ID SEH1_HUMAN Reviewed; 360 AA. AC Q96EE3; A8K5B1; Q8NFU6; Q96MH3; Q9C069; DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 3. DT 27-MAR-2024, entry version 194. DE RecName: Full=Nucleoporin SEH1 {ECO:0000305}; DE AltName: Full=GATOR2 complex protein SEH1 {ECO:0000305}; DE AltName: Full=Nup107-160 subcomplex subunit SEH1; DE AltName: Full=SEC13-like protein; GN Name=SEH1L; Synonyms=SEC13L, SEH1; 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] (ISOFORMS A AND B). RC TISSUE=Liver; RA Pan H., Yu Y., Shen L., Huo K.-K., Li Y.-Y.; RT "cDNA cloning of a human homolog of yeast SEH1 gene."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND VARIANT ASN-342. RC TISSUE=Adrenal gland; RA Li Y., Gu Y., Peng Y., Fu S., Gu J., Zhang L., Jiang C., Yu Y., Han Z., RA Wang Y., Chen Z., Fu G.; RT "A novel gene expressed in human adrenal gland."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANT ASN-342. RC TISSUE=Skeletal muscle; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Eye; 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 [6] RP FUNCTION, ASSOCIATION WITH THE NUP107-160 COMPLEX, AND SUBCELLULAR RP LOCATION. 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 [7] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17363900; DOI=10.1038/sj.emboj.7601642; RA Zuccolo M., Alves A., Galy V., Bolhy S., Formstecher E., Racine V., RA Sibarita J.-B., Fukagawa T., Shiekhattar R., Yen T., Doye V.; RT "The human Nup107-160 nuclear pore subcomplex contributes to proper RT kinetochore functions."; RL EMBO J. 26:1853-1864(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE NUP107-160 RP COMPLEX. RX PubMed=17360435; DOI=10.1073/pnas.0700058104; RA Glavy J.S., Krutchinsky A.N., Cristea I.M., Berke I.C., Boehmer T., RA Blobel G., Chait B.T.; RT "Cell-cycle-dependent phosphorylation of the nuclear pore Nup107-160 RT subcomplex."; RL Proc. Natl. Acad. Sci. U.S.A. 104:3811-3816(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 (ISOFORM B), AND RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-190, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP INTERACTION WITH SESN1; SESN2 AND SESN3. RX PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014; RA Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M., RA Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.; RT "The Sestrins interact with GATOR2 to negatively regulate the amino-acid- RT sensing pathway upstream of mTORC1."; RL Cell Rep. 9:1-8(2014). RN [12] RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SESN2. RX PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019; RA Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C., Akopiants K., RA Guan K.L., Karin M., Budanov A.V.; RT "Sestrins inhibit mTORC1 kinase activation through the GATOR complex."; RL Cell Rep. 9:1281-1291(2014). RN [13] RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH CASTOR2 AND CASTOR1. RX PubMed=26972053; DOI=10.1016/j.cell.2016.02.035; RA Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K., Wyant G.A., RA Wang T., Harper J.W., Gygi S.P., Sabatini D.M.; RT "The CASTOR proteins are arginine sensors for the mTORC1 pathway."; RL Cell 165:153-164(2016). RN [14] RP FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND INTERACTION WITH RRAG RP PROTEINS. RX PubMed=23723238; DOI=10.1126/science.1232044; RA Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W., Ottina K.A., RA Grabiner B.C., Spear E.D., Carter S.L., Meyerson M., Sabatini D.M.; RT "A Tumor suppressor complex with GAP activity for the Rag GTPases that RT signal amino acid sufficiency to mTORC1."; RL Science 340:1100-1106(2013). RN [15] RP FUNCTION, AND ACTIVITY REGULATION. RX PubMed=27487210; DOI=10.1038/nature19079; RA Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U., RA Sabatini D.M.; RT "Mechanism of arginine sensing by CASTOR1 upstream of mTORC1."; RL Nature 536:229-233(2016). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [17] RP SUBCELLULAR LOCATION. RX PubMed=28199306; DOI=10.1038/nature21423; RA Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M., Shen K., RA Condon K.J., Petri S., Kedir J., Scaria S.M., Abu-Remaileh M., RA Frankel W.N., Sabatini D.M.; RT "KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to RT regulate mTORC1."; RL Nature 543:438-442(2017). RN [18] RP FUNCTION, AND IDENTIFICATION IN GATOR2 COMPLEX. RX PubMed=36528027; DOI=10.1016/j.molcel.2022.11.021; RA Jiang C., Dai X., He S., Zhou H., Fang L., Guo J., Liu S., Zhang T., RA Pan W., Yu H., Fu T., Li D., Inuzuka H., Wang P., Xiao J., Wei W.; RT "Ring domains are essential for GATOR2-dependent mTORC1 activation."; RL Mol. Cell 83:74-89(2023). RN [19] {ECO:0007744|PDB:7UHY} RP STRUCTURE BY ELECTRON MICROSCOPY (3.66 ANGSTROMS) IN COMPLEX WITH WDR59; RP SEC13 AND MIOS, FUNCTION, ACTIVITY REGULATION, IDENTIFICATION IN GATOR2 RP COMPLEX, AND INTERACTION WITH SESN2. RX PubMed=35831510; DOI=10.1038/s41586-022-04939-z; RA Valenstein M.L., Rogala K.B., Lalgudi P.V., Brignole E.J., Gu X., RA Saxton R.A., Chantranupong L., Kolibius J., Quast J.P., Sabatini D.M.; RT "Structure of the nutrient-sensing hub GATOR2."; RL Nature 607:610-616(2022). CC -!- FUNCTION: Component of the Nup107-160 subcomplex of the nuclear pore CC complex (NPC). The Nup107-160 subcomplex is required for the assembly CC of a functional NPC (PubMed:15146057, PubMed:17363900). The Nup107-160 CC subcomplex is also required for normal kinetochore microtubule CC attachment, mitotic progression and chromosome segregation. This CC subunit plays a role in recruitment of the Nup107-160 subcomplex to the CC kinetochore (PubMed:15146057, PubMed:17363900). CC {ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900}. CC -!- FUNCTION: As a component of the GATOR2 complex, functions as an CC activator of the amino acid-sensing branch of the mTORC1 signaling CC pathway (PubMed:25457612, PubMed:23723238, PubMed:27487210, CC PubMed:36528027, PubMed:35831510). The GATOR2 complex indirectly CC activates mTORC1 through the inhibition of the GATOR1 subcomplex CC (PubMed:23723238, PubMed:27487210, PubMed:36528027, PubMed:35831510). CC GATOR2 probably acts as an E3 ubiquitin-protein ligase toward GATOR1 CC (PubMed:36528027). In the presence of abundant amino acids, the GATOR2 CC complex mediates ubiquitination of the NPRL2 core component of the CC GATOR1 complex, leading to GATOR1 inactivation (PubMed:36528027). In CC the absence of amino acids, GATOR2 is inhibited, activating the GATOR1 CC complex (PubMed:25457612, PubMed:26972053, PubMed:27487210). Within the CC GATOR2 complex, SEC13 and SEH1L are required to stabilize the complex CC (PubMed:35831510). {ECO:0000269|PubMed:23723238, CC ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:26972053, CC ECO:0000269|PubMed:27487210, ECO:0000269|PubMed:35831510, CC ECO:0000269|PubMed:36528027}. CC -!- ACTIVITY REGULATION: The GATOR2 complex is negatively regulated by the CC upstream amino acid sensors CASTOR1 and SESN2, which sequester the CC GATOR2 complex in absence of amino acids (PubMed:26972053, CC PubMed:25457612, PubMed:27487210, PubMed:35831510). In the presence of CC abundant amino acids, GATOR2 is released from CASTOR1 and SESN2 and CC activated (PubMed:26972053, PubMed:25457612, PubMed:27487210, CC PubMed:35831510). {ECO:0000269|PubMed:25457612, CC ECO:0000269|PubMed:26972053, ECO:0000269|PubMed:27487210, CC ECO:0000269|PubMed:35831510}. CC -!- SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear pore CC complex (NPC) (PubMed:17360435). The Nup107-160 subcomplex includes CC NUP160, NUP133, NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13 CC (PubMed:17360435). The SEH1 subunit appears to be only weakly CC associated with the Nup107-160 subcomplex (PubMed:17360435). Component CC of the GATOR2 subcomplex, composed of MIOS, SEC13, SEH1L, WDR24 and CC WDR59 (PubMed:23723238). The GATOR2 complex interacts with CASTOR1 and CC CASTOR2; the interaction is negatively regulated by arginine CC (PubMed:26972053, PubMed:36528027, PubMed:35831510). The GATOR2 complex CC interacts with SESN1, SESN2 and SESN3; the interaction is negatively CC regulated by amino acids (PubMed:25263562, PubMed:25457612). SESN1, CC SESN2 and SESN3 convey leucine availability via direct interaction with CC SEH1L and WDR24 (PubMed:35831510). {ECO:0000269|PubMed:17360435, CC ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25263562, CC ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:26972053, CC ECO:0000269|PubMed:35831510, ECO:0000269|PubMed:36528027}. CC -!