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Protein ecdysoneless homolog (Human suppressor of GCR two) (hSGT1)

 ECD_HUMAN               Reviewed;         644 AA.
O95905; C9JX46; E9PAW8;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 145.
RecName: Full=Protein ecdysoneless homolog {ECO:0000250|UniProtKB:Q9W032};
AltName: Full=Human suppressor of GCR two {ECO:0000303|PubMed:9928932};
Short=hSGT1 {ECO:0000303|PubMed:9928932};
Name=ECD;
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 1), AND FUNCTION.
TISSUE=Brain;
PubMed=9928932; DOI=10.1007/s004380050926;
Sato T., Jigami Y., Suzuki T., Uemura H.;
"A human gene, hSGT1, can substitute for GCR2, which encodes a general
regulatory factor of glycolytic gene expression in Saccharomyces
cerevisiae.";
Mol. Gen. Genet. 260:535-540(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Signet-ring cell carcinoma;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[6]
FUNCTION, INTERACTION WITH TP53 AND MDM2, AND SUBCELLULAR LOCATION.
PubMed=16849563; DOI=10.1158/0008-5472.CAN-06-0722;
Zhang Y., Chen J., Gurumurthy C.B., Kim J., Bhat I., Gao Q., Dimri G.,
Lee S.W., Band H., Band V.;
"The human orthologue of Drosophila ecdysoneless protein interacts
with p53 and regulates its function.";
Cancer Res. 66:7167-7175(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, 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-503; SER-505 AND
SER-518, 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).
[9]
FUNCTION, AND INTERACTION WITH RB1; RBL1 AND RBL2.
PubMed=19640839; DOI=10.1074/jbc.M109.030551;
Kim J.H., Gurumurthy C.B., Naramura M., Zhang Y., Dudley A.T.,
Doglio L., Band H., Band V.;
"Role of mammalian Ecdysoneless in cell cycle regulation.";
J. Biol. Chem. 284:26402-26410(2009).
[10]
FUNCTION, INTERACTION WITH EP300, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ILE-481; ASP-484; LEU-489; ASP-510; ASP-512 AND
ASP-520.
PubMed=19919181; DOI=10.1515/BC.2010.004;
Kim J.H., Gurumurthy C.B., Band H., Band V.;
"Biochemical characterization of human Ecdysoneless reveals a role in
transcriptional regulation.";
Biol. Chem. 391:9-19(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
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).
[13]
TISSUE SPECIFICITY.
PubMed=22270930; DOI=10.1007/s10549-011-1946-8;
Zhao X., Mirza S., Alshareeda A., Zhang Y., Gurumurthy C.B., Bele A.,
Kim J.H., Mohibi S., Goswami M., Lele S.M., West W., Qiu F.,
Ellis I.O., Rakha E.A., Green A.R., Band H., Band V.;
"Overexpression of a novel cell cycle regulator ecdysoneless in breast
cancer: a marker of poor prognosis in HER2/neu-overexpressing breast
cancer patients.";
Breast Cancer Res. Treat. 134:171-180(2012).
[14]
TISSUE SPECIFICITY.
PubMed=22977192; DOI=10.1158/1078-0432.CCR-12-1789;
Dey P., Rachagani S., Chakraborty S., Singh P.K., Zhao X.,
Gurumurthy C.B., Anderson J.M., Lele S., Hollingsworth M.A., Band V.,
Batra S.K.;
"Overexpression of ecdysoneless in pancreatic cancer and its role in
oncogenesis by regulating glycolysis.";
Clin. Cancer Res. 18:6188-6198(2012).
[15]
FUNCTION, AND INTERACTION WITH TXNIP.
PubMed=23880345; DOI=10.1016/j.bbrc.2013.07.036;
Suh H.W., Yun S., Song H., Jung H., Park Y.J., Kim T.D., Yoon S.R.,
Choi I.;
"TXNIP interacts with hEcd to increase p53 stability and activity.";
Biochem. Biophys. Res. Commun. 438:264-269(2013).
[16]
INTERACTION WITH PIH1D1.
PubMed=24656813; DOI=10.1016/j.celrep.2014.03.013;
Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M.,
O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.;
"Phosphorylation-dependent PIH1D1 interactions define substrate
specificity of the R2TP cochaperone complex.";
Cell Rep. 7:19-26(2014).
[17]
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).
[18]
FUNCTION.
