Q56B11 · PELP1_RAT
- ProteinProline-, glutamic acid- and leucine-rich protein 1
- GenePelp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1130 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
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. 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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | euchromatin | |
Cellular Component | MLL1 complex | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Molecular Function | chromatin binding | |
Molecular Function | SUMO binding | |
Biological Process | cellular response to estrogen stimulus | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | rRNA processing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProline-, glutamic acid- and leucine-rich protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ56B11
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mainly found in the nucleoplasm, with low levels detected in the cytoplasm. Also found associated with the plasma membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000252138 | 2-1130 | Proline-, glutamic acid- and leucine-rich protein 1 | |||
Sequence: AAAVLSGPTTGSPAGAPGGPGGLSAAGSGPRLRLLLLESVSGLLQPRTGSHVAPVHPPIQWAPYLPGLMCLLRLHGTAGGAQNLSALGALVNLSNAHLSSIKTRFEGLCLLSLLVGESPTELFQQHCVSWLRSIQQVLQSQDSPPTMELAVAILRDLLRYASQLPTLFRDISTNHLPGLLTSLLGLRPQCEQSALEGMKACVTYFPRACGFLKGKLASFFLSRLDSLNPQLQQLACECYSRLPSLGAGFSQGLKHTENWEQELHSLLTSLHSLLGSLFEETETAPVQSEGPGVEMLLSPSEDDNTHVLLQLWQRFSGLARCLGLMLSSEFGAPVSVPVQEILDLICRILGISSKNINLLGDGPLRLLLLPSLHLEALDLLSALILACGGRLLRFGALISRLLPQVLNTWSTGRDALAPGQERPYSTIRTKVYAILELWVQVCGASAGMLQGGASGEALLTHLLSDISPPADALKLCSTRGSSDGGLQSGKPSAPKKLKLDMGEALAPPSQRKGDRNADSDVCAAALRGLSRTILMCGPLVKEETHRRLHDLVLPLVMSVQQGEVLGSSPYNSSCCRLELYRLLLALLLAPSPRCPPPLSCALKAFSLGQWEDSLEVSSFCSEALVTCSALTHPRVPPLQSSGPACPTPAPVPPPEAPSSFRAPAFHTPGPMPSIGALPSPGPVPSAGPIPTVGSMSSAGSVPSTGPVPSRPGPPATANHLGLAVPGLVSVPPRLLPGSENHRAGSGEDPVLAPSGTPPPSIPPDETFGGRVPRPAFVHYDKEEASDVEISLESDSDDSVVIVPEGLPSLPPPPSGTPPPVAPIGPPTASPPVPAKEDSEELPATPGPLPPPPPPPPPVSGPVTLPPPQLVPEGTPGGGGPTAMEEDLTVININSSDEEEEEEEEEEEEDEDVEEEDFEEEEEDEEEYFEEEEEEEEFEEEFEEEEGELEEEEEEEEEELEEVEDVEFGSAGEVEEGGPPPPTLPPALPPTDSPKVQPEAEPEPGLLLEVEEPGAEDGPGPEIAPTLAPEVLPSQEEVEREGESPTAGPPQELVEEESSAPPTLLEEGTEGGGDKVPPPPETPAQEEMETETEASAPQGKEQDDTAAMLADFIDCPPDDEKPPPATEPDS | ||||||
Modified residue | 13 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 478 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 482 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 757 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 761 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1034 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1044 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in ovary, uterus, muscle and many regions of brain including hypothalamus, cortex, hippocampus and pituitary. Expressed in neurin and glia cells.
Interaction
Subunit
Interacts with HRS, RXRA, SUMO2, HDAC2, RB1 and STAT3. Interacts with PI3K, SRC and EGFR in cytoplasm. Interacts with ESR1, the interaction is enhanced by 17-beta-estradiol; the interaction increases ESR1 transcriptional activity (By similarity).
Interacts with CREBBP and EP300 in a ligand-dependent manner (By similarity).
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
Interacts with CREBBP and EP300 in a ligand-dependent manner (By similarity).
