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UniProtKB - P20263 (PO5F1_MOUSE)

Entry version 189 (16 Oct 2019)
Sequence version 1 (01 Feb 1991)
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Protein

POU domain, class 5, transcription factor 1

Gene

Pou5f1

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

Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') (PubMed:1972777, PubMed:1690859, PubMed:1967980, PubMed:17525163, PubMed:23376973). Forms a trimeric complex with SOX2 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (PubMed:17097055, PubMed:17496161, PubMed:19740739). Critical for early embryogenesis and for embryonic stem cell pluripotency (PubMed:1972777, PubMed:1690859, PubMed:17496161, PubMed:18662995, PubMed:19740739, PubMed:29153991, PubMed:23376973).10 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei150DNACombined sources1 Publication1
Binding sitei157DNACombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi223 – 282HomeoboxPROSITE-ProRule annotation1 PublicationAdd BLAST60

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionDevelopmental protein, DNA-binding
Biological processTranscription, Transcription regulation

<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:
POU domain, class 5, transcription factor 1
Alternative name(s):
NF-A3
Octamer-binding protein 3
Short name:
Oct-3
Octamer-binding protein 4
Short name:
Oct-4
Octamer-binding transcription factor 3
Short name:
OTF-3
<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:Pou5f1
Synonyms:Oct-3, Oct-4, Otf-3, Otf3
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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 17

Organism-specific databases

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

More...MGIi		MGI:101893 Pou5f1

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi118K → R: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 70% lower expression of YES1. Reduced DNA binding. No change in nuclear location. No change in nuclear localization. Absence of sumoylation; when associated with R-215 and R-244. 3 Publications1
Mutagenesisi120E → A: Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 55% lower expression of YES1. 1 Publication1
Mutagenesisi122 – 352Missing : Loss of MAPK9 binding. Absence of Ser-347 phosphorylation. 1 PublicationAdd BLAST231
Mutagenesisi166V → K: No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location. 1 Publication1
Mutagenesisi206 – 222NNENL…TLVQA → SSSGSPTNLDKIAAQGR: Reduced DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location. 1 PublicationAdd BLAST17
Mutagenesisi206 – 210NNENL → AAAAA: Loss of self-renewal ability in iPS cells. 1 Publication5
Mutagenesisi206N → A: No change in DNA binding. Reduced self-renewal ability in iPS cells. No change in nuclear location. 1 Publication1
Mutagenesisi207N → A: No change in DNA binding. No change in nuclear location. 1 Publication1
Mutagenesisi208E → A: No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location. 1 Publication1
Mutagenesisi209N → A: No change in DNA binding. Reduced self-renewal ability in iPS cells. No change in nuclear location. 1 Publication1
Mutagenesisi210L → A: No change in DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location. No loss of ability to bind SOX2. Reduced levels of CHD4 and SMARCA4 in a POU5F1 pulldown assay. 1 Publication1
Mutagenesisi211Q → A: No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location. 1 Publication1
Mutagenesisi211Q → R: No change in DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location. 1 Publication1
Mutagenesisi212E → A: No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location. 1 Publication1
Mutagenesisi215K → R: No change in sumoylation; when associated with R-244. Loss of sumoylation. No change in nuclear localization; when associated with R-118 and R-244. 1 Publication1
Mutagenesisi244K → R: No change in sumoylation. No change in sumoylation; when associated with R-215. Loss of sumoylation; when associated with R-118 and R-215. No change in nuclear localization; when associated with R-118 and R-215. 1 Publication1
Mutagenesisi347S → A: Absence of phosphorylation. Reduced protein degradation. Reduced self-renewal ability in ES cells. No change in FBXW4 binding. Loss of FBXW8 binding. 1 Publication1

<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 ‘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_00001007491 – 352POU domain, class 5, transcription factor 1Add BLAST352

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 residuei106Phosphoserine; by MAPKBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)3 Publications
Modified residuei228PhosphothreonineBy similarity1
Modified residuei229PhosphoserineBy similarity1
Modified residuei282PhosphoserineBy similarity1
Modified residuei347Phosphoserine; by MAPK8 and MAPK91 Publication1

<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

Sumoylation enhances the protein stability, DNA binding and transactivation activity. Sumoylation is required for enhanced YES1 expression.3 Publications
Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination by WWP2 leading to proteasomal degradation.2 Publications
ERK1/2-mediated phosphorylation at Ser-106 promotes nuclear exclusion and proteasomal degradation. Phosphorylation at Thr-228 and Ser-229 decrease DNA-binding and alters ability to activate transcription (By similarity). JNK1/2-mediated phosphorylation at Ser-347 promotes proteasomal degradation (PubMed:29153991).By similarity1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P20263

