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UniProtKB - P49715 (CEBPA_HUMAN)

Entry version 185 (08 May 2019)
Sequence version 3 (05 Feb 2008)
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Protein

CCAAT/enhancer-binding protein alpha

Gene

CEBPA

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

Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes (PubMed:11242107). During early embryogenesis, plays essential and redundant functions with CEBPB. Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). 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 (By similarity). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Downregulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters. Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC. 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 similarity2 Publications
Isoform 3: Can act as dominant-negative. Binds DNA and have transctivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation (PubMed:14660596).By similarity1 Publication
Isoform 4: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi285 – 300By similarityAdd BLAST16

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

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, Developmental protein, DNA-binding
Biological processHost-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-381340 Transcriptional regulation of white adipocyte differentiation

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

More...SignaLinki		P49715

SIGNOR Signaling Network Open Resource

More...SIGNORi		P49715

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
CCAAT/enhancer-binding protein alphaImported
Short name:
C/EBP alphaImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CEBPAImported
Synonyms:CEBPImported
<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 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:1833 CEBPA

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		116897 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P49715

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Leukemia, acute myelogenous (AML)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.
See also OMIM:601626
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_07267784H → L in AML; no effect on expression; no effect on DNA-binding or transactivation activity. 1 PublicationCorresponds to variant dbSNP:rs28931590EnsemblClinVar.1
Natural variantiVAR_072678312Q → QK in AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity. 1 Publication1

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>Mutagenesisi55I → A: Decreased interaction with TRIB1. 1 Publication1
Mutagenesisi57E → T: No effect on interaction with TRIB1. 1 Publication1
Mutagenesisi58H → D: No effect on interaction with TRIB1. 1 Publication1
Mutagenesisi59E → A: Decreased interaction with TRIB1. 1 Publication1
Mutagenesisi61S → A: Decreased interaction with TRIB1. 1 Publication1
Mutagenesisi62I → A: Decreased interaction with TRIB1. 1 Publication1
Mutagenesisi63D → A: No effect on interaction with TRIB1. 1 Publication1
Mutagenesisi64I → A: Decreased interaction with TRIB1. 1 Publication1
Mutagenesisi65S → A: No effect on interaction with TRIB1. 1 Publication1
Mutagenesisi67Y → A: Decreased interaction with TRIB1. 1 Publication1
Mutagenesisi67Y → F: No effect on interaction with TRIB1. 1 Publication1
Mutagenesisi68I → A: Decreased interaction with TRIB1. 1 Publication1
Mutagenesisi69D → A: No effect on interaction with TRIB1. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		1050

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		CEBPA

MalaCards human disease database

More...MalaCardsi		CEBPA
MIMi601626 phenotype

Open Targets

More...OpenTargetsi		ENSG00000245848

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		319480 Acute myeloid leukemia with CEBPA somatic mutations
102724 Acute myeloid leukemia with t(8;21)(q22;q22) translocation
319465 Inherited acute myeloid leukemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26376

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CEBPA

Domain mapping of disease mutations (DMDM)

More...DMDMi		166898082

<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_00000766131 – 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 residuei161N6-acetyllysine; alternateCombined sources1
<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-linki161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei190Phosphoserine1 Publication1
Modified residuei226Phosphothreonine; by GSK3By similarity1
Modified residuei230Phosphothreonine; by GSK3By similarity1
Modified residuei234Phosphoserine; by GSK3By similarity1

<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

Phosphorylation at Ser-190 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-190 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation (PubMed:15107404). Phosphorylation at Thr-226 and Thr-230 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-226 and Thr-230 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
Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2.By similarity
Ubiquitinated by COP1 upon interaction with TRIB1.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P49715

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P49715

MaxQB - The MaxQuant DataBase

More...MaxQBi		P49715

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

More...PaxDbi		P49715

PeptideAtlas

More...PeptideAtlasi		P49715

PRoteomics IDEntifications database

More...PRIDEi		P49715

ProteomicsDB human proteome resource

More...ProteomicsDBi		56054

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P49715

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

More...PhosphoSitePlusi		P49715

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000245848 Expressed in 209 organ(s), highest expression level in adipose tissue of abdominal region

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P49715 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA052734
HPA065037
HPA067937

