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Protein ELYS (Embryonic large molecule derived from yolk sac) (Protein MEL-28) (Putative AT-hook-containing transcription factor 1)

 ELYS_HUMAN              Reviewed;        2266 AA.
Q8WYP5; A6NGM0; A8MSG9; A8MZ86; Q7Z4E3; Q8IZA4; Q96EH9; Q9Y4Q6;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 3.
07-NOV-2018, entry version 141.
RecName: Full=Protein ELYS;
AltName: Full=Embryonic large molecule derived from yolk sac;
AltName: Full=Protein MEL-28;
AltName: Full=Putative AT-hook-containing transcription factor 1;
Name=AHCTF1; Synonyms=ELYS, TMBS62; ORFNames=MSTP108;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Fetal liver;
PubMed=11952839; DOI=10.1046/j.1365-2443.2002.00529.x;
Kimura N., Takizawa M., Okita K., Natori O., Igarashi K., Ueno M.,
Nakashima K., Nobuhisa I., Taga T.;
"Identification of a novel transcription factor, ELYS, expressed
predominantly in mouse foetal haematopoietic tissues.";
Genes Cells 7:435-446(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Lymphoblast;
Lightfoot J., Alon N., Buchwald M.;
"Cloning of a cDNA that provides partial correction of mitomycin C
sensitivity in Fanconi anemia FA-D1 cells.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1522-2266 (ISOFORMS 1/2/3).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1753-2266 (ISOFORMS 1/2/3).
TISSUE=Heart;
Liu B., Zhao B., Wang X.Y., Liu Y.Q., Sheng H., Qin B.M., Zhang Q.,
Zheng W.Y., Xu H.S., Liu B.H., Lu H., Gong Q., Hui R.T.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2037-2266 (ISOFORMS 1/2/3).
TISSUE=Retinoblastoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232; SER-1283 AND
SER-1996, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2222 AND SER-2226, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
FUNCTION, ASSOCIATION WITH THE NUP107-160 COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=17098863; DOI=10.1073/pnas.0608484103;
Rasala B.A., Orjalo A.V., Shen Z., Briggs S., Forbes D.J.;
"ELYS is a dual nucleoporin/kinetochore protein required for nuclear
pore assembly and proper cell division.";
Proc. Natl. Acad. Sci. U.S.A. 103:17801-17806(2006).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17235358; DOI=10.1038/sj.embor.7400889;
Franz C., Walczak R., Yavuz S., Santarella R., Gentzel M., Askjaer P.,
Galy V., Hetzer M., Mattaj I.W., Antonin W.;
"MEL-28/ELYS is required for the recruitment of nucleoporins to
chromatin and postmitotic nuclear pore complex assembly.";
EMBO Rep. 8:165-172(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-1222, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1283; SER-1541;
SER-1878; SER-2120; SER-2222 AND SER-2226, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1142; SER-1150;
SER-1155; SER-1160; THR-1175; SER-1250; SER-1541; SER-1729; SER-1806;
THR-1808; SER-1878; SER-1884; SER-1898; SER-2060; SER-2089; SER-2120;
SER-2123; SER-2154 AND SER-2212, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1283; SER-1541; SER-1884
AND SER-2222, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1160; SER-1232;
SER-1283; SER-1297; THR-1369; SER-1513; SER-1533; SER-1541; SER-1878;
SER-1898; SER-1944; SER-1946; SER-2043; SER-2044; SER-2120; SER-2154;
SER-2212; SER-2222 AND SER-2226, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1142; SER-1160;
SER-1214; SER-1283; THR-1517; SER-1533; SER-1541 AND SER-1944, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-528; SER-1153;
SER-1160; SER-1214; SER-1218; SER-1222; SER-1232; SER-1250; THR-1257;
SER-1283; THR-1369; SER-1513; SER-1541; SER-1944; SER-2089; SER-2212;
SER-2222 AND SER-2226, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
SUBCELLULAR LOCATION.
PubMed=27341616; DOI=10.1371/journal.pgen.1006131;
Gomez-Saldivar G., Fernandez A., Hirano Y., Mauro M., Lai A.,
Ayuso C., Haraguchi T., Hiraoka Y., Piano F., Askjaer P.;
"Identification of conserved MEL-28/ELYS domains with essential roles
in nuclear assembly and chromosome segregation.";
PLoS Genet. 12:E1006131-E1006131(2016).
-!- FUNCTION: Required for the assembly of a functional nuclear pore
complex (NPC) on the surface of chromosomes as nuclei form at the
end of mitosis. May initiate NPC assembly by binding to chromatin
and recruiting the Nup107-160 subcomplex of the NPC. Also required
for the localization of the Nup107-160 subcomplex of the NPC to
the kinetochore during mitosis and for the completion of
cytokinesis. {ECO:0000269|PubMed:17098863,
ECO:0000269|PubMed:17235358}.
