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Proline-, glutamic acid- and leucine-rich protein 1 (Modulator of non-genomic activity of estrogen receptor) (Transcription factor HMX3)

 PELP1_HUMAN             Reviewed;        1130 AA.
Q8IZL8; O15450; Q5EGN3; Q6NTE6; Q96FT1; Q9BU60;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 2.
30-AUG-2017, entry version 132.
RecName: Full=Proline-, glutamic acid- and leucine-rich protein 1;
AltName: Full=Modulator of non-genomic activity of estrogen receptor;
AltName: Full=Transcription factor HMX3;
Name=PELP1; Synonyms=HMX3, MNAR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH ESR1; ESR2;
AR; NR3C1 AND SRC.
PubMed=12415108; DOI=10.1073/pnas.192569699;
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
"Estrogen receptor-interacting protein that modulates its nongenomic
activity-crosstalk with Src/Erk phosphorylation cascade.";
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Lung, and Testis;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-356, FUNCTION, INTERACTION WITH ESR1;
CREBBP AND EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
DOMAIN.
PubMed=11481323; DOI=10.1074/jbc.M103783200;
Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A.,
Kumar R.;
"Molecular cloning and characterization of PELP1, a novel human
coregulator of estrogen receptor alpha.";
J. Biol. Chem. 276:38272-38279(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 70-1130.
Lei W., Harrod K.S.;
"Human transcription factor HMX3.";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND INTERACTION WITH RB1.
PubMed=12682072; DOI=10.1074/jbc.M212822200;
Balasenthil S., Vadlamudi R.K.;
"Functional interactions between the estrogen receptor coactivator
PELP1/MNAR and retinoblastoma protein.";
J. Biol. Chem. 278:22119-22127(2003).
[6]
FUNCTION, AND INTERACTION WITH ESR1 AND SRC.
PubMed=14963108; DOI=10.1210/me.2003-0335;
Barletta F., Wong C.-W., McNally C., Komm B.S., Katzenellenbogen B.,
Cheskis B.J.;
"Characterization of the interactions of estrogen receptor and MNAR in
the activation of cSrc.";
Mol. Endocrinol. 18:1096-1108(2004).
[7]
FUNCTION, AND INTERACTION WITH HISTONE H1 AND H3.
PubMed=15374949; DOI=10.1158/0008-5472.CAN-04-1786;
Nair S.S., Mishra S.K., Yang Z., Balasenthil S., Kumar R.,
Vadlamudi R.K.;
"Potential role of a novel transcriptional coactivator PELP1 in
histone H1 displacement in cancer cells.";
Cancer Res. 64:6416-6423(2004).
[8]
FUNCTION, DOMAIN, AND INTERACTION WITH HDAC2.
PubMed=15456770; DOI=10.1074/jbc.M406831200;
Choi Y.B., Ko J.K., Shin J.;
"The transcriptional corepressor, PELP1, recruits HDAC2 and masks
histones using two separate domains.";
J. Biol. Chem. 279:50930-50941(2004).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15579769; DOI=10.1210/jc.2004-0909;
Vadlamudi R.K., Balasenthil S., Broaddus R.R., Gustafsson J.-A.,
Kumar R.;
"Deregulation of estrogen receptor coactivator proline-, glutamic
acid-, and leucine-rich protein-1/modulator of nongenomic activity of
estrogen receptor in human endometrial tumors.";
J. Clin. Endocrinol. Metab. 89:6130-6138(2004).
[10]
FUNCTION, INTERACTION WITH PI3K AND EGFR, AND SUBCELLULAR LOCATION.
PubMed=16140940; DOI=10.1158/0008-5472.CAN-05-0614;
Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z.,
Sahin A.A., Kumar R.;
"Functional implications of altered subcellular localization of PELP1
in breast cancer cells.";
Cancer Res. 65:7724-7732(2005).
[11]
FUNCTION, AND INTERACTION WITH STAT3.
PubMed=15994929; DOI=10.1158/0008-5472.CAN-04-4664;
Manavathi B., Nair S.S., Wang R.-A., Kumar R., Vadlamudi R.K.;
"Proline-, glutamic acid-, and leucine-rich protein-1 is essential in
growth factor regulation of signal transducers and activators of
transcription 3 activation.";
Cancer Res. 65:5571-5577(2005).
[12]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, 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).
[14]
FUNCTION, AND INTERACTION WITH RXRA.