PubMed=24722212; DOI=10.1371/journal.pgen.1004287;
Claudius A.K., Romani P., Lamkemeyer T., Jindra M., Uhlirova M.;
"Unexpected role of the steroid-deficiency protein ecdysoneless in
pre-mRNA splicing.";
PLoS Genet. 10:E1004287-E1004287(2014).
[19]
PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH RUVBL1,
ASSOCIATION WITH THE R2TP COMPLEX, AND MUTAGENESIS OF SER-503;
SER-505; SER-518; SER-572; SER-579 AND SER-584.
PubMed=26711270; DOI=10.1128/MCB.00594-15;
Mir R.A., Bele A., Mirza S., Srivastava S., Olou A.A., Ammons S.A.,
Kim J.H., Gurumurthy C.B., Qiu F., Band H., Band V.;
"A novel interaction of ecdysoneless (ECD) protein with R2TP complex
component RUVBL1 is required for the functional role of ECD in cell
cycle progression.";
Mol. Cell. Biol. 36:886-899(2015).
[20]
VARIANT GLY-281.
PubMed=11090341; DOI=10.1086/316954;
Bork J.M., Peters L.M., Riazuddin S., Bernstein S.L., Ahmed Z.M.,
Ness S.L., Polomeno R., Ramesh A., Schloss M., Srisailpathy C.R.S.,
Wayne S., Bellman S., Desmukh D., Ahmed Z., Khan S.N.,
Kaloustian V.M.D., Li X.C., Lalwani A., Riazuddin S.,
Bitner-Glindzicz M., Nance W.E., Liu X.-Z., Wistow G., Smith R.J.H.,
Griffith A.J., Wilcox E.R., Friedman T.B., Morell R.J.;
"Usher syndrome 1D and nonsyndromic autosomal recessive deafness
DFNB12 are caused by allelic mutations of the novel cadherin-like gene
CDH23.";
Am. J. Hum. Genet. 68:26-37(2001).
-!- FUNCTION: Regulator of p53/TP53 stability and function. Inhibits
MDM2-mediated degradation of p53/TP53 possibly by cooperating in
part with TXNIP (PubMed:16849563, PubMed:23880345). May be
involved transcriptional regulation. In vitro has intrinsic
transactivation activity enhanced by EP300. May be a
transcriptional activator required for the expression of
glycolytic genes (PubMed:19919181, PubMed:9928932). Involved in
regulation of cell cycle progression. Proposed to disrupt Rb-E2F
binding leading to transcriptional activation of E2F proteins
(PubMed:19640839). The cell cycle -regulating function may depend
on its RUVBL1-mediated association with the R2TP complex
(PubMed:26711270). May play a role in regulation of pre-mRNA
splicing (PubMed:24722212). {ECO:0000269|PubMed:16849563,
ECO:0000269|PubMed:19640839, ECO:0000269|PubMed:19919181,
ECO:0000269|PubMed:23880345, ECO:0000269|PubMed:26711270,
ECO:0000305|PubMed:24722212, ECO:0000305|PubMed:9928932}.
-!- SUBUNIT: Interacts with TP53, MDM2, TXNIP (PubMed:16849563,
PubMed:23880345). Interacts (phosphorylated) with PIH1D1.
Interacts with RUVBL1 mediating the PIH1D1-independent association
with the R2TP complex (PubMed:24656813, PubMed:26711270).
Interacts with RB1, RBL1 and RBL2; ECD competes with E2F1 for
binding to hypophospshorylated RB1 (PubMed:19640839). Interacts
with EP300 (PubMed:19919181). {ECO:0000269|PubMed:16849563,
ECO:0000269|PubMed:19640839, ECO:0000269|PubMed:19919181,
ECO:0000269|PubMed:23880345, ECO:0000269|PubMed:24656813,
ECO:0000269|PubMed:26711270}.
-!- INTERACTION:
Q9NWS0:PIH1D1; NbExp=11; IntAct=EBI-2557598, EBI-357318;
Q6P2Q9:PRPF8; NbExp=2; IntAct=EBI-2557598, EBI-538479;
Q9Y265:RUVBL1; NbExp=7; IntAct=EBI-2557598, EBI-353675;
Q9H3M7:TXNIP; NbExp=5; IntAct=EBI-2557598, EBI-1369170;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16849563,
ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270}. Nucleus
{ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181,
ECO:0000269|PubMed:26711270}. Note=Predominantly is located in the
cytoplasm. {ECO:0000269|PubMed:16849563,
ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O95905-1; Sequence=Displayed;
Name=2;
IsoId=O95905-2; Sequence=VSP_045670;
Note=No experimental confirmation available.;
Name=3;
IsoId=O95905-3; Sequence=VSP_045671;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in muscle and heart. Over-
expressed in pancreatic and breast cancers.
