ID ELYS_HUMAN Reviewed; 2266 AA. AC Q8WYP5; A6NGM0; A8MSG9; A8MZ86; Q7Z4E3; Q8IZA4; Q96EH9; Q9Y4Q6; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 3. DT 27-MAR-2024, entry version 173. DE RecName: Full=Protein ELYS; DE AltName: Full=Embryonic large molecule derived from yolk sac; DE AltName: Full=Protein MEL-28; DE AltName: Full=Putative AT-hook-containing transcription factor 1; GN Name=AHCTF1; Synonyms=ELYS, TMBS62; ORFNames=MSTP108; 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] (ISOFORM 3). RC TISSUE=Fetal liver; RX PubMed=11952839; DOI=10.1046/j.1365-2443.2002.00529.x; RA Kimura N., Takizawa M., Okita K., Natori O., Igarashi K., Ueno M., RA Nakashima K., Nobuhisa I., Taga T.; RT "Identification of a novel transcription factor, ELYS, expressed RT predominantly in mouse foetal haematopoietic tissues."; RL Genes Cells 7:435-446(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Lymphoblast; RA Lightfoot J., Alon N., Buchwald M.; RT "Cloning of a cDNA that provides partial correction of mitomycin C RT sensitivity in Fanconi anemia FA-D1 cells."; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1522-2266 (ISOFORMS 1/2/3). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1753-2266 (ISOFORMS 1/2/3). RC TISSUE=Heart; RA Liu B., Zhao B., Wang X.Y., Liu Y.Q., Sheng H., Qin B.M., Zhang Q., RA Zheng W.Y., Xu H.S., Liu B.H., Lu H., Gong Q., Hui R.T.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2037-2266 (ISOFORMS 1/2/3). RC TISSUE=Retinoblastoma; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232; SER-1283 AND SER-1996, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2222 AND SER-2226, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP FUNCTION, ASSOCIATION WITH THE NUP107-160 COMPLEX, AND SUBCELLULAR RP LOCATION. RX PubMed=17098863; DOI=10.1073/pnas.0608484103; RA Rasala B.A., Orjalo A.V., Shen Z., Briggs S., Forbes D.J.; RT "ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore RT assembly and proper cell division."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17801-17806(2006). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17235358; DOI=10.1038/sj.embor.7400889; RA Franz C., Walczak R., Yavuz S., Santarella R., Gentzel M., Askjaer P., RA Galy V., Hetzer M., Mattaj I.W., Antonin W.; RT "MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin RT and postmitotic nuclear pore complex assembly."; RL EMBO Rep. 8:165-172(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-1222, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1283; SER-1541; RP SER-1878; SER-2120; SER-2222 AND SER-2226, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1142; SER-1150; SER-1155; RP SER-1160; THR-1175; SER-1250; SER-1541; SER-1729; SER-1806; THR-1808; RP SER-1878; SER-1884; SER-1898; SER-2060; SER-2089; SER-2120; SER-2123; RP SER-2154 AND SER-2212, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1283; SER-1541; SER-1884 AND RP SER-2222, 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1160; SER-1232; RP SER-1283; SER-1297; THR-1369; SER-1513; SER-1533; SER-1541; SER-1878; RP SER-1898; SER-1944; SER-1946; SER-2043; SER-2044; SER-2120; SER-2154; RP SER-2212; SER-2222 AND SER-2226, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1142; SER-1160; SER-1214; RP SER-1283; THR-1517; SER-1533; SER-1541 AND SER-1944, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-528; SER-1153; RP SER-1160; SER-1214; SER-1218; SER-1222; SER-1232; SER-1250; THR-1257; RP SER-1283; THR-1369; SER-1513; SER-1541; SER-1944; SER-2089; SER-2212; RP SER-2222 AND SER-2226, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP SUBCELLULAR LOCATION. RX PubMed=27341616; DOI=10.1371/journal.pgen.1006131; RA Gomez-Saldivar G., Fernandez A., Hirano Y., Mauro M., Lai A., Ayuso C., RA Haraguchi T., Hiraoka Y., Piano F., Askjaer P.; RT "Identification of conserved MEL-28/ELYS domains with essential roles in RT nuclear assembly and chromosome segregation."; RL PLoS Genet. 