NUP58_HUMAN
ID NUP58_HUMAN Reviewed; 599 AA.
AC Q9BVL2; A6NI12; B4DZJ1; O43160; Q5JRG2; Q5JRG5;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Nucleoporin p58/p45 {ECO:0000305};
DE AltName: Full=58 kDa nucleoporin {ECO:0000312|HGNC:HGNC:20261};
DE AltName: Full=Nucleoporin-like protein 1;
GN Name=NUP58 {ECO:0000312|HGNC:HGNC:20261}; Synonyms=KIAA0410, NUPL1;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT THR-34.
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 THR-331, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-331, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-331, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the nuclear pore complex, a complex required for
CC the trafficking across the nuclear membrane.
CC {ECO:0000250|UniProtKB:P70581}.
CC -!- SUBUNIT: Component of the p62 complex, a complex at least composed of
CC NUP62, NUP54, and NUP58. Interacts with NUTF2. Interacts with SRP1-
CC alpha and Importin p97 proteins when they are together, but not with
CC SRP1-alpha protein alone (By similarity).
CC {ECO:0000250|UniProtKB:P70581}.
CC -!- INTERACTION:
CC Q9BVL2; Q9P2A4: ABI3; NbExp=7; IntAct=EBI-2811583, EBI-742038;
CC Q9BVL2; O95994: AGR2; NbExp=5; IntAct=EBI-2811583, EBI-712648;
CC Q9BVL2; Q99996-3: AKAP9; NbExp=3; IntAct=EBI-2811583, EBI-11022349;
CC Q9BVL2; Q9NP70: AMBN; NbExp=3; IntAct=EBI-2811583, EBI-11893530;
CC Q9BVL2; Q52LW3-2: ARHGAP29; NbExp=3; IntAct=EBI-2811583, EBI-22012297;
CC Q9BVL2; Q96DX5-3: ASB9; NbExp=3; IntAct=EBI-2811583, EBI-25843552;
CC Q9BVL2; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-2811583, EBI-9089489;
CC Q9BVL2; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-2811583, EBI-718459;
CC Q9BVL2; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-2811583, EBI-742750;
CC Q9BVL2; O75934: BCAS2; NbExp=3; IntAct=EBI-2811583, EBI-1050106;
CC Q9BVL2; P20749: BCL3; NbExp=3; IntAct=EBI-2811583, EBI-958997;
CC Q9BVL2; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-2811583, EBI-2837444;
CC Q9BVL2; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-2811583, EBI-741210;
CC Q9BVL2; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-2811583, EBI-12300031;
CC Q9BVL2; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-2811583, EBI-749253;
CC Q9BVL2; Q96JB2-2: COG3; NbExp=6; IntAct=EBI-2811583, EBI-9091495;
CC Q9BVL2; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-2811583, EBI-3866319;
CC Q9BVL2; Q96MW5: COG8; NbExp=3; IntAct=EBI-2811583, EBI-720875;
CC Q9BVL2; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-2811583, EBI-25836642;
CC Q9BVL2; Q9BT78: COPS4; NbExp=3; IntAct=EBI-2811583, EBI-742413;
CC Q9BVL2; P24310: COX7A1; NbExp=3; IntAct=EBI-2811583, EBI-25876196;
CC Q9BVL2; O75935-2: DCTN3; NbExp=3; IntAct=EBI-2811583, EBI-12091947;
CC Q9BVL2; Q14154: DELE1; NbExp=3; IntAct=EBI-2811583, EBI-2805660;
CC Q9BVL2; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-2811583, EBI-21529239;
CC Q9BVL2; Q14117: DPYS; NbExp=3; IntAct=EBI-2811583, EBI-12275416;
CC Q9BVL2; Q9H410: DSN1; NbExp=3; IntAct=EBI-2811583, EBI-1001144;
CC Q9BVL2; H3BUJ7: E4F1; NbExp=3; IntAct=EBI-2811583, EBI-10178160;
CC Q9BVL2; O00303: EIF3F; NbExp=3; IntAct=EBI-2811583, EBI-711990;
CC Q9BVL2; P41970: ELK3; NbExp=3; IntAct=EBI-2811583, EBI-1758534;
