PELP1_HUMAN
ID PELP1_HUMAN Reviewed; 1130 AA.
AC Q8IZL8; O15450; Q5EGN3; Q6NTE6; Q96FT1; Q9BU60;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Proline-, glutamic acid- and leucine-rich protein 1;
DE AltName: Full=Modulator of non-genomic activity of estrogen receptor;
DE AltName: Full=Transcription factor HMX3;
GN Name=PELP1; Synonyms=HMX3, MNAR;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-356, FUNCTION, INTERACTION WITH ESR1;
RP CREBBP AND EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=11481323; DOI=10.1074/jbc.m103783200;
RA Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A.,
RA Kumar R.;
RT "Molecular cloning and characterization of PELP1, a novel human coregulator
RT of estrogen receptor alpha.";
RL J. Biol. Chem. 276:38272-38279(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-1130.
RA Lei W., Harrod K.S.;
RT "Human transcription factor HMX3.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP RETRACTED PAPER.
RX PubMed=12415108; DOI=10.1073/pnas.192569699;
RA Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
RT "Estrogen receptor-interacting protein that modulates its nongenomic
RT activity-crosstalk with Src/Erk phosphorylation cascade.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002).
RN [5]
RP RETRACTION NOTICE OF PUBMED:12415108.
RX PubMed=19666546; DOI=10.1073/pnas.0908685106;
RA Wong C.W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 106:14180-14180(2009).
RN [6]
RP FUNCTION, AND INTERACTION WITH RB1.
RX PubMed=12682072; DOI=10.1074/jbc.m212822200;
RA Balasenthil S., Vadlamudi R.K.;
RT "Functional interactions between the estrogen receptor coactivator
RT PELP1/MNAR and retinoblastoma protein.";
RL J. Biol. Chem. 278:22119-22127(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH ESR1 AND SRC.
RX PubMed=14963108; DOI=10.1210/me.2003-0335;
RA Barletta F., Wong C.-W., McNally C., Komm B.S., Katzenellenbogen B.,
RA Cheskis B.J.;
RT "Characterization of the interactions of estrogen receptor and MNAR in the
RT activation of cSrc.";
RL Mol. Endocrinol. 18:1096-1108(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH HISTONE H1 AND H3.
RX PubMed=15374949; DOI=10.1158/0008-5472.can-04-1786;
RA Nair S.S., Mishra S.K., Yang Z., Balasenthil S., Kumar R., Vadlamudi R.K.;
RT "Potential role of a novel transcriptional coactivator PELP1 in histone H1
RT displacement in cancer cells.";
RL Cancer Res. 64:6416-6423(2004).
RN [9]
RP FUNCTION, DOMAIN, AND INTERACTION WITH HDAC2.
RX PubMed=15456770; DOI=10.1074/jbc.m406831200;
RA Choi Y.B., Ko J.K., Shin J.;
RT "The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones
RT using two separate domains.";
RL J. Biol. Chem. 279:50930-50941(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15579769; DOI=10.1210/jc.2004-0909;
RA Vadlamudi R.K., Balasenthil S., Broaddus R.R., Gustafsson J.-A., Kumar R.;
RT "Deregulation of estrogen receptor coactivator proline-, glutamic acid-,
RT and leucine-rich protein-1/modulator of nongenomic activity of estrogen
RT receptor in human endometrial tumors.";
RL J. Clin. Endocrinol. Metab. 89:6130-6138(2004).
RN [11]
RP FUNCTION, INTERACTION WITH PI3K AND EGFR, AND SUBCELLULAR LOCATION.
RX PubMed=16140940; DOI=10.1158/0008-5472.can-05-0614;
RA Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z.,
RA Sahin A.A., Kumar R.;
RT "Functional implications of altered subcellular localization of PELP1 in
RT breast cancer cells.";
RL Cancer Res. 65:7724-7732(2005).
RN [12]
RP FUNCTION, AND INTERACTION WITH STAT3.
