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Protein

CCAAT/enhancer-binding protein beta

Gene

Cebpb

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

Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:16585579, PubMed:17911624, PubMed:18486321, PubMed:20111005). Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis (PubMed:9727068, PubMed:10635333, PubMed:17301242, PubMed:17601773, PubMed:19478079, PubMed:24061474, PubMed:24216764). The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant functions with CEBPA (PubMed:15509779). Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage (PubMed:9727068, PubMed:10635333, PubMed:16585579). Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also a role in intracellular bacteria killing (PubMed:17911624). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:15985551, PubMed:17301242, PubMed:17601773, PubMed:20194620). Essential for female reproduction because of a critical role in ovarian follicle development (PubMed:9303532). Restricts osteoclastogenesis (PubMed:19440205). Together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity).1 PublicationBy similarity17 Publications
Isoform 2: Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4+ T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing.1 Publication
Isoform 3: Acts as a dominant negative through heterodimerization with isoform 2 (By similarity). Promotes osteoblast differentiation and osteoclastogenesis (PubMed:19440205).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, DNA-binding
Biological processDifferentiation, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)

<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 betaImported
Short name:
C/EBP beta
Alternative name(s):
AGP/EBP
Interleukin-6-dependent-binding protein
Short name:
IL-6DBP
Liver-enriched transcriptional activator
Short name:
LAP
<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:CebpbImported
<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 2

Organism-specific databases

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

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MGIi
MGI:88373 Cebpb

<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; 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 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

Embryos display defects in brown fat tissue development (PubMed:19641492). Females are sterile, ovaries lack corpora lutea (PubMed:9303532). Upon bacterial infection, animals show impaired bactericidal activity and die within 3 days (PubMed:17911624). Posthepatectomy, animals show a reduced regenerative response with DNA synthesis decreased to 25% of normal in hepatocytes and a prolonged period of hypoglycemia (PubMed:9727068). Animals show osteopenia with decreased bone formation and enhanced ostecolastogensis. Long bones have a 1.6 fold diminished bone volume with a reduction of the number and thickness of bone trabeculae (PubMed:19440205). Mutants of isoform 2 show impaired CSF3/G-CSF production by macrophages, IFNG production by CD4+ T-cells and granuloma formation in liver. Upon bacterial infection, mutants of isoform 2 die within 6 days. Resistant to LPS-induced endotoxin shock (PubMed:17911624). Double knockout CEBPA and CEBPB results in embryonic developmental arrest and death at around E10 to E11, associated with a gross placenta failure (PubMed:15509779).6 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>Mutagenesisi39K → A or Q: No effect on interaction with EP300. 1 Publication1
Mutagenesisi39K → R: Dominant negative. Loss of transactivation activity. No effect on interaction with EP300. 1 Publication1
Mutagenesisi98K → R: No effect on transactivation activity. Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-101 and R-102. 2 Publications1
Mutagenesisi101K → R: Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity; when associated with R-98 and R-102. 1 Publication1
Mutagenesisi102K → R: Not acetylated and no increase of transactivation activity after glucocorticoid-stimulation; when associated with R-98 and R-101. 1 Publication1
Mutagenesisi133K → R: Not sumoylated. Decreases ubiquitination and increases stability. Loss of proliferation inhibition in T cells. No effect on transactivation activity. 3 Publications1
Mutagenesisi135E → A: Not sumoylated and not ubiquitinated. 1 Publication1
Mutagenesisi179T → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-184 and A-188. 1 Publication1
Mutagenesisi180S → A: Highly increases transactivation activity; when associated with A-181. 1 Publication1
Mutagenesisi181S → A: Highly increases transactivation activity; when associated with A-180. 1 Publication1
Mutagenesisi184S → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-188. 1 Publication1
Mutagenesisi188T → A: Disruption of phosphorylation by MAPK and GSK3B, acquisition of DNA-binding activity and transactivation function; when associated with A-179 and A-184. 1 Publication1
Mutagenesisi215K → R: No effect on transactivation activity. 1 Publication1
Mutagenesisi217T → A: Loss of hepatocyte proliferation induction by TGFA. 1 Publication1
Mutagenesisi217T → E: Induces hepatocyte proliferation. 1 Publication1
Mutagenesisi276S → A: Reduces phosphorylation in response to calcium. 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_00000766181 – 296CCAAT/enhancer-binding protein betaAdd BLAST296

