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

Overview
FAAH Degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids, thereby serving to terminate the signaling functions of these molecules. Hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates. Homodimer. Highly expressed in the brain, small intestine, pancreas, skeletal muscle and testis. Also expressed in the kidney, liver, lung, placenta and prostate. Inhibited by O-aryl carbamates and alpha-keto heterocytes. Belongs to the amidase family. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; EC 3.5.1.99; Hydrolase; EC 3.1.-.-
Cellular Component: cytoskeleton; cytoplasm; integral to membrane; endomembrane system
Molecular Function: carbon-nitrogen ligase activity, with glutamine as amido-N-donor; fatty acid amide hydrolase activity; acylglycerol lipase activity
Biological Process: fatty acid catabolic process
Reference #:  O00519 (UniProtKB)
Alt. Names/Synonyms: Anandamide amidohydrolase 1; FAAH; FAAH-1; FAAH1; fatty acid amide hydrolase; Fatty-acid amide hydrolase 1; MGC102823; MGC138146; Oleamide hydrolase 1
Gene Symbols: FAAH
Molecular weight: 63,066 Da
Basal Isoelectric point: 7.82  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

FAAH

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 R49 VRARQRQRAGLENMD
0 1 R57 AGLENMDRAAQRFRL
0 1 S88-p QLVQKLHsRELAPEA
0 1 T99-p APEAVLFtYVGKAWE
0 1 K142 YGVPVSLKECFTYKG
0 1 S241-p LGTDIGGsIRFPSSF
0 1 K255 FCGICGLKPTGNRLS
0 1 Y329-p SQPLRVGyYETDNyT
0 2 Y335-p GyYETDNyTMPSPAM
0 1 H370 FLPSNIPHALETLST
0 1 S430-p KPLLPRLsAFLsNMK
0 1 S434-p PRLsAFLsNMKSRsA
0 1 S440-p LsNMKSRsAGKLWEL
0 1 T472 LDLDVVLTPMLAPAL
0 1 A483 APALDLNAPGRATGA
0 7 Y526 QMEHYRGYFGDIWDK
  mouse

 
R49-m1 TRARQKQrAGLETMD
K57-ub AGLETMDkAVQRFRL
S88 QLVQKLQSGELSPEA
T99 SPEAVLFTYLGKAWE
K142-ub YGVPVSLkECFSYKG
S241 LGTDIGGSIRFPSAF
K255-ub FCGICGLkPTGNRLS
Y329 SRPLRVGYYETDNYT
Y335 GYYETDNYTMPTPAM
Y370-p FLPNNIPyALEVLSA
A430 KPLFPRLAAFLNSMC
N434 PRLAAFLNSMCPRSA
S440 LNSMCPRSAEKLWEL
T472-p MNLDVVLtPMLGPAL
T483-p GPALDLNtPGRATGA
Y526 QMEHYKGYFGDMWDN
  rat

 
R49 TRARQKQRASLETMD
K57 ASLETMDKAVQRFRL
S88 QLVQKLQSGELSPEA
T99 SPEAVFFTYLGKAWE
K142 YGVPVSLKECFSYKG
S241 LGTDIGGSIRFPSAF
K255 FCGICGLKPTGNRLS
Y329 SRPLRVGYYETDNYT
Y335 GYYETDNYTMPSPAM
Y370 FLPNNIPYALEVLSA
A430 KPLFPRLAAFLNSMR
N434 PRLAAFLNSMRPRSA
S440 LNSMRPRSAEKLWKL
T472 MNLDVLLTPMLGPAL
T483 GPALDLNTPGRATGA
Y526-p QMELYKGyFGDIWDI
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