NUP62_HUMAN
ID NUP62_HUMAN Reviewed; 522 AA.
AC P37198; B3KWU5; Q503A4; Q6GTM2; Q96C43; Q9NSL1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Nuclear pore glycoprotein p62;
DE AltName: Full=62 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup62;
GN Name=NUP62;
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], FUNCTION, SUBCELLULAR LOCATION, AND VARIANT
RP THR-283.
RX PubMed=1915414;
RA Carmo-Fonseca M., Kern H., Hurt E.C.;
RT "Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1
RT show sequence homology and a similar domain organization.";
RL Eur. J. Cell Biol. 55:17-30(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-283.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
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], AND VARIANT THR-283.
RC TISSUE=Pancreas, Skin, and Urinary bladder;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP INTERACTION WITH CAPG.
RX PubMed=18266911; DOI=10.1111/j.1600-0854.2008.00720.x;
RA Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C.,
RA Vandekerckhove J., Gettemans J.;
RT "A new role for nuclear transport factor 2 and Ran: nuclear import of
RT CapG.";
RL Traffic 9:695-707(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, 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 [13]
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 [14]
RP INTERACTION WITH OSBPL8.
RX PubMed=21698267; DOI=10.1371/journal.pone.0021078;
RA Zhou T., Li S., Zhong W., Vihervaara T., Beaslas O., Perttila J., Luo W.,
RA Jiang Y., Lehto M., Olkkonen V.M., Yan D.;
RT "OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid
RT levels and interacts with the nucleoporin Nup62.";
RL PLoS ONE 6:E21078-E21078(2011).
RN [15]
RP INTERACTION WITH HIKESHI.
RX PubMed=22541429; DOI=10.1016/j.cell.2012.02.058;
RA Kose S., Furuta M., Imamoto N.;
RT "Hikeshi, a nuclear import carrier for hsp70s, protects cells from heat
RT shock-induced nuclear damage.";
RL Cell 149:578-589(2012).
RN [16]
RP INTERACTION WITH EPSTEIN-BARR VIRUS BGLF4.
RX PubMed=22623767; DOI=10.1128/jvi.01058-12;
RA Chang C.W., Lee C.P., Huang Y.H., Yang P.W., Wang J.T., Chen M.R.;
RT "Epstein-Barr virus protein kinase BGLF4 targets the nucleus through
RT interaction with nucleoporins.";
RL J. Virol. 86:8072-8085(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP FUNCTION, INTERACTION WITH SAS6 AND TUBG1, AND SUBCELLULAR LOCATION.
RX PubMed=24107630; DOI=10.4161/cc.26671;
RA Hashizume C., Moyori A., Kobayashi A., Yamakoshi N., Endo A., Wong R.W.;
RT "Nucleoporin Nup62 maintains centrosome homeostasis.";
RL Cell Cycle 12:3804-3816(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-418, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [20]
RP INTERACTION WITH MCM3AP.
RX PubMed=23652018; DOI=10.1038/ncomms2823;
RA Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P.,
RA Goodman M.F., Sakaguchi N.;
RT "GANP regulates recruitment of AID to immunoglobulin variable regions by
RT modulating transcription and nucleosome occupancy.";
RL Nat. Commun. 4:1830-1830(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 INVOLVEMENT IN SNDI, AND VARIANT SNDI PRO-391.
RX PubMed=16786527; DOI=10.1002/ana.20902;
RA Basel-Vanagaite L., Muncher L., Straussberg R., Pasmanik-Chor M., Yahav M.,
RA Rainshtein L., Walsh C.A., Magal N., Taub E., Drasinover V., Shalev H.,
RA Attia R., Rechavi G., Simon A.J., Shohat M.;
RT "Mutated nup62 causes autosomal recessive infantile bilateral striatal
RT necrosis.";
RL Ann. Neurol. 60:214-222(2006).
RN [23]
RP INTERACTION WITH NUP88.