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
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MAAAVLSGPTTGSPAGAPGGPGGL | ||||||
Region | 2-80 | Required for modulation of ESR1 transcriptional activity | ||||
Sequence: AAAVLSGPTTGSPAGAPGGPGGLSAAGSGPRLRLLLLESVSGLLQPRTGSHVAPVHPPIQWAPYLPGLMCLLRLHGTAG | ||||||
Motif | 33-37 | LXXLL motif 1 | ||||
Sequence: LRLLL | ||||||
Motif | 69-73 | LXXLL motif 2 | ||||
Sequence: LMCLL | ||||||
Motif | 111-115 | LXXLL motif 3 | ||||
Sequence: LLSLL | ||||||
Region | 121-189 | Required for modulation of ESR1 transcriptional activity | ||||
Sequence: TELFQQHCVSWLRSIQQVLQSQDSPPTMELAVAILRDLLRYASQLPTLFRDISTNHLPGLLTSLLGLRP | ||||||
Motif | 155-159 | LXXLL motif 4 | ||||
Sequence: LRDLL | ||||||
Motif | 177-181 | LXXLL motif 5 | ||||
Sequence: LPGLL | ||||||
Motif | 264-268 | LXXLL motif 6 | ||||
Sequence: LHSLL | ||||||
Motif | 271-275 | LXXLL motif 7 | ||||
Sequence: LHSLL | ||||||
Motif | 365-369 | LXXLL motif 8 | ||||
Sequence: LRLLL | ||||||
Motif | 460-464 | LXXLL motif 9 | ||||
Sequence: LTHLL | ||||||
Motif | 580-584 | LXXLL motif 10 | ||||
Sequence: LYRLL | ||||||
Motif | 585-589 | LXXLL motif 11 | ||||
Sequence: LALLL | ||||||
Region | 639-773 | Disordered | ||||
Sequence: LQSSGPACPTPAPVPPPEAPSSFRAPAFHTPGPMPSIGALPSPGPVPSAGPIPTVGSMSSAGSVPSTGPVPSRPGPPATANHLGLAVPGLVSVPPRLLPGSENHRAGSGEDPVLAPSGTPPPSIPPDETFGGRVP | ||||||
Compositional bias | 640-660 | Pro residues | ||||
Sequence: QSSGPACPTPAPVPPPEAPSS | ||||||
Compositional bias | 674-688 | Pro residues | ||||
Sequence: SIGALPSPGPVPSAG | ||||||
Compositional bias | 691-705 | Polar residues | ||||
Sequence: PTVGSMSSAGSVPST | ||||||
Region | 785-1130 | Disordered | ||||
Sequence: ASDVEISLESDSDDSVVIVPEGLPSLPPPPSGTPPPVAPIGPPTASPPVPAKEDSEELPATPGPLPPPPPPPPPVSGPVTLPPPQLVPEGTPGGGGPTAMEEDLTVININSSDEEEEEEEEEEEEDEDVEEEDFEEEEEDEEEYFEEEEEEEEFEEEFEEEEGELEEEEEEEEEELEEVEDVEFGSAGEVEEGGPPPPTLPPALPPTDSPKVQPEAEPEPGLLLEVEEPGAEDGPGPEIAPTLAPEVLPSQEEVEREGESPTAGPPQELVEEESSAPPTLLEEGTEGGGDKVPPPPETPAQEEMETETEASAPQGKEQDDTAAMLADFIDCPPDDEKPPPATEPDS | ||||||
Compositional bias | 806-833 | Pro residues | ||||
Sequence: GLPSLPPPPSGTPPPVAPIGPPTASPPV | ||||||
Compositional bias | 844-874 | Pro residues | ||||
Sequence: ATPGPLPPPPPPPPPVSGPVTLPPPQLVPEG | ||||||
Compositional bias | 892-971 | Acidic residues | ||||
Sequence: NINSSDEEEEEEEEEEEEDEDVEEEDFEEEEEDEEEYFEEEEEEEEFEEEFEEEEGELEEEEEEEEEELEEVEDVEFGSA | ||||||
Compositional bias | 978-997 | Pro residues | ||||
Sequence: GPPPPTLPPALPPTDSPKVQ | ||||||
Compositional bias | 1114-1130 | Basic and acidic residues | ||||
Sequence: DCPPDDEKPPPATEPDS |
Domain
The Glu-rich region mediates histones interaction.
The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the association with nuclear receptor ESR1.
Sequence similarities
Belongs to the RIX1/PELP1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,130
- Mass (Da)119,139
- Last updated2005-05-24 v2
- ChecksumA5216F56C80D0BE8
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JSQ9 | A0A0G2JSQ9_RAT | Pelp1 | 1177 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 190 | in Ref. 2; AAI01891 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 519 | in Ref. 2; AAI01891 | ||||
Sequence: D → N | ||||||
Compositional bias | 640-660 | Pro residues | ||||
Sequence: QSSGPACPTPAPVPPPEAPSS | ||||||
Compositional bias | 674-688 | Pro residues | ||||
Sequence: SIGALPSPGPVPSAG | ||||||
Compositional bias | 691-705 | Polar residues | ||||
Sequence: PTVGSMSSAGSVPST | ||||||
Compositional bias | 806-833 | Pro residues | ||||
Sequence: GLPSLPPPPSGTPPPVAPIGPPTASPPV | ||||||
Sequence conflict | 824 | in Ref. 2; AAI01891 | ||||
Sequence: I → T | ||||||
Compositional bias | 844-874 | Pro residues | ||||
Sequence: ATPGPLPPPPPPPPPVSGPVTLPPPQLVPEG | ||||||
Compositional bias | 892-971 | Acidic residues | ||||
Sequence: NINSSDEEEEEEEEEEEEDEDVEEEDFEEEEEDEEEYFEEEEEEEEFEEEFEEEEGELEEEEEEEEEELEEVEDVEFGSA | ||||||
Sequence conflict | 913 | in Ref. 2; AAI01891 | ||||
Sequence: V → E | ||||||
Compositional bias | 978-997 | Pro residues | ||||
Sequence: GPPPPTLPPALPPTDSPKVQ | ||||||
Compositional bias | 1114-1130 | Basic and acidic residues | ||||
Sequence: DCPPDDEKPPPATEPDS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY970831 EMBL· GenBank· DDBJ | AAX81519.2 EMBL· GenBank· DDBJ | mRNA | ||
BC101890 EMBL· GenBank· DDBJ | AAI01891.1 EMBL· GenBank· DDBJ | mRNA |