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Protein Page:
14-3-3 epsilon (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
14-3-3 epsilon a protein of the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. A multifunctional regulator of the cell signaling processes. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold
Cellular Component: kinesin complex; mitochondrion; melanosome; cytosol
Molecular Function: protein domain specific binding; protein binding; enzyme binding; histone deacetylase binding; phosphoprotein binding; phosphoserine binding
Biological Process: negative regulation of protein amino acid dephosphorylation; nerve growth factor receptor signaling pathway; apoptosis; virus-host interaction; hippocampus development; neuron migration; mitotic cell cycle; cerebral cortex development; G2/M transition of mitotic cell cycle; protein targeting
Reference #:  P62258 (UniProtKB)
Alt. Names/Synonyms: 14-3-3 epsilon; 14-3-3 protein epsilon; 14-3-3E; 1433E; FLJ45465; FLJ53559; KCIP-1; MDCR; MDS; mitochondrial import stimulation factor L subunit; protein kinase C inhibitor protein-1; tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon polypeptide; tyrosine 3/tryptophan 5 -monooxygenase activation protein, epsilon polypeptide; YWHAE
Gene Symbols: YWHAE
Molecular weight: 29,174 Da
Basal Isoelectric point: 4.63  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis  |  Cell Cycle: G2/M DNA Damage Checkpoint  |  Hippo Signaling  |  MAPK/Erk in Growth and Differentiation  |  Mitochondrial Control of Apoptosis  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

14-3-3 epsilon
Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: K50‑a, K118‑a, K123‑a

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

 
0 2 Y9 DDREDLVYQAkLAEQ
0 38 K12-u EDLVYQAkLAEQAER
0 4 K28-a DEMVESMkKVAGMDV
0 1 K28-u DEMVESMkKVAGMDV
0 1 K29 EMVESMkKVAGMDVE
0 1 T38-p AGMDVELtVEERNLL
0 9 S46-p VEERNLLsVAykNVI
0 5 Y49-p RNLLsVAykNVIGAR
0 2 K50-a NLLsVAykNVIGARR
0 116 K50-u NLLsVAykNVIGARR
0 2 S64-p RASWRIIssIEQkEE
0 1 S65-p ASWRIIssIEQkEEN
0 1 K69-a IIssIEQkEENkGGE
0 10 K69-u IIssIEQkEENkGGE
0 3 K73-u IEQkEENkGGEDKLk
0 2 K78 ENkGGEDKLkMIREY
0 3 K80-u kGGEDKLkMIREYRQ
0 3 T91-p EYRQMVEtELKLICC
0 38 K106-u DILDVLDkHLIPAAN
0 2 K106-a DILDVLDkHLIPAAN
0 3 K118-a AANTGESkVFYykMk
0 3 K118-u AANTGESkVFYykMk
0 5 Y122-p GESkVFYykMkGDYH
0 1 K123-a ESkVFYykMkGDYHR
0 15 K123-u ESkVFYykMkGDYHR
0 1 K125 kVFYykMKGDYHRyL
0 44 K125-u kVFYykMkGDYHRyL
0 3 Y131-p MkGDYHRyLAEFATG
0 1 T137 RyLAEFATGNDRkEA
0 2 K142-a FATGNDRkEAAENSL
0 42 K142-u FATGNDRkEAAENSL
0 2 K153-u ENSLVAYkAASDIAM
0 1 Y181-p ALNFSVFyYEILNSP
0 35 K196-u DRACRLAkAAFDDAI
1 2 T208-p DAIAELDtLsEEsyK
0 20 S210-p IAELDtLsEEsyKDS
0 1 S213-p LDtLsEEsyKDSTLI
1 3 Y214-p DtLsEEsyKDSTLIM
0 1 S233 DNLTLWTSDMQGdGE
0 1 D238-ca WTSDMQGdGEEQNkE
0 4 K244-u GdGEEQNkEALQDVE
  mouse