{ECO:0000269|PubMed:22270930, ECO:0000269|PubMed:22977192}.
-!- PTM: Phosphorylated predominantly by CK2 on two serine-containing
clusters; involved in cell cycle regulation activity.
{ECO:0000269|PubMed:26711270}.
-!- SIMILARITY: Belongs to the ECD family. {ECO:0000305}.
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EMBL; D88208; BAA75199.1; -; mRNA.
EMBL; AK315711; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK225519; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC016394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000721; AAH00721.1; -; mRNA.
CCDS; CCDS44433.1; -. [O95905-2]
CCDS; CCDS44434.1; -. [O95905-3]
CCDS; CCDS7321.1; -. [O95905-1]
RefSeq; NP_001129224.1; NM_001135752.1. [O95905-3]
RefSeq; NP_001129225.1; NM_001135753.1. [O95905-2]
RefSeq; NP_009196.1; NM_007265.2. [O95905-1]
UniGene; Hs.631822; -.
ProteinModelPortal; O95905; -.
SMR; O95905; -.
BioGrid; 116450; 69.
IntAct; O95905; 34.
STRING; 9606.ENSP00000401566; -.
iPTMnet; O95905; -.
PhosphoSitePlus; O95905; -.
BioMuta; ECD; -.
EPD; O95905; -.
MaxQB; O95905; -.
PaxDb; O95905; -.
PeptideAtlas; O95905; -.
PRIDE; O95905; -.
Ensembl; ENST00000372979; ENSP00000362070; ENSG00000122882. [O95905-1]
Ensembl; ENST00000430082; ENSP00000401566; ENSG00000122882. [O95905-3]
Ensembl; ENST00000454759; ENSP00000395786; ENSG00000122882. [O95905-2]
GeneID; 11319; -.
KEGG; hsa:11319; -.
UCSC; uc001jtn.4; human. [O95905-1]
CTD; 11319; -.
DisGeNET; 11319; -.
EuPathDB; HostDB:ENSG00000122882.10; -.
GeneCards; ECD; -.
HGNC; HGNC:17029; ECD.
HPA; HPA006465; -.
MIM; 616464; gene.
neXtProt; NX_O95905; -.
OpenTargets; ENSG00000122882; -.
PharmGKB; PA143485450; -.
eggNOG; KOG2406; Eukaryota.
eggNOG; ENOG410XR07; LUCA.
GeneTree; ENSGT00390000015361; -.
HOGENOM; HOG000029899; -.
HOVERGEN; HBG023145; -.
InParanoid; O95905; -.
OMA; ELCIIPA; -.
OrthoDB; EOG091G081H; -.
PhylomeDB; O95905; -.
TreeFam; TF324229; -.
ChiTaRS; ECD; human.
GeneWiki; ECD_(gene); -.
GenomeRNAi; 11319; -.
PRO; PR:O95905; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000122882; -.
CleanEx; HS_ECD; -.
ExpressionAtlas; O95905; baseline and differential.
Genevisible; O95905; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0006110; P:regulation of glycolytic process; TAS:ProtInc.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
InterPro; IPR010770; Ecd.
PANTHER; PTHR13060; PTHR13060; 1.
Pfam; PF07093; SGT1; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Cytoplasm;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 644 Protein ecdysoneless homolog.
/FTId=PRO_0000220844.
REGION 439 644 Transcription activation.
{ECO:0000269|PubMed:19919181}.
REGION 481 497 Involved in nuclear export.
{ECO:0000269|PubMed:19919181}.
REGION 502 532 Acidic region required for
transactivation activity.
{ECO:0000269|PubMed:19919181}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648}.
VAR_SEQ 262 304 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_045670.
VAR_SEQ 375 375 E -> ERLEVQWRDPGLLQAPPPGFTPFICLSLLSTWDN
(in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045671.
VARIANT 45 45 R -> Q (in dbSNP:rs3812619).
/FTId=VAR_051970.
VARIANT 281 281 R -> G (could be a rare polymorphism;
dbSNP:rs151023501).
{ECO:0000269|PubMed:11090341}.
/FTId=VAR_012191.
VARIANT 452 452 E -> Q (in dbSNP:rs3736518).
/FTId=VAR_051971.