12:E1006131-E1006131(2016). CC -!- FUNCTION: Required for the assembly of a functional nuclear pore CC complex (NPC) on the surface of chromosomes as nuclei form at the end CC of mitosis. May initiate NPC assembly by binding to chromatin and CC recruiting the Nup107-160 subcomplex of the NPC. Also required for the CC localization of the Nup107-160 subcomplex of the NPC to the kinetochore CC during mitosis and for the completion of cytokinesis. CC {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:17235358}. CC -!- SUBUNIT: Associates with the Nup107-160 subcomplex of the NPC. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8CJF7}. Nucleus CC {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:27341616}. Nucleus CC envelope {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:27341616}. CC Nucleus matrix {ECO:0000269|PubMed:17098863}. Chromosome, centromere, CC kinetochore {ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:27341616}. CC Nucleus, nucleoplasm {ECO:0000269|PubMed:17098863}. Nucleus, nuclear CC pore complex {ECO:0000269|PubMed:17098863}. Note=Localizes to the CC nuclear pore complex (NPC) throughout interphase. Localizes to the CC kinetochore from prophase, and this appears to require the Nup107-160 CC subcomplex of the NPC. Localizes to the periphery of chromatin from CC late anaphase. {ECO:0000269|PubMed:17098863}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8WYP5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WYP5-2; Sequence=VSP_019844; CC Name=3; CC IsoId=Q8WYP5-3; Sequence=VSP_042691; CC -!- DOMAIN: The N-terminus forms a highly conserved seven-bladed beta CC propeller decorated with long loops and mediates anchorage to the CC Nup107-160 subcomplex of the nuclear pore, synergistically with the CC central alpha domain. The disordered C-terminus is responsible for the CC interactions with chromatin (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ELYS family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAN65622.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAQ13621.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB78516.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AB059277; BAB78516.1; ALT_INIT; mRNA. DR EMBL; AY157619; AAN65622.1; ALT_FRAME; mRNA. DR EMBL; AC113174; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL080144; CAB45737.1; -; mRNA. DR EMBL; AF173978; AAQ13621.1; ALT_INIT; mRNA. DR EMBL; BC012307; AAH12307.1; -; mRNA. DR CCDS; CCDS1629.2; -. [Q8WYP5-3] DR CCDS; CCDS91190.1; -. [Q8WYP5-1] DR CCDS; CCDS91191.1; -. [Q8WYP5-2] DR PIR; T12528; T12528. DR RefSeq; NP_001310271.1; NM_001323342.1. [Q8WYP5-1] DR RefSeq; NP_056261.4; NM_015446.4. [Q8WYP5-3] DR RefSeq; XP_006711821.1; XM_006711758.1. DR PDB; 7R5J; EM; 50.00 A; T0/T1=1-2266. DR PDB; 7R5K; EM; 12.00 A; T0/T1=1-2266. DR PDBsum; 7R5J; -. DR PDBsum; 7R5K; -. DR AlphaFoldDB; Q8WYP5; -. DR EMDB; EMD-14321; -. DR EMDB; EMD-14322; -. DR SMR; Q8WYP5; -. DR BioGRID; 117414; 160. DR ComplexPortal; CPX-873; Nuclear pore complex. DR IntAct; Q8WYP5; 42. DR MINT; Q8WYP5; -. DR STRING; 9606.ENSP00000355465; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; Q8WYP5; 19 sites, 1 O-linked glycan (19 sites). DR iPTMnet; Q8WYP5; -. DR PhosphoSitePlus; Q8WYP5; -. DR SwissPalm; Q8WYP5; -. DR