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 residuei3Omega-N-methylated arginine; by CARM11 Publication1
Modified residuei39N6-acetyllysine; alternate1 Publication1
Modified residuei39N6-methylated lysine; alternate1 Publication1
Modified residuei98N6-acetyllysine; by KAT2A and KAT2B1 Publication1
Modified residuei101N6-acetyllysine; by KAT2A and KAT2B1 Publication1
Modified residuei102N6-acetyllysine; by KAT2A and KAT2B; alternate1 Publication1
<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-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate3 Publications
Cross-linki133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei179Phosphothreonine; by GSK3-beta3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi180O-linked (GlcNAc) serine1 Publication1
Glycosylationi181O-linked (GlcNAc) serine1 Publication1
Modified residuei184Phosphoserine; by GSK3-betaCombined sources3 Publications1
Modified residuei188Phosphothreonine; by RPS6KA1, CDK2 and MAPKCombined sources4 Publications1
Cross-linki211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki213Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei217Phosphothreonine; by RPS6KA1 and PKC/PRKCA1 Publication1
Modified residuei239Phosphoserine; by PKC/PRKCABy similarity1
Modified residuei276Phosphoserine; by CaMK21 Publication1
Cross-linki283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

<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 by polymeric chains of SUMO2 or SUMO3. Sumoylation at Lys-133 is required for inhibition of T-cells proliferation (PubMed:16585579). In adipocytes, sumoylation at Lys-133 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation (PubMed:24061474). Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (PubMed:20194620).By similarity3 Publications
Ubiquitinated, leading to proteasomal degradation.1 Publication
Phosphorylated at Thr-188 by MAPK and CDK2, serves to prime phosphorylation at Thr-179 and Ser-184 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-188 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation. Phosphorylation at Thr-217 enhances transactivation activity. Phosphorylation at Ser-276 in response to calcium increases transactivation activity (PubMed:1314426). Phosphorylated at Thr-188 by RPS6KA1 (By similarity).By similarity3 Publications
O-glycosylated, glycosylation at Ser-180 and Ser-181 prevents phosphorylation on Thr-188, Ser-184 and Thr-179 and DNA binding activity which delays the adipocyte differentiation program.1 Publication
Acetylated. Acetylation at Lys-39 is an important and dynamic regulatory event that contributes to its ability to transactivate target genes, including those associated with adipogenesis and adipocyte function. Deacetylation by HDAC1 represses its transactivation activity (PubMed:18486321). Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 98-102, this acetylation is strongly induced by glucocorticoid treatment and enhances transactivation activity (PubMed:17301242).2 Publications
Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2, inhibits transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-188.1 Publication1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

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PaxDbi
P28033

PeptideAtlas

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PeptideAtlasi
P28033

PRoteomics IDEntifications database

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PRIDEi
P28033

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P28033

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

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PhosphoSitePlusi
P28033

<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

Abundantly expressed in myoblasts. Enriched in brown adipose tissue (BAT) versus white adipose tissue (WAT). Expressed in hepatocytes (at protein level). Expressed in T lymphocytes (PubMed:16585579). The expression in granulosa cells of antral follicles is induced by luteinizing hormone (PubMed:9303532). Expressed in chondrocytes and osteoblasts (at protein level) (PubMed:19440205).5 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

