NUP50_MOUSE
ID NUP50_MOUSE Reviewed; 466 AA.
AC Q9JIH2; Q3TG43; Q3TN17; Q6P1F4; Q6PAL4; Q8C2Y6; Q9CU02; Q9JK85;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 163.
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=Npap60;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=10891500; DOI=10.1128/mcb.20.15.5631-5642.2000;
RA Smitherman M., Lee K., Swanger J., Kapur R., Clurman B.E.;
RT "Characterization and targeted disruption of murine nup50, a p27(Kip1)-
RT interacting component of the nuclear pore complex.";
RL Mol. Cell. Biol. 20:5631-5642(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=10811608; DOI=10.1093/emboj/19.10.2168;
RA Mueller D., Thieke K., Buergin A., Dickmanns A., Eilers M.;
RT "Cyclin E-mediated elimination of p27 requires its interaction with the
RT nuclear pore-associated protein mNPAP60.";
RL EMBO J. 19:2168-2180(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Amnion, Bone marrow, Ovary, Pituitary, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-126 AND LYS-448, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-46 IN COMPLEX WITH KPNA2, AND
RP FUNCTION.
RX PubMed=16222336; DOI=10.1038/sj.emboj.7600843;
RA Matsuura Y., Stewart M.;
RT "Nup50/Npap60 function in nuclear protein import complex disassembly and
RT importin recycling.";
RL EMBO J. 24:3681-3689(2005).
CC -!- FUNCTION: Component of the nuclear pore complex that has a direct role
CC in nuclear protein import (PubMed:10811608). Actively displaces NLSs
CC from importin-alpha, and facilitates disassembly of the importin-
CC alpha:beta-cargo complex and importin recycling (PubMed:16222336).
CC Interacts with regulatory proteins of cell cycle progression including
CC CDKN1B (PubMed:10891500, PubMed:10811608). This interaction is required
CC for correct intracellular transport and degradation of CDKN1B
CC (PubMed:10811608). {ECO:0000269|PubMed:10811608,
CC ECO:0000269|PubMed:10891500, ECO:0000269|PubMed:16222336}.
CC -!- SUBUNIT: Does not interact with TPR (By similarity). Interacts with
CC Importin alpha-2, Importin beta, Importin beta-2, NUP153, Ran binding
CC protein 7, CDKN1B and itself. {ECO:0000250,
CC ECO:0000269|PubMed:16222336}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. 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. Dissociates from the NPC structure
CC early during prophase of mitosis. Associates with the newly formed
CC nuclear membrane during telophase. In the testis, the localization
CC changes during germ cell differentiation from the nuclear surface in
CC spermatocytes to the whole nucleus (interior) in spermatids and back to
CC the nuclear surface in spermatozoa. {ECO:0000250|UniProtKB:O08587,
CC ECO:0000250|UniProtKB:Q9UKX7}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels. Highest in the
CC developing neural tube and adult testes.
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 -!- DISRUPTION PHENOTYPE: NUP50 targeted disruption results in a complex
CC phenotype characterized by neural tube defects, exencephaly,
CC intrauterine growth retardation, and late embryonic lethality.
CC {ECO:0000269|PubMed:10891500}.
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DR EMBL; AF229256; AAF34721.1; -; mRNA.
DR EMBL; AF251799; AAF70057.1; -; mRNA.
DR EMBL; AK018983; BAB31500.1; -; mRNA.
DR EMBL; AK087706; BAC39975.1; -; mRNA.
DR EMBL; AK133371; BAE21620.1; -; mRNA.
DR EMBL; AK133562; BAE21727.1; -; mRNA.
DR EMBL; AK141750; BAE24822.1; -; mRNA.
DR EMBL; AK151947; BAE30821.1; -; mRNA.
DR EMBL; AK152309; BAE31115.1; -; mRNA.
DR EMBL; AK161713; BAE36546.1; -; mRNA.
DR EMBL; AK165581; BAE38272.1; -; mRNA.
DR EMBL; AK168888; BAE40705.1; -; mRNA.
DR EMBL; CH466550; EDL04446.1; -; Genomic_DNA.
DR EMBL; BC059239; AAH59239.1; -; mRNA.
DR EMBL; BC060234; AAH60234.1; -; mRNA.
DR EMBL; BC065102; AAH65102.1; -; mRNA.
DR CCDS; CCDS27714.1; -.
DR RefSeq; NP_057923.2; NM_016714.2.
DR PDB; 2C1M; X-ray; 2.20 A; B=1-46.
DR PDBsum; 2C1M; -.
DR AlphaFoldDB; Q9JIH2; -.
DR SMR; Q9JIH2; -.
