NUP85_HUMAN
ID NUP85_HUMAN Reviewed; 656 AA.
AC Q9BW27; B4DMQ3; B4DPW1; Q8NDI4; Q9H9U1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nuclear pore complex protein Nup85;
DE AltName: Full=85 kDa nucleoporin;
DE AltName: Full=FROUNT;
DE AltName: Full=Nucleoporin Nup75;
DE AltName: Full=Nucleoporin Nup85;
DE AltName: Full=Pericentrin-1;
GN Name=NUP85; Synonyms=NUP75, PCNT1;
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX.
RX PubMed=12196509; DOI=10.1083/jcb.200206106;
RA Cronshaw J.M., Krutchinsky A.N., Zhang W., Chait B.T., Matunis M.J.;
RT "Proteomic analysis of the mammalian nuclear pore complex.";
RL J. Cell Biol. 158:915-927(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN CCR2 SIGNALING,
RP INTERACTION WITH CCR2, AND SUBCELLULAR LOCATION.
RX PubMed=15995708; DOI=10.1038/ni1222;
RA Terashima Y., Onai N., Murai M., Enomoto M., Poonpiriya V., Hamada T.,
RA Motomura K., Suwa M., Ezaki T., Haga T., Kanegasaki S., Matsushima K.;
RT "Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte
RT chemotaxis.";
RL Nat. Immunol. 6:827-835(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
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] (ISOFORM 1).
RC TISSUE=Colon;
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 FUNCTION IN NPC ASSEMBLY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP NUP160; NUP133 AND SEC13.
RX PubMed=12718872; DOI=10.1016/s1097-2765(03)00116-3;
RA Harel A., Orjalo A.V., Vincent T., Lachish-Zalait A., Vasu S., Shah S.,
RA Zimmerman E., Elbaum M., Forbes D.J.;
RT "Removal of a single pore subcomplex results in vertebrate nuclei devoid of
RT nuclear pores.";
RL Mol. Cell 11:853-864(2003).
RN [9]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE NUP107-160 COMPLEX, AND
RP INTERACTION WITH NUP37; NUP107; NUP43 AND SEC13.
RX PubMed=15146057; DOI=10.1091/mbc.e03-12-0878;
RA Loieodice I., Alves A., Rabut G., Van Overbeek M., Ellenberg J.,
RA Sibarita J.-B., Doye V.;
RT "The entire Nup107-160 complex, including three new members, is targeted as
RT one entity to kinetochores in mitosis.";
RL Mol. Biol. Cell 15:3333-3344(2004).
RN [10]
RP FUNCTION IN SPINDLE ASSEMBLY, AND SUBCELLULAR LOCATION.
RX PubMed=16807356; DOI=10.1091/mbc.e05-11-1061;
RA Orjalo A.V., Arnaoutov A., Shen Z., Boyarchuk Y., Zeitlin S.G.,
RA Fontoura B., Briggs S., Dasso M., Forbes D.J.;
RT "The Nup107-160 nucleoporin complex is required for correct bipolar spindle
RT assembly.";
RL Mol. Biol. Cell 17:3806-3818(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [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 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 [15]
RP FUNCTION, INTERACTION WITH NUP160, INVOLVEMENT IN NPHS17, VARIANTS NPHS17
RP VAL-477; PRO-581 AND TRP-645, AND CHARACTERIZATION OF VARIANTS NPHS17
RP VAL-477; PRO-581 AND TRP-645.