RX PubMed=30543681; DOI=10.1371/journal.pgen.1007845;
RA Bonnin E., Cabochette P., Filosa A., Juehlen R., Komatsuzaki S.,
RA Hezwani M., Dickmanns A., Martinelli V., Vermeersch M., Supply L.,
RA Martins N., Pirenne L., Ravenscroft G., Lombard M., Port S., Spillner C.,
RA Janssens S., Roets E., Van Dorpe J., Lammens M., Kehlenbach R.H.,
RA Ficner R., Laing N.G., Hoffmann K., Vanhollebeke B., Fahrenkrog B.;
RT "Biallelic mutations in nucleoporin NUP88 cause lethal fetal akinesia
RT deformation sequence.";
RL PLoS Genet. 14:E1007845-E1007845(2018).
CC -!- FUNCTION: Essential component of the nuclear pore complex
CC (PubMed:1915414). The N-terminal is probably involved in
CC nucleocytoplasmic transport (PubMed:1915414). The C-terminal is
CC involved in protein-protein interaction probably via coiled-coil
CC formation, promotes its association with centrosomes and may function
CC in anchorage of p62 to the pore complex (PubMed:1915414,
CC PubMed:24107630). Plays a role in mitotic cell cycle progression by
CC regulating centrosome segregation, centriole maturation and spindle
CC orientation (PubMed:24107630). It might be involved in protein
CC recruitment to the centrosome after nuclear breakdown
CC (PubMed:24107630). {ECO:0000269|PubMed:1915414,
CC ECO:0000269|PubMed:24107630}.
CC -!- SUBUNIT: Component of the p62 complex, a complex at least composed of
CC NUP62, NUP54, and NUP58 (By similarity). Interacts with NUP88
CC (PubMed:30543681). Interacts with NUTF2 (By similarity). Interacts with
CC HIKESHI (PubMed:22541429). Interacts with OSBPL8 (PubMed:21698267).
CC Interacts with CAPG (PubMed:18266911). Interacts with SAS6 and TUBG1 at
CC the centrosome (PubMed:24107630). Interacts with MCM3AP isoform GANP
CC (PubMed:23652018). {ECO:0000250|UniProtKB:P17955,
CC ECO:0000269|PubMed:18266911, ECO:0000269|PubMed:21698267,
CC ECO:0000269|PubMed:22541429, ECO:0000269|PubMed:23652018,
CC ECO:0000269|PubMed:24107630, ECO:0000269|PubMed:30543681}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-barr virus BGLF4;
CC this interaction allows BGLF4 nuclear entry.
CC {ECO:0000269|PubMed:22623767}.
CC -!- INTERACTION:
CC P37198; Q9NYB9: ABI2; NbExp=6; IntAct=EBI-347978, EBI-743598;
CC P37198; Q13444: ADAM15; NbExp=3; IntAct=EBI-347978, EBI-77818;
CC P37198; Q8TD06: AGR3; NbExp=6; IntAct=EBI-347978, EBI-3925742;
CC P37198; P53365: ARFIP2; NbExp=3; IntAct=EBI-347978, EBI-638194;
CC P37198; O15265: ATXN7; NbExp=2; IntAct=EBI-347978, EBI-708350;
CC P37198; Q12934: BFSP1; NbExp=3; IntAct=EBI-347978, EBI-10227494;
CC P37198; Q12934-2: BFSP1; NbExp=3; IntAct=EBI-347978, EBI-12123320;
CC P37198; Q9UL45: BLOC1S6; NbExp=6; IntAct=EBI-347978, EBI-465781;
CC P37198; Q9NWQ9: C14orf119; NbExp=5; IntAct=EBI-347978, EBI-725606;
CC P37198; Q8TAB5: C1orf216; NbExp=6; IntAct=EBI-347978, EBI-747505;
CC P37198; Q969G5: CAVIN3; NbExp=3; IntAct=EBI-347978, EBI-3893101;
CC P37198; Q6ZUS5: CCDC121; NbExp=4; IntAct=EBI-347978, EBI-2836982;
CC P37198; Q8IYE0: CCDC146; NbExp=5; IntAct=EBI-347978, EBI-10749669;