-!- SUBUNIT: Associates with the Nup107-160 subcomplex of the NPC.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8CJF7}.
Nucleus {ECO:0000269|PubMed:17098863,
ECO:0000269|PubMed:27341616}. Nucleus envelope
{ECO:0000269|PubMed:17098863, ECO:0000269|PubMed:27341616}.
Nucleus matrix {ECO:0000269|PubMed:17098863}. Chromosome,
centromere, kinetochore {ECO:0000269|PubMed:17098863,
ECO:0000269|PubMed:27341616}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:17098863}. Nucleus, nuclear pore complex
{ECO:0000269|PubMed:17098863}. Note=Localizes to the nuclear pore
complex (NPC) throughout interphase. Localizes to the kinetochore
from prophase, and this appears to require the Nup107-160
subcomplex of the NPC. Localizes to the periphery of chromatin
from late anaphase. {ECO:0000269|PubMed:17098863}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8WYP5-1; Sequence=Displayed;
Name=2;
IsoId=Q8WYP5-2; Sequence=VSP_019844;
Name=3;
IsoId=Q8WYP5-3; Sequence=VSP_042691;
-!- DOMAIN: The N-terminus forms a highly conserved seven-bladed beta
propeller decorated with long loops and mediates anchorage to the
Nup107-160 subcomplex of the nuclear pore, synergistically with
the central alpha domain. The disordered C-terminus is responsible
for the interactions with chromatin (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the ELYS family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN65622.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAQ13621.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB78516.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB059277; BAB78516.1; ALT_INIT; mRNA.
EMBL; AY157619; AAN65622.1; ALT_FRAME; mRNA.
EMBL; AC113174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL080144; CAB45737.1; -; mRNA.
EMBL; AF173978; AAQ13621.1; ALT_INIT; mRNA.
EMBL; BC012307; AAH12307.1; -; mRNA.
CCDS; CCDS1629.2; -. [Q8WYP5-3]
PIR; T12528; T12528.
RefSeq; NP_001310271.1; NM_001323342.1. [Q8WYP5-1]
RefSeq; NP_056261.4; NM_015446.4. [Q8WYP5-3]
RefSeq; XP_006711821.1; XM_006711758.1. [Q8WYP5-2]
UniGene; Hs.300887; -.
ProteinModelPortal; Q8WYP5; -.
SMR; Q8WYP5; -.
BioGrid; 117414; 24.
IntAct; Q8WYP5; 27.
MINT; Q8WYP5; -.
STRING; 9606.ENSP00000355465; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q8WYP5; -.
PhosphoSitePlus; Q8WYP5; -.
BioMuta; AHCTF1; -.
DMDM; 259016354; -.
EPD; Q8WYP5; -.
MaxQB; Q8WYP5; -.
PaxDb; Q8WYP5; -.
PeptideAtlas; Q8WYP5; -.
PRIDE; Q8WYP5; -.
ProteomicsDB; 75181; -.
ProteomicsDB; 75182; -. [Q8WYP5-2]
ProteomicsDB; 75183; -. [Q8WYP5-3]
Ensembl; ENST00000326225; ENSP00000355465; ENSG00000153207. [Q8WYP5-3]
Ensembl; ENST00000366508; ENSP00000355464; ENSG00000153207. [Q8WYP5-2]
GeneID; 25909; -.
KEGG; hsa:25909; -.
UCSC; uc001ibv.3; human. [Q8WYP5-1]
CTD; 25909; -.
EuPathDB; HostDB:ENSG00000153207.14; -.
GeneCards; AHCTF1; -.
HGNC; HGNC:24618; AHCTF1.
HPA; HPA031658; -.
MIM; 610853; gene.
neXtProt; NX_Q8WYP5; -.
OpenTargets; ENSG00000153207; -.
PharmGKB; PA142672631; -.
eggNOG; ENOG410IG0H; Eukaryota.
eggNOG; ENOG410XQV6; LUCA.
GeneTree; ENSGT00390000018900; -.
InParanoid; Q8WYP5; -.
OMA; GSCRFID; -.
OrthoDB; EOG091G006H; -.
PhylomeDB; Q8WYP5; -.
TreeFam; TF350425; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
ChiTaRS; AHCTF1; human.
GeneWiki; AHCTF1; -.
GenomeRNAi; 25909; -.
PMAP-CutDB; Q8WYP5; -.
PRO; PR:Q8WYP5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000153207; Expressed in 227 organ(s), highest expression level in testis.
CleanEx; HS_AHCTF1; -.
ExpressionAtlas; Q8WYP5; baseline and differential.
