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P49715 (CEBPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CCAAT/enhancer-binding protein alpha

Short name=C/EBP alpha
Gene names
Name:CEBPA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

C/EBP is a DNA-binding protein that recognizes two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers.

Subunit structure

Interacts with PRDM16 By similarity. Binds DNA as a dimer and can form stable heterodimers with C/EBP beta and gamma. Interacts with UBN1. Interacts with HBV protein X. Interacts with ZNF638; this interaction increases transcriptional activation By similarity. Ref.5 Ref.6

Subcellular location

Nucleus.

Sequence similarities

Belongs to the bZIP family. C/EBP subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: Ensembl

brown fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: Ensembl

cytokine-mediated signaling pathway

Non-traceable author statement PubMed 15664994. Source: UniProtKB

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

generation of precursor metabolites and energy

Traceable author statement PubMed 8643605. Source: ProtInc

inner ear development

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

macrophage differentiation

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

myeloid cell differentiation

Non-traceable author statement PubMed 15664994. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase III promoter

Inferred from direct assay PubMed 12695546. Source: UniProtKB

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to vitamin B2

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement PubMed 8643605. Source: ProtInc

transcription, DNA-templated

Inferred from direct assay PubMed 15664994. Source: UniProtKB

urea cycle

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

white fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentRb-E2F complex

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from electronic annotation. Source: Ensembl

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 8643605. Source: ProtInc

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.1. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12695546PubMed 15664994. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 15664994. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 12695546. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDX1P479023EBI-1172054,EBI-8514176
E2P031222EBI-1172054,EBI-7028618From a different organism.
E2P064224EBI-1172054,EBI-7136851From a different organism.
PARP1P098742EBI-1172054,EBI-355676

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358CCAAT/enhancer-binding protein alpha
PRO_0000076613

Regions

Domain282 – 34564bZIP
Region286 – 31328Basic motif By similarity
Region317 – 34529Leucine-zipper By similarity
Compositional bias99 – 1046Poly-Gly
Compositional bias183 – 1897Poly-Pro

Amino acid modifications

Modified residue1611N6-acetyllysine Ref.7

Experimental info

Sequence conflict40 – 412AQ → PK in AAC50235. Ref.1
Sequence conflict95 – 984VGPT → WAH in CAA72289. Ref.2
Sequence conflict2411L → V in CAA72289. Ref.2
Sequence conflict248 – 2503GPG → ALA in CAA72289. Ref.2
Sequence conflict2691S → T in AAC50235. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49715 [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: 574C0A049E25BCAC

FASTA35837,561
        10         20         30         40         50         60 
MESADFYEAE PRPPMSSHLQ SPPHAPSSAA FGFPRGAGPA QPPAPPAAPE PLGGICEHET 

        70         80         90        100        110        120 
SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAVGPTGG GGGGDFDYPG APAGPGGAVM 

       130        140        150        160        170        180 
PGGAHGPPPG YGCAAAGYLD GRLEPLYERV GAPALRPLVI KQEPREEDEA KQLALAGLFP 

       190        200        210        220        230        240 
YQPPPPPPPS HPHPHPPPAH LAAPHLQFQI AHCGQTTMHL QPGHPTPPPT PVPSPHPAPA 

       250        260        270        280        290        300 
LGAAGLPGPG SALKGLGAAH PDLRASGGSG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR 

       310        320        330        340        350 
DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL VKAMGNCA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, sequence, and expression patterns of the human gene encoding CCAAT/enhancer binding protein alpha (C/EBP alpha)."
Antonson P., Xanthopoulos K.G.
Biochem. Biophys. Res. Commun. 215:106-113(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Umbilical cord.
[2]"Transcription factor C/EBP-alpha: novel sites of expression and cloning of the human gene."
Swart G.W.M., van Groningen J.J.M., van Ruissen F., Bergers M., Schalwijk J.
Biol. Chem. Hoppe-Seyler 378:373-379(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]SeattleSNPs variation discovery resource
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-133.
Tissue: Pancreas.
[5]"Interaction of hepatitis B viral X protein and CCAAT/enhancer-binding protein alpha synergistically activates the hepatitis B viral enhancer II/pregenomic promoter."
Choi B.H., Park G.T., Rho H.M.
J. Biol. Chem. 274:2858-2865(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HBV PROTEIN X.
[6]"Ubinuclein, a novel nuclear protein interacting with cellular and viral transcription factors."
Aho S., Buisson M., Pajunen T., Ryoo Y.W., Giot J.-F., Gruffat H., Sergeant A., Uitto J.
J. Cell Biol. 148:1165-1176(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBN1.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U34070 Genomic DNA. Translation: AAC50235.1.
Y11525 mRNA. Translation: CAA72289.1.
EU048234 Genomic DNA. Translation: ABS82765.1.
BC027902 mRNA. Translation: AAH27902.1.
PIRJC4311.
RefSeqNP_004355.2. NM_004364.4.
UniGeneHs.76171.

3D structure databases

ProteinModelPortalP49715.
SMRP49715. Positions 281-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107479. 95 interactions.
IntActP49715. 13 interactions.
MINTMINT-264048.

PTM databases

PhosphoSiteP49715.

Polymorphism databases

DMDM166898082.

Proteomic databases

PRIDEP49715.

Protocols and materials databases

DNASU1050.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000498907; ENSP00000427514; ENSG00000245848.
GeneID1050.
KEGGhsa:1050.
UCSCuc002nun.3. human.

Organism-specific databases

CTD1050.
GeneCardsGC19M033790.
H-InvDBHIX0040095.
HGNCHGNC:1833. CEBPA.
MIM116897. gene.
neXtProtNX_P49715.
Orphanet319480. Acute myeloid leukemia with CEBPA somatic mutations.
102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
319465. Inherited acute myeloid leukemia.
PharmGKBPA26376.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000013112.
HOVERGENHBG050879.
InParanoidP49715.
KOK09055.
OMAPPPGYGC.
OrthoDBEOG7R56TQ.
PhylomeDBP49715.
TreeFamTF105008.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkP49715.

Gene expression databases

BgeeP49715.
CleanExHS_CEBPA.
GenevestigatorP49715.

Family and domain databases

InterProIPR004827. bZIP.
IPR016468. CCAAT/enhancer-binding.
[Graphical view]
PfamPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCEBPA.
GenomeRNAi1050.
NextBio4397.
PROP49715.
SOURCESearch...

Entry information

Entry nameCEBPA_HUMAN
AccessionPrimary (citable) accession number: P49715
Secondary accession number(s): A7LNP2, P78319, Q05CA4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM