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Protein Page:
EAPP (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
EAPP May play an important role in the fine-tuning of both major E2F1 activities, the regulation of the cell-cycle and the induction of apoptosis. Promotes S-phase entry, and inhibits p14(ARP) expression. Interacts with E2F1. The C-terminal half binds the N- terminal of E2F1. Also interacts with E2F2 and E2F3, but not E2F4. Ubiquitously expressed. Highest levels in heart, placenta, skeletal muscle and pancreas. Lower levels in brain, lung and kidney. In the brain, expressed in all regions with high levels in the cerebellum and cerebral cortex. Expressed in COS1 and transformed skin fibroblasts. Note: This description may include information from UniProtKB.
Cellular Component: Golgi apparatus; cytoplasm; nucleus
Biological Process: positive regulation of RNA elongation from RNA polymerase II promoter; positive regulation of cell proliferation
Reference #:  Q56P03 (UniProtKB)
Alt. Names/Synonyms: BM036; C14orf11; E2F-associated phosphoprotein; EAPP; FLJ20578; MGC4957
Gene Symbols: EAPP
Molecular weight: 32,762 Da
Basal Isoelectric point: Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

EAPP

Protein Structure Not Found.


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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 1 S17-p PYAVEEPsDEEPALs
0 1 S24-p sDEEPALsssEDEVD
0 1 S25-p DEEPALsssEDEVDV
0 1 S26-p EEPALsssEDEVDVL
0 1 T50-p KLIRECLtGEsEsss
0 1 S53-p RECLtGEsEsssEDE
0 2 S55-p CLtGEsEsssEDEFE
0 1 S56-p LtGEsEsssEDEFEK
0 2 S57-p tGEsEsssEDEFEKE
0 1 S87-p LSSLGTGsSSGNGkV
0 14 K93-u GsSSGNGkVATAPTR
0 20 S109-p YDDIYFDsDsEDEDR
0 20 S111-p DIYFDsDsEDEDRAV
0 1 A117 DsEDEDRAVQVtKKK
0 2 T121-p EDRAVQVtKKKKKKQ
  mouse

 
S17 PYAVEEPSDEEPALS
S24 SDEEPALSSSEDELD
S25 DEEPALSSSEDELDV
S26 EEPALSSSEDELDVL
T50 KLIRECLTGESEsSs
S53 RECLTGESEsSsEDE
S55-p CLTGESEsSsEDEFE
S56 LTGESEsSsEDEFEK
S57-p TGESEsSsEDEFEKE
S87 LSSLGTGSSSGVAkV
K93-u GSSSGVAkVGGVTEK
S109-p YDEIYFDsDsEDEDK
S111-p EIYFDsDsEDEDKtV
T117-p DsEDEDKtVtKKKKK
T119-p EDEDKtVtKKKKKKQ
  rat

 
S17 PYAVEEPSDEEPALS
S24 SDEEPALSSSEDEVD
S25 DEEPALSSSEDEVDV
S26 EEPALSSSEDEVDVL
T50 KLIRECLTGESESSE
S53 RECLTGESESSEDEF
S55 CLTGESESSEDEFEK
S56 LTGESESSEDEFEKE
- gap
S86 LSSLGTGSSSGVAKV
K92 GSSSGVAKVGGVTTK
S108 YDAVYFDSDSEDEDK
S110 AVYFDSDSEDEDKAV
A116 DSEDEDKAVTKKKKK
T118 EDEDKAVTKKKKKKQ
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