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Entry version 165 (08 May 2019)
Sequence version 2 (23 Jan 2002)
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Protein

CCAAT/enhancer-binding protein alpha

Gene

Cebpa

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 coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta (PubMed:8415748, PubMed:15107404, PubMed:15589173). Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB (PubMed:15509779). Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP) (PubMed:24367003). Critical for the proper development of the liver and the lung (PubMed:8798745). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (PubMed:1935900, PubMed:8090719). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Downregulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters (PubMed:11672531). Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC (PubMed:17627282). To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2 (PubMed:17290224). In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (PubMed:17090532).By similarity13 Publications
Isoform 3: Can act as dominant-negative. Binds DNA and have transctivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation.By similarity1 Publication
Isoform 4: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi286 – 301By similarityAdd BLAST16

<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, Developmental 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:
CCAAT/enhancer-binding protein alphaImported
Short name:
C/EBP alphaImported
<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:CebpaImported
Synonyms:Cebp1 Publication
<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 7

Organism-specific databases

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

More...
MGIi
MGI:99480 Cebpa

<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

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 in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutants die of hypoglycemia at 7-10h after bith. They have defects in the control of hepatic growth and lung development. The liver architecture is disturbed with acinar formation. They show hyperproliferation of type II pneumocytes and disturbed alveolar architecture. At the molecular level, accumulation of glycogen and lipids in the liver and adipose tissues is impaired, and the mutant animals are severely hypoglycemic (PubMed:8798745). In very few cases (less than 1%) mutants are able to survive up to 4 weeks but they are sevrely retarded in development. At 2 weeks, they are about half the size of their littermates, very thin and with skin problems. Conditional knockout in adults leads to a lack of granulopoiesis in all hematopoietic organs with no mature peripheral blood granulocytes and the presence of >30% immature myeloid cells in the bone marrow, but without anemia or thrombocytopenia. Animals rarely survive 4 to 5 weeks of age due to sepsis as a result of granulocytopenia (PubMed:15589173). Double knockout CEBPA and CEBPB results in embryonic developmental arrest and death at around 10 dpc to 11 dpc, associated with a gross placenta failure (PubMed:15509779).3 Publications

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>Mutagenesisi182 – 188PPPPPPP → APPPAPA: No effect on DNA-binding or interaction with CDK2 and CDK4. No effect on cell cycle inhibition. 1 Publication7
Mutagenesisi184 – 186PPP → AAA: No effect on DNA-binding or interaction with CDK2 and CDK4. No effect on cell cycle inhibition. 1 Publication3
Mutagenesisi193S → A: No effect on DNA-binding. Loss of interaction with CDK2 and CDK4 as well as cell cycle inhibition. 1 Publication1
Mutagenesisi222 – 230TPPPTPVPS → APPPAPVPA: Decreases phosphorylated form. Deregulation of hepatic glucose metabolism. 1 Publication9
Mutagenesisi286Y → A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia. 1 Publication1
Mutagenesisi288V → A: No effect on DNA-binding, no effect on repression of E2F1:TFDP1-mediated transcription and no effect on adipogenesis and granulopoiesis; when associated with A-291. 1 Publication1
Mutagenesisi291E → A: No effect on DNA-binding, no effect on repression of E2F1:TFDP1-mediated transcription and no effect on adipogenesis and granulopoiesis; when associated with A-288. 1 Publication1
Mutagenesisi295I → A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia; when associated with A-298. 1 Publication1
Mutagenesisi298R → A: No effect on DNA-binding, represses E2F1:TFDP1-mediated transcription and causes adipose hypoplasia and myeloid dysplasia; when associated with A-295. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3616358

<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_00000766141 – 359CCAAT/enhancer-binding protein alphaAdd BLAST359

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 residuei159N6-acetyllysine; alternateBy 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-linki159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei193Phosphoserine1 Publication1
Modified residuei222Phosphothreonine; by GSK31 Publication1
Modified residuei226Phosphothreonine; by GSK31 Publication1
Modified residuei230Phosphoserine; by GSK31 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

Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2.By similarity
Phosphorylation at Ser-193 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-193 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation (PubMed:15107404). Phosphorylation at Thr-222 and Thr-226 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-222 and Thr-226 are phosphorylated only during feeding but not during fasting (PubMed:17290224). Phosphorylation of the GSK3 consensus sites selectively decreases transactivation activity on IRE-controlled promoters (PubMed:17290224).2 Publications
Ubiquitinated by COP1 upon interaction with TRIB1.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P53566

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

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PaxDbi
P53566

PRoteomics IDEntifications database

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PRIDEi
P53566

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P53566

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

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PhosphoSitePlusi
P53566

<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

Isoform 2 and isoform 3 are expressed in adipose tissue and liver (at protein level).1 Publication