At E9.5, expressed in the chorionic plate and ectoplacental cone. From E10.5 to at least E11.5, is also expressed in the trophoblast cells of the three placenta layers (PubMed:15509779). Expressed in monocytic precursors but is vanished during differentiation into osteoclasts. The expression increases during osteoblast differentiation (PubMed:19440205).2 Publications

<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

Up-regulated by cold exposure.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000056501 Expressed in 273 organ(s), highest expression level in adrenal gland

CleanEx database of gene expression profiles

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CleanExi
MM_CEBPB

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P28033 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P28033 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. Interacts with ATF4. Binds DNA as a heterodimer with ATF4 (PubMed:11018027). Interacts with MYB; within the complex, MYB and CEBPB bind to different promoter regions (PubMed:11792321). Can form stable heterodimers with CEBPA, CEBPD and CEBPE (By similarity). Isoform 2 and isoform 3 also form heterodimers (By similarity). Interacts with TRIM28 and PTGES2 (PubMed:9742105, PubMed:15879117). Interacts with PRDM16 (PubMed:19641492). Interacts with CCDC85B (PubMed:15644333). Forms a complex with THOC5 (PubMed:19015024). Interacts with ZNF638; this interaction increases transcriptional activation (PubMed:21602272). Interacts with CIDEA and CIDEC (PubMed:22245780). Interaction with CIDEA increases transcriptional activation of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH. Interaction with CIDEC increases transcriptional activation of SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. Interacts with DDIT3/CHOP. Interacts with EP300; recruits EP300 to chromatin. Interacts with RORA; the interaction disrupts interaction with EP300 (PubMed:19324970). Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1 (PubMed:20111005). Interacts with KAT2A and KAT2B (PubMed:17301242). Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (PubMed:24216764). Interacts with NFE2L1; the heterodimer represses expression of DSPP during odontoblast differentiation (By similarity).By similarity14 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)

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BioGridi
198669, 15 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-66 CHOP-C/EBPbeta complex
CPX-68 C/EBPbeta complex
CPX-685 c-Myb-C/EBPbeta complex

Database of interacting proteins

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DIPi
DIP-37539N

Protein interaction database and analysis system

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IntActi
P28033, 14 interactors

Molecular INTeraction database

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MINTi
P28033

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000069850

<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

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P28033

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

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SMRi
P28033

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P28033

<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>Domaini222 – 285bZIPPROSITE-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 – 22Required for Lys-133 sumoylationBy similarityAdd BLAST22
Regioni22 – 104Required for MYC transcriptional repression1 PublicationAdd BLAST83
Regioni226 – 246Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni248 – 255Leucine-zipperPROSITE-ProRule annotation8

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 biasi120 – 129Pro-rich10
Compositional biasi170 – 191Pro/Ser-richAdd BLAST22

<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
ENSGT00940000162137

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000013112

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050879

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P28033

KEGG Orthology (KO)

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KOi
K10048

Identification of Orthologs from Complete Genome Data

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OMAi
CKKPAEY

Database of Orthologous Groups

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OrthoDBi
EOG091G11FC

Database for complete collections of gene phylogenies

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PhylomeDBi
P28033

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 (3)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 3 <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
Isoform 1 (identifier: P28033-1) [UniParc]FASTAAdd to basket
Also known as: a, C/EBPbeta-FL, LAP*

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
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA
60 70 80 90 100
EPAIGEHERA IDFSPYLEPL APAADFAAPA PAHHDFLSDL FADDYGAKPS
110 120 130 140 150
KKPADYGYVS LGRAGAKAAP PACFPPPPPA ALKAEPGFEP ADCKRADDAP
160 170 180 190 200
AMAAGFPFAL RAYLGYQATP SGSSGSLSTS SSSSPPGTPS PADAKAAPAA
210 220 230 240 250
CFAGPPAAPA KAKAKKTVDK LSDEYKMRRE RNNIAVRKSR DKAKMRNLET
260 270 280 290
QHKVLELTAE NERLQKKVEQ LSRELSTLRN LFKQLPEPLL ASAGHC
Length:296
Mass (Da):31,446
Last modified:August 1, 1992 - 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:i827AC4AFC209AE89
GO
Isoform 2 (identifier: P28033-3) [UniParc]FASTAAdd to basket
Also known as: b, C/EBPbeta-LAP