PubMed=16574651; DOI=10.1074/jbc.M601593200;
Singh R.R., Gururaj A.E., Vadlamudi R.K., Kumar R.;
"9-cis-retinoic acid up-regulates expression of transcriptional
coregulator PELP1, a novel coactivator of the retinoid X receptor
alpha pathway.";
J. Biol. Chem. 281:15394-15404(2006).
[15]
FUNCTION, AND INTERACTION WITH HRS.
PubMed=16352611; DOI=10.1074/jbc.M510368200;
Rayala S.K., den Hollander P., Balasenthil S., Molli P.R., Bean A.J.,
Vadlamudi R.K., Wang R.-A., Kumar R.;
"Hepatocyte growth factor-regulated tyrosine kinase substrate (HRS)
interacts with PELP1 and activates MAPK.";
J. Biol. Chem. 281:4395-4403(2006).
[16]
INTERACTION WITH SUMO2.
PubMed=16567619; DOI=10.1073/pnas.0601066103;
Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A.,
Shi Y., Shi Y., Gill G.;
"NXP-2 association with SUMO-2 depends on lysines required for
transcriptional repression.";
Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006).
[17]
INTERACTION WITH BCAS3.
PubMed=17505058; DOI=10.1210/me.2006-0514;
Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
"Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
coactivator, through proline-, glutamic acid-, and leucine-rich
protein-1 (PELP1).";
Mol. Endocrinol. 21:1847-1860(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481; THR-745
AND SER-1043, 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).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481 AND
SER-1033, 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).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481; THR-488;
THR-745; SER-1033 AND SER-1043, 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).
[24]
FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=22872859; DOI=10.1074/mcp.M112.017194;
Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S.,
van Dijk T.B.;
"Five friends of methylated chromatin target of protein-arginine-
methyltransferase[prmt]-1 (chtop), a complex linking arginine
methylation to desumoylation.";
Mol. Cell. Proteomics 11:1263-1273(2012).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481 AND
SER-1033, 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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND 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).
-!- FUNCTION: Coactivator of estrogen receptor-mediated transcription
and a corepressor of other nuclear hormone receptors and sequence-
specific transcription factors. Plays a role in estrogen receptor
(ER) genomic activity when present in the nuclear compartment by
activating the ER target genes in a hormonal stimulation dependent
manner. Can facilitate ER non-genomic signaling via SRC and PI3K
interaction in the cytosol. Plays a role in E2-mediated cell cycle
progression by interacting with RB1. May have important functional
implications in ER/growth factor cross-talk. Interacts with
several growth factor signaling components including EGFR and HRS.
Involved in nuclear receptor signaling via its interaction with AR
and NR3C1. May promote tumorigenesis via its interaction with and
modulation of several oncogenes including SRC, PI3K, STAT3 and
EGFR. Plays a role in cancer cell metastasis via its ability to
modulate E2-mediated cytoskeleton changes and cell migration via
its interaction with SRC and PI3K. Functions as the key
stabilizing component of the Five Friends of Methylated CHTOP
(5FMC) complex; the 5FMC complex is recruited to ZNF148 by
methylated CHTOP, leading to desumoylation of ZNF148 and
subsequent transactivation of ZNF148 target genes.
{ECO:0000269|PubMed:11481323, ECO:0000269|PubMed:12415108,
ECO:0000269|PubMed:12682072, ECO:0000269|PubMed:14963108,
ECO:0000269|PubMed:15374949, ECO:0000269|PubMed:15456770,
ECO:0000269|PubMed:15579769, ECO:0000269|PubMed:15994929,
ECO:0000269|PubMed:16140940, ECO:0000269|PubMed:16352611,
ECO:0000269|PubMed:16574651, ECO:0000269|PubMed:22872859}.
-!- SUBUNIT: Interacts with HRS, RXRA, SUMO2, HDAC2, RB1 and STAT3.
Interacts with PI3K, SRC and EGFR in cytoplasm. Interacts with
ESR1 and ESR2 and this interaction is enhanced by 17-beta-
estradiol. Interacts with CREBBP, EP300, AR and NR3C1 in a ligand-
dependent manner. Forms two complexes in the presence of 17-beta-
estradiol; one with SRC and ESR1 and another with LCK and ESR1.
Interacts with histone H1 and H3 with a greater affinity for H1.
Component of some MLL1/MLL complex, at least composed of the core
components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well
as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31,
RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7,
TAF9 and TEX10. Core component of the 5FMC complex, at least
composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex
interacts with methylated CHTOP and ZNF148. Interacts with NOL9.
