SEH1_HUMAN
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 03-AUG-2022, entry version 185.
DE RecName: Full=Nucleoporin SEH1 {ECO:0000305};
DE AltName: Full=GATOR 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, 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 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.
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).
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. The Nup107-160 subcomplex is also required for
CC normal kinetochore microtubule attachment, mitotic progression and
CC chromosome segregation. This subunit plays a role in recruitment of the
CC Nup107-160 subcomplex to the kinetochore. {ECO:0000269|PubMed:15146057,
CC ECO:0000269|PubMed:17363900}.
CC -!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
CC within the amino acid-sensing branch of the TORC1 signaling pathway.
CC Indirectly activates mTORC1 and the TORC1 signaling pathway through the
CC inhibition of the GATOR1 subcomplex (PubMed:23723238). It is negatively
CC regulated by the upstream amino acid sensors SESN2 and CASTOR1
CC (PubMed:25457612, PubMed:27487210). {ECO:0000269|PubMed:23723238,
CC ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
CC -!- SUBUNIT: Component of the Nup107-160 subcomplex of the nuclear pore
CC complex (NPC). The Nup107-160 subcomplex includes NUP160, NUP133,
CC NUP107, NUP98, NUP85, NUP43, NUP37, SEH1 and SEC13. The SEH1 subunit
CC appears to be only weakly associated with the Nup107-160 subcomplex.
CC Within the GATOR complex, component of the GATOR2 subcomplex, made of
CC MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly
CC interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers
CC (PubMed:17360435, PubMed:23723238). The GATOR2 complex interacts with
CC CASTOR2 and CASTOR1; the interaction is negatively regulated by
CC arginine (PubMed:26972053). The GATOR2 complex interacts with SESN1,
CC SESN2 and SESN3; the interaction is negatively regulated by amino acids
CC (PubMed:25263562, PubMed:25457612). {ECO:0000269|PubMed:17360435,
CC ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25263562,
CC ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:26972053}.
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}.
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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 PDBsum; 5A9Q; -.
DR PDBsum; 7PEQ; -.
DR AlphaFoldDB; Q96EE3; -.
DR SMR; Q96EE3; -.
DR BioGRID; 123629; 134.
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; Q96EE3; -.
DR PeptideAtlas; Q96EE3; -.
DR PRIDE; Q96EE3; -.
DR ProteomicsDB; 76398; -. [Q96EE3-2]
DR ProteomicsDB; 76399; -. [Q96EE3-1]
DR Antibodypedia; 48526; 21 antibodies from 10 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 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; 944756at2759; -.
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; 712 hits in 1090 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 198 other tissues.
DR ExpressionAtlas; Q96EE3; baseline and differential.
DR Genevisible; Q96EE3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0061700; C:GATOR2 complex; IDA:SGD.
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; IC: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:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IC:ComplexPortal.
DR GO; GO:0006999; P:nuclear pore organization; IMP:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP: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; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037597; Nucleoporin_Seh1.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF3; PTHR11024:SF3; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
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
