ELYS_MOUSE
ID ELYS_MOUSE Reviewed; 2243 AA.
AC Q8CJF7; B2RRC8; Q8BVJ5; Q8VD55;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Yolk sac;
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 [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=12745078; DOI=10.1016/s0006-291x(03)00772-1;
RA Okita K., Takizawa M., Ueno M., Kimura N., Nobuhisa I., Taga T.;
RT "Genomic organization and characterization of the mouse ELYS gene.";
RL Biochem. Biophys. Res. Commun. 305:327-332(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2082-2243.
RC STRAIN=C57BL/6J; TISSUE=Fetal head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15507119; DOI=10.1111/j.1365-2443.2004.00791.x;
RA Okita K., Kiyonari H., Nobuhisa I., Kimura N., Aizawa S., Taga T.;
RT "Targeted disruption of the mouse ELYS gene results in embryonic death at
RT peri-implantation development.";
RL Genes Cells 9:1083-1091(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080 AND SER-1218, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; THR-1083; SER-1138;
RP SER-1214; SER-1218; SER-1381; SER-1541; SER-1928; SER-2188 AND SER-2198,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2221, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-494, REPEATS, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF TYR-284 AND 272-PHE--ARG-280.
RX PubMed=23499022; DOI=10.1016/j.str.2013.02.006;
RA Bilokapic S., Schwartz T.U.;
RT "Structural and functional studies of the 252 kDa nucleoporin ELYS reveal
RT distinct roles for its three tethered domains.";
RL Structure 21:572-580(2013).
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 (By similarity).
CC Has also been proposed to function as a transcription factor which may
CC play a specific role in hematopoietic tissues (PubMed:11952839).
CC {ECO:0000250, ECO:0000269|PubMed:11952839}.
CC -!- SUBUNIT: Associates with the Nup107-160 subcomplex of the NPC.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11952839}.
CC Nucleus, nuclear pore complex {ECO:0000269|PubMed:23499022}. Nucleus
CC matrix {ECO:0000269|PubMed:23499022}. Cytoplasm
CC {ECO:0000269|PubMed:11952839}. Note=Localizes to the nuclear pore
CC complex (NPC) throughout interphase. Localizes to the kinetochore from
CC prophase, and this appears to require the Nup107-160 subcomplex of the
CC NPC. Localizes to the periphery of chromatin from late anaphase (By
CC similarity). {ECO:0000250|UniProtKB:Q8WYP5}.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in testis,
CC lung and kidney. Expressed in T-cells, B-cells and granulocytes in bone
CC marrow. {ECO:0000269|PubMed:11952839}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo at 3.5 dpc and 6.5
CC dpc. Higher expression is detected at 10.5 dpc nad then progressively
CC decreases. Highly expressed in fetal hematopoietic tissues including
CC liver, spleen and thymus. Expressed in the endothelium lining the
CC dorsal aorta of 11.5 dpc embryos (at protein level).
CC {ECO:0000269|PubMed:11952839, ECO:0000269|PubMed:15507119}.
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 (PubMed:23499022).
CC {ECO:0000269|PubMed:23499022}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality before 7.5 dpc. Impaired
CC proliferation of the inner cells of the blastocyst due at least in part
CC to increased apoptosis. {ECO:0000269|PubMed:15507119}.
CC -!- SIMILARITY: Belongs to the ELYS family. {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; AB059278; BAB78517.1; -; mRNA.
DR EMBL; AB081498; BAC22610.1; -; Genomic_DNA.
DR EMBL; BC138343; AAI38344.1; -; mRNA.
DR EMBL; BC138344; AAI38345.1; -; mRNA.
DR EMBL; AK078022; BAC37101.2; ALT_SEQ; mRNA.
DR CCDS; CCDS15564.1; -.
DR RefSeq; NP_080651.2; NM_026375.2.
DR PDB; 4I0O; X-ray; 1.90 A; A=1-494.
DR PDBsum; 4I0O; -.
DR AlphaFoldDB; Q8CJF7; -.
DR SMR; Q8CJF7; -.
DR BioGRID; 230549; 4.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q8CJF7; 1.
DR STRING; 10090.ENSMUSP00000027768; -.
DR iPTMnet; Q8CJF7; -.
DR PhosphoSitePlus; Q8CJF7; -.
DR EPD; Q8CJF7; -.
DR jPOST; Q8CJF7; -.
DR MaxQB; Q8CJF7; -.
DR PaxDb; Q8CJF7; -.
DR PeptideAtlas; Q8CJF7; -.
DR PRIDE; Q8CJF7; -.
DR ProteomicsDB; 277580; -.
DR Antibodypedia; 20836; 111 antibodies from 18 providers.
DR DNASU; 226747; -.
DR Ensembl; ENSMUST00000027768; ENSMUSP00000027768; ENSMUSG00000026491.