Interacts with BCAS3. {ECO:0000269|PubMed:11481323,
ECO:0000269|PubMed:12415108, ECO:0000269|PubMed:12682072,
ECO:0000269|PubMed:14963108, ECO:0000269|PubMed:15374949,
ECO:0000269|PubMed:15456770, ECO:0000269|PubMed:15960975,
ECO:0000269|PubMed:15994929, ECO:0000269|PubMed:16140940,
ECO:0000269|PubMed:16352611, ECO:0000269|PubMed:16567619,
ECO:0000269|PubMed:16574651, ECO:0000269|PubMed:17505058,
ECO:0000269|PubMed:22872859}.
-!- INTERACTION:
P84243:H3F3B; NbExp=11; IntAct=EBI-716449, EBI-120658;
O60341:KDM1A; NbExp=6; IntAct=EBI-716449, EBI-710124;
Q9NU22:MDN1; NbExp=3; IntAct=EBI-716449, EBI-1050480;
P19838:NFKB1; NbExp=2; IntAct=EBI-716449, EBI-300010;
P06748:NPM1; NbExp=3; IntAct=EBI-716449, EBI-78579;
Q9H4L4:SENP3; NbExp=5; IntAct=EBI-716449, EBI-2880236;
P61956:SUMO2; NbExp=4; IntAct=EBI-716449, EBI-473220;
Q9BV38:WDR18; NbExp=3; IntAct=EBI-716449, EBI-727429;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus.
Cytoplasm. Note=Mainly found in the nucleoplasm, with low levels
detected in the cytoplasm (By similarity). Also found associated
with the plasma membrane. Mainly in cytoplasm in a subset of
breast tumors. Localization is widely deregulated in endometrial
cancers with predominantly cytoplasm localization in high-grade
endometrial tumors. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:11481323}.
-!- DOMAIN: The Glu-rich region mediates histones interaction.
-!- DOMAIN: The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for
the association with nuclear receptor ESR1.
-!- SEQUENCE CAUTION:
Sequence=AAC17708.2; Type=Frameshift; Positions=656, 672; Evidence={ECO:0000305};
Sequence=AAC17708.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AF547989; AAN41255.1; -; mRNA.
EMBL; BC002875; AAH02875.2; -; mRNA.
EMBL; BC010457; AAH10457.2; -; mRNA.
EMBL; BC069058; AAH69058.1; -; mRNA.
EMBL; U88153; AAC17708.2; ALT_SEQ; mRNA.
EMBL; AY882602; AAW80659.1; -; mRNA.
RefSeq; NP_001265170.1; NM_001278241.1.
RefSeq; NP_055204.3; NM_014389.2.
UniGene; Hs.744899; -.
ProteinModelPortal; Q8IZL8; -.
BioGrid; 117973; 66.
ELM; Q8IZL8; -.
IntAct; Q8IZL8; 28.
MINT; MINT-1185355; -.
STRING; 9606.ENSP00000301396; -.
iPTMnet; Q8IZL8; -.
PhosphoSitePlus; Q8IZL8; -.
SwissPalm; Q8IZL8; -.
BioMuta; PELP1; -.
DMDM; 115502553; -.
EPD; Q8IZL8; -.
MaxQB; Q8IZL8; -.
PaxDb; Q8IZL8; -.
PeptideAtlas; Q8IZL8; -.
PRIDE; Q8IZL8; -.
Ensembl; ENST00000574876; ENSP00000461625; ENSG00000141456.
GeneID; 27043; -.
KEGG; hsa:27043; -.
UCSC; uc059zun.1; human.
CTD; 27043; -.
DisGeNET; 27043; -.
GeneCards; PELP1; -.
HGNC; HGNC:30134; PELP1.
HPA; HPA053966; -.
HPA; HPA056028; -.
HPA; HPA060760; -.
MIM; 609455; gene.
neXtProt; NX_Q8IZL8; -.
OpenTargets; ENSG00000141456; -.
PharmGKB; PA142671186; -.
eggNOG; ENOG410IJ4S; Eukaryota.
eggNOG; ENOG4110K7C; LUCA.
GeneTree; ENSGT00730000111225; -.
HOVERGEN; HBG080634; -.
InParanoid; Q8IZL8; -.
KO; K16913; -.
PhylomeDB; Q8IZL8; -.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-8849473; PTK6 Expression.
SIGNOR; Q8IZL8; -.
ChiTaRS; PELP1; human.
GenomeRNAi; 27043; -.
PRO; PR:Q8IZL8; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141456; -.
CleanEx; HS_HMX3; -.
CleanEx; HS_PELP1; -.
ExpressionAtlas; Q8IZL8; baseline and differential.
Genevisible; Q8IZL8; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR031193; PELP1.
InterPro; IPR012583; RIX1_N.
