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Protein Page:
C/EBP-epsilon (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
C/EBP-epsilon 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. Belongs to the bZIP family. C/EBP subfamily. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; DNA binding protein; Transcription factor
Molecular Function: protein homodimerization activity; sequence-specific DNA binding; protein heterodimerization activity; transcription factor activity
Biological Process: macrophage differentiation; transcription, DNA-dependent; cytokine biosynthetic process; defense response to bacterium; defense response; phagocytosis
Reference #:  Q15744 (UniProtKB)
Alt. Names/Synonyms: C/EBP epsilon; C/EBP-epsilon; CCAAT/enhancer binding protein (C/EBP), epsilon; CCAAT/enhancer-binding protein epsilon; CEBPE; CRP1
Gene Symbols: CEBPE
Molecular weight: 30,603 Da
Basal Isoelectric point: 9.13  Predict pI for various phosphorylation states
Select Structure to View Below

C/EBP-epsilon

Protein Structure Not Found.


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Sites Implicated In
cell differentiation, altered: T74‑p
transcription, induced: T74‑p
molecular association, regulation: T74‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
2 6 T74-p RGLKGPGtPAFPHYL
0 7 Y107-p KALGPGIySSPGSYD
2 0 K121-s DPRAVAVkEEPRGPE
0 6 S181-p ATAAPPCsPLLKAPs
0 1 S188-p sPLLKAPsPAGPLHK
0 1 L193 APsPAGPLHKGKKAV
  mouse

 
A74 RSLKGPGAPSFPHYL
Y107-p KALGPGIySNPGSYD
K121 DPRAVAVKEEPRGPE
S181-p AAAAPPCsPLLKAPs
S188-p sPLLKAPsPAGPsHK
S193-p APsPAGPsHKGKKAV
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