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UniProtKB - P17676 (CEBPB_HUMAN)

Entry version 207 (08 May 2019)
Sequence version 2 (22 Aug 2003)
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Protein

CCAAT/enhancer-binding protein beta

Gene

CEBPB

Organism
Homo sapiens (Human)
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:1741402, PubMed:9374525, PubMed:12048245, PubMed:18647749). Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. 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. 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. 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 (By similarity). 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:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity).1 PublicationBy similarity4 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.By similarity
Isoform 3: Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938). Promotes osteoblast differentiation and osteoclastogenesis (By similarity).By similarity1 Publication

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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 functionActivator, DNA-binding
Biological processDifferentiation, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-381340 Transcriptional regulation of white adipocyte differentiation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P17676

SIGNOR Signaling Network Open Resource

More...SIGNORi		P17676

<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 betaImported
Alternative name(s):
Liver activator protein
Short name:
LAP
Liver-enriched inhibitory protein
Short name:
LIP
Nuclear factor NF-IL61 Publication
Transcription factor 5
Short name:
TCF-5
<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
Synonyms:TCF5
ORF Names:PP9092
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 20

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:1834 CEBPB

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		189965 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P17676

<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

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>Mutagenesisi235T → S: Loss of transactivation activity in response to IFNG. 1 Publication1
Mutagenesisi288S → A: Loss of nuclear translocation. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		1051

Open Targets

More...OpenTargetsi		ENSG00000172216

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26377

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CEBPB

Domain mapping of disease mutations (DMDM)

More...DMDMi		34223718

<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_00000766171 – 345CCAAT/enhancer-binding protein betaAdd BLAST345

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 residuei43N6-acetyllysine; alternateBy similarity1
Modified residuei43N6-methylated lysine; alternateBy similarity1
Modified residuei129N6-acetyllysine; by KAT2A and KAT2BBy similarity1
Modified residuei132N6-acetyllysine; by KAT2A and KAT2BBy similarity1
Modified residuei133N6-acetyllysine; by KAT2A and KAT2B; 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-linki133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki187Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei226Phosphothreonine; by GSK3-betaBy similarity1
<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>Glycosylationi227O-linked (GlcNAc) serineBy similarity1
Glycosylationi228O-linked (GlcNAc) serineBy similarity1
Modified residuei231Phosphoserine; by GSK3-betaBy similarity1
Modified residuei235Phosphothreonine; by RPS6KA1, CDK2 and MAPK2 Publications1
Cross-linki260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei266Phosphothreonine; by RPS6KA1 and PKC/PRKCABy similarity1
Modified residuei288Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei325Phosphoserine; by CaMK2By similarity1
Cross-linki332Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<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

Methylated. Methylation at Arg-3 by CARM1 and at Lys-43 by EHMT2 inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-235.2 Publications
Sumoylated by polymeric chains of SUMO2 or SUMO3 (PubMed:12810706). Sumoylation at Lys-174 is required for inhibition of T-cells proliferation. In adipocytes, sumoylation at Lys-174 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation. Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (By similarity).By similarity1 Publication
Ubiquitinated, leading to proteasomal degradation.By similarity
Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-235 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation. Phosphorylation at Thr-266 enhances transactivation activity. Phosphorylation at Ser-325 in response to calcium increases transactivation activity. Phosphorylated at Thr-235 by RPS6KA1 (PubMed:11684016).By similarity1 Publication
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.By similarity
Acetylated. Acetylation at Lys-43 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. Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 129-133, this acetylation is strongly induced by glucocorticoid treatment and enhances transactivation activity.By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P17676

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P17676

MaxQB - The MaxQuant DataBase

More...MaxQBi		P17676

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

More...PaxDbi		P17676

PeptideAtlas

More...PeptideAtlasi		P17676

PRoteomics IDEntifications database

More...PRIDEi		P17676

ProteomicsDB human proteome resource

More...ProteomicsDBi		53503

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P17676

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

More...PhosphoSitePlusi		P17676

<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 at low levels in the lung, kidney and spleen.

<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

By ER stress.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000172216 Expressed in 240 organ(s), highest expression level in layer of synovial tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P17676 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004213
HPA061355
HPA062267