BioMuta; AHCTF1; -. DR DMDM; 259016354; -. DR EPD; Q8WYP5; -. DR jPOST; Q8WYP5; -. DR MassIVE; Q8WYP5; -. DR MaxQB; Q8WYP5; -. DR PaxDb; 9606-ENSP00000355465; -. DR PeptideAtlas; Q8WYP5; -. DR ProteomicsDB; 75181; -. [Q8WYP5-1] DR ProteomicsDB; 75182; -. [Q8WYP5-2] DR ProteomicsDB; 75183; -. [Q8WYP5-3] DR Pumba; Q8WYP5; -. DR Antibodypedia; 20836; 122 antibodies from 18 providers. DR DNASU; 25909; -. DR Ensembl; ENST00000326225.3; ENSP00000355465.1; ENSG00000153207.16. [Q8WYP5-3] DR Ensembl; ENST00000366508.5; ENSP00000355464.1; ENSG00000153207.16. [Q8WYP5-2] DR Ensembl; ENST00000648844.2; ENSP00000497061.2; ENSG00000153207.16. [Q8WYP5-1] DR GeneID; 25909; -. DR KEGG; hsa:25909; -. DR MANE-Select; ENST00000648844.2; ENSP00000497061.2; NM_001323342.2; NP_001310271.1. DR UCSC; uc001ibv.3; human. [Q8WYP5-1] DR AGR; HGNC:24618; -. DR CTD; 25909; -. DR GeneCards; AHCTF1; -. DR HGNC; HGNC:24618; AHCTF1. DR HPA; ENSG00000153207; Low tissue specificity. DR MIM; 610853; gene. DR neXtProt; NX_Q8WYP5; -. DR OpenTargets; ENSG00000153207; -. DR PharmGKB; PA142672631; -. DR VEuPathDB; HostDB:ENSG00000153207; -. DR eggNOG; ENOG502QU0D; Eukaryota. DR GeneTree; ENSGT00390000018900; -. DR HOGENOM; CLU_001145_0_0_1; -. DR InParanoid; Q8WYP5; -. DR OMA; KWNHDCL; -. DR OrthoDB; 3152445at2759; -. DR PhylomeDB; Q8WYP5; -. DR TreeFam; TF350425; -. DR PathwayCommons; Q8WYP5; -. DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR SignaLink; Q8WYP5; -. DR SIGNOR; Q8WYP5; -. DR BioGRID-ORCS; 25909; 728 hits in 1162 CRISPR screens. DR ChiTaRS; AHCTF1; human. DR GeneWiki; AHCTF1; -. DR GenomeRNAi; 25909; -. DR Pharos; Q8WYP5; Tbio. DR PRO; PR:Q8WYP5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8WYP5; Protein. DR Bgee; ENSG00000153207; Expressed in endothelial cell and 202 other cell types or tissues. DR ExpressionAtlas; Q8WYP5; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005643; C:nuclear pore; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB. DR DisProt; DP01549; -. DR InterPro; IPR032040; ELYS-bb. DR InterPro; IPR025151; ELYS_dom. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR PANTHER; PTHR21583; ELYS PROTEIN; 1. DR PANTHER; PTHR21583:SF8; PROTEIN ELYS; 1. DR Pfam; PF13934; ELYS; 1. DR Pfam; PF16687; ELYS-bb; 1. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1. DR Genevisible; Q8WYP5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere; KW Chromosome; Cytoplasm; DNA-binding; Kinetochore; mRNA transport; KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport; KW Reference proteome; Translocation; Transport. FT CHAIN 1..2266 FT /note="Protein ELYS" FT /id="PRO_0000246319" FT DNA_BIND 1971..1983 FT /note="A.T hook" FT /evidence="ECO:0000250|UniProtKB:Q5U249" FT REGION 1..981 FT /note="Necessary for cytoplasmic localization" FT /evidence="ECO:0000250|UniProtKB:Q8CJF7" FT REGION 1..494 FT /note="Seven-bladed beta propeller repeats" FT /evidence="ECO:0000250|UniProtKB:Q8CJF7" FT REGION 591..1092 FT /note="Important for nuclear localization" FT /evidence="ECO:0000269|PubMed:27341616" FT REGION 1019..2266 FT /note="Disordered" FT /evidence="ECO:0000250|UniProtKB:Q8CJF7" FT REGION 1149..2266 FT /note="Necessary for nuclear localization" FT /evidence="ECO:0000250|UniProtKB:Q8CJF7" FT REGION 1446..1698 FT /note="Mediates transcriptional activity" FT /evidence="ECO:0000250|UniProtKB:Q8CJF7" FT REGION 1842..2266 FT /note="Important for nuclear localization and chromatin FT binding" FT /evidence="ECO:0000269|PubMed:27341616" FT COMPBIAS 1207..1225 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1285..1299 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1300..1321 