RX PubMed=30179222; DOI=10.1172/jci98688;
RA Braun D.A., Lovric S., Schapiro D., Schneider R., Marquez J., Asif M.,
RA Hussain M.S., Daga A., Widmeier E., Rao J., Ashraf S., Tan W., Lusk C.P.,
RA Kolb A., Jobst-Schwan T., Schmidt J.M., Hoogstraten C.A., Eddy K.,
RA Kitzler T.M., Shril S., Moawia A., Schrage K., Khayyat A.I.A., Lawson J.A.,
RA Gee H.Y., Warejko J.K., Hermle T., Majmundar A.J., Hugo H., Budde B.,
RA Motameny S., Altmueller J., Noegel A.A., Fathy H.M., Gale D.P.,
RA Waseem S.S., Khan A., Kerecuk L., Hashmi S., Mohebbi N., Ettenger R.,
RA Serdaroglu E., Alhasan K.A., Hashem M., Goncalves S., Ariceta G.,
RA Ubetagoyena M., Antonin W., Baig S.M., Alkuraya F.S., Shen Q., Xu H.,
RA Antignac C., Lifton R.P., Mane S., Nuernberg P., Khokha M.K.,
RA Hildebrandt F.;
RT "Mutations in multiple components of the nuclear pore complex cause
RT nephrotic syndrome.";
RL J. Clin. Invest. 128:4313-4328(2018).
CC -!- FUNCTION: Essential component of the nuclear pore complex (NPC) that
CC seems to be required for NPC assembly and maintenance
CC (PubMed:12718872). As part of the NPC Nup107-160 subcomplex plays a
CC role in RNA export and in tethering NUP96/Nup98 and NUP153 to the
CC nucleus (PubMed:12718872). The Nup107-160 complex seems to be required
CC for spindle assembly during mitosis (PubMed:16807356). NUP85 is
CC required for membrane clustering of CCL2-activated CCR2
CC (PubMed:15995708). Seems to be involved in CCR2-mediated chemotaxis of
CC monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-
CC kinase-Rac-lammellipodium protrusion cascade (PubMed:15995708).
CC Involved in nephrogenesis (PubMed:30179222).
CC {ECO:0000269|PubMed:12718872, ECO:0000269|PubMed:15995708,
CC ECO:0000269|PubMed:16807356, ECO:0000269|PubMed:30179222}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC) (PubMed:12196509).
CC Component of the NPC Nup107-160 subcomplex, consisting of at least
CC NUP107, NUP98/Nup96, NUP160, NUP133, NUP85, NUP37, NUP43 and SEC13
CC (PubMed:15146057). Interacts with NUP160, NUP133 and SEC13
CC (PubMed:12718872, PubMed:30179222). Interacts with NUP37, NUP107 and
CC NUP43 (PubMed:15146057). Interacts with CCR2 (PubMed:15995708).
CC {ECO:0000269|PubMed:12196509, ECO:0000269|PubMed:12718872,
CC ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:15995708,
CC ECO:0000269|PubMed:30179222}.
CC -!- INTERACTION:
CC Q9BW27; P41597-2: CCR2; NbExp=3; IntAct=EBI-716392, EBI-14807859;
CC Q9BW27; Q7L5D6: GET4; NbExp=3; IntAct=EBI-716392, EBI-711823;
CC Q9BW27; Q8WUM0: NUP133; NbExp=2; IntAct=EBI-716392, EBI-295695;
CC Q9BW27; Q12769: NUP160; NbExp=3; IntAct=EBI-716392, EBI-295715;
CC Q9BW27; Q96EE3: SEH1L; NbExp=3; IntAct=EBI-716392, EBI-922818;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:12196509, ECO:0000269|PubMed:12718872}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:12718872,
CC ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:16807356}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:16807356}. Cytoplasm
CC {ECO:0000269|PubMed:15995708}. Nucleus membrane
CC {ECO:0000269|PubMed:12196509}. Note=During mitosis, localizes to the
CC kinetochores and spindle poles (PubMed:12718872, PubMed:16807356). Upon
CC CCl2 stimulation translocates from the cytoplasm to the membrane and
CC colocalizes with CCR2 at the front of migrating cells
CC (PubMed:15995708). {ECO:0000269|PubMed:12718872,
CC ECO:0000269|PubMed:15995708, ECO:0000269|PubMed:16807356}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BW27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BW27-2; Sequence=VSP_056080, VSP_056081, VSP_056082;
CC Name=3;
CC IsoId=Q9BW27-3; Sequence=VSP_056079;
CC -!- DISEASE: Nephrotic syndrome 17 (NPHS17) [MIM:618176]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form that progresses to end-stage renal failure.