<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

At 9.5 dpc, expressed in the chorionic plate. From 10.5 to at least 11.5 dpc, is also expressed in the trophoblasts of the labyrinthine layer.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000034957 Expressed in 200 organ(s), highest expression level in white adipose tissue

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P53566 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P53566 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

Binds DNA as a homodimer and as a heterodimer. Can form stable heterodimers with CEBPB, CEBPD, CEBPE and CEBPG (By similarity). Interacts with PRDM16 (PubMed:19641492). Interacts with UBN1 (By similarity). Interacts with ZNF638; this interaction increases transcriptional activation (PubMed:21602272). Interacts with the complex TFDP2:E2F1; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (By similarity). Interacts with RB1 (PubMed:15107404). Interacts (when phosphorylated at SER-193) with CDK2, CDK4, E2F4 and SMARCA2 (PubMed:15107404). Interacts with SREBPF1 (PubMed:17290224). Interacts with FOXO1 (via the Fork-head domain); the interaction increases when FOXO1 is deacetylated (PubMed:17090532, PubMed:17627282). Isoform 1 and isoform 4 interact with TAF1A and UBTF. Isoform 4 interacts with NPM1 (By similarity). Interacts (via recognition sequence) with TRIB1 (By similarity).By similarity6 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
198667, 122 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-65 CHOP-C/EBPalpha complex
CPX-67 C/EBPalpha complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P53566

Database of interacting proteins

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DIPi
DIP-44054N

Protein interaction database and analysis system

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IntActi
P53566, 11 interactors

Molecular INTeraction database

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MINTi
P53566

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000096129

<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

3D structure databases

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

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SMRi
P53566

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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>Domaini283 – 346bZIPPROSITE-ProRule annotationAdd BLAST64

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>Regioni1 – 70Required to repress E2F1:TFDP1-mediated transcription, to inhibit cell cycle and to induce adipocyte differentiationBy similarityAdd BLAST70
Regioni54 – 72Required for interaction with TRIB1By similarityAdd BLAST19
Regioni126 – 200Required to induce adipocyte differentiationBy similarityAdd BLAST75
Regioni180 – 194Required to functionally cooperate with SREBF1 in promoter activation1 PublicationAdd BLAST15
Regioni240 – 359Interaction with FOXO11 PublicationAdd BLAST120
Regioni287 – 314Basic motifPROSITE-ProRule annotationAdd BLAST28
Regioni318 – 346Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

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 biasi99 – 102Poly-Gly4
Compositional biasi181 – 190Poly-Pro10
Compositional biasi262 – 271Poly-Gly10

<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 recognition sequence (54-72) is required for interaction with TRIB1.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 bZIP family. C/EBP subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3119 Eukaryota
ENOG410YJ8G LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000162646

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000013112

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P53566

KEGG Orthology (KO)

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KOi
K09055

Identification of Orthologs from Complete Genome Data

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OMAi
QIAHCAQ

Database of Orthologous Groups

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OrthoDBi
1284308at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P53566

TreeFam database of animal gene trees

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TreeFami
TF105008

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004827 bZIP
IPR016468 C/EBP_chordates

Pfam protein domain database

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Pfami
View protein in Pfam
PF07716 bZIP_2, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF005879 CCAAT/enhancer-binding, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00338 BRLZ, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50217 BZIP, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)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 describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P53566-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MESADFYEVE PRPPMSSHLQ SPPHAPSNAA FGFPRGAGPA PPPAPPAAPE
60 70 80 90 100
PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAAGPAGG
110 120 130 140 150
GGDFDYPGAP AGPGGAVMSA GAHGPPPGYG CAAAGYLDGR LEPLYERVGA
160 170 180 190 200
PALRPLVIKQ EPREEDEAKQ LALAGLFPYQ PPPPPPPPHP HASPAHLAAP
210 220 230 240 250
HLQFQIAHCG QTTMHLQPGH PTPPPTPVPS PHAAPALGAA GLPGPGSALK
260 270 280 290 300
GLAGAHPDLR TGGGGGGSGA GAGKAKKSVD KNSNEYRVRR ERNNIAVRKS
310 320 330 340 350
RDKAKQRNVE TQQKVLELTS DNDRLRKRVE QLSRELDTLR GIFRQLPESS

LVKAMGNCA
Length:359
Mass (Da):37,430
Last modified:January 23, 2002 - 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:i1E6CC09A330BEFEF
GO
Isoform 2 (identifier: P53566-3) [UniParc]FASTAAdd to basket
Also known as: C/EBPalpha-p421 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.

Show »
Length:345
Mass (Da):35,781
Checksum:i50B6625758216AF1
GO
Isoform 3 (identifier: P53566-4) [UniParc]FASTAAdd to basket
Also known as: C/EBPalpha-p301 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.