RX PubMed=15994929; DOI=10.1158/0008-5472.can-04-4664;
RA Manavathi B., Nair S.S., Wang R.-A., Kumar R., Vadlamudi R.K.;
RT "Proline-, glutamic acid-, and leucine-rich protein-1 is essential in
RT growth factor regulation of signal transducers and activators of
RT transcription 3 activation.";
RL Cancer Res. 65:5571-5577(2005).
RN [13]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY
RP 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 [15]
RP FUNCTION, AND INTERACTION WITH RXRA.
RX PubMed=16574651; DOI=10.1074/jbc.m601593200;
RA Singh R.R., Gururaj A.E., Vadlamudi R.K., Kumar R.;
RT "9-cis-retinoic acid up-regulates expression of transcriptional coregulator
RT PELP1, a novel coactivator of the retinoid X receptor alpha pathway.";
RL J. Biol. Chem. 281:15394-15404(2006).
RN [16]
RP FUNCTION, AND INTERACTION WITH HRS.
RX PubMed=16352611; DOI=10.1074/jbc.m510368200;
RA Rayala S.K., den Hollander P., Balasenthil S., Molli P.R., Bean A.J.,
RA Vadlamudi R.K., Wang R.-A., Kumar R.;
RT "Hepatocyte growth factor-regulated tyrosine kinase substrate (HRS)
RT interacts with PELP1 and activates MAPK.";
RL J. Biol. Chem. 281:4395-4403(2006).
RN [17]
RP INTERACTION WITH SUMO2.
RX PubMed=16567619; DOI=10.1073/pnas.0601066103;
RA Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y.,
RA Shi Y., Gill G.;
RT "NXP-2 association with SUMO-2 depends on lysines required for
RT transcriptional repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006).
RN [18]
RP INTERACTION WITH BCAS3.
RX PubMed=17505058; DOI=10.1210/me.2006-0514;
RA Gururaj A.E., Peng S., Vadlamudi R.K., Kumar R.;
RT "Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha
RT coactivator, through proline-, glutamic acid-, and leucine-rich protein-1
RT (PELP1).";
RL Mol. Endocrinol. 21:1847-1860(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481; THR-745 AND
RP SER-1043, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481 AND SER-1033,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [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 [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [24]
RP IDENTIFICATION IN THE PELP1 COMPLEX, SUBCELLULAR LOCATION, SUMOYLATION AT
RP LYS-826, AND MUTAGENESIS OF LYS-826.
RX PubMed=21326211; DOI=10.1038/emboj.2011.33;
RA Finkbeiner E., Haindl M., Muller S.;
RT "The SUMO system controls nucleolar partitioning of a novel mammalian
RT ribosome biogenesis complex.";
RL EMBO J. 30:1067-1078(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481; THR-488;
RP THR-745; SER-1033 AND SER-1043, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [26]
RP FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
RN [27]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-481 AND SER-1033,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND IDENTIFICATION BY
RP 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 [31]
RP SUMOYLATION, AND INTERACTION WITH MDN1.
RX PubMed=27814492; DOI=10.1016/j.molcel.2016.09.039;
RA Raman N., Weir E., Mueller S.;
RT "The AAA ATPase MDN1 acts as a SUMO-targeted regulator in mammalian pre-
RT ribosome remodeling.";
RL Mol. Cell 64:607-615(2016).
CC -!- FUNCTION: Coactivator of estrogen receptor-mediated transcription and a
CC corepressor of other nuclear hormone receptors and sequence-specific
CC transcription factors (PubMed:14963108). Plays a role in estrogen
CC receptor (ER) genomic activity when present in the nuclear compartment
CC by activating the ER target genes in a hormonal stimulation dependent
CC manner. Can facilitate ER non-genomic signaling via SRC and PI3K
CC interaction in the cytosol. Plays a role in E2-mediated cell cycle
CC progression by interacting with RB1. May have important functional
CC implications in ER/growth factor cross-talk. Interacts with several
CC growth factor signaling components including EGFR and HRS. Functions as
CC the key stabilizing component of the Five Friends of Methylated CHTOP
CC (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated
CC CHTOP, leading to desumoylation of ZNF148 and subsequent
CC transactivation of ZNF148 target genes. Component of the PELP1 complex
CC involved in the nucleolar steps of 28S rRNA maturation and the
CC subsequent nucleoplasmic transit of the pre-60S ribosomal subunit.