CC NPHS17 is an autosomal recessive, steroid-resistant progressive form
CC with onset in the first decade of life. {ECO:0000269|PubMed:30179222}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the nucleoporin Nup85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD38749.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF514995; AAM76706.1; -; mRNA.
DR EMBL; AF498261; AAM18528.1; -; mRNA.
DR EMBL; AK022611; BAB14130.1; -; mRNA.
DR EMBL; AK297574; BAG59965.1; -; mRNA.
DR EMBL; AK298519; BAG60723.1; -; mRNA.
DR EMBL; AL833893; CAD38749.1; ALT_INIT; mRNA.
DR EMBL; AC022211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89251.1; -; Genomic_DNA.
DR EMBL; BC000697; AAH00697.1; -; mRNA.
DR CCDS; CCDS32730.1; -. [Q9BW27-1]
DR RefSeq; NP_001290205.1; NM_001303276.1. [Q9BW27-3]
DR RefSeq; NP_079120.1; NM_024844.4. [Q9BW27-1]
DR PDB; 5A9Q; EM; 23.00 A; 8/H/Q/Z=1-656.
DR PDB; 7PEQ; EM; 35.00 A; AH/BH/CH/DH=1-656.
DR PDBsum; 5A9Q; -.
DR PDBsum; 7PEQ; -.
DR AlphaFoldDB; Q9BW27; -.
DR SMR; Q9BW27; -.
DR BioGRID; 122985; 115.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; Q9BW27; -.
DR IntAct; Q9BW27; 44.
DR MINT; Q9BW27; -.
DR STRING; 9606.ENSP00000245544; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q9BW27; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BW27; -.
DR MetOSite; Q9BW27; -.
DR PhosphoSitePlus; Q9BW27; -.
DR BioMuta; NUP85; -.
DR DMDM; 74733394; -.
DR EPD; Q9BW27; -.
DR jPOST; Q9BW27; -.
DR MassIVE; Q9BW27; -.
DR MaxQB; Q9BW27; -.
DR PaxDb; Q9BW27; -.
DR PeptideAtlas; Q9BW27; -.
DR PRIDE; Q9BW27; -.
DR ProteomicsDB; 4631; -.
DR ProteomicsDB; 4821; -.
DR ProteomicsDB; 79251; -. [Q9BW27-1]
DR Antibodypedia; 32118; 232 antibodies from 31 providers.
DR DNASU; 79902; -.
DR Ensembl; ENST00000245544.9; ENSP00000245544.4; ENSG00000125450.11. [Q9BW27-1]
DR GeneID; 79902; -.
DR KEGG; hsa:79902; -.
DR MANE-Select; ENST00000245544.9; ENSP00000245544.4; NM_024844.5; NP_079120.1.
DR UCSC; uc002jng.2; human. [Q9BW27-1]
DR CTD; 79902; -.
DR DisGeNET; 79902; -.
DR GeneCards; NUP85; -.
DR HGNC; HGNC:8734; NUP85.
DR HPA; ENSG00000125450; Low tissue specificity.
DR MalaCards; NUP85; -.
DR MIM; 170285; gene.
DR MIM; 618176; phenotype.
DR neXtProt; NX_Q9BW27; -.
DR OpenTargets; ENSG00000125450; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR Orphanet; 808; Seckel syndrome.
DR PharmGKB; PA142671241; -.
DR VEuPathDB; HostDB:ENSG00000125450; -.
DR eggNOG; KOG2271; Eukaryota.
DR GeneTree; ENSGT00390000000204; -.
DR InParanoid; Q9BW27; -.
DR OMA; ELMEWLN; -.
DR OrthoDB; 588551at2759; -.
DR PhylomeDB; Q9BW27; -.
DR TreeFam; TF323240; -.
DR PathwayCommons; Q9BW27; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
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-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
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-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
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-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q9BW27; -.
DR SIGNOR; Q9BW27; -.
DR BioGRID-ORCS; 79902; 735 hits in 1053 CRISPR screens.
DR ChiTaRS; NUP85; human.
DR GeneWiki; NUP85; -.
DR GenomeRNAi; 79902; -.
DR Pharos; Q9BW27; Tbio.
DR PRO; PR:Q9BW27; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BW27; protein.
DR Bgee; ENSG00000125450; Expressed in cerebellar hemisphere and 169 other tissues.
DR ExpressionAtlas; Q9BW27; baseline and differential.
DR Genevisible; Q9BW27; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; IC:ComplexPortal.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0048246; P:macrophage chemotaxis; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0072006; P:nephron development; IMP:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR InterPro; IPR011502; Nucleoporin_Nup85.
DR PANTHER; PTHR13373; PTHR13373; 1.
DR Pfam; PF07575; Nucleopor_Nup85; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Disease variant; Kinetochore; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..656
FT /note="Nuclear pore complex protein Nup85"
FT /id="PRO_0000324187"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R480"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_056079"
FT VAR_SEQ 1..31
FT /note="MEELDGEPTVTLIPGVNSKKNQMYFDWGPGE -> MAASSAARSPFCQQWSS
FT SGTCVRFFLLKWPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056080"
FT VAR_SEQ 32..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056081"
FT VAR_SEQ 591..656
FT /note="IFSAEQTYELMRCLEDLTSRRPVHGESDTEQLQDDDIETTKVEMLRLSLARN
FT LARAIIREGSLEGS -> KVAAAVVFFACQSLLELSCIAVADVRVSSFVVLPVRVYSP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056082"
FT VARIANT 477
FT /note="A -> V (in NPHS17; unknown pathological
FT significance; dbSNP:rs1568094661)"
FT /evidence="ECO:0000269|PubMed:30179222"
FT /id="VAR_081364"
FT VARIANT 581
FT /note="A -> P (in NPHS17; decreased function in
FT nephrogenesis; unable to fully rescue morpholino-induced
FT nephrogenesis defects in Xenopus; decreased interaction
FT with NUP160; dbSNP:rs1321552081)"
FT /evidence="ECO:0000269|PubMed:30179222"
FT /id="VAR_081365"
FT VARIANT 645
FT /note="R -> W (in NPHS17; loss of function in
FT nephrogenesis; unable to rescue morpholino-induced
FT nephrogenesis defects in Xenopus; decreased interaction
FT with NUP160; dbSNP:rs368572297)"
FT /evidence="ECO:0000269|PubMed:30179222"
FT /id="VAR_081366"
FT CONFLICT 501
FT /note="L -> P (in Ref. 3; BAB14130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 75019 MW; 1AE2BA17D9CADF3D CRC64;
MEELDGEPTV TLIPGVNSKK NQMYFDWGPG EMLVCETSFN KKEKSEMVPS CPFIYIIRKD
VDVYSQILRK LFNESHGIFL GLQRIDEELT GKSRKSQLVR VSKNYRSVIR ACMEEMHQVA
IAAKDPANGR QFSSQVSILS AMELIWNLCE ILFIEVAPAG PLLLHLLDWV RLHVCEVDSL
SADVLGSENP SKHDSFWNLV TILVLQGRLD EARQMLSKEA DASPASAGIC RIMGDLMRTM
PILSPGNTQT LTELELKWQH WHEECERYLQ DSTFATSPHL ESLLKIMLGD EAALLEQKEL
LSNWYHFLVT RLLYSNPTVK PIDLHYYAQS SLDLFLGGES SPEPLDNILL AAFEFDIHQV
IKECSIALSN WWFVAHLTDL LDHCKLLQSH NLYFGSNMRE FLLLEYASGL FAHPSLWQLG
VDYFDYCPEL GRVSLELHIE RIPLNTEQKA LKVLRICEQR QMTEQVRSIC KILAMKAVRN
NRLGSALSWS IRAKDAAFAT LVSDRFLRDY CERGCFSDLD LIDNLGPAMM LSDRLTFLGK
YREFHRMYGE KRFADAASLL LSLMTSRIAP RSFWMTLLTD ALPLLEQKQV IFSAEQTYEL
MRCLEDLTSR RPVHGESDTE QLQDDDIETT KVEMLRLSLA RNLARAIIRE GSLEGS
