ELYS_HUMAN
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 03-AUG-2022, entry version 164.
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};
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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 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. [Q8WYP5-2]
DR AlphaFoldDB; Q8WYP5; -.
DR SMR; Q8WYP5; -.
DR BioGRID; 117414; 129.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR IntAct; Q8WYP5; 38.
DR MINT; Q8WYP5; -.
DR STRING; 9606.ENSP00000355465; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q8WYP5; 1 site, 1 O-linked glycan (1 site).
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; Q8WYP5; -.
DR PeptideAtlas; Q8WYP5; -.
DR PRIDE; Q8WYP5; -.
DR ProteomicsDB; 75181; -. [Q8WYP5-1]
DR ProteomicsDB; 75182; -. [Q8WYP5-2]
DR ProteomicsDB; 75183; -. [Q8WYP5-3]
DR Antibodypedia; 20836; 111 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 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; 1040332at2759; -.
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; 703 hits in 1082 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 201 other tissues.
DR ExpressionAtlas; Q8WYP5; baseline and differential.
DR Genevisible; Q8WYP5; HS.
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: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; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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; IC: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 Pfam; PF13934; ELYS; 1.
DR Pfam; PF16687; ELYS-bb; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; DNA-binding; Kinetochore; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW 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
