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

 PELP1_MOUSE             Reviewed;        1123 AA.
Q9DBD5; Q5F2E2; Q6PEM0; Q91YM9;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
28-MAR-2018, entry version 133.
RecName: Full=Proline-, glutamic acid- and leucine-rich protein 1;
AltName: Full=Modulator of non-genomic activity of estrogen receptor;
Name=Pelp1; Synonyms=Mnar;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N;
TISSUE=Embryonic brain, Liver, and Mammary gland;
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).
[4]
TISSUE SPECIFICITY.
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, INTERACTION OF THE 5FMC
COMPLEX WITH CHTOP AND ZNF148, INTERACTION WITH NOL9, 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).
-!- 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 (By similarity). 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
(PubMed:22872859). Component of the PELP1 complex involved in the
nucleolar steps of 28S rRNA maturation and the subsequent
nucleoplasmic transit of the pre-60S ribosomal subunit. Regulates
pre-60S association of the critical remodeling factor MDN1 (By
similarity). {ECO:0000250|UniProtKB:Q8IZL8,
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 (By similarity). 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 (PubMed:22872859). Interacts with BCAS3 (By
similarity). Component of the PELP1 complex, composed of at least
PELP1, TEX10 and WDR18. The complex interacts (via PELP1) with
MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome
particles (By similarity). {ECO:0000250|UniProtKB:Q8IZL8,
ECO:0000269|PubMed:22872859}.
-!- INTERACTION:
P12813:Nr4a1; NbExp=3; IntAct=EBI-6909114, EBI-10896863;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q8IZL8}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:22872859}. Nucleus
{ECO:0000269|PubMed:22872859}. Cytoplasm
{ECO:0000269|PubMed:22872859}. Note=Mainly found in the
nucleoplasm, with low levels detected in the cytoplasm. Also found
associated with the plasma membrane.
{ECO:0000269|PubMed:22872859}.
-!- TISSUE SPECIFICITY: Widely expressed with high levels in testis,
ovary, uterus and pituitary gland. {ECO:0000269|PubMed:11481323}.
-!- DOMAIN: The Glu-rich region mediates histones interaction.
{ECO:0000250}.
-!- DOMAIN: The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for
the association with nuclear receptor ESR1. {ECO:0000250}.
-!- PTM: Transiently sumoylated, preferentially conjugated to SUMO2 or
SUMO3. Sumoylation causes nucleolar exclusion of PELP1 and
promotes the recruitment of MDN1 to pre-60S particles.
Desumoylation by SUMO isopeptidase SENP3 is needed to release both
PELP1 and MDN1 from pre-ribosomes. {ECO:0000250|UniProtKB:Q8IZL8}.
-!- SIMILARITY: Belongs to the RIX1/PELP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK005027; BAB23754.1; -; mRNA.
EMBL; AL596096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC016444; AAH16444.1; -; mRNA.
EMBL; BC057987; AAH57987.1; -; mRNA.
EMBL; BC090620; AAH90620.1; -; mRNA.
CCDS; CCDS24945.1; -.
RefSeq; NP_083507.3; NM_029231.4.
UniGene; Mm.340601; -.
ProteinModelPortal; Q9DBD5; -.
BioGrid; 217350; 5.
IntAct; Q9DBD5; 4.
MINT; Q9DBD5; -.
STRING; 10090.ENSMUSP00000019065; -.
iPTMnet; Q9DBD5; -.
PhosphoSitePlus; Q9DBD5; -.
EPD; Q9DBD5; -.
MaxQB; Q9DBD5; -.
PaxDb; Q9DBD5; -.
PeptideAtlas; Q9DBD5; -.
PRIDE; Q9DBD5; -.
Ensembl; ENSMUST00000019065; ENSMUSP00000019065; ENSMUSG00000018921.
GeneID; 75273; -.
KEGG; mmu:75273; -.
UCSC; uc007jup.2; mouse.
CTD; 27043; -.
MGI; MGI:1922523; Pelp1.
eggNOG; ENOG410IJ4S; Eukaryota.
eggNOG; ENOG4110K7C; LUCA.
GeneTree; ENSGT00730000111225; -.
HOGENOM; HOG000115494; -.
HOVERGEN; HBG080634; -.
InParanoid; Q9DBD5; -.
KO; K16913; -.
OMA; ACECYSR; -.
OrthoDB; EOG091G039A; -.
