PO210_HUMAN
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 03-AUG-2022, entry version 162.
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 AlphaFoldDB; Q8TEM1; -.
DR BioGRID; 116831; 137.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR IntAct; Q8TEM1; 55.
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 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; Q8TEM1; -.
DR PeptideAtlas; Q8TEM1; -.
DR PRIDE; Q8TEM1; -.
DR ProteomicsDB; 74472; -. [Q8TEM1-1]
DR ProteomicsDB; 74473; -. [Q8TEM1-2]
DR Antibodypedia; 10858; 207 antibodies from 26 providers.
DR DNASU; 23225; -.
DR Ensembl; ENST00000254508.7; ENSP00000254508.5; ENSG00000132182.12. [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 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; AELHIRE; -.
DR OrthoDB; 843414at2759; -.
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; 19 hits in 1088 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 160 other tissues.
DR Genevisible; Q8TEM1; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; 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; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC: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; PTHR23019; 1.
DR Pfam; PF02368; Big_2; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW 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
