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UniProtKB - P05554 (CEBPA_RAT)

Entry version 173 (25 May 2022)
Sequence version 3 (01 Feb 1996)
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Protein

CCAAT/enhancer-binding protein alpha

Gene

Cebpa

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

Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta (PubMed:8367486, PubMed:11672531, PubMed:16735515, PubMed:20176812).

Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB (By similarity).

Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP) (PubMed:11672531).

Critical for the proper development of the liver and the lung (By similarity).

Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (PubMed:11672531).

To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Down-regulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters (PubMed:11672531).

Proliferation arrest also depends on a functional binding to SWI/SNF complex (By similarity).

In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC1. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity).

By similarity4 Publications

Can act as dominant-negative. Binds DNA and have transctivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation.

By similarity1 Publication

Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation.

By similarity

Miscellaneous

The V296A substitution has little effect on the binding of CEBPA to its consensus site (5'-GCAAT-3'), while greatly increasing affinity for cAMP response element (CRE) sites (5'-GTCAT-3').1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi285 – 3001 PublicationAdd BLAST16

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Developmental protein, DNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-9616222, Transcriptional regulation of granulopoiesis

<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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
CCAAT/enhancer-binding protein alphaImported
Short name:
C/EBP alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CebpaImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		2326, Cebpa

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi159K → A or R: Not sumoylated. No effect of sumoylation on cell cycle inhibition. 1 Publication1
Mutagenesisi285Y → A: Decreased transcription factor activity. Strongly decreased transcription factor activity; when associated with R-293. 1 Publication1
Mutagenesisi285Y → A: Increases interaction with TFDP1 and TFDP2, reduces DNA-binding, transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction. 2 Publications1
Mutagenesisi287V → A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-290. 1 Publication1
Mutagenesisi289R → A: Loss of DNA-binding and transcription factor activity. 1 Publication1
Mutagenesisi290E → A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-287. 1 Publication1
Mutagenesisi293N → R: Decreased transcription factor activity. Strongly decreased transcription factor activity; when associated with A-285. 1 Publication1
Mutagenesisi294I → A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-297. 2 Publications1
Mutagenesisi296V → A: No effect on DNA-binding and transcription factor activity, but modified sequence specificity. 1 Publication1
Mutagenesisi297R → A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-294. 2 Publications1
Mutagenesisi299S → D: Isoform 4: Stimulates nucleolar retention of isoform 4. No effect on interaction with NPM1, TAF1A and UBTF. 1 Publication1
Mutagenesisi301D → A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-304. 2 Publications1
Mutagenesisi304K → A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-301. 2 Publications1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000766151 – 358CCAAT/enhancer-binding protein alphaAdd BLAST358

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei159N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei193PhosphoserineBy similarity1
Modified residuei222Phosphothreonine; by GSK3By similarity1
Modified residuei226Phosphothreonine; by GSK3By similarity1
Modified residuei230Phosphoserine; by GSK3By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2.1 Publication
Phosphorylation at Ser-193 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-193 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation. Phosphorylation at Thr-222 and Thr-226 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-222 and Thr-226 are phosphorylated only during feeding but not during fasting. Phosphorylation of the GSK3 consensus sites selectively decreases transactivation activity on IRE-controlled promoters.By similarity
Ubiquitinated by COP1 upon interaction with TRIB1.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P05554

PRoteomics IDEntifications database

More...PRIDEi		P05554

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P05554

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

More...PhosphoSitePlusi		P05554

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

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

Isoform 2 and isoform 3 are not expressed at 1 day before birth, relative concentration of both isoforms increases with the age of the animal, reaching maximal levels in the adulthood.1 Publication

Gene expression databases

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P05554, 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%5Fsection">'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%5Fsection">'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:1884998, PubMed:8367486, PubMed:12578822). Can form stable heterodimers with CEBPB, CEBPD, CEBPE and CEBPG (PubMed:1884998, PubMed:1377818). Can form stable homodimers (also isoform 2 and isoform 3 dimers) and heterodimers with CEBPB (with isoform 2 and isoform 3) and CEBPG (PubMed:1377818, PubMed:8367486).

Interacts with PRDM16 (By similarity).

Interacts with UBN1 (By similarity).

Interacts with ZNF638; this interaction increases transcriptional activation (By similarity).

Interacts with the complex TFDP2:E2F1; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (By similarity).

Interacts with RB1 (By similarity).

Interacts (when phosphorylated at SER-193) with CDK2, CDK4, E2F4 and SMARCA2 (By similarity).

Interacts with SREBPF1 (By similarity).

Interacts with FOXO1 (via the Fork-head domain); the interaction increases when FOXO1 is deacetylated (By similarity).

Interacts with SIX1 (By similarity).

Interacts (via recognition sequence) with TRIB1 (By similarity).

By similarity5 Publications

Interacts with TAF1A and UBTF.

1 Publication

Interacts with NPM1.

1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		246437, 148 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-60, bZIP transcription factor complex, Cebpa-Ddit3
CPX-64, bZIP transcription factor complex, Cebpa-Cebpa

Database of interacting proteins

More...DIPi		DIP-28138N

Protein interaction database and analysis system

More...IntActi		P05554, 5 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000063123