TreeFam; TF331332; -.
Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; Pelp1; mouse.
PRO; PR:Q9DBD5; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018921; -.
CleanEx; MM_PELP1; -.
ExpressionAtlas; Q9DBD5; baseline and differential.
Genevisible; Q9DBD5; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0035327; C:transcriptionally active chromatin; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR031193; PELP1.
InterPro; IPR012583; RIX1_N.
InterPro; IPR012980; Uncharacterised_NUC202.
PANTHER; PTHR45115; PTHR45115; 1.
Pfam; PF08166; NUC202; 2.
Pfam; PF08167; RIX1; 1.
SUPFAM; SSF48371; SSF48371; 3.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Cytoplasm; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19131326}.
CHAIN 2 1123 Proline-, glutamic acid- and leucine-rich
protein 1.
/FTId=PRO_0000252137.
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 365 369 LXXLL motif 8.
MOTIF 460 464 LXXLL motif 9.
MOTIF 580 584 LXXLL motif 10.
MOTIF 585 589 LXXLL motif 11.
COMPBIAS 33 407 Leu-rich.
COMPBIAS 634 876 Pro-rich.
COMPBIAS 893 1094 Glu-rich.
COMPBIAS 974 1121 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 751 751 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 1039 1039 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZL8}.
CONFLICT 566 566 L -> P (in Ref. 3; AAH16444/AAH57987).
{ECO:0000305}.
CONFLICT 864 864 Q -> L (in Ref. 1; BAB23754).
{ECO:0000305}.
SEQUENCE 1123 AA; 118069 MW; 571BF1BD6A705067 CRC64;
MAAAVLSGAS AGSPAGAPGG PGGLSAVGSG PRLRLLLLES ISGLLQPRTA SPVAPVHPPI
QWAPHLPGLM CLLRLHGTAG GAQNLSALGA LVNLSNAHLG SIKTRFEGLC LLSLLIGESP
TELFQQHCVS WLRSIQQVLQ SQDSPSTMEL AVAVLRDLLR HASQLPTLFR DISTNHLPGL
LTSLLGLRPE CEQSALEGMK ACVTYFPRAC GSLKGKLASF FLSRLDSLNP QLQQLACECY
SRLPSLGAGF SQGLKHTENW EQELHSLLTS LHSLLGSLFE ETEPAPVQSE GPGIEMLLSH
SEDGNTHVLL QLRQRFSGLA RCLGLMLSSE FGAPVSVPVQ EILDLICRIL GISSKNINLL
GDGPLRLLLL PSLHLEALDL LSALILACGS RLLRFGALIS RLLPQVLNAW STGRDTLAPG
QERPYSTIRT KVYAILELWV QVCGASAGML QGGASGEALL THLLSDISPP ADALKLCSTR
GSSDGGLQSG KPSAPKKLKL DMGEALAPPS QRKGDRNANS DVCAAALRGL SRTILMCGPL
IKEETHRRLH DLVLPLVMSV QQGEVLGSSP YNSSCCRLGL YRLLLALLLA PSPRCPPPLA
CALKAFSLGQ WEDSLEVSSF CSEALVTCAA LTHPRVPPLQ SSGPACPTPA PVPPPEAPSS
FRAPAFHPPG PMPSIGAVPS TGPLPSAGPI PTVGSMASTG QVPSRPGPPA TANHLGLSVP
GLVSVPPRLL PGPENHRAGS GEDPVLAPSG TPPPSIPPDE TFGGRVPRPA FVHYDKEEAS
DVEISLESDS DDSVVIVPEG LPSLPPAPPS GTPPPAAPAG PPTASPPVPA KEDSEELPAT
PGPPPPPPPP PPPASGPVTL PPPQLVPEGT PGGGGPTAME EDLTVININS SDEEEEEEEE
EEEEDEDEEE EDFEEEEEDE EEYFEEEEEE EEFEEEFEEE EGELEEEEEE EEEELDEVED
VEFGSAGEVE EGGPPPPTLP PALPPSDSPK VQPEAEPEPG LLLEVEEPGP EEVPGPETAP
TLAPEVLPSQ EEGEQEVGSP AAGPPQELVE ESSAPPALLE EGTEGGGDKV PPPPETPAEE
METEAEVPAP QEKEQDDTAA MLADFIDCPP DDEKPPPATE PDS


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