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Length:242
Mass (Da):25,557
Checksum:iDB631CCCFD55BC20
GO
Isoform 4 (identifier: P53566-5) [UniParc]FASTAAdd to basket
Also known as: extended-C/EBPalpha1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRGREPVGALGGRRRQRRHAQAGGRRGSPCRENSNSPM

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Length:396
Mass (Da):41,484
Checksum:i1E63C3CF81CF808B
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
A0A0U1RPE0A0A0U1RPE0_MOUSE
CCAAT/enhancer-binding protein alph...
Cebpa
159Annotation 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 conflicti30 – 54AFGFP…EPLGG → RLWLSPGRGPRAAPSPTCRP GAAGR in AAA37374 (PubMed:2006196).CuratedAdd BLAST25
Sequence conflicti356 – 359GNCA → ATAREARGCGTALGRPPGWR PRGWFRVAGSLGCPGRASQD in AAA37374 (PubMed:2006196).Curated4

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0575491 – 117Missing in isoform 3. 1 PublicationAdd BLAST117
Alternative sequenceiVSP_0575501 – 14Missing in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_0576081M → MRGREPVGALGGRRRQRRHA QAGGRRGSPCRENSNSPM in isoform 4. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M62362 Genomic DNA Translation: AAA37374.1
AC150683 Genomic DNA No translation available.
BC011118 mRNA Translation: AAH11118.1
BC028890 mRNA Translation: AAH28890.1
BC051102 mRNA Translation: AAH51102.1
BC058161 mRNA Translation: AAH58161.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS21145.1 [P53566-1]

Protein sequence database of the Protein Information Resource

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PIRi
I49575

NCBI Reference Sequences

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RefSeqi
NP_001274443.1, NM_001287514.1 [P53566-5]
NP_001274444.1, NM_001287515.1 [P53566-3]
NP_001274450.1, NM_001287521.1 [P53566-4]
NP_031704.2, NM_007678.3 [P53566-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000042985; ENSMUSP00000096129; ENSMUSG00000034957 [P53566-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
12606

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:12606

UCSC genome browser

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UCSCi
uc009gjl.2 mouse [P53566-1]

Keywords - Coding sequence diversityi

Alternative initiation

<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
M62362 Genomic DNA Translation: AAA37374.1
AC150683 Genomic DNA No translation available.
BC011118 mRNA Translation: AAH11118.1
BC028890 mRNA Translation: AAH28890.1
BC051102 mRNA Translation: AAH51102.1
BC058161 mRNA Translation: AAH58161.1
CCDSiCCDS21145.1 [P53566-1]
PIRiI49575
RefSeqiNP_001274443.1, NM_001287514.1 [P53566-5]
NP_001274444.1, NM_001287515.1 [P53566-3]
NP_001274450.1, NM_001287521.1 [P53566-4]
NP_031704.2, NM_007678.3 [P53566-1]

3D structure databases

SMRiP53566
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198667, 122 interactors
ComplexPortaliCPX-65 CHOP-C/EBPalpha complex
CPX-67 C/EBPalpha complex
CORUMiP53566
DIPiDIP-44054N
IntActiP53566, 11 interactors
MINTiP53566
STRINGi10090.ENSMUSP00000096129

Chemistry databases

ChEMBLiCHEMBL3616358

PTM databases

iPTMnetiP53566
PhosphoSitePlusiP53566

Proteomic databases

MaxQBiP53566
PaxDbiP53566
PRIDEiP53566

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042985; ENSMUSP00000096129; ENSMUSG00000034957 [P53566-1]
GeneIDi12606
KEGGimmu:12606
UCSCiuc009gjl.2 mouse [P53566-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1050
MGIiMGI:99480 Cebpa

Phylogenomic databases

eggNOGiKOG3119 Eukaryota
ENOG410YJ8G LUCA
GeneTreeiENSGT00940000162646
HOGENOMiHOG000013112
InParanoidiP53566
KOiK09055
OMAiQIAHCAQ
OrthoDBi1284308at2759
PhylomeDBiP53566
TreeFamiTF105008

Miscellaneous databases

Protein Ontology

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PROi
PR:P53566

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000034957 Expressed in 200 organ(s), highest expression level in white adipose tissue
ExpressionAtlasiP53566 baseline and differential
GenevisibleiP53566 MM

Family and domain databases

InterProiView protein in InterPro
IPR004827 bZIP
IPR016468 C/EBP_chordates
PfamiView protein in Pfam
PF07716 bZIP_2, 1 hit
PIRSFiPIRSF005879 CCAAT/enhancer-binding, 1 hit
SMARTiView protein in SMART
SM00338 BRLZ, 1 hit
PROSITEiView protein in PROSITE
PS50217 BZIP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiCEBPA_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: P53566
Secondary accession number(s): Q91XB6
<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 1, 1996
Last sequence update: January 23, 2002
Last modified: May 8, 2019
This is version 165 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

Complete proteome, 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
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