CC Regulates pre-60S association of the critical remodeling factor MDN1
CC (PubMed:21326211). May promote tumorigenesis via its interaction with
CC and modulation of several oncogenes including SRC, PI3K, STAT3 and
CC EGFR. Plays a role in cancer cell metastasis via its ability to
CC modulate E2-mediated cytoskeleton changes and cell migration via its
CC interaction with SRC and PI3K. {ECO:0000269|PubMed:11481323,
CC ECO:0000269|PubMed:12682072, ECO:0000269|PubMed:14963108,
CC ECO:0000269|PubMed:15374949, ECO:0000269|PubMed:15456770,
CC ECO:0000269|PubMed:15579769, ECO:0000269|PubMed:15994929,
CC ECO:0000269|PubMed:16140940, ECO:0000269|PubMed:16352611,
CC ECO:0000269|PubMed:16574651, ECO:0000269|PubMed:21326211,
CC ECO:0000269|PubMed:22872859}.
CC -!- SUBUNIT: Interacts with HRS, RXRA, SUMO2, HDAC2, RB1 and STAT3.
CC Interacts with PI3K, SRC and EGFR in cytoplasm. Interacts with ESR1,
CC the interaction is enhanced by 17-beta-; the interaction increases ESR1
CC transcriptional activity (PubMed:11481323, PubMed:14963108). Interacts
CC with CREBBP and EP300 in a ligand-dependent manner (PubMed:11481323).
CC Forms two complexes in the presence of 17-beta-estradiol; one with SRC
CC (via the SH3 domain) and ESR1 and another with LCK and ESR1
CC (PubMed:14963108). Interacts with histone H1 and H3 with a greater
CC affinity for H1. Component of some MLL1/MLL complex, at least composed
CC of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5,
CC as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
CC KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Core component of the 5FMC complex, at least composed of PELP1,
CC LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated
CC CHTOP and ZNF148. Interacts with NOL9. Interacts with BCAS3. Component
CC of the PELP1 complex, composed of at least PELP1, TEX10 and WDR18. The
CC complex interacts (via PELP1) with MDN1 (via its hexameric AAA ATPase
CC ring) and the pre-60S ribosome particles (PubMed:21326211,
CC PubMed:27814492). {ECO:0000269|PubMed:11481323,
CC ECO:0000269|PubMed:12682072, ECO:0000269|PubMed:14963108,
CC ECO:0000269|PubMed:15374949, ECO:0000269|PubMed:15456770,
CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:15994929,
CC ECO:0000269|PubMed:16140940, ECO:0000269|PubMed:16352611,
CC ECO:0000269|PubMed:16567619, ECO:0000269|PubMed:16574651,
CC ECO:0000269|PubMed:17505058, ECO:0000269|PubMed:21326211,
CC ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:27814492}.
CC -!- INTERACTION:
CC Q8IZL8; P84243: H3-3B; NbExp=11; IntAct=EBI-716449, EBI-120658;
CC Q8IZL8; O60341: KDM1A; NbExp=6; IntAct=EBI-716449, EBI-710124;
CC Q8IZL8; Q9NU22: MDN1; NbExp=3; IntAct=EBI-716449, EBI-1050480;
CC Q8IZL8; P19838: NFKB1; NbExp=2; IntAct=EBI-716449, EBI-300010;
CC Q8IZL8; P06748: NPM1; NbExp=3; IntAct=EBI-716449, EBI-78579;
CC Q8IZL8; Q9H4L4: SENP3; NbExp=5; IntAct=EBI-716449, EBI-2880236;
CC Q8IZL8; P61956: SUMO2; NbExp=4; IntAct=EBI-716449, EBI-473220;
CC Q8IZL8; Q9BV38: WDR18; NbExp=5; IntAct=EBI-716449, EBI-727429;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21326211}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:21326211}. Nucleus
CC {ECO:0000269|PubMed:11481323}. Cytoplasm {ECO:0000269|PubMed:11481323}.
