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Protein

Proline-, glutamic acid- and leucine-rich protein 1

Gene

Pelp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. 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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, Repressor
Biological processTranscription

Names & Taxonomyi

Protein namesi
Recommended name:
Proline-, glutamic acid- and leucine-rich protein 1
Alternative name(s):
Modulator of non-genomic activity of estrogen receptor
Gene namesi
Name:Pelp1
Synonyms:Mnar
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1306320. Pelp1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002521382 – 1130Proline-, glutamic acid- and leucine-rich protein 1Add BLAST1129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei13PhosphoserineBy similarity1
Modified residuei478PhosphoserineBy similarity1
Modified residuei482PhosphoserineBy similarity1
Modified residuei757PhosphothreonineBy similarity1
Modified residuei761PhosphoserineBy similarity1
Modified residuei1034PhosphoserineBy similarity1
Modified residuei1044PhosphoserineBy similarity1

Post-translational modificationi

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.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ56B11.
PRIDEiQ56B11.

PTM databases

iPTMnetiQ56B11.
PhosphoSitePlusiQ56B11.

Expressioni

Tissue specificityi

Expressed in ovary, uterus, muscle and many regions of brain including hypothalamus, cortex, hippocampus and pituitary. Expressed in neurin and glia cells.1 Publication

Interactioni

Subunit structurei

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. 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

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ56B11. 3 interactors.
STRINGi10116.ENSRNOP00000026102.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi33 – 37LXXLL motif 15
Motifi69 – 73LXXLL motif 25
Motifi111 – 115LXXLL motif 35
Motifi155 – 159LXXLL motif 45
Motifi177 – 181LXXLL motif 55
Motifi264 – 268LXXLL motif 65
Motifi271 – 275LXXLL motif 75
Motifi365 – 369LXXLL motif 85
Motifi460 – 464LXXLL motif 95
Motifi580 – 584LXXLL motif 105
Motifi585 – 589LXXLL motif 115

Domaini

The Glu-rich region mediates histones interaction.By similarity
The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the association with nuclear receptor ESR1.By similarity

Sequence similaritiesi

Belongs to the RIX1/PELP1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IJ4S. Eukaryota.
ENOG4110K7C. LUCA.
HOGENOMiHOG000115494.
HOVERGENiHBG080634.
InParanoidiQ56B11.
KOiK16913.
PhylomeDBiQ56B11.
TreeFamiTF331332.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiView protein in InterPro
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR031193. PELP1.
IPR012583. RIX1_N.
IPR012980. Uncharacterised_NUC202.
PANTHERiPTHR45115. PTHR45115. 1 hit.
PfamiView protein in Pfam
PF08166. NUC202. 2 hits.
PF08167. RIX1. 1 hit.
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q56B11-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVLSGPT TGSPAGAPGG PGGLSAAGSG PRLRLLLLES VSGLLQPRTG
60 70 80 90 100
SHVAPVHPPI QWAPYLPGLM CLLRLHGTAG GAQNLSALGA LVNLSNAHLS
110 120 130 140 150
SIKTRFEGLC LLSLLVGESP TELFQQHCVS WLRSIQQVLQ SQDSPPTMEL
160 170 180 190 200
AVAILRDLLR YASQLPTLFR DISTNHLPGL LTSLLGLRPQ CEQSALEGMK
210 220 230 240 250
ACVTYFPRAC GFLKGKLASF FLSRLDSLNP QLQQLACECY SRLPSLGAGF
260 270 280 290 300
SQGLKHTENW EQELHSLLTS LHSLLGSLFE ETETAPVQSE GPGVEMLLSP
310 320 330 340 350
SEDDNTHVLL QLWQRFSGLA RCLGLMLSSE FGAPVSVPVQ EILDLICRIL
360 370 380 390 400
GISSKNINLL GDGPLRLLLL PSLHLEALDL LSALILACGG RLLRFGALIS
410 420 430 440 450
RLLPQVLNTW STGRDALAPG QERPYSTIRT KVYAILELWV QVCGASAGML
460 470 480 490 500
QGGASGEALL THLLSDISPP ADALKLCSTR GSSDGGLQSG KPSAPKKLKL
510 520 530 540 550
DMGEALAPPS QRKGDRNADS DVCAAALRGL SRTILMCGPL VKEETHRRLH
560 570 580 590 600
DLVLPLVMSV QQGEVLGSSP YNSSCCRLEL YRLLLALLLA PSPRCPPPLS
610 620 630 640 650
CALKAFSLGQ WEDSLEVSSF CSEALVTCSA LTHPRVPPLQ SSGPACPTPA
660 670 680 690 700
PVPPPEAPSS FRAPAFHTPG PMPSIGALPS PGPVPSAGPI PTVGSMSSAG
710 720 730 740 750
SVPSTGPVPS RPGPPATANH LGLAVPGLVS VPPRLLPGSE NHRAGSGEDP
760 770 780 790 800
VLAPSGTPPP SIPPDETFGG RVPRPAFVHY DKEEASDVEI SLESDSDDSV
810 820 830 840 850
VIVPEGLPSL PPPPSGTPPP VAPIGPPTAS PPVPAKEDSE ELPATPGPLP
860 870 880 890 900
PPPPPPPPVS GPVTLPPPQL VPEGTPGGGG PTAMEEDLTV ININSSDEEE
910 920 930 940 950
EEEEEEEEED EDVEEEDFEE EEEDEEEYFE EEEEEEEFEE EFEEEEGELE
960 970 980 990 1000
EEEEEEEEEL EEVEDVEFGS AGEVEEGGPP PPTLPPALPP TDSPKVQPEA
1010 1020 1030 1040 1050
EPEPGLLLEV EEPGAEDGPG PEIAPTLAPE VLPSQEEVER EGESPTAGPP
1060 1070 1080 1090 1100
QELVEEESSA PPTLLEEGTE GGGDKVPPPP ETPAQEEMET ETEASAPQGK
1110 1120 1130
EQDDTAAMLA DFIDCPPDDE KPPPATEPDS
Length:1,130
Mass (Da):119,139
Last modified:May 24, 2005 - v2
Checksum:iA5216F56C80D0BE8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti190Q → E in AAI01891 (PubMed:15489334).Curated1
Sequence conflicti519D → N in AAI01891 (PubMed:15489334).Curated1
Sequence conflicti824I → T in AAI01891 (PubMed:15489334).Curated1
Sequence conflicti913V → E in AAI01891 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY970831 mRNA. Translation: AAX81519.2.
BC101890 mRNA. Translation: AAI01891.1.
RefSeqiNP_001019441.2. NM_001024270.2.
UniGeneiRn.11628.

Genome annotation databases

GeneIDi360552.
KEGGirno:360552.
UCSCiRGD:1306320. rat.

Similar proteinsi

Entry informationi

Entry nameiPELP1_RAT
AccessioniPrimary (citable) accession number: Q56B11
Secondary accession number(s): Q3MIE2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 24, 2005
Last modified: November 22, 2017
This is version 89 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families