InterPro; IPR012980; Uncharacterised_NUC202.
PANTHER; PTHR24023:SF624; PTHR24023:SF624; 1.
Pfam; PF08166; NUC202; 2.
Pfam; PF08167; RIX1; 1.
SUPFAM; SSF48371; SSF48371; 4.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Cytoplasm; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
Transcription.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 1130 Proline-, glutamic acid- and leucine-rich
protein 1.
/FTId=PRO_0000252135.
MOTIF 33 37 LXXLL motif 1.
MOTIF 69 73 LXXLL motif 2.
MOTIF 111 115 LXXLL motif 3.
MOTIF 155 159 LXXLL motif 4.
MOTIF 177 181 LXXLL motif 5.
MOTIF 264 268 LXXLL motif 6.
MOTIF 271 275 LXXLL motif 7.
MOTIF 364 368 LXXLL motif 8.
MOTIF 459 463 LXXLL motif 9.
MOTIF 579 583 LXXLL motif 10.
MOTIF 584 588 LXXLL motif 11.
COMPBIAS 633 872 Pro-rich.
COMPBIAS 888 1101 Glu-rich.
COMPBIAS 977 1083 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:Q9DBD5}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 488 488 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 745 745 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1033 1033 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1043 1043 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
VARIANT 1126 1126 T -> S (in dbSNP:rs9436).
/FTId=VAR_027766.
CONFLICT 2 2 A -> V (in Ref. 3; AAC17708).
{ECO:0000305}.
CONFLICT 896 896 E -> G (in Ref. 1; AAN41255).
{ECO:0000305}.
CONFLICT 1069 1069 T -> P (in Ref. 1; AAN41255).
{ECO:0000305}.
SEQUENCE 1130 AA; 119700 MW; 7B0DEE7A198DA9A6 CRC64;
MAAAVLSGPS AGSAAGVPGG TGGLSAVSSG PRLRLLLLES VSGLLQPRTG SAVAPVHPPN
RSAPHLPGLM CLLRLHGSVG GAQNLSALGA LVSLSNARLS SIKTRFEGLC LLSLLVGESP
TELFQQHCVS WLRSIQQVLQ TQDPPATMEL AVAVLRDLLR YAAQLPALFR DISMNHLPGL
LTSLLGLRPE CEQSALEGMK ACMTYFPRAC GSLKGKLASF FLSRVDALSP QLQQLACECY
SRLPSLGAGF SQGLKHTESW EQELHSLLAS LHTLLGALYE GAETAPVQNE GPGVEMLLSS
EDGDAHVLLQ LRQRFSGLAR CLGLMLSSEF GAPVSVPVQE ILDFICRTLS VSSKNISLHG
DGPLRLLLLP SIHLEALDLL SALILACGSR LLRFGILIGR LLPQVLNSWS IGRDSLSPGQ
ERPYSTVRTK VYAILELWVQ VCGASAGMLQ GGASGEALLT HLLSDISPPA DALKLRSPRG
SPDGSLQTGK PSAPKKLKLD VGEAMAPPSH RKGDSNANSD VCAAALRGLS RTILMCGPLI
KEETHRRLHD LVLPLVMGVQ QGEVLGSSPY TSSRCRRELY CLLLALLLAP SPRCPPPLAC
ALQAFSLGQR EDSLEVSSFC SEALVTCAAL THPRVPPLQP MGPTCPTPAP VPPPEAPSPF
RAPPFHPPGP MPSVGSMPSA GPMPSAGPMP SAGPVPSARP GPPTTANHLG LSVPGLVSVP
PRLLPGPENH RAGSNEDPIL APSGTPPPTI PPDETFGGRV PRPAFVHYDK EEASDVEISL
ESDSDDSVVI VPEGLPPLPP PPPSGATPPP IAPTGPPTAS PPVPAKEEPE ELPAAPGPLP
PPPPPPPPVP GPVTLPPPQL VPEGTPGGGG PPALEEDLTV ININSSDEEE EEEEEEEEEE
EEEEEEEEDF EEEEEDEEEY FEEEEEEEEE FEEEFEEEEG ELEEEEEEED EEEEEELEEV
EDLEFGTAGG EVEEGAPPPP TLPPALPPPE SPPKVQPEPE PEPGLLLEVE EPGTEEERGA
DTAPTLAPEA LPSQGEVERE GESPAAGPPP QELVEEEPSA PPTLLEEETE DGSDKVQPPP
ETPAEEEMET ETEAEALQEK EQDDTAAMLA DFIDCPPDDE KPPPPTEPDS


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