CC Note=Mainly found in the nucleoplasm, with low levels detected in the
CC cytoplasm (By similarity). Also found associated with the plasma
CC membrane. Mainly in cytoplasm in a subset of breast tumors.
CC Localization is widely deregulated in endometrial cancers with
CC predominantly cytoplasm localization in high-grade endometrial tumors
CC (PubMed:16140940). {ECO:0000250|UniProtKB:Q9DBD5,
CC ECO:0000269|PubMed:16140940}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11481323}.
CC -!- DOMAIN: The Glu-rich region mediates histones interaction.
CC {ECO:0000269|PubMed:15456770}.
CC -!- DOMAIN: The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the
CC association with nuclear receptor ESR1. {ECO:0000269|PubMed:11481323}.
CC -!- PTM: Transiently sumoylated, preferentially conjugated to SUMO2 or
CC SUMO3. Sumoylation causes nucleolar exclusion of PELP1 and promotes the
CC recruitment of MDN1 to pre-60S particles. Desumoylation by SUMO
CC isopeptidase SENP3 is needed to release both PELP1 and MDN1 from pre-
CC ribosomes. {ECO:0000269|PubMed:21326211, ECO:0000269|PubMed:27814492}.
CC -!- MISCELLANEOUS: Expression is increased in breast tumor samples.
CC {ECO:0000269|PubMed:11481323}.
CC -!- SIMILARITY: Belongs to the RIX1/PELP1 family. {ECO:0000305}.
CC -!- CAUTION: There was previous evidence for interactions with AR, NR3C1
CC and ESR2. However this paper was retracted as cell-based data was
CC viewed as unreliable. {ECO:0000305|PubMed:12415108,
CC ECO:0000305|PubMed:19666546}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17708.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC17708.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF547989; AAN41255.1; -; mRNA.
DR EMBL; BC002875; AAH02875.2; -; mRNA.
DR EMBL; BC010457; AAH10457.2; -; mRNA.
DR EMBL; BC069058; AAH69058.1; -; mRNA.
DR EMBL; U88153; AAC17708.2; ALT_SEQ; mRNA.
DR EMBL; AY882602; AAW80659.1; -; mRNA.
DR CCDS; CCDS58503.2; -.
DR RefSeq; NP_001265170.1; NM_001278241.1.
DR RefSeq; NP_055204.3; NM_014389.2.
DR AlphaFoldDB; Q8IZL8; -.
DR BioGRID; 117973; 144.
DR CORUM; Q8IZL8; -.
DR ELM; Q8IZL8; -.
DR IntAct; Q8IZL8; 45.
DR MINT; Q8IZL8; -.
DR STRING; 9606.ENSP00000301396; -.
DR GlyGen; Q8IZL8; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q8IZL8; -.
DR MetOSite; Q8IZL8; -.
DR PhosphoSitePlus; Q8IZL8; -.
DR SwissPalm; Q8IZL8; -.
DR BioMuta; PELP1; -.
DR DMDM; 115502553; -.
DR CPTAC; CPTAC-1629; -.
DR EPD; Q8IZL8; -.
DR jPOST; Q8IZL8; -.
DR MassIVE; Q8IZL8; -.
DR MaxQB; Q8IZL8; -.
DR PaxDb; Q8IZL8; -.
DR PeptideAtlas; Q8IZL8; -.
DR PRIDE; Q8IZL8; -.
DR ProteomicsDB; 71367; -.
DR Antibodypedia; 23315; 286 antibodies from 33 providers.
DR DNASU; 27043; -.
