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Protein

CCAAT/enhancer-binding protein epsilon

Gene

CEBPE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional activator (PubMed:26019275). C/EBP are DNA-binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Required for the promyelocyte-myelocyte transition in myeloid differentiation (PubMed:10359588).2 Publications

GO - Molecular functioni

GO - Biological processi

  • cellular response to lipopolysaccharide Source: Ensembl
  • cytokine biosynthetic process Source: Ensembl
  • defense response Source: ProtInc
  • defense response to bacterium Source: Ensembl
  • granulocyte differentiation Source: UniProtKB
  • macrophage differentiation Source: Ensembl
  • phagocytosis Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB

Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

SIGNORiQ15744.

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein epsilon
Short name:
C/EBP epsilon
Gene namesi
Name:CEBPE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000092067.5.
HGNCiHGNC:1836. CEBPE.

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Specific granule deficiency 1 (SGD1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by recurrent pyogenic infections, defective neutrophil chemotaxis and bactericidal activity, and lack of neutrophil secondary granule proteins. Neutrophils of affected individuals lack lactoferrin and show abnormal nuclear segmentation, bilobed nuclei, low alkaline phosphatase, and increased number of neutrophil mitochondria and ribosomes.
See also OMIM:245480
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078996248 – 249Missing in SGD1; decreased function in positive regulation of DNA-templated transcription; loss of interaction with GATA1; decreased interaction with SPI1; no effect on localization to nucleus; no effect on DNA binding; no effect on dimerization. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1053.
MalaCardsiCEBPE.
MIMi245480. phenotype.
OpenTargetsiENSG00000092067.
Orphaneti169142. Recurrent infection due to specific granule deficiency.
PharmGKBiPA26379.

Polymorphism and mutation databases

BioMutaiCEBPE.
DMDMi62512175.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000766241 – 281CCAAT/enhancer-binding protein epsilonAdd BLAST281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei181PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15744.
MaxQBiQ15744.
PaxDbiQ15744.
PeptideAtlasiQ15744.
PRIDEiQ15744.

PTM databases

iPTMnetiQ15744.
PhosphoSitePlusiQ15744.

Expressioni

Tissue specificityi

Strongest expression occurs in promyelocyte and late-myeloblast-like cell lines.1 Publication

Gene expression databases

BgeeiENSG00000092067.
CleanExiHS_CEBPE.
GenevisibleiQ15744. HS.

Organism-specific databases

HPAiCAB005113.
HPA002928.

Interactioni

Subunit structurei

Binds DNA as a homodimer and as a heterodimer (PubMed:26019275). Can form stable heterodimers with CEBPA, CEBPB and CEBPD (By similarity). Interacts with GATA1 AND SPI1 (PubMed:26019275). Interacts with SMARCD2 (PubMed:28369036).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107482. 45 interactors.
CORUMiQ15744.
ELMiQ15744.
IntActiQ15744. 8 interactors.
MINTiMINT-6609345.
STRINGi9606.ENSP00000206513.

Structurei

Secondary structure

1281
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi37 – 47Combined sources11
Helixi50 – 57Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3T92X-ray1.50A37-61[»]
ProteinModelPortaliQ15744.
SMRiQ15744.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini204 – 267bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni208 – 228Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni230 – 237Leucine-zipperPROSITE-ProRule annotation8

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410ISXR. Eukaryota.
ENOG4111HY3. LUCA.
GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiQ15744.
KOiK10051.
OMAiCDHEASI.
OrthoDBiEOG091G11FC.
PhylomeDBiQ15744.
TreeFamiTF105008.

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.

Sequencei

Sequence statusi: Complete.

Q15744-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHGTYYECE PRGGQQPLEF SGGRAGPGEL GDMCEHEASI DLSAYIESGE
60 70 80 90 100
EQLLSDLFAV KPAPEARGLK GPGTPAFPHY LPPDPRPFAY PPHTFGPDRK
110 120 130 140 150
ALGPGIYSSP GSYDPRAVAV KEEPRGPEGS RAASRGSYNP LQYQVAHCGQ
160 170 180 190 200
TAMHLPPTLA APGQPLRVLK APLATAAPPC SPLLKAPSPA GPLHKGKKAV
210 220 230 240 250
NKDSLEYRLR RERNNIAVRK SRDKAKRRIL ETQQKVLEYM AENERLRSRV
260 270 280
EQLTQELDTL RNLFRQIPEA ANLIKGVGGC S
Length:281
Mass (Da):30,603
Last modified:April 12, 2005 - v2
Checksum:iB0A1DFA88C04C3D0
GO

Sequence cautioni

The sequence AAC51130 differs from that shown. Reason: Frameshift at position 4.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64P → S in AAC51130 (PubMed:9032264).Curated1
Sequence conflicti68G → R in AAC50708 (PubMed:8661101).Curated1
Sequence conflicti68G → R in AAC50709 (PubMed:8661101).Curated1
Sequence conflicti252Q → E in AAC51130 (PubMed:9032264).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078996248 – 249Missing in SGD1; decreased function in positive regulation of DNA-templated transcription; loss of interaction with GATA1; decreased interaction with SPI1; no effect on localization to nucleus; no effect on DNA binding; no effect on dimerization. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48865 Genomic DNA. Translation: AAC50708.1.
U48866 mRNA. Translation: AAC50709.1.
U80982 Genomic DNA. Translation: AAC51130.1. Frameshift.
BC035797 mRNA. Translation: AAH35797.2.
CCDSiCCDS9589.1.
RefSeqiNP_001796.2. NM_001805.3.
UniGeneiHs.558308.

Genome annotation databases

EnsembliENST00000206513; ENSP00000206513; ENSG00000092067.
GeneIDi1053.
KEGGihsa:1053.
UCSCiuc001wiv.3. human.

Similar proteinsi

Entry informationi

Entry nameiCEBPE_HUMAN
AccessioniPrimary (citable) accession number: Q15744
Secondary accession number(s): Q15745, Q8IYI2, Q99803
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 12, 2005
Last modified: September 27, 2017
This is version 153 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families