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Protein Page:
14-3-3 epsilon (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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
Chromosomal Location of Human Ortholog: 17p13.3
Cellular Component: kinesin complex; cytoplasmic vesicle membrane; focal adhesion; membrane; mitochondrion; axon; melanosome; cytosol
Molecular Function: protein domain specific binding; protein binding; enzyme binding; potassium channel regulator activity; protein heterodimerization activity; histone deacetylase binding; phosphoprotein binding; phosphoserine binding
Biological Process: nerve growth factor receptor signaling pathway; viral reproduction; apoptosis; organelle organization and biogenesis; hippocampus development; neuron migration; regulation of caspase activity; regulation of the rate of heart contraction by hormone; substantia nigra development; cerebral cortex development; mitotic cell cycle; G2/M transition of mitotic cell cycle; protein targeting
Disease: Miller-dieker Lissencephaly Syndrome
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
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‑ac, K118‑ac, K123‑ac

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


 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
0 2 Y9 DDREDLVYQAkLAEQ
0 2 K12-ac EDLVYQAkLAEQAER
0 38 K12-ub EDLVYQAkLAEQAER
0 4 K28-ac DEMVESMkkVAGMDV
0 1 K28-ub DEMVESMkkVAGMDV
0 1 K28-sc DEMVESMkkVAGMDV
0 1 K29-ub EMVESMkkVAGMDVE
0 2 T38-p AGMDVELtVEERNLL
0 18 S46-p VEERNLLsVAykNVI
0 6 Y49-p RNLLsVAykNVIGAR
0 3 K50-ac NLLsVAykNVIGARR
0 115 K50-ub NLLsVAykNVIGARR
0 1 K50-sc NLLsVAykNVIGARR
0 3 S64-p RASWRIIssIEQkEE
0 2 S65-p ASWRIIssIEQkEEN
0 3 K69-ac IIssIEQkEENkGGE
0 10 K69-ub IIssIEQkEENkGGE
0 1 K73 IEQkEENKGGEDKLk
0 3 K73-ub IEQkEENkGGEDKLk
0 1 K78 ENkGGEDKLkMIREY
0 2 K78 ENkGGEDKLkMIREY
0 3 K80-ub kGGEDKLkMIREYRQ
0 3 T91-p EYRQMVEtELKLICC
0 37 K106-ub DILDVLDkHLIPAAN
0 2 K106-ac DILDVLDkHLIPAAN
0 5 K118-ac AANTGESkVFYykMk
0 3 K118-ub AANTGESkVFYykMk
0 1 K118-sc AANTGESkVFYykMk
0 6 Y122-p GESkVFYykMkGDYH
0 2 K123-ac ESkVFYykMkGDYHR
0 15 K123-ub ESkVFYykMkGDYHR
0 1 K123-sc ESkVFYykMkGDYHR
0 2 K125 kVFYykMKGDYHRyL
0 44 K125-ub kVFYykMkGDYHRyL
0 7 Y131-p MkGDYHRyLAEFATG
0 2 T137 RyLAEFATGNDRkEA
0 4 K142-ac FATGNDRkEAAENsL
0 41 K142-ub FATGNDRkEAAENsL
0 1 K142-sc FATGNDRkEAAENsL
0 1 S148-p RkEAAENsLVAYkAA
0 1 K153-ac ENsLVAYkAASDIAM
0 2 K153-ub ENsLVAYkAASDIAM
0 1 Y181-p ALNFSVFyYEILNSP
0 1 K196 DRACRLAKAAFDDAI
0 34 K196-ub DRACRLAkAAFDDAI
1 2 T208-p DAIAELDtLsEEsyK
0 35 S210-p IAELDtLsEEsyKDS
0 2 S213-p LDtLsEEsyKDSTLI
1 4 Y214-p DtLsEEsyKDSTLIM
0 1 T232-p RDNLTLWtsDMQGdG
0 5 S233-p DNLTLWtsDMQGdGE
0 1 D238-ca WtsDMQGdGEEQNkE
0 4 K244-ub GdGEEQNkEALQDVE
  14-3-3 epsilon iso2  
- gap
- gap
- gap
K6 __MVESMKKVAGMDV
K6 __MVESMKKVAGMDV
K6 __MVESMKKVAGMDV
K7 _MVESMKKVAGMDVE
T16 AGMDVELTVEERNLL
S24 VEERNLLSVAYKNVI
Y27 RNLLSVAYKNVIGAR
K28 NLLSVAYKNVIGARR
K28 NLLSVAYKNVIGARR
K28 NLLSVAYKNVIGARR
S42 RASWRIISSIEQKEE
S43 ASWRIISSIEQKEEN
K47 IISSIEQKEENKGGE
K47 IISSIEQKEENKGGE
K51 IEQKEENKGGEDKLK
K51 IEQKEENKGGEDKLK
K56 ENKGGEDKLKMIREY
K56 ENKGGEDKLKMIREY
K58 KGGEDKLKMIREYRQ
T69 EYRQMVETELKLICC
K84 DILDVLDKHLIPAAN
K84 DILDVLDKHLIPAAN
K96 AANTGESKVFYYKMK
K96 AANTGESKVFYYKMK
K96 AANTGESKVFYYKMK
Y100 GESKVFYYKMKGDYH
K101 ESKVFYYKMKGDYHR
K101 ESKVFYYKMKGDYHR
K101 ESKVFYYKMKGDYHR
K103 KVFYYKMKGDYHRYL
K103 KVFYYKMKGDYHRYL
Y109 MKGDYHRYLAEFATG
T115 RYLAEFATGNDRKEA
K120 FATGNDRKEAAENSL
K120 FATGNDRKEAAENSL
K120 FATGNDRKEAAENSL
S126 RKEAAENSLVAYKAA
K131 ENSLVAYKAASDIAM
K131 ENSLVAYKAASDIAM
Y159 ALNFSVFYYEILNSP
K174 DRACRLAKAAFDDAI
K174 DRACRLAKAAFDDAI
T186 DAIAELDTLSEESYK
S188 IAELDTLSEESYKDS
S191 LDTLSEESYKDSTLI
Y192 DTLSEESYKDSTLIM
T210 RDNLTLWTSDMQGDG
S211 DNLTLWTSDMQGDGE
D216 WTSDMQGDGEEQNKE
K222 GDGEEQNKEALQDVE
  mouse