CC P37198; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-347978, EBI-10247802;
CC P37198; Q8NCX0: CCDC150; NbExp=3; IntAct=EBI-347978, EBI-10269342;
CC P37198; Q494R4: CCDC153; NbExp=3; IntAct=EBI-347978, EBI-10241443;
CC P37198; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-347978, EBI-10175300;
CC P37198; Q71F23: CENPU; NbExp=3; IntAct=EBI-347978, EBI-2515234;
CC P37198; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-347978, EBI-10181988;
CC P37198; Q9UGL9: CRCT1; NbExp=6; IntAct=EBI-347978, EBI-713677;
CC P37198; Q6W0C5: DPPA3; NbExp=3; IntAct=EBI-347978, EBI-12082590;
CC P37198; O60941: DTNB; NbExp=5; IntAct=EBI-347978, EBI-740402;
CC P37198; O60941-5: DTNB; NbExp=3; IntAct=EBI-347978, EBI-11984733;
CC P37198; P05413: FABP3; NbExp=7; IntAct=EBI-347978, EBI-704216;
CC P37198; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-347978, EBI-2514791;
CC P37198; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-347978, EBI-14103818;
CC P37198; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-347978, EBI-16429135;
CC P37198; O14964: HGS; NbExp=3; IntAct=EBI-347978, EBI-740220;
CC P37198; Q03933: HSF2; NbExp=5; IntAct=EBI-347978, EBI-2556750;
CC P37198; Q03933-2: HSF2; NbExp=3; IntAct=EBI-347978, EBI-10223348;
CC P37198; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-347978, EBI-12056251;
CC P37198; Q8IY31: IFT20; NbExp=3; IntAct=EBI-347978, EBI-744203;
CC P37198; Q70UQ0: IKBIP; NbExp=3; IntAct=EBI-347978, EBI-2557212;
CC P37198; Q9H1K1: ISCU; NbExp=6; IntAct=EBI-347978, EBI-1047335;
CC P37198; Q7Z3B3: KANSL1; NbExp=4; IntAct=EBI-347978, EBI-740244;
CC P37198; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-347978, EBI-2125614;
CC P37198; Q5THT1: KLHL32; NbExp=3; IntAct=EBI-347978, EBI-10247181;
CC P37198; P52292: KPNA2; NbExp=3; IntAct=EBI-347978, EBI-349938;
CC P37198; P04264: KRT1; NbExp=7; IntAct=EBI-347978, EBI-298429;
CC P37198; P35900: KRT20; NbExp=7; IntAct=EBI-347978, EBI-742094;
CC P37198; P12035: KRT3; NbExp=3; IntAct=EBI-347978, EBI-2430095;
CC P37198; P02538: KRT6A; NbExp=3; IntAct=EBI-347978, EBI-702198;
CC P37198; P04259: KRT6B; NbExp=3; IntAct=EBI-347978, EBI-740907;
CC P37198; O95678: KRT75; NbExp=5; IntAct=EBI-347978, EBI-2949715;
CC P37198; P25791: LMO2; NbExp=3; IntAct=EBI-347978, EBI-739696;
CC P37198; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-347978, EBI-739832;
CC P37198; Q9BW11: MXD3; NbExp=3; IntAct=EBI-347978, EBI-741574;
CC P37198; Q7Z3B4: NUP54; NbExp=12; IntAct=EBI-347978, EBI-741048;
CC P37198; Q9BVL2: NUP58; NbExp=7; IntAct=EBI-347978, EBI-2811583;
CC P37198; Q99567: NUP88; NbExp=6; IntAct=EBI-347978, EBI-726178;
CC P37198; P61970: NUTF2; NbExp=7; IntAct=EBI-347978, EBI-591778;
CC P37198; Q9UBU9: NXF1; NbExp=11; IntAct=EBI-347978, EBI-398874;
CC P37198; O43482: OIP5; NbExp=6; IntAct=EBI-347978, EBI-536879;
CC P37198; Q7L8S5: OTUD6A; NbExp=3; IntAct=EBI-347978, EBI-11960139;
CC P37198; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-347978, EBI-448407;