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1336..1353 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1822..1843 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1950..1964 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1969..2014 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2043..2082 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2083..2104 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2165..2190 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 528 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1080 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CJF7" FT MOD_RES 1138 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CJF7" FT MOD_RES 1142 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1150 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1155 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1160 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1175 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1214 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1218 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 1250 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1257 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1283 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1297 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1369 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1371 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CJF7" FT MOD_RES 1513 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1517 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1533 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1541 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1729 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1806 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1808 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1878 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231" FT MOD_RES 1884 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 1898 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 1944 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1946 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1996 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 2043 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 2044 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 2060 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 2089 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2120 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231" FT MOD_RES 2123 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 2154 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 2212 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 2222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 2226 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MDSLAGLSPREAAGVLSLSCVGVCSTCAWAWPHGSM (in FT isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_019844" FT VAR_SEQ 1 FT /note="M -> MAAERRCGSM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11952839" FT /id="VSP_042691" FT VARIANT 874 FT /note="N -> S (in dbSNP:rs2642990)" FT /id="VAR_027037" FT VARIANT 2185 FT /note="L -> V (in dbSNP:rs12410563)" FT /id="VAR_027038" FT CONFLICT 168 FT /note="V -> I (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="Q -> E (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" FT CONFLICT 237 FT /note="V -> A (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="P -> R (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" FT CONFLICT 403 FT /note="D -> G (in Ref. 