- INTERACTION: CC Q96EE3; Q9BW27: NUP85; NbExp=3; IntAct=EBI-922818, EBI-716392; CC Q96EE3; P55735: SEC13; NbExp=3; IntAct=EBI-922818, EBI-1046596; CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore CC {ECO:0000269|PubMed:15146057, ECO:0000269|PubMed:17363900}. Nucleus, CC nuclear pore complex {ECO:0000269|PubMed:15146057, CC ECO:0000269|PubMed:17363900}. Lysosome membrane CC {ECO:0000269|PubMed:28199306}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; Synonyms=SEH1A; CC IsoId=Q96EE3-2; Sequence=Displayed; CC Name=B; Synonyms=SEH1B; CC IsoId=Q96EE3-1; Sequence=VSP_037954; CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}. CC -!- CAUTION: The E3 ubiquitin-protein ligase activity of the GATOR2 complex CC is subject to discussion (PubMed:35831510, PubMed:36528027). According CC to a report, the GATOR2 complex does not catalyze ubiquitination of the CC GATOR1 complex (PubMed:35831510). In contrast, another publication CC showed that the GATOR2 complex mediates ubiquitination of the NPRL2 CC core component of the GATOR1 complex, leading to GATOR1 inactivation CC (PubMed:36528027). {ECO:0000269|PubMed:35831510, CC ECO:0000269|PubMed:36528027}. 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; AF255625; AAM21169.1; -; mRNA. DR EMBL; AF431970; AAM44214.1; -; mRNA. DR EMBL; AF514996; AAM76707.1; -; mRNA. DR EMBL; AF136976; AAG49437.1; -; mRNA. DR EMBL; AK056940; BAB71317.1; -; mRNA. DR EMBL; AK291226; BAF83915.1; -; mRNA. DR EMBL; BC012430; AAH12430.1; -; mRNA. DR CCDS; CCDS32791.1; -. [Q96EE3-1] DR CCDS; CCDS45832.1; -. [Q96EE3-2] DR RefSeq; NP_001013455.1; NM_001013437.1. [Q96EE3-1] DR RefSeq; NP_112493.2; NM_031216.3. [Q96EE3-2] DR PDB; 5A9Q; EM; 23.00 A; 7/G/P/Y=1-360. DR PDB; 7PEQ; EM; 35.00 A; AG/BG/CG/DG=1-360. DR PDB; 7R5J; EM; 50.00 A; O0/O1/O2/O3=1-360. DR PDB; 7R5K; EM; 12.00 A; O0/O1/O2/O3=1-360. DR PDB; 7UHY; EM; 3.66 A; E/F/G=1-357. DR PDBsum; 5A9Q; -. DR PDBsum; 7PEQ; -. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR PDBsum; 7UHY; -. DR AlphaFoldDB; Q96EE3; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; Q96EE3; -. DR BioGRID; 123629; 157. DR ComplexPortal; CPX-6227; GATOR2 complex. DR ComplexPortal; CPX-873; Nuclear pore complex. DR CORUM; Q96EE3; -. DR IntAct; Q96EE3; 81. DR MINT; Q96EE3; -. DR STRING; 9606.ENSP00000382779; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; Q96EE3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96EE3; -. DR PhosphoSitePlus; Q96EE3; -. DR SwissPalm; Q96EE3; -. DR BioMuta; SEH1L; -. DR DMDM; 257051064; -. DR EPD; Q96EE3; -. DR jPOST; Q96EE3; -. DR MassIVE; Q96EE3; -. DR MaxQB; Q96EE3; -. DR PaxDb; 9606-ENSP00000382779; -. DR PeptideAtlas; Q96EE3; -. DR ProteomicsDB; 76398; -. [Q96EE3-2] DR ProteomicsDB; 76399; -. [Q96EE3-1] DR Pumba; Q96EE3; -. DR Antibodypedia; 48526; 39 antibodies from 11 providers. DR DNASU; 81929; -. DR Ensembl; ENST00000262124.15; ENSP00000262124.10; ENSG00000085415.16. [Q96EE3-2] DR Ensembl; ENST00000399892.7; ENSP00000382779.1; ENSG00000085415.16. [Q96EE3-1] DR GeneID; 81929; -. DR KEGG; hsa:81929; -. DR MANE-Select; ENST00000399892.7; ENSP00000382779.1; NM_001013437.2; NP_001013455.1. [Q96EE3-1] DR UCSC; uc002krq.5; human. [Q96EE3-2] DR AGR; HGNC:30379; -. DR CTD; 81929; -. DR DisGeNET; 81929; -. DR GeneCards; SEH1L; -. DR HGNC; HGNC:30379; SEH1L. DR HPA; ENSG00000085415; Low tissue specificity. DR MIM; 609263; gene. DR neXtProt; NX_Q96EE3; -. DR OpenTargets; ENSG00000085415; -. DR PharmGKB; PA134912135; -. DR VEuPathDB; HostDB:ENSG00000085415; -. DR eggNOG; KOG2445; Eukaryota. DR GeneTree; ENSGT00940000153393; -. DR HOGENOM; CLU_032441_1_2_1; -. DR InParanoid; Q96EE3; -. DR