CC Q9BVL2; Q969X5: ERGIC1; NbExp=3; IntAct=EBI-2811583, EBI-781527;
CC Q9BVL2; Q6NXG1-3: ESRP1; NbExp=3; IntAct=EBI-2811583, EBI-21567429;
CC Q9BVL2; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-2811583, EBI-12193763;
CC Q9BVL2; O15287: FANCG; NbExp=3; IntAct=EBI-2811583, EBI-81610;
CC Q9BVL2; Q9BQS8-2: FYCO1; NbExp=3; IntAct=EBI-2811583, EBI-25905795;
CC Q9BVL2; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-2811583, EBI-618189;
CC Q9BVL2; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-2811583, EBI-9088619;
CC Q9BVL2; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-2811583, EBI-2857315;
CC Q9BVL2; Q9NS71: GKN1; NbExp=3; IntAct=EBI-2811583, EBI-3933251;
CC Q9BVL2; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-2811583, EBI-2514791;
CC Q9BVL2; Q99871: HAUS7; NbExp=3; IntAct=EBI-2811583, EBI-395719;
CC Q9BVL2; P42858: HTT; NbExp=7; IntAct=EBI-2811583, EBI-466029;
CC Q9BVL2; Q8NDH6-2: ICA1L; NbExp=3; IntAct=EBI-2811583, EBI-12141931;
CC Q9BVL2; P80217-2: IFI35; NbExp=3; IntAct=EBI-2811583, EBI-12823003;
CC Q9BVL2; Q8IY31-2: IFT20; NbExp=3; IntAct=EBI-2811583, EBI-11742277;
CC Q9BVL2; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-2811583, EBI-9091197;
CC Q9BVL2; Q13352: ITGB3BP; NbExp=6; IntAct=EBI-2811583, EBI-712105;
CC Q9BVL2; A1A512: KIAA0355; NbExp=3; IntAct=EBI-2811583, EBI-25844799;
CC Q9BVL2; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-2811583, EBI-739493;
CC Q9BVL2; Q6P597: KLC3; NbExp=3; IntAct=EBI-2811583, EBI-1643885;
CC Q9BVL2; P57682: KLF3; NbExp=3; IntAct=EBI-2811583, EBI-8472267;
CC Q9BVL2; Q13887: KLF5; NbExp=3; IntAct=EBI-2811583, EBI-2696013;
CC Q9BVL2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2811583, EBI-3044087;
CC Q9BVL2; Q7Z3Y7: KRT28; NbExp=3; IntAct=EBI-2811583, EBI-11980489;
CC Q9BVL2; Q14525: KRT33B; NbExp=6; IntAct=EBI-2811583, EBI-1049638;
CC Q9BVL2; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-2811583, EBI-9088829;
CC Q9BVL2; Q9BV99: LRRC61; NbExp=3; IntAct=EBI-2811583, EBI-2350424;
CC Q9BVL2; P27338: MAOB; NbExp=3; IntAct=EBI-2811583, EBI-3911344;
CC Q9BVL2; Q13503: MED21; NbExp=3; IntAct=EBI-2811583, EBI-394678;
CC Q9BVL2; O14770-4: MEIS2; NbExp=3; IntAct=EBI-2811583, EBI-8025850;
CC Q9BVL2; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-2811583, EBI-8487781;
CC Q9BVL2; Q9NYP9: MIS18A; NbExp=6; IntAct=EBI-2811583, EBI-1104552;
CC Q9BVL2; Q9BV20: MRI1; NbExp=3; IntAct=EBI-2811583, EBI-747381;
CC Q9BVL2; P02795: MT2A; NbExp=3; IntAct=EBI-2811583, EBI-996616;
CC Q9BVL2; Q8IXH7: NELFCD; NbExp=3; IntAct=EBI-2811583, EBI-536725;
CC Q9BVL2; Q13562: NEUROD1; NbExp=3; IntAct=EBI-2811583, EBI-3908303;
CC Q9BVL2; Q7Z3B4: NUP54; NbExp=12; IntAct=EBI-2811583, EBI-741048;
CC Q9BVL2; P37198: NUP62; NbExp=7; IntAct=EBI-2811583, EBI-347978;
CC Q9BVL2; O43482: OIP5; NbExp=3; IntAct=EBI-2811583, EBI-536879;
CC Q9BVL2; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-2811583, EBI-25830200;
CC Q9BVL2; Q9ULW8: PADI3; NbExp=3; IntAct=EBI-2811583, EBI-10488185;
CC Q9BVL2; Q9BPZ3: PAIP2; NbExp=3; IntAct=EBI-2811583, EBI-2957445;
CC Q9BVL2; Q9BR81: PCDHGC3; NbExp=3; IntAct=EBI-2811583, EBI-22012354;
CC Q9BVL2; P57054: PIGP; NbExp=3; IntAct=EBI-2811583, EBI-17630288;
