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Entry version 165 (05 Jun 2019)
Sequence version 1 (01 May 1991)
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Protein

CCAAT/enhancer-binding protein beta

Gene

Cebpb

Organism
Rattus norvegicus (Rat)
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:8336793). Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis (PubMed:10635333). 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 (By similarity). 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:10635333). 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 (By similarity). 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 (PubMed:15308669).By 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:1934061). 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

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-RNO-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 betaImported
Alternative name(s):
C/EBP-related protein 2
Interleukin-6-dependent-binding protein
Short name:
IL-6DBP
Liver-enriched inhibitory protein
Short name:
LIP
Liver-enriched transcriptional activator
Short name:
LAP
Silencer factor B
Short name:
SF-B
<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:Crp2, Nf-il61 Publication, Sfb
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 3

Organism-specific databases

Rat genome database

More...
RGDi
2327 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 & 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>Mutagenesisi105S → A: No effect on DNA-binding. Loss of transactivation activity. Loss of hepatocyte proliferation induction by TGFA. 2 Publications1
Mutagenesisi105S → D: No effect on DNA-binding. Increases transactivation activity. 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_00000766191 – 297CCAAT/enhancer-binding protein betaAdd BLAST297

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 CARM1By similarity1
Modified residuei39N6-acetyllysine; alternateBy similarity1
Modified residuei39N6-methylated lysine; alternateBy similarity1
Modified residuei99N6-acetyllysine; by KAT2A and KAT2BBy similarity1
Modified residuei102N6-acetyllysine; by KAT2A and KAT2BBy similarity1
Modified residuei103N6-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-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei105Phosphoserine; by RPS6KA1 and PKC/PRKCA2 Publications1
Cross-linki134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei180Phosphothreonine; 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>Glycosylationi181O-linked (GlcNAc) serineBy similarity1
Glycosylationi182O-linked (GlcNAc) serineBy similarity1
Modified residuei185Phosphoserine; by GSK3-betaBy similarity1
Modified residuei189Phosphothreonine; by RPS6KA1, CDK2 and MAPKBy similarity1
Cross-linki212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei240Phosphoserine; by PKC/PRKCABy similarity1
Modified residuei277Phosphoserine; by CaMK2By similarity1
Cross-linki284Glycyl 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

Phosphorylated at Thr-189 by MAPK and CDK2, serves to prime phosphorylation at Thr-180 and Ser-185 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-189 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation (By similarity). Phosphorylation at Ser-105 enhances transactivation activity (PubMed:8336793). Phosphorylation at Ser-277 in response to calcium increases transactivation activity. Phosphorylated at Thr-189 by RPS6KA1 (By similarity).By similarity1 Publication
Methylated. Methylation at Arg-3 by CARM1 and at Lys-39 by EHMT2 inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-189.By similarity
Sumoylated by polymeric chains of SUMO2 or SUMO3 (By similarity). Sumoylation at Lys-134 is required for inhibition of T-cells proliferation. In adipocytes, sumoylation at Lys-134 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation. Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (By similarity).By similarity
Ubiquitinated, leading to proteasomal degradation.By similarity
O-glycosylated, glycosylation at Ser-181 and Ser-182 prevents phosphorylation on Thr-189, Ser-185 and Thr-180 and DNA binding activity which delays the adipocyte differentiation program.By similarity
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. Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 99-103, 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

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

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PaxDbi
P21272

PeptideAtlas

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PeptideAtlasi
P21272

PRoteomics IDEntifications database

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PRIDEi
P21272

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P21272

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

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PhosphoSitePlusi
P21272

<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

Liver and lung.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000057347 Expressed in 9 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P21272 RN

<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:1934061). Interacts with MYB; within the complex, MYB and CEBPB bind to different promoter regions. Interacts with ATF4. Binds DNA as a heterodimer with ATF4 (By similarity). Can form stable heterodimers with CEBPA, CEBPD, CEBPE and CEBPG (PubMed:1377818, PubMed:1884998). Isoform 2 and isoform 3 also form heterodimers (PubMed:1934061). 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. Interacts with DDIT3/CHOP.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 (By similarity). 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 (PubMed:15308669).By similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
246438, 101 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-62 CHOP-C/EBPbeta complex
CPX-63 C/EBPbeta complex

Database of interacting proteins

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DIPi
DIP-28139N

Protein interaction database and analysis system

More...
IntActi
P21272, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000065222

<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
P21272

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>Domaini223 – 286bZIPPROSITE-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-134 sumoylationBy similarityAdd BLAST22
Regioni22 – 105Required for MYC transcriptional repressionBy similarityAdd BLAST84
Regioni227 – 247Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni249 – 256Leucine-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 biasi121 – 130Pro-rich10
Compositional biasi171 – 192Pro/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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P21272

