NU160_HUMAN
ID NU160_HUMAN Reviewed; 1436 AA.
AC Q12769; B4DYE8; B4E2J9; Q08AD3; Q7Z5X6; Q96GB3; Q9H660;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Nuclear pore complex protein Nup160;
DE AltName: Full=160 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup160;
GN Name=NUP160; Synonyms=KIAA0197, NUP120;
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 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 31-1436 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE
RP MRNA] OF 32-1436 (ISOFORM 2), AND VARIANT THR-40.
RC TISSUE=Small intestine, Testis, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-351.
RC TISSUE=Muscle, and Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-1436 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11564755; DOI=10.1083/jcb.200101081;
RA Belgareh N., Rabut G., Bai S.W., van Overbeek M., Beaudouin J., Daigle N.,
RA Zatsepina O.V., Pasteau F., Labas V., Fromont-Racine M., Ellenberg J.,
RA Doye V.;
RT "An evolutionarily conserved NPC subcomplex, which redistributes in part to
RT kinetochores in mammalian cells.";
RL J. Cell Biol. 154:1147-1160(2001).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11684705; DOI=10.1083/jcb.200108007;
RA Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.;
RT "Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA
RT export.";
RL J. Cell Biol. 155:339-354(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-490; SER-949 AND
RP SER-1157, AND IDENTIFICATION BY 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 [15]
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 [16]
RP INVOLVEMENT IN NPHS19, AND VARIANTS NPHS19 LYS-803 AND 910-ARG--LEU-1436
RP DEL.
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).
RN [17]
RP VARIANTS NPHS19 LYS-803 AND 1173-ARG--LEU-1436 DEL.
RX PubMed=30910934; DOI=10.1681/asn.2018080786;
RA Zhao F., Zhu J.Y., Richman A., Fu Y., Huang W., Chen N., Pan X., Yi C.,
RA Ding X., Wang S., Wang P., Nie X., Huang J., Yang Y., Yu Z., Han Z.;
RT "Mutations in NUP160 Are Implicated in Steroid-Resistant Nephrotic
RT Syndrome.";
RL J. Am. Soc. Nephrol. 30:840-853(2019).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC (PubMed:11564755, PubMed:11684705). Involved in poly(A)+ RNA transport.
CC {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC) (PubMed:11564755,
CC PubMed:11684705). Forms part of the NUP160 subcomplex in the nuclear
CC pore which is composed of NUP160, NUP133, NUP107 and NUP96
CC (PubMed:11564755, PubMed:11684705). This complex plays a role in RNA
CC export and in tethering NUP98 and NUP153 to the nucleus
CC (PubMed:11564755, PubMed:11684705). {ECO:0000269|PubMed:11564755,
CC ECO:0000269|PubMed:11684705}.
CC -!- INTERACTION:
CC Q12769; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-295715, EBI-529989;
CC Q12769; P62508: ESRRG; NbExp=3; IntAct=EBI-295715, EBI-2834260;
CC Q12769; Q9BW27: NUP85; NbExp=3; IntAct=EBI-295715, EBI-716392;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:11564755, ECO:0000269|PubMed:11684705}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q12769-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12769-2; Sequence=VSP_007093, VSP_007094;
CC Name=3;
CC IsoId=Q12769-3; Sequence=VSP_037350, VSP_037351, VSP_037352,
CC VSP_037353;
CC -!- DISEASE: Nephrotic syndrome 19 (NPHS19) [MIM:618178]: 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 NPHS19 is an autosomal recessive, steroid-resistant form with onset in
CC the first or second decade of life, resulting in chronic kidney
CC disease. {ECO:0000269|PubMed:30179222, ECO:0000269|PubMed:30910934}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09822.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA12110.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=BAB15406.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG65161.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK026236; BAB15406.1; ALT_INIT; mRNA.
DR EMBL; AK302396; BAG63710.1; -; mRNA.
DR EMBL; AK304308; BAG65161.1; ALT_INIT; mRNA.
DR EMBL; AC021443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008700; AAH08700.1; -; mRNA.
DR EMBL; BC009822; AAH09822.1; ALT_INIT; mRNA.
DR EMBL; BC125227; AAI25228.1; -; mRNA.
DR EMBL; BC125228; AAI25229.1; -; mRNA.
DR EMBL; D83781; BAA12110.1; ALT_SEQ; mRNA.
DR CCDS; CCDS81567.1; -. [Q12769-2]
DR PIR; G02870; G02870.