<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 (PubMed:11018027, PubMed:11257229, PubMed:11792321). 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 CEBPD (PubMed:1741402). Can form stable heterodimers with CEBPA and CEBPE (By similarity). Isoform 2 and isoform 3 also form heterodimers. Interacts with TRIM28 and PTGES2. Interacts with PRDM16. Interacts with CCDC85B. Forms a complex with THOC5. Interacts with ZNF638; this interaction increases transcriptional activation. Interacts with CIDEA and CIDEC; these interactions increase transcriptional activation of a subset of CEBPB downstream target genes (By similarity). Interacts with DDIT3/CHOP (PubMed:20829347). Interacts with EP300; recruits EP300 to chromatin. Interacts with RORA; the interaction disrupts interaction with EP300. Interacts (not methylated) with MED23, MED26, SMARCA2, SMARCB1 and SMARCC1 (PubMed:20111005). Interacts with KAT2A and KAT2B (By similarity). Interacts with ATF5; EP300 is required for ATF5 and CEBPB interaction and DNA binding (By similarity). Interacts with NFE2L1; the heterodimer represses expression of DSPP during odontoblast differentiation (By similarity).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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107480, 72 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3361 C/EBPbeta complex
CPX-504 c-Myb-C/EBPbeta complex
CPX-70 CHOP-C/EBPbeta complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P17676

Database of interacting proteins

More...DIPi		DIP-35345N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P17676

Protein interaction database and analysis system

More...IntActi		P17676, 25 interactors

Molecular INTeraction database

More...MINTi		P17676

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000305422

<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

1345
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1GTWX-ray1.85A/B259-336[»]
1GU4X-ray1.80A/B259-336[»]
1GU5X-ray2.10A/B259-336[»]
1H88X-ray2.80A/B259-336[»]
1H89X-ray2.45A/B273-336[»]
1H8AX-ray2.23A/B259-336[»]
1HJBX-ray3.00A/B/D/E259-345[»]
1IO4X-ray3.00A/B259-336[»]
2E42X-ray1.80A/B259-336[»]
2E43X-ray2.10A/B259-336[»]
6MG1X-ray1.75A/B269-344[»]
6MG2X-ray1.93A/B269-344[»]
6MG3X-ray2.05A/B269-344[»]

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

More...SMRi		P17676

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P17676

<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>Domaini271 – 334bZIPPROSITE-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 – 24Required for Lys-174 sumoylationAdd BLAST24
Regioni24 – 135Required for MYC transcriptional repressionBy similarityAdd BLAST112
Regioni275 – 295Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni297 – 304Leucine-zipperPROSITE-ProRule annotation8

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi116 – 1249aaTAD9

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 biasi162 – 170Poly-Pro9

<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 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

<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

More...eggNOGi		ENOG410ISXW Eukaryota
ENOG410XX4P LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000162137

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000013112

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P17676

KEGG Orthology (KO)

More...KOi		K10048

Identification of Orthologs from Complete Genome Data

More...OMAi		GGKNCKK

Database of Orthologous Groups

More...OrthoDBi		1284308at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P17676

TreeFam database of animal gene trees

More...TreeFami		TF105008

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004827 bZIP
IPR016468 C/EBP_chordates

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07716 bZIP_2, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF005879 CCAAT/enhancer-binding, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00338 BRLZ, 1 hit

PROSITE; a protein domain and family database

More...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: P17676-1) [UniParc]FASTAAdd to basket
Also known as: C/EBPbeta-FL

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
MQRLVAWDPA CLPLPPPPPA FKSMEVANFY YEADCLAAAY GGKAAPAAPP 
        60         70         80         90        100
AARPGPRPPA GELGSIGDHE RAIDFSPYLE PLGAPQAPAP ATATDTFEAA 
       110        120        130        140        150
PPAPAPAPAS SGQHHDFLSD LFSDDYGGKN CKKPAEYGYV SLGRLGAAKG 
       160        170        180        190        200
ALHPGCFAPL HPPPPPPPPP AELKAEPGFE PADCKRKEEA GAPGGGAGMA 
       210        220        230        240        250
AGFPYALRAY LGYQAVPSGS SGSLSTSSSS SPPGTPSPAD AKAPPTACYA 
       260        270        280        290        300
GAAPAPSQVK SKAKKTVDKH SDEYKIRRER NNIAVRKSRD KAKMRNLETQ 
       310        320        330        340 
HKVLELTAEN ERLQKKVEQL SRELSTLRNL FKQLPEPLLA SSGHC
Length:345
Mass (Da):36,106
Last modified:August 22, 2003 - 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:i9B725BD6CCAA771D
GO
Isoform 2 (identifier: P17676-2) [UniParc]FASTAAdd to basket
Also known as: C/EBPbeta-LAP

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Show »
Length:322
Mass (Da):33,592
Checksum:i842B381C36DFA8CE
GO
Isoform 3 (identifier: P17676-3) [UniParc]FASTAAdd to basket
Also known as: C/EBPbeta-LIP

The sequence of this isoform differs from the canonical sequence as follows:
     1-198: Missing.