KEGG Orthology (KO)

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KOi
K10048

Identification of Orthologs from Complete Genome Data

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OMAi
GGKNCKK

Database of Orthologous Groups

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OrthoDBi
1284308at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P21272

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>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: P21272-1) [UniParc]FASTAAdd to basket
Also known as: 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
MHRLLAWDAA CLPPPPAAFR PMEVANFYYE PDCLAYGAKA ARAAPRAPAA
60 70 80 90 100
EPAIGEHERA IDFSPYLEPL APAAADFAAP APAHHDFLSD LFADDYGAKP
110 120 130 140 150
SKKPSDYGYV SLGRAGAKAA PPACFPPPPP AALKAEPGFE PADCKRADDA
160 170 180 190 200
PAMAAGFPFA LRAYLGYQAT PSGSSGSLST SSSSSPPGTP SPADAKAAPA
210 220 230 240 250
ACFAGPPAAP AKAKAKKAVD KLSDEYKMRR ERNNIAVRKS RDKAKMRNLE
260 270 280 290
TQHKVLELTA ENERLQKKVE QLSRELSTLR NLFKQLPEPL LASAGHC
Note: Not detected in rat liver.
Length:297
Mass (Da):31,503
Last modified:May 1, 1991 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC2511FDB65527789
GO
Isoform 2 (identifier: P21272-2) [UniParc]FASTAAdd to basket
Also known as: LAP

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

Note: Major form in.
Show »
Length:276
Mass (Da):29,190
Checksum:i2A621B294E8E3652
GO
Isoform 3 (identifier: P21272-3) [UniParc]FASTAAdd to basket
Also known as: LIP

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: Missing.

Show »
Length:145
Mass (Da):15,567
Checksum:iDD1E45FE483F5968
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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0533151 – 152Missing in isoform 3. CuratedAdd BLAST152
Alternative sequenceiVSP_0533161 – 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
M57235 mRNA Translation: AAA19669.1
X54626 Genomic DNA Translation: CAA38443.1
BC129071 mRNA Translation: AAI29072.1
X60769 mRNA Translation: CAA43179.1
AY056052 Genomic DNA Translation: AAA40972.1

Protein sequence database of the Protein Information Resource

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PIRi
A35914

NCBI Reference Sequences

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RefSeqi
NP_001288644.1, NM_001301715.1 [P21272-2]
NP_001288649.1, NM_001301720.1 [P21272-3]
NP_077039.3, NM_024125.5 [P21272-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000083876; ENSRNOP00000071427; ENSRNOG00000057347 [P21272-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
24253

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:24253

UCSC genome browser

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UCSCi
RGD:2327 rat [P21272-1]

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
M57235 mRNA Translation: AAA19669.1
X54626 Genomic DNA Translation: CAA38443.1
BC129071 mRNA Translation: AAI29072.1
X60769 mRNA Translation: CAA43179.1
AY056052 Genomic DNA Translation: AAA40972.1
PIRiA35914
RefSeqiNP_001288644.1, NM_001301715.1 [P21272-2]
NP_001288649.1, NM_001301720.1 [P21272-3]
NP_077039.3, NM_024125.5 [P21272-1]

3D structure databases

SMRiP21272
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246438, 101 interactors
ComplexPortaliCPX-62 CHOP-C/EBPbeta complex
CPX-63 C/EBPbeta complex
DIPiDIP-28139N
IntActiP21272, 2 interactors
STRINGi10116.ENSRNOP00000065222

PTM databases

iPTMnetiP21272
PhosphoSitePlusiP21272

Proteomic databases

PaxDbiP21272
PeptideAtlasiP21272
PRIDEiP21272

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000083876; ENSRNOP00000071427; ENSRNOG00000057347 [P21272-1]
GeneIDi24253
KEGGirno:24253
UCSCiRGD:2327 rat [P21272-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1051
RGDi2327 Cebpb

Phylogenomic databases

eggNOGiKOG3119 Eukaryota
ENOG410YJ8G LUCA
GeneTreeiENSGT00940000162137
HOGENOMiHOG000013112
InParanoidiP21272
KOiK10048
OMAiGGKNCKK
OrthoDBi1284308at2759
PhylomeDBiP21272
TreeFamiTF105008

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P21272

Gene expression databases

BgeeiENSRNOG00000057347 Expressed in 9 organ(s), highest expression level in liver
GenevisibleiP21272 RN

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_RAT
<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: P21272
Secondary accession number(s): A2VD03
<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: May 1, 1991
Last sequence update: May 1, 1991
Last modified: June 5, 2019
This is version 165 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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