ID PO210_HUMAN Reviewed; 1887 AA. AC Q8TEM1; A6NN56; O94980; Q6NXG6; Q8NBJ1; Q9H6C8; Q9UFP3; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 27-MAR-2024, entry version 171. DE RecName: Full=Nuclear pore membrane glycoprotein 210; DE Short=Nuclear pore protein gp210; DE AltName: Full=Nuclear envelope pore membrane protein POM 210; DE Short=POM210; DE AltName: Full=Nucleoporin Nup210; DE AltName: Full=Pore membrane protein of 210 kDa; DE Flags: Precursor; GN Name=NUP210; Synonyms=KIAA0906; ORFNames=PSEC0245; 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 GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Spleen; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 763-1887 (ISOFORM 1), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 412-1887 (ISOFORM 2), AND VARIANT LEU-786. RC TISSUE=Brain, and Spleen; 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] OF 965-1887 (ISOFORM 1), VARIANTS RP SER-1752 AND MET-1787, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1405-1887 (ISOFORM 1), AND RP VARIANTS SER-1752 AND MET-1787. RC TISSUE=Ovary tumor; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1460-1887 (ISOFORM 1), AND RP VARIANTS SER-1752 AND MET-1787. 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 [7] RP SUBCELLULAR LOCATION. RC TISSUE=Cervix carcinoma; RX PubMed=2195063; DOI=10.1172/jci114696; RA Courvalin J.-C., Lassoued K., Bartnik E., Blobel G., Wozniak R.W.; RT "The 210-kD nuclear envelope polypeptide recognized by human autoantibodies RT in primary biliary cirrhosis is the major glycoprotein of the nuclear RT pore."; RL J. Clin. Invest. 86:279-285(1990). RN [8] RP FUNCTION. RC TISSUE=Cervix carcinoma; RX PubMed=14517331; DOI=10.1091/mbc.e03-04-0260; RA Cohen M., Feinstein N., Wilson K.L., Gruenbaum Y.; RT "Nuclear pore protein gp210 is essential for viability in HeLa cells and RT Caenorhabditis elegans."; RL Mol. Biol. Cell 14:4230-4237(2003). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1874; SER-1881 AND SER-1886, RP AND IDENTIFICATION BY 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-405; ASN-926 AND ASN-1441. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844; SER-1874 AND SER-1881, RP AND IDENTIFICATION BY 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 THR-1844; SER-1874 AND SER-1881, RP AND IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844, 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844; SER-1874; SER-1877 AND RP SER-1881, 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP VARIANT LEU-786, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17488105; DOI=10.1021/pr0700908; RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A., RA Hendrickson R.C., Stephenson J.L. Jr.; RT "Detection and validation of non-synonymous coding SNPs from orthogonal RT analysis of shotgun proteomics data."; RL J. Proteome Res. 6:2331-2340(2007). CC -!- FUNCTION: Nucleoporin essential for nuclear pore assembly and fusion, CC nuclear pore spacing, as well as structural integrity. CC {ECO:0000269|PubMed:14517331}. CC -!- SUBUNIT: Forms dimers and possibly higher-order oligomers. CC {ECO:0000250}. CC -!