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds DNA as a homodimer and as a heterodimer. Can form stable heterodimers with CEBPB, CEBPD, CEBPE and CEBPG (By similarity). Interacts with PRDM16 (By similarity). Interacts with UBN1 (PubMed:10725330). 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 (PubMed:20176812). Interacts with RB1 (PubMed:15107404). Interacts (when phosphorylated at SER-190) with CDK2, CDK4, E2F4 and SMARCA2 (PubMed:15107404). Interacts with SREBPF1 (By similarity). Interacts with FOXO1 (via the Fork-head domain); the interaction increases when FOXO1 is deacetylated (By similarity). Isoform 1 and isoform 4 interacts with TAF1A and UBTF (PubMed:20075868). Isoform 4 interacts with NPM1 (PubMed:20075868). Interacts (via recognition sequence) with TRIB1 (PubMed:20410507, PubMed:26455797).By similarity6 Publications
(Microbial infection) Interacts with HBV protein X.1 Publication

<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		107479, 99 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-69 CHOP-C/EBPalpha complex
CPX-71 C/EBPalpha complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P49715

Database of interacting proteins

More...DIPi		DIP-37882N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P49715

Protein interaction database and analysis system

More...IntActi		P49715, 23 interactors

Molecular INTeraction database

More...MINTi		P49715

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000427514

<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

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
6DC0X-ray2.80A/B51-75[»]

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

More...SMRi		P49715

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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>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 differentiationBy similarityAdd BLAST70
Regioni54 – 72Required for interaction with TRIB11 PublicationAdd BLAST19
Regioni128 – 204Required to induce adipocyte differentiationBy similarityAdd BLAST77
Regioni182 – 198Required to functionally cooperate with SREBF1 in promoter activationBy similarityAdd BLAST17
Regioni244 – 358Interaction with FOXO1By similarityAdd BLAST115
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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi99 – 104Poly-Gly6
Compositional biasi183 – 189Poly-Pro7

<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 TRIB1.1 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		KOG3119 Eukaryota
ENOG410YJ8G LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000162646

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000013112

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P49715

KEGG Orthology (KO)

More...KOi		K09055

Identification of Orthologs from Complete Genome Data

More...OMAi		QIAHCAQ

Database of Orthologous Groups

More...OrthoDBi		1284308at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P49715

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 (4)i

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

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform 1 (identifier: P49715-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MESADFYEAE PRPPMSSHLQ SPPHAPSSAA FGFPRGAGPA QPPAPPAAPE 
        60         70         80         90        100
PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAVGPTGG 
       110        120        130        140        150
GGGGDFDYPG APAGPGGAVM PGGAHGPPPG YGCAAAGYLD GRLEPLYERV 
       160        170        180        190        200
GAPALRPLVI KQEPREEDEA KQLALAGLFP YQPPPPPPPS HPHPHPPPAH 
       210        220        230        240        250
LAAPHLQFQI AHCGQTTMHL QPGHPTPPPT PVPSPHPAPA LGAAGLPGPG 
       260        270        280        290        300
SALKGLGAAH PDLRASGGSG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR 
       310        320        330        340        350
DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL 

VKAMGNCA
Length:358
Mass (Da):37,561
Last modified:February 5, 2008 - 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:i574C0A049E25BCAC
GO
Isoform 2 (identifier: P49715-2) [UniParc]FASTAAdd to basket
Also known as: C/EBPalpha-p421 Publication

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

Show »
Length:344
Mass (Da):35,940
Checksum:i49EB5DC3749152A6
GO
Isoform 3 (identifier: P49715-3) [UniParc]FASTAAdd to basket
Also known as: C/EBPalpha-p301 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Show »
Length:239
Mass (Da):25,540
Checksum:i4A9F7812303016A0
GO
Isoform 4 (identifier: P49715-4) [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 → MRGRGRAGSPGGRRRRPAQAGGRRGSPCRENSNSPM

Show »
Length:393
Mass (Da):41,249
Checksum:i123630D5A4AD5634
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 conflicti40 – 41AQ → PK in AAC50235 (PubMed:7575576).Curated2
Sequence conflicti95 – 98VGPT → WAH in CAA72289 (Ref. 2) Curated4
Sequence conflicti241L → V in CAA72289 (Ref. 2) Curated1
Sequence conflicti248 – 250GPG → ALA in CAA72289 (Ref. 2) Curated3
Sequence conflicti269S → T in AAC50235 (PubMed:7575576).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07267784H → L in AML; no effect on expression; no effect on DNA-binding or transactivation activity. 1 PublicationCorresponds to variant dbSNP:rs28931590EnsemblClinVar.1
Natural variantiVAR_072678312Q → QK in AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity. 1 Publication1

