Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 142 (11 Dec 2019)
Sequence version 2 (17 Oct 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

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

Gene

Pelp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (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).By similarity1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Repressor
Biological processTranscription

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-6791226 Major pathway of rRNA processing in the nucleolus and cytosol

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Proline-, glutamic acid- and leucine-rich protein 1
Alternative name(s):
Modulator of non-genomic activity of estrogen receptor
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Pelp1
Synonyms:Mnar
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1922523 Pelp1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002521372 – 1123Proline-, glutamic acid- and leucine-rich protein 1Add BLAST1122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei13PhosphoserineCombined sources1
Modified residuei478PhosphoserineBy similarity1
Modified residuei482PhosphoserineBy similarity1
Modified residuei751PhosphothreonineBy similarity1
Modified residuei755PhosphoserineCombined sources1
Modified residuei1029PhosphoserineBy similarity1
Modified residuei1039PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9DBD5

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9DBD5

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9DBD5

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9DBD5

PeptideAtlas

More...
PeptideAtlasi
Q9DBD5

PRoteomics IDEntifications database

More...
PRIDEi
Q9DBD5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9DBD5

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9DBD5

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed with high levels in testis, ovary, uterus and pituitary gland.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000018921 Expressed in 274 organ(s), highest expression level in vestibular organ

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9DBD5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9DBD5 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 (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).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
P128133EBI-6909114,EBI-10896863

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
217350, 5 interactors

Protein interaction database and analysis system

More...
IntActi
Q9DBD5, 4 interactors

Molecular INTeraction database

More...
MINTi
Q9DBD5

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000019065

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9DBD5 protein

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>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

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi33 – 407Leu-richAdd BLAST375
Compositional biasi634 – 876Pro-richAdd BLAST243
Compositional biasi893 – 1094Glu-richAdd BLAST202
Compositional biasi974 – 1121Pro-richAdd BLAST148

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RIX1/PELP1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IJ4S Eukaryota
ENOG4110K7C LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00730000111225

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000115494

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9DBD5

KEGG Orthology (KO)

More...
KOi
K16913

Identification of Orthologs from Complete Genome Data

More...
OMAi
YRTLELW

Database of Orthologous Groups

More...
OrthoDBi
427039at2759

TreeFam database of animal gene trees

More...
TreeFami
TF331332

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016024 ARM-type_fold
IPR012583 RIX1_N
IPR012980 Uncharacterised_NUC202

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08166 NUC202, 2 hits
PF08167 RIX1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9DBD5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAAVLSGAS AGSPAGAPGG PGGLSAVGSG PRLRLLLLES ISGLLQPRTA
60 70 80 90 100
SPVAPVHPPI QWAPHLPGLM CLLRLHGTAG GAQNLSALGA LVNLSNAHLG
110 120 130 140 150
SIKTRFEGLC LLSLLIGESP TELFQQHCVS WLRSIQQVLQ SQDSPSTMEL
160 170 180 190 200
AVAVLRDLLR HASQLPTLFR DISTNHLPGL LTSLLGLRPE CEQSALEGMK
210 220 230 240 250
ACVTYFPRAC GSLKGKLASF FLSRLDSLNP QLQQLACECY SRLPSLGAGF
260 270 280 290 300
SQGLKHTENW EQELHSLLTS LHSLLGSLFE ETEPAPVQSE GPGIEMLLSH
310 320 330 340 350
SEDGNTHVLL QLRQRFSGLA RCLGLMLSSE FGAPVSVPVQ EILDLICRIL
360 370 380 390 400
GISSKNINLL GDGPLRLLLL PSLHLEALDL LSALILACGS RLLRFGALIS
410 420 430 440 450
RLLPQVLNAW STGRDTLAPG QERPYSTIRT KVYAILELWV QVCGASAGML
460 470 480 490 500
QGGASGEALL THLLSDISPP ADALKLCSTR GSSDGGLQSG KPSAPKKLKL
510 520 530 540 550
DMGEALAPPS QRKGDRNANS DVCAAALRGL SRTILMCGPL IKEETHRRLH
560 570 580 590 600
DLVLPLVMSV QQGEVLGSSP YNSSCCRLGL YRLLLALLLA PSPRCPPPLA
610 620 630 640 650
CALKAFSLGQ WEDSLEVSSF CSEALVTCAA LTHPRVPPLQ SSGPACPTPA
660 670 680 690 700
PVPPPEAPSS FRAPAFHPPG PMPSIGAVPS TGPLPSAGPI PTVGSMASTG
710 720 730 740 750
QVPSRPGPPA TANHLGLSVP GLVSVPPRLL PGPENHRAGS GEDPVLAPSG
760 770 780 790 800
TPPPSIPPDE TFGGRVPRPA FVHYDKEEAS DVEISLESDS DDSVVIVPEG
810 820 830 840 850
LPSLPPAPPS GTPPPAAPAG PPTASPPVPA KEDSEELPAT PGPPPPPPPP
860 870 880 890 900
PPPASGPVTL PPPQLVPEGT PGGGGPTAME EDLTVININS SDEEEEEEEE
910 920 930 940 950
EEEEDEDEEE EDFEEEEEDE EEYFEEEEEE EEFEEEFEEE EGELEEEEEE
960 970 980 990 1000
EEEELDEVED VEFGSAGEVE EGGPPPPTLP PALPPSDSPK VQPEAEPEPG
1010 1020 1030 1040 1050
LLLEVEEPGP EEVPGPETAP TLAPEVLPSQ EEGEQEVGSP AAGPPQELVE
1060 1070 1080 1090 1100
ESSAPPALLE EGTEGGGDKV PPPPETPAEE METEAEVPAP QEKEQDDTAA
1110 1120
MLADFIDCPP DDEKPPPATE PDS
Length:1,123
Mass (Da):118,069
Last modified:October 17, 2006 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i571BF1BD6A705067
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q9D4T3Q9D4T3_MOUSE
Proline-, glutamic acid- and leucin...
Pelp1
164Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti566L → P in AAH16444 (PubMed:15489334).Curated1
Sequence conflicti566L → P in AAH57987 (PubMed:15489334).Curated1
Sequence conflicti864Q → L in BAB23754 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK005027 mRNA Translation: BAB23754.1
AL596096 Genomic DNA No translation available.
BC016444 mRNA Translation: AAH16444.1
BC057987 mRNA Translation: AAH57987.1
BC090620 mRNA Translation: AAH90620.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS24945.1