- INTERACTION: CC Q8TEM1; Q9NRI5: DISC1; NbExp=2; IntAct=EBI-372826, EBI-529989; CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:2195063}. Nucleus membrane CC {ECO:0000269|PubMed:2195063}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:2195063}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:2195063}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:2195063}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8TEM1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TEM1-2; Sequence=VSP_018567, VSP_018568; CC -!- TISSUE SPECIFICITY: Ubiquitous expression, with highest levels in lung, CC liver, pancreas, testis, and ovary, intermediate levels in brain, CC kidney, and spleen, and lowest levels in heart and skeletal muscle. CC {ECO:0000269|PubMed:10048485}. CC -!- PTM: N-glycosylated, but not all potential glycosylation sites may be CC used. Contains high-mannose type oligosaccharides (By similarity). CC {ECO:0000250}. CC -!- PTM: Phosphorylated at Ser-1881 in mitosis specifically; not CC phosphorylated in interphase. {ECO:0000250}. CC -!- MISCELLANEOUS: Recognized by antinuclear autoantibodies in primary CC biliary cirrhosis. CC -!- MISCELLANEOUS: Knockdown of NUP210 causes nuclear membranes to CC accumulate aberrant structures termed twinned and fusion-arrested CC membranes and nuclear pore complex to cluster. Induces cell death and CC chromatin disruptions. CC -!- SIMILARITY: Belongs to the NUP210 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15332.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC11688.1; Type=Erroneous initiation; Evidence={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; AC027124; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC069246; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC067089; AAH67089.1; -; mRNA. DR EMBL; AK026042; BAB15332.1; ALT_INIT; mRNA. DR EMBL; AK074101; BAB84927.1; -; mRNA. DR EMBL; AB020713; BAA74929.1; -; mRNA. DR EMBL; AK075545; BAC11688.1; ALT_INIT; mRNA. DR EMBL; AL117527; CAB55979.2; -; mRNA. DR CCDS; CCDS33704.1; -. [Q8TEM1-1] DR PIR; T17289; T17289. DR RefSeq; NP_079199.2; NM_024923.3. [Q8TEM1-1] DR PDB; 7R5J; EM; 50.00 A; 10/11/12/13/14/15/16/17=1-1887. DR PDB; 7R5K; EM; 12.00 A; 10/11/12/13/14/15/16/17=1-1887. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR AlphaFoldDB; Q8TEM1; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; Q8TEM1; -. DR BioGRID; 116831; 180. DR ComplexPortal; CPX-873; Nuclear pore complex. DR IntAct; Q8TEM1; 68. DR MINT; Q8TEM1; -. DR STRING; 9606.ENSP00000254508; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyConnect; 1579; 8 N-Linked glycans (5 sites). DR GlyCosmos; Q8TEM1; 12 sites, 7 glycans. DR GlyGen; Q8TEM1; 14 sites, 9 N-linked glycans (5 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q8TEM1; -. DR PhosphoSitePlus; Q8TEM1; -. DR SwissPalm; Q8TEM1; -. DR BioMuta; NUP210; -. DR DMDM; 116242720; -. DR EPD; Q8TEM1; -. DR jPOST; Q8TEM1; -. DR MassIVE; Q8TEM1; -. DR MaxQB; Q8TEM1; -. DR PaxDb; 9606-ENSP00000254508; -. DR PeptideAtlas; Q8TEM1; -. DR ProteomicsDB; 74472; -. [Q8TEM1-1] DR ProteomicsDB; 74473; -. [Q8TEM1-2] DR Pumba; Q8TEM1; -. DR Antibodypedia; 10858; 236 antibodies from 27 providers. DR DNASU; 23225; -. DR Ensembl; ENST00000254508.7; ENSP00000254508.5; ENSG00000132182.13. [Q8TEM1-1] DR GeneID; 23225; -. DR KEGG; hsa:23225; -. DR MANE-Select; ENST00000254508.7; ENSP00000254508.5; NM_024923.4; NP_079199.2. DR UCSC; uc003bxv.3; human. [Q8TEM1-1] DR AGR; HGNC:30052; -. DR CTD; 23225; -. DR DisGeNET; 23225; -. DR GeneCards; NUP210; -. DR HGNC; HGNC:30052; NUP210. DR HPA; ENSG00000132182; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 607703; gene. DR neXtProt; NX_Q8TEM1; -. DR OpenTargets; ENSG00000132182; -. DR PharmGKB; PA128394614; -. DR VEuPathDB; HostDB:ENSG00000132182; -. DR eggNOG; KOG1833; Eukaryota. DR GeneTree; ENSGT00390000009491; -. DR HOGENOM; CLU_001205_1_1_1; -. DR InParanoid; Q8TEM1; -. DR OMA; YLCLVTM; -. DR OrthoDB; 6312at2759; -. DR PhylomeDB; Q8TEM1; -. DR TreeFam; TF313331; -. DR PathwayCommons; Q8TEM1; -. 