CC Q9BVL2; P55347: PKNOX1; NbExp=6; IntAct=EBI-2811583, EBI-1373569;
CC Q9BVL2; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-2811583, EBI-2692890;
CC Q9BVL2; Q6P1K2: PMF1; NbExp=3; IntAct=EBI-2811583, EBI-713832;
CC Q9BVL2; Q8N490-3: PNKD; NbExp=3; IntAct=EBI-2811583, EBI-25879276;
CC Q9BVL2; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-2811583, EBI-25835994;
CC Q9BVL2; P35998: PSMC2; NbExp=3; IntAct=EBI-2811583, EBI-359710;
CC Q9BVL2; Q96EN9: REX1BD; NbExp=3; IntAct=EBI-2811583, EBI-745810;
CC Q9BVL2; P47804-3: RGR; NbExp=3; IntAct=EBI-2811583, EBI-25834767;
CC Q9BVL2; Q96EP0: RNF31; NbExp=3; IntAct=EBI-2811583, EBI-948111;
CC Q9BVL2; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-2811583, EBI-25837959;
CC Q9BVL2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-2811583, EBI-358489;
CC Q9BVL2; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-2811583, EBI-10696971;
CC Q9BVL2; Q92783-2: STAM; NbExp=3; IntAct=EBI-2811583, EBI-12025738;
CC Q9BVL2; O75886: STAM2; NbExp=3; IntAct=EBI-2811583, EBI-373258;
CC Q9BVL2; Q14765: STAT4; NbExp=3; IntAct=EBI-2811583, EBI-1186538;
CC Q9BVL2; Q8N4C7: STX19; NbExp=3; IntAct=EBI-2811583, EBI-8484990;
CC Q9BVL2; A1L190: SYCE3; NbExp=3; IntAct=EBI-2811583, EBI-10283466;
CC Q9BVL2; O75528: TADA3; NbExp=3; IntAct=EBI-2811583, EBI-473249;
CC Q9BVL2; Q86WV5: TEN1; NbExp=3; IntAct=EBI-2811583, EBI-2562799;
CC Q9BVL2; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-2811583, EBI-12090309;
CC Q9BVL2; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-2811583, EBI-9089156;
CC Q9BVL2; Q13077: TRAF1; NbExp=9; IntAct=EBI-2811583, EBI-359224;
CC Q9BVL2; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-2811583, EBI-11525489;
CC Q9BVL2; Q96A04: TSACC; NbExp=3; IntAct=EBI-2811583, EBI-740411;
CC Q9BVL2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2811583, EBI-12806590;
CC Q9BVL2; Q99598: TSNAX; NbExp=3; IntAct=EBI-2811583, EBI-742638;
CC Q9BVL2; O60636: TSPAN2; NbExp=3; IntAct=EBI-2811583, EBI-3914288;
CC Q9BVL2; Q6PID6: TTC33; NbExp=3; IntAct=EBI-2811583, EBI-2555404;
CC Q9BVL2; P49459: UBE2A; NbExp=3; IntAct=EBI-2811583, EBI-2339348;
CC Q9BVL2; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-2811583, EBI-10173939;
CC Q9BVL2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2811583, EBI-947187;
CC Q9BVL2; Q9H347: UBQLN3; NbExp=3; IntAct=EBI-2811583, EBI-25832660;
CC Q9BVL2; Q8NEZ2: VPS37A; NbExp=3; IntAct=EBI-2811583, EBI-2850578;
CC Q9BVL2; P58304: VSX2; NbExp=3; IntAct=EBI-2811583, EBI-6427899;
CC Q9BVL2; Q86U90: YRDC; NbExp=3; IntAct=EBI-2811583, EBI-21659356;
CC Q9BVL2; Q8IWT0-2: ZBTB8OS; NbExp=3; IntAct=EBI-2811583, EBI-12956041;
CC Q9BVL2; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-2811583, EBI-25831733;
CC Q9BVL2; O95229: ZWINT; NbExp=3; IntAct=EBI-2811583, EBI-1001132;
CC Q9BVL2; B7Z3E8; NbExp=3; IntAct=EBI-2811583, EBI-25831617;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P70581}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P70581}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P70581}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P70581}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P70581}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P70581}. Note=Biased towards cytoplasmic side.