NCBI Reference Sequences

More...
RefSeqi
NP_083507.3, NM_029231.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000019065; ENSMUSP00000019065; ENSMUSG00000018921

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
75273

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:75273

UCSC genome browser

More...
UCSCi
uc007jup.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005027 mRNA Translation: BAB23754.1
AL596096 Genomic DNA No translation available.
BC016444 mRNA Translation: AAH16444.1
BC057987 mRNA Translation: AAH57987.1
BC090620 mRNA Translation: AAH90620.1
CCDSiCCDS24945.1
RefSeqiNP_083507.3, NM_029231.4

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi217350, 5 interactors
IntActiQ9DBD5, 4 interactors
MINTiQ9DBD5
STRINGi10090.ENSMUSP00000019065

PTM databases

iPTMnetiQ9DBD5
PhosphoSitePlusiQ9DBD5

Proteomic databases

EPDiQ9DBD5
jPOSTiQ9DBD5
MaxQBiQ9DBD5
PaxDbiQ9DBD5
PeptideAtlasiQ9DBD5
PRIDEiQ9DBD5

Genome annotation databases

EnsembliENSMUST00000019065; ENSMUSP00000019065; ENSMUSG00000018921
GeneIDi75273
KEGGimmu:75273
UCSCiuc007jup.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
27043
MGIiMGI:1922523 Pelp1

Phylogenomic databases

eggNOGiENOG410IJ4S Eukaryota
ENOG4110K7C LUCA
GeneTreeiENSGT00730000111225
HOGENOMiHOG000115494
InParanoidiQ9DBD5
KOiK16913
OMAiYRTLELW
OrthoDBi427039at2759
TreeFamiTF331332

Enzyme and pathway databases

ReactomeiR-MMU-6791226 Major pathway of rRNA processing in the nucleolus and cytosol

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Pelp1 mouse

Protein Ontology

More...
PROi
PR:Q9DBD5
RNActiQ9DBD5 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000018921 Expressed in 274 organ(s), highest expression level in vestibular organ
ExpressionAtlasiQ9DBD5 baseline and differential
GenevisibleiQ9DBD5 MM

Family and domain databases

InterProiView protein in InterPro
IPR016024 ARM-type_fold
IPR012583 RIX1_N
IPR012980 Uncharacterised_NUC202
PfamiView protein in Pfam
PF08166 NUC202, 2 hits
PF08167 RIX1, 1 hit
SUPFAMiSSF48371 SSF48371, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPELP1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9DBD5
Secondary accession number(s): Q5F2E2, Q6PEM0, Q91YM9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: December 11, 2019
This is version 142 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again