Show »
Length:147
Mass (Da):15,938
Checksum:i3D75D9D752E47B88
GO

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 conflicti241A → P no nucleotide entry (PubMed:7635140).Curated1
Sequence conflicti253A → G in CAA36794 (PubMed:2112087).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016300195G → S1 PublicationCorresponds to variant dbSNP:rs4253440Ensembl.1

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_0533131 – 198Missing in isoform 3. CuratedAdd BLAST198
Alternative sequenceiVSP_0533141 – 23Missing in isoform 2. CuratedAdd BLAST23

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
X52560 Genomic DNA Translation: CAA36794.1
AF289608 mRNA Translation: AAL55792.1
AY193834 Genomic DNA Translation: AAN86350.1
AK291536 mRNA Translation: BAF84225.1
AL161937 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75629.1
BC007538 mRNA Translation: AAH07538.1
BC021931 mRNA Translation: AAH21931.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13429.1 [P17676-1]

Protein sequence database of the Protein Information Resource

More...PIRi		S12788
S66246

NCBI Reference Sequences

More...RefSeqi		NP_001272807.1, NM_001285878.1 [P17676-2]
NP_001272808.1, NM_001285879.1 [P17676-3]
NP_005185.2, NM_005194.3 [P17676-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000303004; ENSP00000305422; ENSG00000172216 [P17676-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1051

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1051

UCSC genome browser

More...UCSCi		uc002xvi.4 human [P17676-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52560 Genomic DNA Translation: CAA36794.1
AF289608 mRNA Translation: AAL55792.1
AY193834 Genomic DNA Translation: AAN86350.1
AK291536 mRNA Translation: BAF84225.1
AL161937 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75629.1
BC007538 mRNA Translation: AAH07538.1
BC021931 mRNA Translation: AAH21931.1
CCDSiCCDS13429.1 [P17676-1]
PIRiS12788
S66246
RefSeqiNP_001272807.1, NM_001285878.1 [P17676-2]
NP_001272808.1, NM_001285879.1 [P17676-3]
NP_005185.2, NM_005194.3 [P17676-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GTWX-ray1.85A/B259-336[»]
1GU4X-ray1.80A/B259-336[»]
1GU5X-ray2.10A/B259-336[»]
1H88X-ray2.80A/B259-336[»]
1H89X-ray2.45A/B273-336[»]
1H8AX-ray2.23A/B259-336[»]
1HJBX-ray3.00A/B/D/E259-345[»]
1IO4X-ray3.00A/B259-336[»]
2E42X-ray1.80A/B259-336[»]
2E43X-ray2.10A/B259-336[»]
6MG1X-ray1.75A/B269-344[»]
6MG2X-ray1.93A/B269-344[»]
6MG3X-ray2.05A/B269-344[»]
SMRiP17676
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107480, 72 interactors
ComplexPortaliCPX-3361 C/EBPbeta complex
CPX-504 c-Myb-C/EBPbeta complex
CPX-70 CHOP-C/EBPbeta complex
CORUMiP17676
DIPiDIP-35345N
ELMiP17676
IntActiP17676, 25 interactors
MINTiP17676
STRINGi9606.ENSP00000305422

PTM databases

iPTMnetiP17676
PhosphoSitePlusiP17676

Polymorphism and mutation databases

BioMutaiCEBPB
DMDMi34223718

Proteomic databases

EPDiP17676
jPOSTiP17676
MaxQBiP17676
PaxDbiP17676
PeptideAtlasiP17676
PRIDEiP17676
ProteomicsDBi53503

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		1051
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303004; ENSP00000305422; ENSG00000172216 [P17676-1]
GeneIDi1051
KEGGihsa:1051
UCSCiuc002xvi.4 human [P17676-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1051
DisGeNETi1051

GeneCards: human genes, protein and diseases

More...GeneCardsi		CEBPB

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0174729
HGNCiHGNC:1834 CEBPB
HPAiCAB004213
HPA061355
HPA062267
MIMi189965 gene
neXtProtiNX_P17676
OpenTargetsiENSG00000172216
PharmGKBiPA26377

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410ISXW Eukaryota
ENOG410XX4P LUCA
GeneTreeiENSGT00940000162137
HOGENOMiHOG000013112
InParanoidiP17676
KOiK10048
OMAiGGKNCKK
OrthoDBi1284308at2759
PhylomeDBiP17676
TreeFamiTF105008

Enzyme and pathway databases

ReactomeiR-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-381340 Transcriptional regulation of white adipocyte differentiation
SignaLinkiP17676
SIGNORiP17676

Miscellaneous databases

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

More...ChiTaRSi		CEBPB human
EvolutionaryTraceiP17676

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CEBPB

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1051

Protein Ontology

More...PROi		PR:P17676

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000172216 Expressed in 240 organ(s), highest expression level in layer of synovial tissue
GenevisibleiP17676 HS

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_HUMAN
<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: P17676
Secondary accession number(s): A8K671, Q96IH2, Q9H4Z5
<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, 1990
Last sequence update: August 22, 2003
Last modified: May 8, 2019
This is version 207 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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