 
Y9-p DDREDLVyQAkLAEQ
K12-u EDLVyQAkLAEQAER
K28-a DEMVESMkkVAGMDV
K28 DEMVESMKkVAGMDV
K29-u EMVESMkkVAGMDVE
T38 AGMDVELTVEERNLL
S46-p VEERNLLsVAykNVI
Y49-p RNLLsVAykNVIGAR
K50 NLLsVAyKNVIGARR
K50-u NLLsVAykNVIGARR
S64 RASWRIISSIEQkEE
S65 ASWRIISSIEQkEEN
K69 IISSIEQKEENkGGE
K69-u IISSIEQkEENkGGE
K73-u IEQkEENkGGEDkLk
K78-u ENkGGEDkLkMIREY
K80-u kGGEDkLkMIREYRQ
T91 EYRQMVETELKLICC
K106-u DILDVLDkHLIPAAN
K106-a DILDVLDkHLIPAAN
K118 AANTGESKVFYYkMk
K118-u AANTGESkVFYYkMk
Y122 GESkVFYYkMkGDYH
K123 ESkVFYYKMkGDYHR
K123-u ESkVFYYkMkGDYHR
K125-a kVFYYkMkGDYHRyL
K125-u kVFYYkMkGDYHRyL
Y131-p MkGDYHRyLAEFAtG
T137-p RyLAEFAtGNDRkEA
K142 FAtGNDRKEAAENSL
K142-u FAtGNDRkEAAENSL
K153 ENSLVAYKAASDIAM
Y181 ALNFSVFYYEILNSP
K196-u DRACRLAkAAFDDAI
T208 DAIAELDTLsEESyK
S210-p IAELDTLsEESyKDS
S213 LDTLsEESyKDSTLI
Y214-p DTLsEESyKDSTLIM
S233-p DNLTLWTsDMQGDGE
D238 WTsDMQGDGEEQNkE
K244-u GDGEEQNkEALQDVE
  rat

 
Y9 DDREDLVYQAkLAEQ
K12-u EDLVYQAkLAEQAER
K28 DEMVESMKKVAGMDV
K28 DEMVESMKKVAGMDV
K29 EMVESMKKVAGMDVE
T38 AGMDVELTVEERNLL
S46 VEERNLLSVAYkNVI
Y49 RNLLSVAYkNVIGAR
K50 NLLSVAYKNVIGARR
K50-u NLLSVAYkNVIGARR
S64 RASWRIISSIEQKEE
S65 ASWRIISSIEQKEEN
K69 IISSIEQKEENKGGE
K69 IISSIEQKEENKGGE
K73 IEQKEENKGGEDKLK
K78 ENKGGEDKLKMIREY
K80 KGGEDKLKMIREYRQ
T91 EYRQMVETELKLICC
K106-u DILDVLDkHLIPAAN
K106 DILDVLDKHLIPAAN
K118 AANTGESKVFYYKMK
K118 AANTGESKVFYYKMK
Y122 GESKVFYYKMKGDYH
K123 ESKVFYYKMKGDYHR
K123 ESKVFYYKMKGDYHR
K125 KVFYYKMKGDYHRYL
K125 KVFYYKMKGDYHRYL
Y131 MKGDYHRYLAEFATG
T137 RYLAEFATGNDRkEA
K142 FATGNDRKEAAENSL
K142-u FATGNDRkEAAENSL
K153 ENSLVAYKAASDIAM
Y181 ALNFSVFYYEILNSP
K196 DRACRLAKAAFDDAI
T208 DAIAELDTLSEESYK
S210 IAELDTLSEESYKDS
S213 LDTLSEESYKDSTLI
Y214 DTLSEESYKDSTLIM
S233 DNLTLWTSDMQGDGE
D238 WTSDMQGDGEEQNKE
K244 GDGEEQNKEALQDVE
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