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-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR SignaLink; Q8TEM1; -. DR SIGNOR; Q8TEM1; -. DR BioGRID-ORCS; 23225; 21 hits in 1168 CRISPR screens. DR ChiTaRS; NUP210; human. DR GenomeRNAi; 23225; -. DR Pharos; Q8TEM1; Tbio. DR PRO; PR:Q8TEM1; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8TEM1; Protein. DR Bgee; ENSG00000132182; Expressed in endometrium epithelium and 162 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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; IBA:GO_Central. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR003343; Big_2. DR InterPro; IPR008964; Invasin/intimin_cell_adhesion. DR InterPro; IPR045197; NUP210-like. DR PANTHER; PTHR23019:SF2; NUCLEAR PORE MEMBRANE GLYCOPROTEIN 210; 1. DR PANTHER; PTHR23019; NUCLEAR PORE MEMBRANE GLYCOPROTEIN GP210-RELATED; 1. DR Pfam; PF02368; Big_2; 1. DR SMART; SM00635; BID_2; 1. DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1. DR Genevisible; Q8TEM1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Glycoprotein; KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; KW Protein transport; Reference proteome; Signal; Translocation; KW Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..26 FT /evidence="ECO:0000250" FT CHAIN 27..1887 FT /note="Nuclear pore membrane glycoprotein 210" FT /id="PRO_0000236046" FT TOPO_DOM 27..1808 FT /note="Perinuclear space" FT /evidence="ECO:0000305" FT TRANSMEM 1809..1829 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1830..1887 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 1078..1151 FT /note="BIG2" FT /evidence="ECO:0000255" FT REGION 1853..1887 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1844 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1874 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1877 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1881 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1886 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT CARBOHYD 44 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 337 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 405 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 484 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 681 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 801 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 926 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1039 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1116 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1135 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1362 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1441 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VAR_SEQ 947..967 FT /note="HPLLPGSSTIMIHDLCLVFPA -> SLGHRSPLLVFIPYLGCCVVN (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_018567" FT VAR_SEQ 968..1887 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_018568" FT