CC P37198; Q96BD5: PHF21A; NbExp=7; IntAct=EBI-347978, EBI-745085;
CC P37198; Q13526: PIN1; NbExp=6; IntAct=EBI-347978, EBI-714158;
CC P37198; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-347978, EBI-455078;
CC P37198; O75971: SNAPC5; NbExp=3; IntAct=EBI-347978, EBI-749483;
CC P37198; A1L4H1: SSC5D; NbExp=6; IntAct=EBI-347978, EBI-10172867;
CC P37198; P51687: SUOX; NbExp=6; IntAct=EBI-347978, EBI-3921347;
CC P37198; Q9NVV9: THAP1; NbExp=12; IntAct=EBI-347978, EBI-741515;
CC P37198; Q04727-2: TLE4; NbExp=3; IntAct=EBI-347978, EBI-12117860;
CC P37198; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-347978, EBI-11059915;
CC P37198; P40222: TXLNA; NbExp=8; IntAct=EBI-347978, EBI-359793;
CC P37198; P10599: TXN; NbExp=3; IntAct=EBI-347978, EBI-594644;
CC P37198; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-347978, EBI-739895;
CC P37198; Q9Y3C0: WASHC3; NbExp=8; IntAct=EBI-347978, EBI-712969;
CC P37198; Q96QU8: XPO6; NbExp=3; IntAct=EBI-347978, EBI-1022896;
CC P37198; Q96QU8-2: XPO6; NbExp=3; IntAct=EBI-347978, EBI-10293124;
CC P37198; Q9H614; NbExp=3; IntAct=EBI-347978, EBI-10249899;
CC P37198; E5LBS6: ORF10; Xeno; NbExp=2; IntAct=EBI-347978, EBI-14033439;
CC P37198; P10238: UL54; Xeno; NbExp=3; IntAct=EBI-347978, EBI-6883946;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:1915414}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:24107630}. Nucleus envelope
CC {ECO:0000269|PubMed:24107630}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:24107630}. Note=Central region of the nuclear pore,
CC within the transporter (PubMed:1915414). During mitotic cell division,
CC it associates with the poles of the mitotic spindle (PubMed:24107630).
CC {ECO:0000269|PubMed:1915414, ECO:0000269|PubMed:24107630}.
CC -!- DOMAIN: Contains FG repeats.
CC -!- PTM: O-glycosylated. Contains about 10 N-acetylglucosamine side chain
CC sites predicted for the entire protein, among which only one in the C-
CC terminal. {ECO:0000305}.
CC -!- PTM: The inner channel of the NPC has a different redox environment
CC from the cytoplasm and allows the formation of interchain disulfide
CC bonds between some nucleoporins, the significant increase of these
CC linkages upon oxidative stress reduces the permeability of the NPC.
CC {ECO:0000250}.
CC -!- DISEASE: Infantile striatonigral degeneration (SNDI) [MIM:271930]:
CC Neurological disorder characterized by symmetrical degeneration of the
CC caudate nucleus, putamen, and occasionally the globus pallidus, with
CC little involvement of the rest of the brain. The clinical features
CC include developmental regression, choreoathetosis, dystonia,
CC spasticity, dysphagia, failure to thrive, nystagmus, optic atrophy, and
CC intellectual disability. {ECO:0000269|PubMed:16786527}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
CC {ECO:0000305}.
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DR EMBL; X58521; CAA41411.1; -; mRNA.
DR EMBL; AL162061; CAB82399.1; -; mRNA.
DR EMBL; AK125857; BAG54257.1; -; mRNA.