DR Ensembl; ENST00000572293.7; ENSP00000460300.2; ENSG00000141456.16.
DR Ensembl; ENST00000574876.5; ENSP00000461625.1; ENSG00000141456.16.
DR GeneID; 27043; -.
DR KEGG; hsa:27043; -.
DR MANE-Select; ENST00000572293.7; ENSP00000460300.2; NM_014389.3; NP_055204.4.
DR UCSC; uc059zun.1; human.
DR CTD; 27043; -.
DR DisGeNET; 27043; -.
DR GeneCards; PELP1; -.
DR HGNC; HGNC:30134; PELP1.
DR HPA; ENSG00000141456; Low tissue specificity.
DR MIM; 609455; gene.
DR neXtProt; NX_Q8IZL8; -.
DR OpenTargets; ENSG00000141456; -.
DR PharmGKB; PA142671186; -.
DR VEuPathDB; HostDB:ENSG00000141456; -.
DR eggNOG; ENOG502QQE7; Eukaryota.
DR GeneTree; ENSGT00730000111225; -.
DR InParanoid; Q8IZL8; -.
DR OMA; GMKACMI; -.
DR OrthoDB; 427039at2759; -.
DR PhylomeDB; Q8IZL8; -.
DR PathwayCommons; Q8IZL8; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-8849473; PTK6 Expression.
DR SignaLink; Q8IZL8; -.
DR SIGNOR; Q8IZL8; -.
DR BioGRID-ORCS; 27043; 602 hits in 987 CRISPR screens.
DR ChiTaRS; PELP1; human.
DR GenomeRNAi; 27043; -.
DR Pharos; Q8IZL8; Tbio.
DR PRO; PR:Q8IZL8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IZL8; protein.
DR Bgee; ENSG00000141456; Expressed in tendon of biceps brachii and 206 other tissues.
DR ExpressionAtlas; Q8IZL8; baseline and differential.
DR Genevisible; Q8IZL8; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032183; F:SUMO binding; IMP:UniProtKB.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012583; RIX1_N.
DR InterPro; IPR012980; Uncharacterised_NUC202.
DR Pfam; PF08166; NUC202; 2.
DR Pfam; PF08167; RIX1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..1130
FT /note="Proline-, glutamic acid- and leucine-rich protein 1"
FT /id="PRO_0000252135"
FT REGION 2..80
FT /note="Required for modulation of ESR1 transcriptional
FT activity"
FT /evidence="ECO:0000269|PubMed:14963108"
FT REGION 121..189
FT /note="Required for modulation of ESR1 transcriptional
FT activity"
FT /evidence="ECO:0000269|PubMed:14963108"
FT REGION 473..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..37
FT /note="LXXLL motif 1"
FT MOTIF 69..73
FT /note="LXXLL motif 2"
FT MOTIF 111..115
FT /note="LXXLL motif 3"
FT MOTIF 155..159
FT /note="LXXLL motif 4"
FT MOTIF 177..181
FT /note="LXXLL motif 5"
FT MOTIF 264..268
FT /note="LXXLL motif 6"
FT MOTIF 271..275
FT /note="LXXLL motif 7"
FT MOTIF 364..368
FT /note="LXXLL motif 8"
FT MOTIF 459..463
FT /note="LXXLL motif 9"
FT MOTIF 579..583
FT /note="LXXLL motif 10"
FT MOTIF 584..588
FT /note="LXXLL motif 11"
FT COMPBIAS 639..701
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..968
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBD5"
FT MOD_RES 477
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 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 488
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 745
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 826
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:21326211"
FT VARIANT 1126
FT /note="T -> S (in dbSNP:rs9436)"
FT /id="VAR_027766"
FT MUTAGEN 826
FT /note="K->R: Not sumoylated."
FT /evidence="ECO:0000269|PubMed:21326211"
FT CONFLICT 2
FT /note="A -> V (in Ref. 2; AAC17708)"
FT /evidence="ECO:0000305"
SQ 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