2; AAN65622)" FT /evidence="ECO:0000305" FT CONFLICT 646 FT /note="T -> A (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" FT CONFLICT 743 FT /note="D -> G (in Ref. 2; AAN65622)" FT /evidence="ECO:0000305" FT CONFLICT 753 FT /note="A -> G (in Ref. 2; AAN65622)" FT /evidence="ECO:0000305" FT CONFLICT 1134 FT /note="F -> S (in Ref. 2; AAN65622)" FT /evidence="ECO:0000305" FT CONFLICT 1207 FT /note="L -> P (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" FT CONFLICT 1270 FT /note="L -> P (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" FT CONFLICT 1737 FT /note="S -> F (in Ref. 4; CAB45737)" FT /evidence="ECO:0000305" FT CONFLICT 1797 FT /note="S -> F (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" FT CONFLICT 1830 FT /note="E -> G (in Ref. 2; AAN65622)" FT /evidence="ECO:0000305" FT CONFLICT 2128 FT /note="K -> E (in Ref. 2; AAN65622)" FT /evidence="ECO:0000305" FT CONFLICT 2187 FT /note="K -> E (in Ref. 6; AAH12307)" FT /evidence="ECO:0000305" FT CONFLICT 2213 FT /note="P -> L (in Ref. 1; BAB78516)" FT /evidence="ECO:0000305" SQ SEQUENCE 2266 AA; 252498 MW; 465452FD42ACCFAE CRC64; MRDLRAQVTS GLLPFPEVTL QALGEDEITL ESVLRGKFAA GKNGLACLAC GPQLEVVNSI TGERLSAYRF SGVNEQPPVV LAVKEFSWQK RTGLLIGLEE TEGSVLCLYD LGISKVVKAV VLPGRVTAIE PIINHGGASA STQHLHPSLR WLFGVAAVVT DVGQILLVDL CLDDLSCNQN EVEASDLEVL TGIPAEVPHI RESVMRQGRH LCFQLVSPTG TAVSTLSYIS RTNQLAVGFS DGYLALWNMK SMKREYYIQL ESGQVPVYAV TFQEPENDPR NCCYLWAVQS TQDSEGDVLS LHLLQLAFGN RKCLASGQIL YEGLEYCEER YTLDLTGGMF PLRGQTSNTK LLGCQSIEKF RSHGDREEGV NEALSPDTSV SVFTWQVNIY GQGKPSVYLG LFDINRWYHA QMPDSLRSGE YLHNCSYFAL WSLESVVSRT SPHGILDILV HERSLNRGVP PSYPPPEQFF NPSTYNFDAT CLLNSGVVHL TCTGFQKETL TFLKKSGPSL NELIPDGYNR CLVAGLLSPR FVDVQPSSLS QEEQLEAILS AAIQTSSLGL LTGYIRRWIT EEQPNSATNL RFVLEWTWNK VVLTKEEFDR LCVPLFDGSC HFMDPQTIQS IQQCYLLLSN LNIVLSCFAS EAREITERGL IDLSNKFVVS HLICQYAQVV LWFSHSGLLP EGIDDSVQLS RLCYNYPVIQ NYYTSRRQKF ERLSRGKWNP DCLMIDGLVS QLGERIEKLW KRDEGGTGKY PPASLHAVLD MYLLDGVTEA AKHSITIYLL LDIMYSFPNK TDTPIESFPT VFAISWGQVK LIQGFWLIDH NDYESGLDLL FHPATAKPLS WQHSKIIQAF MSQGEHRQAL RYIQTMKPTV SSGNDVILHL TVLLFNRCMV EAWNFLRQHC NRLNIEELLK HMYEVCQEMG LMEDLLKLPF TDTEQECLVK FLQSSASVQN HEFLLVHHLQ RANYVPALKL NQTLKINVMN DRDPRLRERS LARNSILDQY GKILPRVHRK LAIERAKPYH LSTSSVFRLV SRPKPLSAVP KQVVTGTVLT RSVFINNVLS KIGEVWASKE PINSTTPFNS SKIEEPSPIV YSLPAPELPE AFFGTPISKA SQKISRLLDL VVQPVPRPSQ CSEFIQQSSM KSPLYLVSRS LPSSSQLKGS PQAISRASEL HLLETPLVVK KAKSLAMSVT TSGFSEFTPQ SILRSTLRST PLASPSPSPG RSPQRLKETR ISFVEEDVHP KWIPGAADDS KLEVFTTPKK CAVPVETEWL KSKDRTTSFF LNSPEKEHQE MDEGSQSLEK LDVSKGNSSV SITSDETTLE YQDAPSPEDL EETVFTASKP KSSSTALTTN VTEQTEKDGD KDVFASEVTP SDLQKQMGNL EDAETKDLLV AAEAFSELNH LSPVQGTEAS LCAPSVYEGK IFTQKSKVPV LDEGLTSVET YTPAIRANDN KSMADVLGDG GNSSLTISEG PIVSERRLNQ EVALNLKEDH EVEVGVLKES VDLPEEKLPI SDSPPDTQEI HVIEQEKLEA QDSGEEARNL SFNELYPSGT LKLQYNFDTI DQQFCDLADN KDTAECDIAE VDGELFVAQS NFTLILEGEE GEVEPGDFAS SDVLPKAANT ATEEKLVCSG ENDNHGQIAN LPSAVTSDQK SQKVDTLPYV PEPIKVAIAE NLLDVIKDTR SKEITSDTME QSIHETIPLV SQNIMCPTKL VKSAFKTAQE TSTMTMNVSQ VDDVVSSKTR TRGQRIQNVN VKSAQQEASA DVATPKMPGQ SVRKKTRKAK EISEASENIY SDVRGLSQNQ QIPQNSVTPR RGRRKKEVNQ DILENTSSVE QELQITTGRE SKRLKSSQLL EPAVEETTKK EVKVSSVTKR TPRRIKRSVE NQESVEIIND LKVSTVTSPS RMIRKLRSTN LDASENTGNK QDDKSSDKQL RIKHVRRVRG REVSPSDVRE DSNLESSQLT VQAEFDMSAI PRKRGRPRKI NPSEDVGSKA VKEERSPKKK EAPSIRRRST RNTPAKSENV DVGKPALGKS ILVPNEELSM VMSSKKKLTK KTESQSQKRS LHSVSEERTD EMTHKETNEQ EERLLATASF TKSSRSSRTR SSKAILLPDL SEPNNEPLFS PASEVPRKAK AKKIEVPAQL KELVSDLSSQ FVISPPALRS RQKNTSNKNK LEDELKDDAQ SVETLGKPKA KRIRTSKTKQ ASKNTEKESA WSPPPIEIRL ISPLASPADG VKSKPRKTTE VTGTGLGRNR KKLSSYPKQI LRRKML //