. [Q9UKX7-2]
GeneID; 10762; -.
KEGG; hsa:10762; -.
UCSC; uc003bfr.4; human. [Q9UKX7-1]
CTD; 10762; -.
DisGeNET; 10762; -.
EuPathDB; HostDB:ENSG00000093000.18; -.
GeneCards; NUP50; -.
HGNC; HGNC:8065; NUP50.
HPA; HPA047162; -.
HPA; HPA048328; -.
MIM; 604646; gene.
neXtProt; NX_Q9UKX7; -.
OpenTargets; ENSG00000093000; -.
PharmGKB; PA31852; -.
eggNOG; KOG2724; Eukaryota.
eggNOG; ENOG410YPHB; LUCA.
GeneTree; ENSGT00440000035348; -.
HOVERGEN; HBG052697; -.
InParanoid; Q9UKX7; -.
KO; K14295; -.
OMA; TFLFHGN; -.
OrthoDB; EOG091G0HML; -.
PhylomeDB; Q9UKX7; -.
TreeFam; TF106504; -.
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.
SIGNOR; Q9UKX7; -.
EvolutionaryTrace; Q9UKX7; -.
GeneWiki; NUP50; -.
GenomeRNAi; 10762; -.
PMAP-CutDB; Q9UKX7; -.
PRO; PR:Q9UKX7; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000093000; -.
CleanEx; HS_NUP50; -.
ExpressionAtlas; Q9UKX7; baseline and differential.
Genevisible; Q9UKX7; HS.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0008536; F:Ran GTPase binding; IBA:GO_Central.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
GO; GO:0016032; P:viral process; TAS:Reactome.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR015007; NUP2/50/61.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000156; Ran_bind_dom.
Pfam; PF08911; NUP50; 1.
Pfam; PF00638; Ran_BP1; 1.
SMART; SM00160; RanBD; 1.
PROSITE; PS50196; RANBD1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Isopeptide bond; Membrane; mRNA transport; Nuclear pore complex;
Nucleus; Phosphoprotein; Protein transport; Reference proteome;
Repeat; Translocation; Transport; Ubl conjugation.
CHAIN 1 468 Nuclear pore complex protein Nup50.
/FTId=PRO_0000204868.
REPEAT 76 77 1.
REPEAT 113 114 2.
REPEAT 225 226 3.
REPEAT 273 274 4.
REPEAT 303 304 5.
DOMAIN 335 468 RanBD1. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
REGION 76 304 5 X 2 AA repeats of F-G.
REGION 144 206 Binding to CDKN1B. {ECO:0000250}.
COMPBIAS 55 91 Gly-rich.
COMPBIAS 268 330 Ser-rich.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JIH2}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 83 83 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 127 127 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JIH2}.
MOD_RES 208 208 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JIH2}.
MOD_RES 246 246 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 259 259 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 450 450 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JIH2}.
CROSSLNK 353 353 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 28 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040633.
CONFLICT 235 235 T -> S (in Ref. 1; AAD53401).
{ECO:0000305}.
TURN 12 14 {ECO:0000244|PDB:3TJ3}.
STRAND 15 17 {ECO:0000244|PDB:3TJ3}.
HELIX 32 37 {ECO:0000244|PDB:3TJ3}.
STRAND 358 368 {ECO:0000244|PDB:2EC1}.
STRAND 370 385 {ECO:0000244|PDB:2EC1}.
STRAND 387 401 {ECO:0000244|PDB:2EC1}.
TURN 420 422 {ECO:0000244|PDB:2EC1}.
STRAND 423 428 {ECO:0000244|PDB:2EC1}.
STRAND 436 441 {ECO:0000244|PDB:2EC1}.
STRAND 443 448 {ECO:0000244|PDB:2EC1}.
HELIX 452 467 {ECO:0000244|PDB:2EC1}.
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


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