DR GeneID; 226747; -.
DR KEGG; mmu:226747; -.
DR UCSC; uc011wxn.1; mouse.
DR CTD; 25909; -.
DR MGI; MGI:1915033; Ahctf1.
DR VEuPathDB; HostDB:ENSMUSG00000026491; -.
DR eggNOG; ENOG502QU0D; Eukaryota.
DR GeneTree; ENSGT00390000018900; -.
DR HOGENOM; CLU_001145_0_0_1; -.
DR InParanoid; Q8CJF7; -.
DR OMA; KWNHDCL; -.
DR OrthoDB; 1040332at2759; -.
DR PhylomeDB; Q8CJF7; -.
DR TreeFam; TF350425; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 226747; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Ahctf1; mouse.
DR PRO; PR:Q8CJF7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CJF7; protein.
DR Bgee; ENSMUSG00000026491; Expressed in embryonic post-anal tail and 266 other tissues.
DR ExpressionAtlas; Q8CJF7; baseline and differential.
DR Genevisible; Q8CJF7; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0031080; C:nuclear pore outer ring; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS: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:0030097; P:hemopoiesis; TAS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISS: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; ISS:UniProtKB.
DR DisProt; DP01548; -.
DR InterPro; IPR032040; ELYS-bb.
DR InterPro; IPR025151; ELYS_dom.
DR Pfam; PF13934; ELYS; 1.
DR Pfam; PF16687; ELYS-bb; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Developmental protein; DNA-binding; Kinetochore;
KW Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transcription; Translocation;
KW Transport.
FT CHAIN 1..2243
FT /note="Protein ELYS"
FT /id="PRO_0000246320"
FT DNA_BIND 1955..1967
FT /note="A.T hook"
FT /evidence="ECO:0000250|UniProtKB:Q5U249"
FT REGION 1..981
FT /note="Necessary for cytoplasmic localization"
FT /evidence="ECO:0000269|PubMed:11952839"
FT REGION 1..494
FT /note="Seven-bladed beta propeller repeats"
FT /evidence="ECO:0000269|PubMed:23499022"
FT REGION 591..1092
FT /note="Important for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT REGION 1019..2243
FT /note="Disordered"
FT /evidence="ECO:0000303|PubMed:23499022"
FT REGION 1149..2243
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000269|PubMed:11952839"
FT REGION 1447..1694
FT /note="Mediates transcriptional activity"
FT /evidence="ECO:0000269|PubMed:11952839"
FT REGION 1828..2243
FT /note="Important for nuclear localization and chromatin
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT COMPBIAS 1348..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1887..1901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1993..2007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1083
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1517
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1870
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 1980
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 2021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 2099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 2132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 2188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYP5"
FT MOD_RES 2221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 272..280
FT /note="FQEPENDPR->GSGSGSGSG: Abolishes nuclear pore
FT localization; when associated with S-284."
FT /evidence="ECO:0000269|PubMed:23499022"
FT MUTAGEN 284
FT /note="Y->S: Abolishes nuclear pore localization; when
FT associated with 272-GSGSGSGSG-280."
FT /evidence="ECO:0000269|PubMed:23499022"
FT CONFLICT 1207
FT /note="F -> L (in Ref. 1; BAB78517)"
FT /evidence="ECO:0000305"
FT CONFLICT 1379
FT /note="A -> T (in Ref. 1; BAB78517)"
FT /evidence="ECO:0000305"
FT CONFLICT 1414