PeptideAtlas

More...PeptideAtlasi		P20263

PRoteomics IDEntifications database

More...PRIDEi		P20263

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P20263

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

More...PhosphoSitePlusi		P20263

<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

Expressed the totipotent and pluripotent stem cells of the pregastrulation embryo. Also expressed in primordial germ cells and in the female germ line. Absent from adult tissues.2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Down-regulated during differentiation to endoderm and mesoderm.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Repressed by retinoic acid (RA).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000024406 Expressed in 75 organ(s), highest expression level in morula

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P20263 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P20263 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 PKM.

Interacts with WWP2 (By similarity).

Interacts with UBE2I and ZSCAN10 (PubMed:17496161, PubMed:19740739).

Interacts with PCGF1 (By similarity).

Interacts with ESRRB; recruits ESRRB near the POU5F1-SOX2 element in the NANOG proximal promoter; the interaction is DNA independent (PubMed:18662995).

Interacts with ZNF322 (PubMed:24550733).

Interacts with MAPK8 and MAPK9; the interaction allows MAPK8 and MAPK9 to phosphorylate POU5F1 on Ser-347 (PubMed:29153991).

Interacts (when phosphorylated on Ser-347) with FBXW8 (PubMed:29153991).

Interacts with FBXW4 (PubMed:29153991).

By similarity5 Publications

<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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		202313, 304 interactors

Database of interacting proteins

More...DIPi		DIP-29931N

Protein interaction database and analysis system

More...IntActi		P20263, 141 interactors

Molecular INTeraction database

More...MINTi		P20263

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000025271

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P20263

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P20263

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini131 – 205POU-specificPROSITE-ProRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni173 – 179DNA bindingCombined sources1 Publication7
Regioni186 – 189DNA bindingCombined sources1 Publication4

<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 POU-specific domain mediates interaction with PKM.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 POU transcription factor family. Class-5 subfamily.Curated

Keywords - Domaini

Homeobox

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3802 Eukaryota
ENOG410XQ7X LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155046

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000089941

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P20263

KEGG Orthology (KO)

More...KOi		K09367

Identification of Orthologs from Complete Genome Data

More...OMAi		LENMFLQ

Database of Orthologous Groups

More...OrthoDBi		841019at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P20263

TreeFam database of animal gene trees

More...TreeFami		TF316413

Family and domain databases

Conserved Domains Database

More...CDDi		cd00086 homeodomain, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009057 Homeobox-like_sf
IPR017970 Homeobox_CS
IPR001356 Homeobox_dom
IPR010982 Lambda_DNA-bd_dom_sf
IPR013847 POU
IPR000327 POU_dom
IPR015585 POU_dom_5

The PANTHER Classification System

More...PANTHERi		PTHR11636:SF86 PTHR11636:SF86, 2 hits

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00046 Homeodomain, 1 hit
PF00157 Pou, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00028 POUDOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00389 HOX, 1 hit
SM00352 POU, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46689 SSF46689, 1 hit
SSF47413 SSF47413, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00027 HOMEOBOX_1, 1 hit
PS50071 HOMEOBOX_2, 1 hit
PS00035 POU_1, 1 hit
PS00465 POU_2, 1 hit
PS51179 POU_3, 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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P20263-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGHLASDFA FSPPPGGGDG SAGLEPGWVD PRTWLSFQGP PGGPGIGPGS 
        60         70         80         90        100
EVLGISPCPP AYEFCGGMAY CGPQVGLGLV PQVGVETLQP EGQAGARVES 
       110        120        130        140        150
NSEGTSSEPC ADRPNAVKLE KVEPTPEESQ DMKALQKELE QFAKLLKQKR 
       160        170        180        190        200
ITLGYTQADV GLTLGVLFGK VFSQTTICRF EALQLSLKNM CKLRPLLEKW 
       210        220        230        240        250
VEEADNNENL QEICKSETLV QARKRKRTSI ENRVRWSLET MFLKCPKPSL 
       260        270        280        290        300
QQITHIANQL GLEKDVVRVW FCNRRQKGKR SSIEYSQREE YEATGTPFPG 
       310        320        330        340        350
GAVSFPLPPG PHFGTPGYGS PHFTTLYSVP FPEGEAFPSV PVTALGSPMH 