DR BioGRID; 201817; 6.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR DIP; DIP-46130N; -.
DR IntAct; Q9JIH2; 2.
DR MINT; Q9JIH2; -.
DR STRING; 10090.ENSMUSP00000131457; -.
DR iPTMnet; Q9JIH2; -.
DR PhosphoSitePlus; Q9JIH2; -.
DR SwissPalm; Q9JIH2; -.
DR EPD; Q9JIH2; -.
DR MaxQB; Q9JIH2; -.
DR PaxDb; Q9JIH2; -.
DR PeptideAtlas; Q9JIH2; -.
DR PRIDE; Q9JIH2; -.
DR ProteomicsDB; 287858; -.
DR DNASU; 18141; -.
DR Ensembl; ENSMUST00000165443; ENSMUSP00000131457; ENSMUSG00000016619.
DR Ensembl; ENSMUST00000230411; ENSMUSP00000155656; ENSMUSG00000016619.
DR GeneID; 18141; -.
DR KEGG; mmu:18141; -.
DR UCSC; uc007xcq.1; mouse.
DR CTD; 10762; -.
DR MGI; MGI:1351502; Nup50.
DR VEuPathDB; HostDB:ENSMUSG00000016619; -.
DR eggNOG; KOG2724; Eukaryota.
DR GeneTree; ENSGT00440000035348; -.
DR HOGENOM; CLU_032593_0_0_1; -.
DR InParanoid; Q9JIH2; -.
DR OMA; DTNPLCD; -.
DR OrthoDB; 793797at2759; -.
DR PhylomeDB; Q9JIH2; -.
DR TreeFam; TF106504; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 18141; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Nup50; mouse.
DR EvolutionaryTrace; Q9JIH2; -.
DR PRO; PR:Q9JIH2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9JIH2; protein.
DR Bgee; ENSMUSG00000016619; Expressed in ileal epithelium and 260 other tissues.
DR Genevisible; Q9JIH2; MM.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR DisProt; DP01879; -.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID50016; -.
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; Isopeptide bond; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; Ubl conjugation.
FT CHAIN 1..466
FT /note="Nuclear pore complex protein Nup50"
FT /id="PRO_0000204869"
FT REPEAT 76..77
FT /note="1"
FT REPEAT 112..113
FT /note="2"
FT REPEAT 225..226
FT /note="3"
FT REPEAT 271..272
FT /note="4"
FT REPEAT 301..302
FT /note="5"
FT DOMAIN 333..466
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..302
FT /note="5 X 2 AA repeats of F-G"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..205
FT /note="Binding to CDKN1B"
FT REGION 200..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT MOD_RES 448
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 351
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKX7"
FT CONFLICT 127..135
FT /note="KISSPKCNN -> VSNPKTNGD (in Ref. 2; AAF70057)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="Q -> H (in Ref. 3; BAE40705)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="L -> P (in Ref. 1; AAF34721)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="E -> D (in Ref. 3; AAH60234)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="A -> P (in Ref. 1; AAF34721)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..441
FT /note="LPA -> IKV (in Ref. 3; BAB31500)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="E -> K (in Ref. 3; BAB31500)"
FT /evidence="ECO:0000305"
FT CONFLICT 462..464
FT /note="EKK -> QKT (in Ref. 3; BAB31500)"
FT /evidence="ECO:0000305"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2C1M"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:2C1M"
SQ SEQUENCE 466 AA; 49485 MW; 8B9216CBB613661A CRC64;
MAKRVAEKEL TDRNWDEEDE VEEMGTFSVA SEEVMKNRAV KKAKRRNVGF ESDSGGAFKG
FKGLVVPSGG GGFSGFGGSG GKPLEGLTNG NSTDNATPFS NVKTAAEPKA AFGSFAVNGP
TTLVDKKISS PKCNNSNQPP SSGPASSTAC PGNAYHKQLA GLNCSVRDWI VKHVNTNPLC
DLTPIFKDYE RYLATIEKQL ENGGGSSSES QTDRATAGME PPSLFGSTKL QQESPFSFHG
NKAEDTSEKV EFTAEKKSDA AQGATSASFS FGKKIESSAL GSLSSGSLTG FSFSAGSSSL
FGKDAAQSKA ASSLFSAKAS ESPAGGGSSE CRDGEEEEND EPPKVVVTEV KEEDAFYSKK
CKLFYKKDNE FKEKGVGTLH LKPTATQKTQ LLVRADTNLG NILLNVLIAP NMPCTRTGKN
NVLIVCVPNP PLDEKQPTLP ATMLIRVKTS EDADELHKIL LEKKDA