CC Central region of the nuclear pore complex, within the transporter.
CC {ECO:0000250|UniProtKB:P70581}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=p58;
CC IsoId=Q9BVL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BVL2-2; Sequence=VSP_007946, VSP_007947;
CC Name=3;
CC IsoId=Q9BVL2-3; Sequence=VSP_045658;
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 -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: In rat, the p62 complex contains two different isoforms
CC of NUP58. Isoform p45 has however not been isolated in human so far.
CC -!- SIMILARITY: Belongs to the NUP58 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23706.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB007870; BAA23706.2; ALT_INIT; mRNA.
DR EMBL; AK302946; BAG64103.1; -; mRNA.
DR EMBL; AL138958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL646102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001104; AAH01104.1; -; mRNA.
DR CCDS; CCDS31949.1; -. [Q9BVL2-3]
DR CCDS; CCDS9314.1; -. [Q9BVL2-1]
DR RefSeq; NP_001008564.1; NM_001008564.1. [Q9BVL2-3]
DR RefSeq; NP_054808.1; NM_014089.3. [Q9BVL2-1]
DR PDB; 4JO7; X-ray; 1.75 A; A/C/E/G=341-428.
DR PDB; 4JO9; X-ray; 2.50 A; B=341-426.
DR PDB; 4JQ5; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=341-425.
DR PDB; 5IJN; EM; 21.40 A; G/M/S/Y=1-599.
DR PDB; 5IJO; EM; 21.40 A; G/M/S/Y=1-599.
DR PDB; 7PER; EM; 35.00 A; G/M/S/Y=1-599.
DR PDBsum; 4JO7; -.
DR PDBsum; 4JO9; -.
DR PDBsum; 4JQ5; -.
DR PDBsum; 5IJN; -.
DR PDBsum; 5IJO; -.
DR PDBsum; 7PER; -.
DR AlphaFoldDB; Q9BVL2; -.
DR SMR; Q9BVL2; -.
DR BioGRID; 115157; 88.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR IntAct; Q9BVL2; 148.
DR MINT; Q9BVL2; -.
DR STRING; 9606.ENSP00000371155; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9BVL2; 54 sites, 2 O-linked glycans (54 sites).
DR iPTMnet; Q9BVL2; -.
DR MetOSite; Q9BVL2; -.
DR PhosphoSitePlus; Q9BVL2; -.
DR BioMuta; NUP58; -.
DR DMDM; 44888845; -.
DR EPD; Q9BVL2; -.
DR jPOST; Q9BVL2; -.
DR MassIVE; Q9BVL2; -.
DR MaxQB; Q9BVL2; -.
DR PaxDb; Q9BVL2; -.
DR PeptideAtlas; Q9BVL2; -.
DR PRIDE; Q9BVL2; -.
DR ProteomicsDB; 1238; -.
DR ProteomicsDB; 79216; -. [Q9BVL2-1]
DR ProteomicsDB; 79217; -. [Q9BVL2-2]
DR Antibodypedia; 22561; 88 antibodies from 21 providers.
DR DNASU; 9818; -.
DR Ensembl; ENST00000381718.7; ENSP00000371137.3; ENSG00000139496.16. [Q9BVL2-3]
DR Ensembl; ENST00000381736.8; ENSP00000371155.3; ENSG00000139496.16. [Q9BVL2-1]
DR Ensembl; ENST00000463407.5; ENSP00000418555.1; ENSG00000139496.16. [Q9BVL2-2]
DR GeneID; 9818; -.
DR KEGG; hsa:9818; -.
DR MANE-Select; ENST00000381736.8; ENSP00000371155.3; NM_014089.4; NP_054808.1.
DR UCSC; uc001uqg.2; human. [Q9BVL2-1]
DR CTD; 9818; -.
DR DisGeNET; 9818; -.
DR GeneCards; NUP58; -.
DR HGNC; HGNC:20261; NUP58.
DR HPA; ENSG00000139496; Low tissue specificity.
DR MIM; 607615; gene.
DR neXtProt; NX_Q9BVL2; -.
DR OpenTargets; ENSG00000139496; -.
DR PharmGKB; PA134981903; -.
DR VEuPathDB; HostDB:ENSG00000139496; -.
DR eggNOG; ENOG502QRD8; Eukaryota.
DR GeneTree; ENSGT00730000111111; -.
DR HOGENOM; CLU_034851_2_0_1; -.
DR InParanoid; Q9BVL2; -.