DR EMBL; CR541721; CAG46522.1; -; mRNA.
DR EMBL; AC011452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52576.1; -; Genomic_DNA.
DR EMBL; BC003663; AAH03663.1; -; mRNA.
DR EMBL; BC014842; AAH14842.1; -; mRNA.
DR EMBL; BC050717; AAH50717.1; -; mRNA.
DR EMBL; BC095410; AAH95410.1; -; mRNA.
DR EMBL; BC101104; AAI01105.1; -; mRNA.
DR EMBL; BC101105; AAI01106.1; -; mRNA.
DR EMBL; BC101106; AAI01107.1; -; mRNA.
DR EMBL; BC101107; AAI01108.1; -; mRNA.
DR CCDS; CCDS12788.1; -.
DR PIR; S41819; S41819.
DR RefSeq; NP_001180286.1; NM_001193357.1.
DR RefSeq; NP_036478.2; NM_012346.4.
DR RefSeq; NP_057637.2; NM_016553.4.
DR RefSeq; NP_714940.1; NM_153718.3.
DR RefSeq; NP_714941.1; NM_153719.3.
DR PDB; 5IJN; EM; 21.40 A; H/N/T/Z=1-522.
DR PDB; 5IJO; EM; 21.40 A; H/N/T/Z=1-522.
DR PDB; 7PER; EM; 35.00 A; H/N/T/Z=1-522.
DR PDBsum; 5IJN; -.
DR PDBsum; 5IJO; -.
DR PDBsum; 7PER; -.
DR AlphaFoldDB; P37198; -.
DR SMR; P37198; -.
DR BioGRID; 117165; 240.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR DIP; DIP-29749N; -.
DR IntAct; P37198; 125.
DR MINT; P37198; -.
DR STRING; 9606.ENSP00000471191; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR CarbonylDB; P37198; -.
DR GlyConnect; 471; 1 O-Linked glycan.
DR GlyGen; P37198; 90 sites, 2 O-linked glycans (88 sites).
DR iPTMnet; P37198; -.
DR PhosphoSitePlus; P37198; -.
DR SwissPalm; P37198; -.
DR BioMuta; NUP62; -.
DR DMDM; 134047855; -.
DR EPD; P37198; -.
DR jPOST; P37198; -.
DR MassIVE; P37198; -.
DR MaxQB; P37198; -.
DR PaxDb; P37198; -.
DR PeptideAtlas; P37198; -.
DR PRIDE; P37198; -.
DR ProteomicsDB; 55266; -.
DR Antibodypedia; 1686; 378 antibodies from 38 providers.
DR DNASU; 23636; -.
DR Ensembl; ENST00000352066.8; ENSP00000305503.3; ENSG00000213024.12.
DR Ensembl; ENST00000422090.2; ENSP00000407331.1; ENSG00000213024.12.
DR Ensembl; ENST00000596217.1; ENSP00000471191.1; ENSG00000213024.12.
DR Ensembl; ENST00000597029.5; ENSP00000473192.1; ENSG00000213024.12.
DR GeneID; 23636; -.
DR KEGG; hsa:23636; -.
DR MANE-Select; ENST00000352066.8; ENSP00000305503.3; NM_016553.5; NP_057637.2.
DR UCSC; uc002pqy.5; human.
DR CTD; 23636; -.
DR DisGeNET; 23636; -.
DR GeneCards; NUP62; -.
DR HGNC; HGNC:8066; NUP62.
DR HPA; ENSG00000213024; Low tissue specificity.
DR MalaCards; NUP62; -.
DR MIM; 271930; phenotype.
DR MIM; 605815; gene.
DR neXtProt; NX_P37198; -.
DR OpenTargets; ENSG00000213024; -.
DR Orphanet; 225154; Familial infantile bilateral striatal necrosis.
DR PharmGKB; PA31854; -.
DR VEuPathDB; HostDB:ENSG00000213024; -.
DR eggNOG; KOG2196; Eukaryota.