 
Y9-p DDREDLVyQAkLAEQ
K12-ac EDLVyQAkLAEQAER
K12-ub EDLVyQAkLAEQAER
K28-ac DEMVESMkkVAGMDV
K28 DEMVESMKkVAGMDV
K28 DEMVESMKkVAGMDV
K29-ub EMVESMkkVAGMDVE
T38 AGMDVELTVEERNLL
S46-p VEERNLLsVAykNVI
Y49-p RNLLsVAykNVIGAR
K50 NLLsVAyKNVIGARR
K50-ub NLLsVAykNVIGARR
K50 NLLsVAyKNVIGARR
S64 RASWRIISSIEQkEE
S65 ASWRIISSIEQkEEN
K69-ac IISSIEQkEENkGGE
K69-ub IISSIEQkEENkGGE
K73 IEQkEENKGGEDkLk
K73-ub IEQkEENkGGEDkLk
K78 ENkGGEDKLkMIREY
K78-ub ENkGGEDkLkMIREY
K80-ub kGGEDkLkMIREYRQ
T91 EYRQMVETELKLICC
K106-ub DILDVLDkHLIPAAN
K106-ac DILDVLDkHLIPAAN
K118-ac AANTGESkVFYYkMk
K118-ub AANTGESkVFYYkMk
K118-sc AANTGESkVFYYkMk
Y122 GESkVFYYkMkGDYH
K123 ESkVFYYKMkGDYHR
K123-ub ESkVFYYkMkGDYHR
K123 ESkVFYYKMkGDYHR
K125-ac kVFYYkMkGDYHRyL
K125-ub kVFYYkMkGDYHRyL
Y131-p MkGDYHRyLAEFAtG
T137-p RyLAEFAtGNDRkEA
K142-ac FAtGNDRkEAAENSL
K142-ub FAtGNDRkEAAENSL
K142-sc FAtGNDRkEAAENSL
S148 RkEAAENSLVAYkAA
K153-ac ENSLVAYkAASDIAM
K153 ENSLVAYKAASDIAM
Y181 ALNFSVFYYEILNSP
K196-ac DRACRLAkAAFDDAI
K196-ub DRACRLAkAAFDDAI
T208 DAIAELDTLsEESyK
S210-p IAELDTLsEESyKDS
S213 LDTLsEESyKDSTLI
Y214-p DTLsEESyKDSTLIM
T232 RDNLTLWTsDMQGDG
S233-p DNLTLWTsDMQGDGE
D238 WTsDMQGDGEEQNkE
K244-ub GDGEEQNkEALQDVE
  rat

 
Y9 DDREDLVYQAkLAEQ
K12-ac EDLVYQAkLAEQAER
K12-ub EDLVYQAkLAEQAER
K28 DEMVESMKKVAGMDV
K28 DEMVESMKKVAGMDV
K28 DEMVESMKKVAGMDV
K29 EMVESMKKVAGMDVE
T38 AGMDVELTVEERNLL
S46-p VEERNLLsVAYkNVI
Y49 RNLLsVAYkNVIGAR
K50-ac NLLsVAYkNVIGARR
K50-ub NLLsVAYkNVIGARR
K50 NLLsVAYKNVIGARR
S64 RASWRIISsIEQkEE
S65-p ASWRIISsIEQkEEN
K69-ac IISsIEQkEENkGGE
K69 IISsIEQKEENkGGE
K73-ac IEQkEENkGGEDkLK
K73 IEQkEENKGGEDkLK
K78-ac ENkGGEDkLKMIREY
K78 ENkGGEDKLKMIREY
K80 kGGEDkLKMIREYRQ
T91 EYRQMVETELKLICC
K106-ub DILDVLDkHLIPAAN
K106 DILDVLDKHLIPAAN
K118-ac AANTGESkVFYYkMk
K118 AANTGESKVFYYkMk
K118 AANTGESKVFYYkMk
Y122 GESkVFYYkMkGDYH
K123-ac ESkVFYYkMkGDYHR
K123 ESkVFYYKMkGDYHR
K123 ESkVFYYKMkGDYHR
K125-ac kVFYYkMkGDYHRyL
K125 kVFYYkMKGDYHRyL
Y131-p MkGDYHRyLAEFAtG
T137-p RyLAEFAtGNDRkEA
K142-ac FAtGNDRkEAAENSL
K142-ub FAtGNDRkEAAENSL
K142 FAtGNDRKEAAENSL
S148 RkEAAENSLVAYKAA
K153 ENSLVAYKAASDIAM
K153 ENSLVAYKAASDIAM
Y181 ALNFSVFYYEILNSP
K196 DRACRLAKAAFDDAI
K196 DRACRLAKAAFDDAI
T208 DAIAELDTLsEEsYK
S210-p IAELDTLsEEsYKDS
S213-p LDTLsEEsYKDSTLI
Y214 DTLsEEsYKDSTLIM
T232 RDNLTLWTSDMQGDG
S233 DNLTLWTSDMQGDGE
D238 WTSDMQGDGEEQNKE
K244 GDGEEQNKEALQDVE
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