DR RefSeq; NP_001305328.1; NM_001318399.1. [Q12769-2]
DR RefSeq; NP_056046.1; NM_015231.2. [Q12769-1]
DR PDB; 5A9Q; EM; 23.00 A; 1/J/S/a=1-1436.
DR PDB; 7PEQ; EM; 35.00 A; AJ/BJ/CJ/DJ=1-1436.
DR PDBsum; 5A9Q; -.
DR PDBsum; 7PEQ; -.
DR AlphaFoldDB; Q12769; -.
DR SMR; Q12769; -.
DR BioGRID; 116879; 147.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; Q12769; -.
DR DIP; DIP-31262N; -.
DR IntAct; Q12769; 51.
DR MINT; Q12769; -.
DR STRING; 9606.ENSP00000367721; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q12769; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12769; -.
DR MetOSite; Q12769; -.
DR PhosphoSitePlus; Q12769; -.
DR SwissPalm; Q12769; -.
DR BioMuta; NUP160; -.
DR DMDM; 238054372; -.
DR EPD; Q12769; -.
DR jPOST; Q12769; -.
DR MassIVE; Q12769; -.
DR MaxQB; Q12769; -.
DR PaxDb; Q12769; -.
DR PeptideAtlas; Q12769; -.
DR PRIDE; Q12769; -.
DR ProteomicsDB; 58912; -. [Q12769-1]
DR ProteomicsDB; 58913; -. [Q12769-2]
DR ProteomicsDB; 58914; -. [Q12769-3]
DR Antibodypedia; 26888; 239 antibodies from 32 providers.
DR DNASU; 23279; -.
DR Ensembl; ENST00000378460.6; ENSP00000367721.2; ENSG00000030066.13. [Q12769-1]
DR Ensembl; ENST00000526870.1; ENSP00000431495.1; ENSG00000030066.13. [Q12769-2]
DR GeneID; 23279; -.
DR KEGG; hsa:23279; -.
DR MANE-Select; ENST00000378460.7; ENSP00000367721.3; NM_015231.3; NP_056046.2.
DR UCSC; uc001ngm.4; human. [Q12769-1]
DR CTD; 23279; -.
DR DisGeNET; 23279; -.
DR GeneCards; NUP160; -.
DR HGNC; HGNC:18017; NUP160.
DR HPA; ENSG00000030066; Low tissue specificity.
DR MalaCards; NUP160; -.
DR MIM; 607614; gene.
DR MIM; 618178; phenotype.
DR neXtProt; NX_Q12769; -.
DR NIAGADS; ENSG00000030066; -.
DR OpenTargets; ENSG00000030066; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA31850; -.
DR VEuPathDB; HostDB:ENSG00000030066; -.
DR eggNOG; KOG4521; Eukaryota.
DR GeneTree; ENSGT00390000000972; -.
DR HOGENOM; CLU_005083_0_0_1; -.
DR InParanoid; Q12769; -.
DR OMA; CQFDQAY; -.
DR OrthoDB; 1793363at2759; -.
DR PhylomeDB; Q12769; -.
DR TreeFam; TF353082; -.
DR PathwayCommons; Q12769; -.
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; Q12769; -.
DR SIGNOR; Q12769; -.
DR BioGRID-ORCS; 23279; 744 hits in 1053 CRISPR screens.
DR ChiTaRS; NUP160; human.
DR GeneWiki; NUP160; -.
DR GenomeRNAi; 23279; -.
DR Pharos; Q12769; Tbio.
DR PRO; PR:Q12769; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q12769; protein.
DR Bgee; ENSG00000030066; Expressed in oocyte and 198 other tissues.
DR ExpressionAtlas; Q12769; baseline and differential.
DR Genevisible; Q12769; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0072006; P:nephron development; IMP:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR021717; Nucleoporin_Nup160.