Genevisible; Q8WYP5; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:NTNU_SB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
InterPro; IPR032040; ELYS-bb.
InterPro; IPR025151; ELYS_dom.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
Pfam; PF13934; ELYS; 1.
Pfam; PF16687; ELYS-bb; 1.
SUPFAM; SSF50998; SSF50998; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Centromere;
Chromosome; Complete proteome; Cytoplasm; DNA-binding; Kinetochore;
mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Translocation;
Transport.
CHAIN 1 2266 Protein ELYS.
/FTId=PRO_0000246319.
DNA_BIND 1971 1983 A.T hook. {ECO:0000250|UniProtKB:Q5U249}.
REGION 1 981 Necessary for cytoplasmic localization.
{ECO:0000250|UniProtKB:Q8CJF7}.
REGION 1 494 Seven-bladed beta propeller repeats.
{ECO:0000250|UniProtKB:Q8CJF7}.
REGION 591 1092 Important for nuclear localization.
{ECO:0000269|PubMed:27341616}.
REGION 1019 2266 Disordered.
{ECO:0000250|UniProtKB:Q8CJF7}.
REGION 1149 2266 Necessary for nuclear localization.
{ECO:0000250|UniProtKB:Q8CJF7}.
REGION 1446 1698 Mediates transcriptional activity.
{ECO:0000250|UniProtKB:Q8CJF7}.
REGION 1842 2266 Important for nuclear localization and
chromatin binding.
{ECO:0000269|PubMed:27341616}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1080 1080 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CJF7}.
MOD_RES 1138 1138 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CJF7}.
MOD_RES 1142 1142 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1150 1150 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1153 1153 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1155 1155 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1175 1175 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1214 1214 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1218 1218 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1222 1222 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:23186163}.
MOD_RES 1232 1232 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1250 1250 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1257 1257 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1283 1283 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1297 1297 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1369 1369 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1371 1371 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CJF7}.
MOD_RES 1513 1513 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1517 1517 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1533 1533 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1541 1541 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1729 1729 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1806 1806 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1808 1808 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1878 1878 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 1884 1884 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1898 1898 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1944 1944 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1946 1946 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1996 1996 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 2043 2043 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2044 2044 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2060 2060 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2089 2089 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2120 2120 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 2123 2123 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2154 2154 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 2212 2212 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2222 2222 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2226 2226 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1 M -> MDSLAGLSPREAAGVLSLSCVGVCSTCAWAWPHGSM
(in isoform 2). {ECO:0000303|Ref.2}.
/FTId=VSP_019844.
VAR_SEQ 1 1 M -> MAAERRCGSM (in isoform 3).
{ECO:0000303|PubMed:11952839}.
/FTId=VSP_042691.
VARIANT 874 874 N -> S (in dbSNP:rs2642990).
/FTId=VAR_027037.
VARIANT 2185 2185 L -> V (in dbSNP:rs12410563).
/FTId=VAR_027038.
CONFLICT 168 168 V -> I (in Ref. 1; BAB78516).
{ECO:0000305}.
CONFLICT 207 207 Q -> E (in Ref. 1; BAB78516).
{ECO:0000305}.
CONFLICT 237 237 V -> A (in Ref. 1; BAB78516).
{ECO:0000305}.
CONFLICT 279 279 P -> R (in Ref. 1; BAB78516).
{ECO:0000305}.
CONFLICT 403 403 D -> G (in Ref. 2; AAN65622).
{ECO:0000305}.
CONFLICT 646 646 T -> A (in Ref. 1; BAB78516).
{ECO:0000305}.
CONFLICT 743 743 D -> G (in Ref. 2; AAN65622).
{ECO:0000305}.
CONFLICT 753 753 A -> G (in Ref. 2; AAN65622).
{ECO:0000305}.
CONFLICT 1134 1134 F -> S (in Ref. 2; AAN65622).
{ECO:0000305}.
CONFLICT 1207 1207 L -> P (in Ref. 1; BAB78516).
{ECO:0000305}.
CONFLICT 1270 1270 L -> P (in Ref. 1; BAB78516).
{ECO:0000305}.
CONFLICT 1737 1737 S -> F (in Ref. 4; CAB45737).
{ECO:0000305}.
CONFLICT 1797 1797 S -> F (in Ref. 1; BAB78516).
{ECO:0000305}.
CONFLICT 1830 1830 E -> G (in Ref. 2; AAN65622).
{ECO:0000305}.
CONFLICT 2128 2128 K -> E (in Ref. 2; AAN65622).
{ECO:0000305}.
CONFLICT 2187 2187 K -> E (in Ref. 6; AAH12307).
{ECO:0000305}.
CONFLICT 2213 2213 P -> L (in Ref. 1; BAB78516).
{ECO:0000305}.
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


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