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Note: Major isoform.
Show »
Length:275
Mass (Da):29,133
Checksum:i717E36841E48752D
GO
Isoform 3 (identifier: P28033-2) [UniParc]FASTAAdd to basket
Also known as: c, C/EBPbeta-LIP

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.

Show »
Length:145
Mass (Da):15,597
Checksum:iC7AFEEE4F98F5978
GO

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0539761 – 151Missing in isoform 3. CuratedAdd BLAST151
Alternative sequenceiVSP_0539771 – 21Missing in isoform 2. CuratedAdd BLAST21

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
M61007 mRNA Translation: AAA37192.1
X62600 mRNA Translation: CAA44484.1
S78572 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

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CCDSi
CCDS17105.1 [P28033-1]

Protein sequence database of the Protein Information Resource

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PIRi
A36366

NCBI Reference Sequences

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RefSeqi
NP_001274667.1, NM_001287738.1 [P28033-3]
NP_001274668.1, NM_001287739.1 [P28033-2]
NP_034013.1, NM_009883.4 [P28033-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.439656

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501 [P28033-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
12608

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:12608

UCSC genome browser

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UCSCi
uc008oaf.2 mouse [P28033-1]

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
M61007 mRNA Translation: AAA37192.1
X62600 mRNA Translation: CAA44484.1
S78572 Genomic DNA No translation available.
CCDSiCCDS17105.1 [P28033-1]
PIRiA36366
RefSeqiNP_001274667.1, NM_001287738.1 [P28033-3]
NP_001274668.1, NM_001287739.1 [P28033-2]
NP_034013.1, NM_009883.4 [P28033-1]
UniGeneiMm.439656

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CI6X-ray2.60B224-285[»]
ProteinModelPortaliP28033
SMRiP28033
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198669, 15 interactors
ComplexPortaliCPX-66 CHOP-C/EBPbeta complex
CPX-68 C/EBPbeta complex
CPX-685 c-Myb-C/EBPbeta complex
DIPiDIP-37539N
IntActiP28033, 14 interactors
MINTiP28033
STRINGi10090.ENSMUSP00000069850

PTM databases

iPTMnetiP28033
PhosphoSitePlusiP28033

Proteomic databases

PaxDbiP28033
PeptideAtlasiP28033
PRIDEiP28033

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
12608
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070642; ENSMUSP00000069850; ENSMUSG00000056501 [P28033-1]
GeneIDi12608
KEGGimmu:12608
UCSCiuc008oaf.2 mouse [P28033-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1051
MGIiMGI:88373 Cebpb

Phylogenomic databases

eggNOGiKOG3119 Eukaryota
ENOG410YJ8G LUCA
GeneTreeiENSGT00940000162137
HOGENOMiHOG000013112
HOVERGENiHBG050879
InParanoidiP28033
KOiK10048
OMAiCKKPAEY
OrthoDBiEOG091G11FC
PhylomeDBiP28033
TreeFamiTF105008

Enzyme and pathway databases

ReactomeiR-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)

Miscellaneous databases

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

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ChiTaRSi
Cebpb mouse
EvolutionaryTraceiP28033

Protein Ontology

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PROi
PR:P28033

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000056501 Expressed in 273 organ(s), highest expression level in adrenal gland
CleanExiMM_CEBPB
ExpressionAtlasiP28033 baseline and differential
GenevisibleiP28033 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

More...
ProtoNeti
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 nameiCEBPB_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: P28033
<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: August 1, 1992
Last sequence update: August 1, 1992
Last modified: December 5, 2018
This is version 177 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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