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Protein Page:
Fe65 (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
Fe65 adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on Y142 (H2AXpY142) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as TIP60, probably explains its trancription activation activity. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; Adaptor/scaffold; Transcription regulation
Cellular Component: growth cone; lamellipodium; cytoplasm; plasma membrane; nuclear speck; synapse; nucleus
Molecular Function: protein binding; histone binding; beta-amyloid binding; chromatin binding; transcription factor binding
Biological Process: axon guidance; extracellular matrix organization and biogenesis; positive regulation of DNA repair; transcription, DNA-dependent; apoptosis; positive regulation of apoptosis; positive regulation of transcription, DNA-dependent; neuron migration; negative regulation of thymidylate synthase biosynthetic process; signal transduction; negative regulation of neuron differentiation; axonogenesis; regulation of transcription, DNA-dependent; double-strand break repair; visual learning; positive regulation of transcription from RNA polymerase II promoter; negative regulation of cell growth; cell cycle arrest; response to DNA damage stimulus
Reference #:  O00213 (UniProtKB)
Alt. Names/Synonyms: adaptor protein FE65a2; amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65); Amyloid beta A4 precursor protein-binding family B member 1; amyloid beta A4 precursor protein-binding, family B, member 1; APBB1; FE65; MGC:9072; Protein Fe65; RIR; stat-like protein
Gene Symbols: APBB1
Molecular weight: 77,244 Da
Basal Isoelectric point: 4.98  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Fe65

Protein Structure Not Found.


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Sites Implicated In
transcription, induced: Y547‑p
molecular association, regulation: Y547‑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

► Hide Isoforms
 
0 2 K48-u QATAVGPkDLRSAMG
0 1 P135 ANRGLRGPGLIISTQ
1 1 S175-p EEEEDLSsPPGLPEP
1 1 S287-p WEPPGRAsPSQGSSP
1 2 S347-p TFPAQSLsPEPLPQE
0 1 S459-p VWGVGRDsGRERDFA
0 1 S517 RCLVNGLSLDHSKLV
2 1 Y547-p VQKFQVYyLGNVPVA
1 0 S610 ECRVRFLSFLAVGRD
0 1 S666 QKCLDARSQASTSCL
0 2 S699-p GVQSLWGsLKPKRLG
1 2 T709-p PKRLGAHtP______
  Fe65 iso2  
K48 QATAVGPKDLRSAMG
P135 ANRGLRGPGLIISTQ
S175 EEEEDLSSPPGLPEP
S287 WEPPGRASPSQGSSP
S347 TFPAQSLSPEPLPQE
S459 VWGVGRDSGRDFAYV
S515 RCLVNGLSLDHSKLV
Y545 VQKFQVYYLGNVPVA
S608 ECRVRFLSFLAVGRD
S664 QKCLDARSQASTSCL
S697 GVQSLWGSLKPKRLG
T707 PKRLGAHTP______
  mouse

 
K48-u QATAVVPkDLRSAMG
S135-p ANRGLHGsALIINTQ
S175 EEEEDLSSPPGLPEP
S287 WEPPGRASPSQGSSP
S347-p SFPAQSLsPEPVPQE
S459 VWGVGRDSGSNRDFA
S517-p RCLVNGLsLDHSKLV
Y547-p VQKFQVYyLGNVPVA
S610 ECRVRFLSFLAVGRD
S666-gl QKCLDARsQTSTSCL
S699-p GVQSLWGsLKPKRLG
T709-p PKRLGSQtP______
  rat

 
K48 QATAVVPKDLRSAMG
S135 ANRGLHGSALIINTQ
S176 EEEEDLSSPQGLPEP
S288 WEPPGRASPSQGNSP
S348 PFSAQSLSPEPVPQE
S460 VWGVGRDSGRERDFA
S518 RCLVNGLSLDHSKLV
Y548 VQKFQVYYLGNVPVA
S611-p ECRVRFLsFLAVGRD
S667 QKCLDARSQTSTSCL
S700 GVQSLWGSLKPKRLG
T710 PKRLGSQTP______
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