<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

1358
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P05554

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

More...SMRi		P05554

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P05554

<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%5Fand%5Fdomains%5Fsection">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>Domaini282 – 345bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 70Required to repress E2F1:TFDP1-mediated transcription, to inhibit cell cycle and to induce adipocyte differentiation1 PublicationAdd BLAST70
Regioni1 – 55DisorderedSequence analysisAdd BLAST55
Regioni54 – 72Required for interaction with TRIB1By similarityAdd BLAST19
Regioni126 – 200Required to induce adipocyte differentiation1 PublicationAdd BLAST75
Regioni176 – 195DisorderedSequence analysisAdd BLAST20
Regioni180 – 194Required to functionally cooperate with SREBF1 in promoter activationBy similarityAdd BLAST15
Regioni213 – 310DisorderedSequence analysisAdd BLAST98
Regioni240 – 358Interaction with FOXO1By similarityAdd BLAST119
Regioni286 – 313Basic motifPROSITE-ProRule annotationAdd BLAST28
Regioni317 – 345Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi36 – 50Pro residuesSequence analysisAdd BLAST15
Compositional biasi177 – 194Pro residuesSequence analysisAdd BLAST18
Compositional biasi218 – 238Pro residuesSequence analysisAdd BLAST21
Compositional biasi277 – 309Basic and acidic residuesSequence analysisAdd BLAST33

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The recognition sequence (54-72) is required for interaction with TRIB1.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the bZIP family. C/EBP subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3119, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_043327_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P05554

Database of Orthologous Groups

More...OrthoDBi		1284308at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P05554

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
IPR046347, bZIP_sf
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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57959, SSF57959, 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%5Flength">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 (4)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 4 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform 1 (identifier: P05554-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MESADFYEAE PRPPMSSHLQ SPPHAPSNAA FGFPRGAGPA PPPAPPAAPE 
        60         70         80         90        100
PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAAGPAGG 
       110        120        130        140        150
GGDFDYPGAP AGPGGAVMSA GAHGPPPGYG CAAAGYLDGR LEPLYERVGA 
       160        170        180        190        200
PALRPLVIKQ EPREEDEAKQ LALAGLFPYQ PPPPPPPPHP HASPAHLAAP 
       210        220        230        240        250
HLQFQIAHCG QTTMHLQPGH PTPPPTPVPS PHPAPAMGAA GLPGPGGSLK 
       260        270        280        290        300
GLAGPHPDLR TGGGGGGGAG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR 
       310        320        330        340        350
DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL 

VKAMGNCA
Length:358
Mass (Da):37,371
Last modified:February 1, 1996 - v3
<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:i4DA8F112F6EA95D0
GO
Isoform 2 (identifier: P05554-2) [UniParc]FASTAAdd to basket
Also known as: CEBPalpha-p421 Publication

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

Show »
Length:344
Mass (Da):35,750
Checksum:i530FA6D51C5E7BDA
GO
Isoform 3 (identifier: P05554-3) [UniParc]FASTAAdd to basket
Also known as: C/EBPalpha-p301 Publication

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

Show »
Length:241
Mass (Da):25,526
Checksum:i16713D706888AA35
GO
Isoform 4 (identifier: P05554-4) [UniParc]FASTAAdd to basket
Also known as: extended-C/EBPalpha1 Publication

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

Note: Mutagenesis in position: 14: RRQR -> AAAA abolishes nucleolar localization and prevents induction of 45S pre-RNA.1 Publication
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Length:395
Mass (Da):41,440
Checksum:i01D1DA74BD4A48C8
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_0575511 – 117Missing in isoform 3. 1 PublicationAdd BLAST117
Alternative sequenceiVSP_0575521 – 14Missing in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_0576091M → MRGRGRVGVLGGRRRQRRHA QAGGRRGSPCRENSNSPM in isoform 4. 1

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
X12752 Genomic DNA Translation: CAA31242.1
AC109741 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...PIRi		S06890, A54265

NCBI Reference Sequences

More...RefSeqi		NP_001274506.1, NM_001287577.1 [P05554-4]
NP_001274507.1, NM_001287578.1 [P05554-2]
NP_001274508.1, NM_001287579.1 [P05554-3]
NP_036656.1, NM_012524.3 [P05554-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24252

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24252

UCSC genome browser

More...UCSCi		RGD:2326, rat [P05554-1]

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
X12752 Genomic DNA Translation: CAA31242.1
AC109741 Genomic DNA No translation available.
PIRiS06890, A54265
RefSeqiNP_001274506.1, NM_001287577.1 [P05554-4]
NP_001274507.1, NM_001287578.1 [P05554-2]
NP_001274508.1, NM_001287579.1 [P05554-3]
NP_036656.1, NM_012524.3 [P05554-1]

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
1NWQX-ray2.80A/C281-340[»]
AlphaFoldDBiP05554
SMRiP05554
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi246437, 148 interactors
ComplexPortaliCPX-60, bZIP transcription factor complex, Cebpa-Ddit3
CPX-64, bZIP transcription factor complex, Cebpa-Cebpa
DIPiDIP-28138N
IntActiP05554, 5 interactors
STRINGi10116.ENSRNOP00000063123

PTM databases

iPTMnetiP05554
PhosphoSitePlusiP05554

Proteomic databases

PaxDbiP05554
PRIDEiP05554

Genome annotation databases

GeneIDi24252
KEGGirno:24252
UCSCiRGD:2326, rat [P05554-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1050
RGDi2326, Cebpa

Phylogenomic databases

eggNOGiKOG3119, Eukaryota
HOGENOMiCLU_043327_2_0_1
InParanoidiP05554
OrthoDBi1284308at2759
PhylomeDBiP05554
TreeFamiTF105008

Enzyme and pathway databases

ReactomeiR-RNO-9616222, Transcriptional regulation of granulopoiesis

Miscellaneous databases

EvolutionaryTraceiP05554

Protein Ontology

More...PROi		PR:P05554

Gene expression databases

GenevisibleiP05554, RN

Family and domain databases

InterProiView protein in InterPro
IPR004827, bZIP
IPR046347, bZIP_sf
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
SUPFAMiSSF57959, SSF57959, 1 hit
PROSITEiView protein in PROSITE
PS50217, BZIP, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCEBPA_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: P05554
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1996
Last modified: May 25, 2022
This is version 173 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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