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 27-MAR-2024, entry version 231. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 PDB; 7R5J; EM; 50.00 A; J0/J1/J2/J3/J4=1-522. DR PDB; 7R5K; EM; 12.00 A; J0/J1/J2/J3/J4=1-522. DR PDBsum; 5IJN; -. DR PDBsum; 5IJO; -. DR PDBsum; 7PER; -. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR AlphaFoldDB; P37198; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; P37198; -. DR BioGRID; 117165; 277. DR ComplexPortal; CPX-873; Nuclear pore complex. DR DIP; DIP-29749N; -. DR IntAct; P37198; 126. 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-GlcNAc glycan. DR GlyCosmos; P37198; 89 sites, 2 glycans. DR GlyGen; P37198; 102 sites, 2 O-linked glycans (101 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; 9606-ENSP00000471191; -. DR PeptideAtlas; P37198; -. DR ProteomicsDB; 55266; -. DR Pumba; P37198; -. DR Antibodypedia; 1686; 433 antibodies from 38 providers. DR DNASU; 23636; -. DR Ensembl; ENST00000352066.8; ENSP00000305503.3; ENSG00000213024.13. DR Ensembl; ENST00000422090.2; ENSP00000407331.1; ENSG00000213024.13. DR Ensembl; ENST00000596217.1; ENSP00000471191.1; ENSG00000213024.13. DR Ensembl; ENST00000596437.6; ENSP00000468842.2; ENSG00000213024.13. DR Ensembl; ENST00000597029.6; ENSP00000473192.1; ENSG00000213024.13. DR Ensembl; ENST00000598301.2; ENSP00000515009.1; ENSG00000213024.13. DR Ensembl; ENST00000599560.6; ENSP00000515013.1; ENSG00000213024.13. DR Ensembl; ENST00000599788.2; ENSP00000468884.2; ENSG00000213024.13. DR Ensembl; ENST00000600583.6; ENSP00000515011.1; ENSG00000213024.13. DR Ensembl; ENST00000600935.2; ENSP00000468839.2; ENSG00000213024.13. DR Ensembl; ENST00000700473.1; ENSP00000515006.1; ENSG00000213024.13. DR Ensembl; ENST00000700474.1; ENSP00000515007.1; ENSG00000213024.13. DR Ensembl; ENST00000700475.1; ENSP00000515008.1; ENSG00000213024.13. DR Ensembl; ENST00000700476.1; ENSP00000515010.1; ENSG00000213024.13. DR Ensembl; ENST00000700477.1; ENSP00000515012.1; ENSG00000213024.13. DR Ensembl; ENST00000700478.1; ENSP00000515014.1; ENSG00000213024.13. 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 AGR; HGNC:8066; -. 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; 11989at2759; -. 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; 654 hits in 1167 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 199 other cell types or tissues. DR ExpressionAtlas; P37198; baseline and differential. 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: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 chromosome alignment; 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: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; NAS:ComplexPortal. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0046601; P:positive regulation of centriole replication; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; NAS: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: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 Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR026010; NSP1/NUP62. DR InterPro; IPR007758; Nucleoporin_NSP1_C. DR PANTHER; PTHR12084:SF0; NUCLEAR PORE GLYCOPROTEIN P62; 1. DR PANTHER; PTHR12084; NUCLEAR PORE GLYCOPROTEIN P62-RELATED; 1. DR Pfam; PF05064; Nsp1_C; 1. DR Genevisible; P37198; HS. 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 //