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_0575471 – 119Missing in isoform 3. Add BLAST119
Alternative sequenceiVSP_0575481 – 14Missing in isoform 2. Add BLAST14
Alternative sequenceiVSP_0576071M → MRGRGRAGSPGGRRRRPAQA GGRRGSPCRENSNSPM 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
U34070 Genomic DNA Translation: AAC50235.1
Y11525 mRNA Translation: CAA72289.1
EU048234 Genomic DNA Translation: ABS82765.1
AC008738 Genomic DNA No translation available.
BC027902 mRNA Translation: AAH27902.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS54243.1 [P49715-1]

Protein sequence database of the Protein Information Resource

More...PIRi		JC4311

NCBI Reference Sequences

More...RefSeqi		NP_001272758.1, NM_001285829.1 [P49715-3]
NP_001274353.1, NM_001287424.1 [P49715-4]
NP_001274364.1, NM_001287435.1 [P49715-2]
NP_004355.2, NM_004364.4 [P49715-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000498907; ENSP00000427514; ENSG00000245848 [P49715-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1050

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1050

UCSC genome browser

More...UCSCi		uc002nun.4 human [P49715-1]

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

<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

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34070 Genomic DNA Translation: AAC50235.1
Y11525 mRNA Translation: CAA72289.1
EU048234 Genomic DNA Translation: ABS82765.1
AC008738 Genomic DNA No translation available.
BC027902 mRNA Translation: AAH27902.1
CCDSiCCDS54243.1 [P49715-1]
PIRiJC4311
RefSeqiNP_001272758.1, NM_001285829.1 [P49715-3]
NP_001274353.1, NM_001287424.1 [P49715-4]
NP_001274364.1, NM_001287435.1 [P49715-2]
NP_004355.2, NM_004364.4 [P49715-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6DC0X-ray2.80A/B51-75[»]
SMRiP49715
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107479, 99 interactors
ComplexPortaliCPX-69 CHOP-C/EBPalpha complex
CPX-71 C/EBPalpha complex
CORUMiP49715
DIPiDIP-37882N
ELMiP49715
IntActiP49715, 23 interactors
MINTiP49715
STRINGi9606.ENSP00000427514

PTM databases

iPTMnetiP49715
PhosphoSitePlusiP49715

Polymorphism and mutation databases

BioMutaiCEBPA
DMDMi166898082

Proteomic databases

EPDiP49715
jPOSTiP49715
MaxQBiP49715
PaxDbiP49715
PeptideAtlasiP49715
PRIDEiP49715
ProteomicsDBi56054

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		1050
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000498907; ENSP00000427514; ENSG00000245848 [P49715-1]
GeneIDi1050
KEGGihsa:1050
UCSCiuc002nun.4 human [P49715-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1050
DisGeNETi1050

GeneCards: human genes, protein and diseases

More...GeneCardsi		CEBPA
GeneReviewsiCEBPA

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0040095
HGNCiHGNC:1833 CEBPA
HPAiHPA052734
HPA065037
HPA067937
MalaCardsiCEBPA
MIMi116897 gene
601626 phenotype
neXtProtiNX_P49715
OpenTargetsiENSG00000245848
Orphaneti319480 Acute myeloid leukemia with CEBPA somatic mutations
102724 Acute myeloid leukemia with t(8;21)(q22;q22) translocation
319465 Inherited acute myeloid leukemia
PharmGKBiPA26376

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3119 Eukaryota
ENOG410YJ8G LUCA
GeneTreeiENSGT00940000162646
HOGENOMiHOG000013112
InParanoidiP49715
KOiK09055
OMAiQIAHCAQ
OrthoDBi1284308at2759
PhylomeDBiP49715
TreeFamiTF105008

Enzyme and pathway databases

ReactomeiR-HSA-381340 Transcriptional regulation of white adipocyte differentiation
SignaLinkiP49715
SIGNORiP49715

Miscellaneous databases

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

More...ChiTaRSi		CEBPA human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CEBPA

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

More...GenomeRNAii		1050

Protein Ontology

More...PROi		PR:P49715

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000245848 Expressed in 209 organ(s), highest expression level in adipose tissue of abdominal region
GenevisibleiP49715 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 nameiCEBPA_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: P49715
Secondary accession number(s): A7LNP2, P78319, Q05CA4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 5, 2008
Last modified: May 8, 2019
This is version 185 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
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 19
    Human chromosome 19: 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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