VARIANT 501 501 N -> S (in dbSNP:rs36152134).
/FTId=VAR_051972.
VARIANT 634 634 D -> G (in dbSNP:rs2271904).
/FTId=VAR_051973.
MUTAGEN 481 481 I->A: Decreases transactivation activity.
{ECO:0000269|PubMed:19919181}.
MUTAGEN 484 484 D->F: Decreases transactivation activity.
{ECO:0000269|PubMed:19919181}.
MUTAGEN 489 489 L->A: Decreases transactivation activity.
{ECO:0000269|PubMed:19919181}.
MUTAGEN 503 503 S->A: Greatly impairs in vitro
phosphorylation by CK2 and impairs cell
cycle regulation activity; when
associated with A-505, A-518, A-572, A-
579 and A-584.
{ECO:0000269|PubMed:26711270}.
MUTAGEN 505 505 S->A: Greatly impairs in vitro
phosphorylation by CK2 and impairs cell
cycle regulation activity; when
associated with A-503, A-518, A-572, A-
579 and A-584.
{ECO:0000269|PubMed:26711270}.
MUTAGEN 510 510 D->R: Increases transactivation activity.
{ECO:0000269|PubMed:19919181}.
MUTAGEN 512 512 D->R: Increases transactivation activity.
{ECO:0000269|PubMed:19919181}.
MUTAGEN 518 518 S->A: Greatly impairs in vitro
phosphorylation by CK2 and impairs cell
cycle regulation activity; when
associated with A-503, A-505, A-572, A-
579 and A-584.
{ECO:0000269|PubMed:26711270}.
MUTAGEN 520 520 D->P: Increases transactivation activity.
{ECO:0000269|PubMed:19919181}.
MUTAGEN 572 572 S->A: Greatly impairs in vitro
phosphorylation by CK2 and impairs cell
cycle regulation activity; when
associated with A-503, A-505, A-518, A-
579 and A-584.
{ECO:0000269|PubMed:26711270}.
MUTAGEN 579 579 S->A: Greatly impairs in vitro
phosphorylation by CK2 and impairs cell
cycle regulation activity; when
associated with A-503, A-505, A-518, A-
572 and A-584.
{ECO:0000269|PubMed:26711270}.
MUTAGEN 584 584 S->A: Greatly impairs in vitro
phosphorylation by CK2 and impairs cell
cycle regulation activity; when
associated with A-503, A-505, A-518, A-
572 and A-579.
{ECO:0000269|PubMed:26711270}.
CONFLICT 28 28 S -> P (in Ref. 2; AK225519).
{ECO:0000305}.
CONFLICT 319 319 F -> S (in Ref. 2; AK225519).
{ECO:0000305}.
CONFLICT 333 333 W -> R (in Ref. 2; AK225519).
{ECO:0000305}.
SEQUENCE 644 AA; 72758 MW; F9B0D2BBFDB38CAF CRC64;
MEETMKLATM EDTVEYCLFL IPDESRDSDK HKEILQKYIE RIITRFAPML VPYIWQNQPF
NLKYKPGKGG VPAHMFGVTK FGDNIEDEWF IVYVIKQITK EFPELVARIE DNDGEFLLIE
AADFLPKWLD PENSTNRVFF CHGELCIIPA PRKSGAESWL PTTPPTIPQA LNIITAHSEK
ILASESIRAA VNRRIRGYPE KIQASLHRAH CFLPAGIVAV LKQRPRLVAA AVQAFYLRDP
IDLRACRVFK TFLPETRIMT SVTFTKCLYA QLVQQRFVPD RRSGYRLPPP SDPQYRAHEL
GMKLAHGFEI LCSKCSPHFS DCKKSLVTAS PLWASFLESL KKNDYFKGLI EGSAQYRERL
EMAENYFQLS VDWPESSLAM SPGEEILTLL QTIPFDIEDL KKEAANLPPE DDDQWLDLSP
DQLDQLLQEA VGKKESESVS KEEKEQNYDL TEVSESMKAF ISKVSTHKGA ELPREPSEAP
ITFDADSFLN YFDKILGPRP NESDSDDLDD EDFECLDSDD DLDFETHEPG EEASLKGTLD
NLKSYMAQMD QELAHTCISK SFTTRNQVEP VSQTTDNNSD EEDSGTGESV MAPVDVDLNL
VSNILESYSS QAGLAGPASN LLQSMGVQLP DNTDHRPTSK PTKN


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