SN
Length:352
Mass (Da):38,216
Last modified:February 1, 1991 - v1
<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:i757E41DF52286714
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E2JL30E2JL30_MOUSE
Octamer-binding transcription facto...
Pou5f1 Oct-3/4
132Annotation 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>
G3UZG9G3UZG9_MOUSE
Oct-3/4 protein
Pou5f1 Oct-3/4
157Annotation 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 conflicti1 – 28Missing in CAA36682 (PubMed:1690859).CuratedAdd BLAST28
Sequence conflicti29V → M in CAA36682 (PubMed:1690859).Curated1
Sequence conflicti31P → S in AAA39844 (PubMed:1915274).Curated1
Sequence conflicti31P → S in AAB19896 (PubMed:1915274).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
M34381 mRNA Translation: AAA39844.1 Sequence problems.
X52437 mRNA Translation: CAA36682.1
S58426
, S58422, S58423, S58424, S58425 Genomic DNA Translation: AAB19896.1
BC068268 mRNA Translation: AAH68268.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS37600.1

Protein sequence database of the Protein Information Resource

More...PIRi		A34672
S17313

NCBI Reference Sequences

More...RefSeqi		NP_038661.2, NM_013633.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000025271; ENSMUSP00000025271; ENSMUSG00000024406

Database of genes from NCBI RefSeq genomes

More...GeneIDi		18999

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:18999

UCSC genome browser

More...UCSCi		uc008chu.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
M34381 mRNA Translation: AAA39844.1 Sequence problems.
X52437 mRNA Translation: CAA36682.1
S58426
, S58422, S58423, S58424, S58425 Genomic DNA Translation: AAB19896.1
BC068268 mRNA Translation: AAH68268.1
CCDSiCCDS37600.1
PIRiA34672
S17313
RefSeqiNP_038661.2, NM_013633.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OCPNMR-A217-282[»]
3L1PX-ray2.80A/B131-282[»]
SMRiP20263
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi202313, 304 interactors
DIPiDIP-29931N
IntActiP20263, 141 interactors
MINTiP20263
STRINGi10090.ENSMUSP00000025271

PTM databases

iPTMnetiP20263
PhosphoSitePlusiP20263

Proteomic databases

PaxDbiP20263
PeptideAtlasiP20263
PRIDEiP20263

Genome annotation databases

EnsembliENSMUST00000025271; ENSMUSP00000025271; ENSMUSG00000024406
GeneIDi18999
KEGGimmu:18999
UCSCiuc008chu.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5460
MGIiMGI:101893 Pou5f1

Phylogenomic databases

eggNOGiKOG3802 Eukaryota
ENOG410XQ7X LUCA
GeneTreeiENSGT00940000155046
HOGENOMiHOG000089941
InParanoidiP20263
KOiK09367
OMAiLENMFLQ
OrthoDBi841019at2759
PhylomeDBiP20263
TreeFamiTF316413

Miscellaneous databases

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

More...ChiTaRSi		Pou5f1 mouse
EvolutionaryTraceiP20263

Protein Ontology

More...PROi		PR:P20263

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000024406 Expressed in 75 organ(s), highest expression level in morula
ExpressionAtlasiP20263 baseline and differential
GenevisibleiP20263 MM

Family and domain databases

CDDicd00086 homeodomain, 1 hit
InterProiView protein in InterPro
IPR009057 Homeobox-like_sf
IPR017970 Homeobox_CS
IPR001356 Homeobox_dom
IPR010982 Lambda_DNA-bd_dom_sf
IPR013847 POU
IPR000327 POU_dom
IPR015585 POU_dom_5
PANTHERiPTHR11636:SF86 PTHR11636:SF86, 2 hits
PfamiView protein in Pfam
PF00046 Homeodomain, 1 hit
PF00157 Pou, 1 hit
PRINTSiPR00028 POUDOMAIN
SMARTiView protein in SMART
SM00389 HOX, 1 hit
SM00352 POU, 1 hit
SUPFAMiSSF46689 SSF46689, 1 hit
SSF47413 SSF47413, 1 hit
PROSITEiView protein in PROSITE
PS00027 HOMEOBOX_1, 1 hit
PS50071 HOMEOBOX_2, 1 hit
PS00035 POU_1, 1 hit
PS00465 POU_2, 1 hit
PS51179 POU_3, 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 nameiPO5F1_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: P20263
Secondary accession number(s): Q63843
<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: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 16, 2019
This is version 189 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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