OMA; NAPTRRW; -. DR OrthoDB; 177928at2759; -. DR PhylomeDB; Q96EE3; -. DR TreeFam; TF105924; -. DR PathwayCommons; Q96EE3; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. [Q96EE3-1] 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. [Q96EE3-1] DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. [Q96EE3-1] 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. [Q96EE3-1] DR Reactome; R-HSA-6784531; tRNA processing in the nucleus. DR Reactome; R-HSA-68877; Mitotic Prometaphase. [Q96EE3-1] 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. [Q96EE3-1] DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. [Q96EE3-1] DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR SignaLink; Q96EE3; -. DR SIGNOR; Q96EE3; -. DR BioGRID-ORCS; 81929; 742 hits in 1169 CRISPR screens. DR ChiTaRS; SEH1L; human. DR GenomeRNAi; 81929; -. DR Pharos; Q96EE3; Tbio. DR PRO; PR:Q96EE3; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q96EE3; Protein. DR Bgee; ENSG00000085415; Expressed in endothelial cell and 200 other cell types or tissues. DR ExpressionAtlas; Q96EE3; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0061700; C:GATOR2 complex; IDA:UniProtKB. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal. DR GO; GO:0005643; C:nuclear pore; NAS:ComplexPortal. DR GO; GO:0031080; C:nuclear pore outer ring; IDA:UniProtKB. DR GO; GO:0035859; C:Seh1-associated complex; IBA:GO_Central. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB. DR GO; GO:0031669; P:cellular response to nutrient levels; IDA:UniProtKB. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl. DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; IMP:UniProtKB. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; NAS:ComplexPortal. DR GO; GO:0006999; P:nuclear pore organization; IMP:UniProtKB. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal. DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0031503; P:protein-containing complex localization; IMP:UniProtKB. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR037363; Sec13/Seh1_fam. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR11024; NUCLEAR PORE COMPLEX PROTEIN SEC13 / SEH1 FAMILY MEMBER; 1. DR PANTHER; PTHR11024:SF3; NUCLEOPORIN SEH1; 1. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 5. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 2. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. DR Genevisible; Q96EE3; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere; KW Chromosome; Chromosome partition; Isopeptide bond; Kinetochore; Lysosome; KW Membrane; Mitosis; mRNA transport; Nuclear pore complex; Nucleus; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; KW Translocation; Transport; Ubl conjugation; WD repeat. FT CHAIN 1..360 FT /note="Nucleoporin SEH1" FT /id="PRO_0000051213" FT REPEAT 10..49 FT /note="WD 1" FT REPEAT 55..96 FT /note="WD 2" FT REPEAT 111..152 FT /note="WD 3" FT REPEAT 160..210 FT /note="WD 4" FT REPEAT 217..258 FT /note="WD 5" FT REPEAT 276..315 FT /note="WD 6" FT REGION 324..360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 12 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 358..360 FT /note="KHS -> YFFTPLDSPRAGSRWSSYAQLLPPPPPPLVEHSCDADTANLQYPH FT PRRRYLSRPLNPLPENEGI (in isoform B)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1" FT /id="VSP_037954" FT VARIANT 342 FT /note="T -> N (in dbSNP:rs6505776)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3" FT /id="VAR_053417" FT CONFLICT 78 FT /note="S -> P (in Ref. 4; BAB71317)" FT /evidence="ECO:0000305" FT MOD_RES Q96EE3-1:365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" SQ SEQUENCE 360 AA; 39649 MW; FB9ED2440C4EC9AB CRC64; MFVARSIAAD HKDLIHDVSF DFHGRRMATC SSDQSVKVWD KSESGDWHCT ASWKTHSGSV WRVTWAHPEF GQVLASCSFD RTAAVWEEIV GESNDKLRGQ SHWVKRTTLV DSRTSVTDVK FAPKHMGLML ATCSADGIVR IYEAPDVMNL SQWSLQHEIS CKLSCSCISW NPSSSRAHSP MIAVGSDDSS PNAMAKVQIF EYNENTRKYA KAETLMTVTD PVHDIAFAPN LGRSFHILAI ATKDVRIFTL KPVRKELTSS GGPTKFEIHI VAQFDNHNSQ VWRVSWNITG TVLASSGDDG CVRLWKANYM DNWKCTGILK GNGSPVNGSS QQGTSNPSLG STIPSLQNSL NGSSAGRKHS //