FT /note="A -> G (in Ref. 1; BAB78517)"
FT /evidence="ECO:0000305"
FT CONFLICT 1718
FT /note="H -> R (in Ref. 1; BAB78517)"
FT /evidence="ECO:0000305"
FT CONFLICT 2084
FT /note="T -> A (in Ref. 4; BAC37101)"
FT /evidence="ECO:0000305"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4I0O"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:4I0O"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:4I0O"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:4I0O"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:4I0O"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 299..313
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 319..336
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 347..359
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 377..389
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 434..440
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:4I0O"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 476..483
FT /evidence="ECO:0007829|PDB:4I0O"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:4I0O"
SQ SEQUENCE 2243 AA; 247646 MW; EEEA09B70F2B5691 CRC64;
MQDLTAQVTS DLLHFPEVTI EALGEDEITL ESVLRGKFAA GKNGLACLAC GPQLEVVNSL
TGERLSAYRF SGVNEQPPVV LAVKEFSWHK RTGLLIGLEE ADGSVLCLYD LGISRVVKAV
VLPGRVTAIE PIINHGGASA STQHLHPSLR WLFGVAAVVT DVGQILLIDL CLDDLSCSQN
EVEASDLEVI TGIPAEVPHI RERVMREGRH LCFQLVSPLG VAISTLSYIN RTNQLAVGFS
DGYLALWNMK SMKREYYTQL EGGRVPVHAV AFQEPENDPR NCCYLWAVQS TQDSEGDVLS
LHLLQLAFGD RKCLASGQIL YEGLEYCEER YTLDLAGGTF PLRGQTSNTK LLGCQSIERF
PSHGDREESM REALSPDTSV SVFTWQVNIY GQGKPSVYLG LFDINRWYHA QMPDSLRSGE
SLHNCSYFAL WSLDSVVSRT SPHHILDILV HERSLNRGVP PSYPPPEQFF NPSTFNFDAT
CLLDSGVIHV TCAGFQKETL TFLKKSGPTL NEVIPDSYNR CLVAGLLSPR LIDIQPSSLS
QEEQLEAILS AAIQTSSLGL LTGYIRTWII EEQPNSAANL RFVLEWTWNK VVLTKEEFDR
LCVPLFDGSC RFIDPQTIQS IQQCHLLLSN LSTVLSCFAM EAQGITERGL VDLSNKHMVT
QLLCQYAHMV LWFCHSGLLP EGLDDALQLS RLRYNYPVIQ NYYTSRRQKS ERSPRGKWNH
DCLMIDGLVS QLGDEVEKLW KRDEGGTGRY PPASIHALLD IYLLDNITEA SKHAITIYLL
LDIMYSFPNK TDTPIESFPT AFAISWGQVK LVQGFWLLDH NDYENGLDLL FHPVTAKPAS
WQHSKIIEAF MSQGEHKQAL RYLQTMKPTV SSSNEVILHL TVLLFNRCMV EAWNLLRQNS
NRVNIEELLK HAYEVCQEMG LMEDLLKLPF TNTEQECLVK FLQSSTSVEN HEFLLVHHLQ
RANYISALKL NQILKNNLMS DRDPRLRERS VTRNSILDQY GKILPRVQRK LAVERAKPYH
LSTSSVFHEV SRPKPLSAFP KKAITGTVLT RSTFISNVLS KIGEVWASHE PRNGVSLFNS
PKTEQPSPVV HSFPHPELPE AFVGTPISNT SQRISRLLDL VVHPVPQPSQ CLEFIQQSPT
RSPLCLLSSS LPLSSQFKRP HQNTSRPSEL LLLETPLIVK KAKSLALSAT SSGFAEFTPP
SILRSGFRTT PLASPSLSPG RSLTPPFRVK ETRISFMEEG MNTHWTDRAT DDRNTKAFVS
TSFHKCGLPA ETEWMKTSDK NTYFPLDVPA KGPQKVVAES LATHSGRLEK LDVSKEDSTA
STRSDQTSLE YHDAPSPEDL EGAVFVSPKP ASSSTELTTN STLQTERDND KDAFKSEGAP
SPVKKQIGTG DAAVEAFSEL SRLDPVERAE ASFAVSSVCE GETSTSNSKT SVLDGIVPIE
SRTSILTADH KESVANTVAD VESSGSTSSK CPVTSERSLG QKLTLNLKED EIEAHVPKEN
VGLPEESPRI SAAPSDTHEI HLIGCENLEV QNSEEEAKNL SFDELYPLGA EKLEYNLSTI
EQQFCDLPDD KDSAECDAAE VDGELFVAQS NFTLILEGEE GEAEASDSAA PNMLPKATKE
KPVCHREPHN QERVTDLPSA VTADQESHKV ETLPYVPEPV KVAIAENLLD VIKDTRSKEA
TPVAAGEAGD EDGAVIVSKA AHSSRLTNST PKTVKEPHAE TVNTSQNDDM VSSRTLTRRQ
HALSLNVTSE QEPSAVATPK KRTRKIKETP ESSERTCSDL KVAPENQLTA QSPPAPRRGK
KKDVSQGTLP SSGAVEPEPE PQGTPGRLRL RTQPPEPAAE ETPSRTKVRL SSVRKGTPRR
LKKSVENGQS TEILDDLKGS EAASHDGTVT ELRNANLEDT QNMEYKQDEH SDQQLPLKRK
RVREREVSVS SVTEEPKLDS SQLPLQTGLD VPATPRKRGR PRKVVPLEAD GGTTGKEQTS
PQKKDVPVVR RSTRNTPARN VSTLEKSVLV PNKEAALVVT SKRRPTKKSA EESSKDPSAA
VSDLAGGAAH TESADRRDGL LAAAALTPSA QGTRTRSRRT MLLTDISEPK TEPLFPPPSV
KVPKKKSKAE NMEAAAQLKE LVSDLSSQFV VSPPALRTRQ KSISNTSKLL GELESDPKPL
EIIEQKPKRS RTVKTRASRN TGKGSSWSPP PVEIKLVSPL ASPVDEIKTG KPRKTAEIAG
KTLGRGRKKP SSFPKQILRR KML