DR OMA; RWYKATI; -.
DR OrthoDB; 885529at2759; -.
DR PhylomeDB; Q9BVL2; -.
DR TreeFam; TF106502; -.
DR PathwayCommons; Q9BVL2; -.
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-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q9BVL2; -.
DR SIGNOR; Q9BVL2; -.
DR BioGRID-ORCS; 9818; 298 hits in 1090 CRISPR screens.
DR ChiTaRS; NUP58; human.
DR GeneWiki; NUPL1; -.
DR GenomeRNAi; 9818; -.
DR Pharos; Q9BVL2; Tbio.
DR PRO; PR:Q9BVL2; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9BVL2; protein.
DR Bgee; ENSG00000139496; Expressed in adrenal tissue and 194 other tissues.
DR ExpressionAtlas; Q9BVL2; baseline and differential.
DR Genevisible; Q9BVL2; HS.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042306; P:regulation of protein import into nucleus; IEA:Ensembl.
DR InterPro; IPR024882; Nucleoporin_p58/p45.
DR PANTHER; PTHR13437; PTHR13437; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Glycoprotein; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..599
FT /note="Nucleoporin p58/p45"
FT /id="PRO_0000204892"
FT REPEAT 7..8
FT /note="1"
FT REPEAT 30..31
FT /note="2"
FT REPEAT 44..45
FT /note="3"
FT REPEAT 63..64
FT /note="4"
FT REPEAT 68..69
FT /note="5"
FT REPEAT 488..489
FT /note="6"
FT REPEAT 492..493
FT /note="7"
FT REPEAT 513..514
FT /note="8"
FT REPEAT 519..520
FT /note="9"
FT REPEAT 529..530
FT /note="10"
FT REPEAT 531..532
FT /note="11"
FT REPEAT 545..546
FT /note="12"
FT REPEAT 568..569
FT /note="13"
FT REPEAT 578..579
FT /note="14"
FT REGION 7..579
FT /note="14 X 2 AA repeats of F-G"
FT REGION 213..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..276
FT /evidence="ECO:0000255"
FT COILED 314..381
FT /evidence="ECO:0000255"
FT COMPBIAS 224..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 84..95
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045658"
FT VAR_SEQ 480..485
FT /note="PQPSLG -> LNAFKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9455477"
FT /id="VSP_007946"
FT VAR_SEQ 486..599
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9455477"
FT /id="VSP_007947"
FT VARIANT 34
FT /note="A -> T (in dbSNP:rs11556093)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_050570"
FT VARIANT 166
FT /note="S -> P (in dbSNP:rs12871608)"
FT /id="VAR_050571"
FT HELIX 345..371
FT /evidence="ECO:0007829|PDB:4JO7"
FT TURN 372..376
FT /evidence="ECO:0007829|PDB:4JQ5"
FT HELIX 382..424
FT /evidence="ECO:0007829|PDB:4JO7"
SQ SEQUENCE 599 AA; 60897 MW; 2CC32E2A1B9E5132 CRC64;
MSTGFSFGSG TLGSTTVAAG GTSTGGVFSF GTGASSNPSV GLNFGNLGST STPATTSAPS
SGFGTGLFGS KPATGFTLGG TNTGIATTIT TGLTLGTPAT TSAATTGFSL GFNKPAASAT
PFALPITSTS ASGLTLSSAL TSTPAASTGF TLNNLGGTTA TTTTASTGLS LGGALAGLGG
SLFQSTNTGT SGLGQNALGL TLGTTAATST AGNEGLGGID FSSSSDKKSD KTGTRPEDSK
ALKDENLPPV ICQDVENLQK FVKEQKQVQE EISRMSSKAM LKVQEDIKAL KQLLSLAANG
IQRNTLNIDK LKIETAQELK NAEIALRTQK TPPGLQHEYA APADYFRILV QQFEVQLQQY
RQQIEELENH LATQANNSHI TPQDLSMAMQ KIYQTFVALA AQLQSIHENV KVLKEQYLGY
RKMFLGDAVD VFETRRAEAK KWQNTPRVTT GPTPFSTMPN AAAVAMAATL TQQQQPATGP
QPSLGVSFGT PFGSGIGTGL QSSGLGSSNL GGFGTSSGFG CSTTGASTFG FGTTNKPSGS
LSAGFGSSST SGFNFSNPGI TASAGLTFGV SNPASAGFGT GGQLLQLKKP PAGNKRGKR