VARIANT 297 FT /note="A -> T (in dbSNP:rs7628051)" FT /id="VAR_028147" FT VARIANT 608 FT /note="I -> V (in dbSNP:rs3732671)" FT /id="VAR_028148" FT VARIANT 755 FT /note="A -> V (in dbSNP:rs6795271)" FT /id="VAR_028149" FT VARIANT 786 FT /note="R -> L (confirmed at protein level; FT dbSNP:rs2280084)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17488105" FT /id="VAR_026474" FT VARIANT 821 FT /note="P -> A (in dbSNP:rs2280085)" FT /id="VAR_028150" FT VARIANT 944 FT /note="A -> P (in dbSNP:rs433032)" FT /id="VAR_028151" FT VARIANT 1096 FT /note="M -> I (in dbSNP:rs2271505)" FT /id="VAR_028152" FT VARIANT 1430 FT /note="D -> E (in dbSNP:rs13081937)" FT /id="VAR_028153" FT VARIANT 1752 FT /note="L -> S (in dbSNP:rs354479)" FT /evidence="ECO:0000269|PubMed:10048485, FT ECO:0000269|PubMed:16303743, ECO:0000269|PubMed:17974005" FT /id="VAR_026475" FT VARIANT 1787 FT /note="V -> M (in dbSNP:rs354478)" FT /evidence="ECO:0000269|PubMed:10048485, FT ECO:0000269|PubMed:16303743, ECO:0000269|PubMed:17974005" FT /id="VAR_026476" FT CONFLICT 1512 FT /note="A -> T (in Ref. 5; BAC11688)" FT /evidence="ECO:0000305" FT CONFLICT 1761 FT /note="P -> S (in Ref. 5; BAC11688)" FT /evidence="ECO:0000305" SQ SEQUENCE 1887 AA; 205111 MW; 70B5C35E685C8DF8 CRC64; MAARGRGLLL LTLSVLLAAG PSAAAAKLNI PKVLLPFTRA TRVNFTLEAS EGCYRWLSTR PEVASIEPLG LDEQQCSQKA VVQARLTQPA RLTSIIFAED ITTGQVLRCD AIVDLIHDIQ IVSTTRELYL EDSPLELKIQ ALDSEGNTFS TLAGLVFEWT IVKDSEADRF SDSHNALRIL TFLESTYIPP SYISEMEKAA KQGDTILVSG MKTGSSKLKA RIQEAVYKNV RPAEVRLLIL ENILLNPAYD VYLMVGTSIH YKVQKIRQGK ITELSMPSDQ YELQLQNSIP GPEGDPARPV AVLAQDTSMV TALQLGQSSL VLGHRSIRMQ GASRLPNSTI YVVEPGYLGF TVHPGDRWVL ETGRLYEITI EVFDKFSNKV YVSDNIRIET VLPAEFFEVL SSSQNGSYHR IRALKRGQTA IDAALTSVVD QDGGVHILQV PVWNQQEVEI HIPITLYPSI LTFPWQPKTG AYQYTIRAHG GSGNFSWSSS SHLVATVTVK GVMTTGSDIG FSVIQAHDVQ NPLHFGEMKV YVIEPHSMEF APCQVEARVG QALELPLRIS GLMPGGASEV VTLSDCSHFD LAVEVENQGV FQPLPGRLPP GSEHCSGIRV KAEAQGSTTL LVSYRHGHVH LSAKITIAAY LPLKAVDPSS VALVTLGSSK EMLFEGGPRP WILEPSKFFQ NVTAEDTDSI GLALFAPHSS RNYQQHWILV TCQALGEQVI ALSVGNKPSL TNPFPAVEPA VVKFVCAPPS RLTLAPVYTS PQLDMSCPLL QQNKQVVPVS SHRNPRLDLA AYDQEGRRFD NFSSLSIQWE STRPVLASIE PELPMQLVSQ DDESGQKKLH GLQAILVHEA SGTTAITATA TGYQESHLSS ARTKQPHDPL VPLSASIELI LVEDVRVSPE EVTIYNHPGI QAELRIREGS GYFFLNTSTA DVVKVAYQEA RGVAMVHPLL PGSSTIMIHD LCLVFPAPAK AVVYVSDIQE LYIRVVDKVE IGKTVKAYVR VLDLHKKPFL AKYFPFMDLK LRAASPIITL VALDEALDNY TITFLIRGVA IGQTSLTASV TNKAGQRINS APQQIEVFPP FRLMPRKVTL LIGATMQVTS EGGPQPQSNI LFSISNESVA LVSAAGLVQG LAIGNGTVSG LVQAVDAETG KVVIISQDLV QVEVLLLRAV RIRAPIMRMR TGTQMPIYVT GITNHQNPFS FGNAVPGLTF HWSVTKRDVL DLRGRHHEAS IRLPSQYNFA MNVLGRVKGR TGLRVVVKAV DPTSGQLYGL ARELSDEIQV QVFEKLQLLN PEIEAEQILM SPNSYIKLQT NRDGAASLSY RVLDGPEKVP VVHVDEKGFL ASGSMIGTST IEVIAQEPFG ANQTIIVAVK VSPVSYLRVS MSPVLHTQNK EALVAVPLGM TVTFTVHFHD NSGDVFHAHS SVLNFATNRD DFVQIGKGPT NNTCVVRTVS VGLTLLRVWD AEHPGLSDFM PLPVLQAISP ELSGAMVVGD VLCLATVLTS LEGLSGTWSS SANSILHIDP KTGVAVARAV GSVTVYYEVA GHLRTYKEVV VSVPQRIMAR HLHPIQTSFQ EATASKVIVA VGDRSSNLRG ECTPTQREVI QALHPETLIS CQSQFKPAVF DFPSQDVFTV EPQFDTALGQ YFCSITMHRL TDKQRKHLSM KKTALVVSAS LSSSHFSTEQ VGAEVPFSPG LFADQAEILL SNHYTSSEIR VFGAPEVLEN LEVKSGSPAV LAFAKEKSFG WPSFITYTVG VLDPAAGSQG PLSTTLTFSS PVTNQAIAIP VTVAFVVDRR GPGPYGASLF QHFLDSYQVM FFTLFALLAG TAVMIIAYHT VCTPRDLAVP AALTPRASPG HSPHYFAASS PTSPNALPPA RKASPPSGLW SPAYASH //