DR PANTHER; PTHR21286; PTHR21286; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..1436
FT /note="Nuclear pore complex protein Nup160"
FT /id="PRO_0000204851"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..250
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037350"
FT VAR_SEQ 175..224
FT /note="SELVVDSQMQSIFTDIGKVDFTDPCNYQLIPAVPGISPNSTASTAWLSSD
FT -> SVSWLSAISFISQITLGVTNVVLERCLLELKEIWILVIPHQAYFDSYRLK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007093"
FT VAR_SEQ 225..1436
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007094"
FT VAR_SEQ 367
FT /note="Q -> QRRGFAMLPGLKLLSSSSPPTSASQCAGITSVNHSTQPEFF (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037351"
FT VAR_SEQ 694..695
FT /note="AQ -> GK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037352"
FT VAR_SEQ 696..1436
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037353"
FT VARIANT 40
FT /note="A -> T (in dbSNP:rs2305984)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_055409"
FT VARIANT 351
FT /note="T -> A (in dbSNP:rs3816605)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055410"
FT VARIANT 803
FT /note="E -> K (in NPHS19; unknown pathological
FT significance; dbSNP:rs775637217)"
FT /evidence="ECO:0000269|PubMed:30179222,
FT ECO:0000269|PubMed:30910934"
FT /id="VAR_081362"
FT VARIANT 910..1436
FT /note="Missing (in NPHS19; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30179222"
FT /id="VAR_081363"
FT VARIANT 1173..1436
FT /note="Missing (in NPHS19; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30910934"
FT /id="VAR_083006"
FT CONFLICT 152
FT /note="I -> K (in Ref. 1; BAG65161)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="G -> S (in Ref. 4; BAA12110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1436 AA; 162121 MW; 274C063A3CE69F48 CRC64;
MLHLSAAPPA PPPEVTATAR PCLCSVGRRG DGGKMAAAGA LERSFVELSG AERERPRHFR
EFTVCSIGTA NAVAGAVKYS ESAGGFYYVE SGKLFSVTRN RFIHWKTSGD TLELMEESLD
INLLNNAIRL KFQNCSVLPG GVYVSETQNR VIILMLTNQT VHRLLLPHPS RMYRSELVVD
SQMQSIFTDI GKVDFTDPCN YQLIPAVPGI SPNSTASTAW LSSDGEALFA LPCASGGIFV
LKLPPYDIPG MVSVVELKQS SVMQRLLTGW MPTAIRGDQS PSDRPLSLAV HCVEHDAFIF
ALCQDHKLRM WSYKEQMCLM VADMLEYVPV KKDLRLTAGT GHKLRLAYSP TMGLYLGIYM
HAPKRGQFCI FQLVSTESNR YSLDHISSLF TSQETLIDFA LTSTDIWALW HDAENQTVVK
YINFEHNVAG QWNPVFMQPL PEEEIVIRDD QDPREMYLQS LFTPGQFTNE ALCKALQIFC
RGTERNLDLS WSELKKEVTL AVENELQGSV TEYEFSQEEF RNLQQEFWCK FYACCLQYQE
ALSHPLALHL NPHTNMVCLL KKGYLSFLIP SSLVDHLYLL PYENLLTEDE TTISDDVDIA
RDVICLIKCL RLIEESVTVD MSVIMEMSCY NLQSPEKAAE QILEDMITID VENVMEDICS
KLQEIRNPIH AIGLLIREMD YETEVEMEKG FNPAQPLNIR MNLTQLYGSN TAGYIVCRGV
HKIASTRFLI CRDLLILQQL LMRLGDAVIW GTGQLFQAQQ DLLHRTAPLL LSYYLIKWGS
ECLATDVPLD TLESNLQHLS VLELTDSGAL MANRFVSSPQ TIVELFFQEV ARKHIISHLF
SQPKAPLSQT GLNWPEMITA ITSYLLQLLW PSNPGCLFLE CLMGNCQYVQ LQDYIQLLHP
WCQVNVGSCR FMLGRCYLVT GEGQKALECF CQAASEVGKE EFLDRLIRSE DGEIVSTPRL
QYYDKVLRLL DVIGLPELVI QLATSAITEA GDDWKSQATL RTCIFKHHLD LGHNSQAYEA
LTQIPDSSRQ LDCLRQLVVV LCERSQLQDL VEFPYVNLHN EVVGIIESRA RAVDLMTHNY
YELLYAFHIY RHNYRKAGTV MFEYGMRLGR EVRTLRGLEK QGNCYLAALN CLRLIRPEYA
WIVQPVSGAV YDRPGASPKR NHDGECTAAP TNRQIEILEL EDLEKECSLA RIRLTLAQHD
PSAVAVAGSS SAEEMVTLLV QAGLFDTAIS LCQTFKLPLT PVFEGLAFKC IKLQFGGEAA
QAEAWAWLAA NQLSSVITTK ESSATDEAWR LLSTYLERYK VQNNLYHHCV INKLLSHGVP
LPNWLINSYK KVDAAELLRL YLNYDLLEEA VDLVSEYVDA VLGKGHQYFG IEFPLSATAP
MVWLPYSSID QLLQALGENS ANSHNIALSQ KILDKLEDYQ QKVDKATRDL LYRRTL