DR GeneTree; ENSGT00940000161737; -.
DR InParanoid; P37198; -.
DR OMA; EMMSKQV; -.
DR OrthoDB; 1420505at2759; -.
DR PhylomeDB; P37198; -.
DR TreeFam; TF324795; -.
DR PathwayCommons; P37198; -.
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; P37198; -.
DR SIGNOR; P37198; -.
DR BioGRID-ORCS; 23636; 620 hits in 1084 CRISPR screens.
DR GeneWiki; Nucleoporin_62; -.
DR GenomeRNAi; 23636; -.
DR Pharos; P37198; Tbio.
DR PRO; PR:P37198; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P37198; protein.
DR Bgee; ENSG00000213024; Expressed in right testis and 197 other tissues.
DR ExpressionAtlas; P37198; baseline and differential.
DR Genevisible; P37198; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0051425; F:PTB domain binding; IEA:Ensembl.
DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0008219; P:cell death; IMP:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0098534; P:centriole assembly; IMP:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0007100; P:mitotic centrosome separation; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IDA:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0046601; P:positive regulation of centriole replication; IMP:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; IMP:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:UniProtKB.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; NAS:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR InterPro; IPR026010; NSP1/NUP62.
DR InterPro; IPR007758; Nucleoporin_NSP1_C.
DR InterPro; IPR033072; NUP62_met.
DR PANTHER; PTHR12084; PTHR12084; 1.
DR PANTHER; PTHR12084:SF12; PTHR12084:SF12; 1.
DR Pfam; PF05064; Nsp1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Disulfide bond; Glycoprotein; Host-virus interaction;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..522
FT /note="Nuclear pore glycoprotein p62"
FT /id="PRO_0000204880"
FT REPEAT 6..7
FT /note="1"
FT REPEAT 44..45
FT /note="2"
FT REPEAT 76..77
FT /note="3"
FT REPEAT 114..115
FT /note="4"
FT REPEAT 142..143
FT /note="5"
FT REGION 6..143
FT /note="5 X 2 AA repeats of F-G"
FT REGION 169..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..458
FT /note="Required for centrosome localization"
FT /evidence="ECO:0000269|PubMed:24107630"
FT COILED 328..458
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 373
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 468
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT DISULFID 475
FT /note="Interchain (with NUP155)"
FT /evidence="ECO:0000250"
FT DISULFID 506
FT /note="Interchain (with NUP155)"
FT /evidence="ECO:0000250"
FT VARIANT 139
FT /note="G -> S (in dbSNP:rs3745489)"
FT /id="VAR_028064"
FT VARIANT 233
FT /note="A -> S (in dbSNP:rs2290772)"
FT /id="VAR_013467"
FT VARIANT 283
FT /note="S -> T (in dbSNP:rs1062798)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:1915414"
FT /id="VAR_028065"
FT VARIANT 391
FT /note="Q -> P (in SNDI; dbSNP:rs121917865)"
FT /evidence="ECO:0000269|PubMed:16786527"
FT /id="VAR_034904"
FT CONFLICT 418..419
FT /note="SG -> RA (in Ref. 1; CAA41411)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="E -> Q (in Ref. 1; CAA41411)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="E -> V (in Ref. 1; CAA41411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 53255 MW; 1FF65018452719A3 CRC64;
MSGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP ATSTPSTGLF
SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS NTAATPAMAN PSGFGLGSSN
LTNAISSTVT SSQGTAPTGF VFGPSTTSVA PATTSGGFSF TGGSTAQPSG FNIGSAGNSA
QPTAPATLPF TPATPAATTA GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC
TPVTTAGAPT AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA
GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH FLQQATQVNA
WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ KELEDLLSPL EELVKEQSGT
IYLQHADEER EKTYKLAENI DAQLKRMAQD LKDIIEHLNT SGAPADTSDP LQQICKILNA
HMDSLQWIDQ NSALLQRKVE EVTKVCEGRR KEQERSFRIT FD
