UniProt ID | FAAH1_HUMAN | |
---|---|---|
UniProt AC | O00519 | |
Protein Name | Fatty-acid amide hydrolase 1 | |
Gene Name | FAAH | |
Organism | Homo sapiens (Human). | |
Sequence Length | 579 | |
Subcellular Localization |
Endomembrane system Single-pass membrane protein . Cytoplasm, cytoskeleton . Seems to be attached to intracellular membranes and a portion of the cytoskeletal network. |
|
Protein Description | 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.. | |
Protein Sequence | MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYTSSQPLRVGYYETDNYTMPSPAMRRAVLETKQSLEAAGHTLVPFLPSNIPHALETLSTGGLFSDGGHTFLQNFKGDFVDPCLGDLVSILKLPQWLKGLLAFLVKPLLPRLSAFLSNMKSRSAGKLWELQHEIEVYRKTVIAQWRALDLDVVLTPMLAPALDLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
88 | Phosphorylation | QLVQKLHSRELAPEA HHHHHHHHCCCCCCC | 37.58 | - | |
99 | Phosphorylation | APEAVLFTYVGKAWE CCCCEEEEEECCCEE | 17.09 | 20058876 | |
241 | Phosphorylation | LGTDIGGSIRFPSSF CCCCCCCCEECCCCC | 12.84 | 12060782 | |
289 | Phosphorylation | PMARDVESLALCLRA CCCCCHHHHHHHHHH | 20.84 | 24667141 | |
329 | Phosphorylation | SQPLRVGYYETDNYT CCCEEEEEEECCCCC | 8.69 | 22817900 | |
330 | Phosphorylation | QPLRVGYYETDNYTM CCEEEEEEECCCCCC | 13.36 | 24043423 | |
332 | Phosphorylation | LRVGYYETDNYTMPS EEEEEEECCCCCCCC | 17.27 | 24043423 | |
335 | Phosphorylation | GYYETDNYTMPSPAM EEEECCCCCCCCHHH | 13.76 | 22817900 | |
336 | Phosphorylation | YYETDNYTMPSPAMR EEECCCCCCCCHHHH | 28.94 | 24043423 | |
339 | Phosphorylation | TDNYTMPSPAMRRAV CCCCCCCCHHHHHHH | 17.92 | 24043423 | |
406 | Phosphorylation | PCLGDLVSILKLPQW HHHHHHHHHHHHHHH | 29.51 | 24719451 | |
423 | Ubiquitination | GLLAFLVKPLLPRLS HHHHHHHHHHHHHHH | 31.90 | - | |
430 | Phosphorylation | KPLLPRLSAFLSNMK HHHHHHHHHHHHHCC | 20.46 | - | |
434 | Phosphorylation | PRLSAFLSNMKSRSA HHHHHHHHHCCCCCC | 28.55 | - | |
440 | Phosphorylation | LSNMKSRSAGKLWEL HHHCCCCCCHHHHHH | 48.76 | - | |
454 | Phosphorylation | LQHEIEVYRKTVIAQ HHHHHHHHHHHHHHH | 8.13 | - | |
488 | Phosphorylation | LNAPGRATGAVSYTM CCCCCCCCCCCCHHH | 25.06 | 22210691 | |
493 | Phosphorylation | RATGAVSYTMLYNCL CCCCCCCHHHHHHHH | 6.92 | 22210691 | |
513 | Phosphorylation | VVPVTTVTAEDEAQM EEEEEEEECCHHHHH | 23.41 | 22210691 | |
573 | Phosphorylation | REVERLMTPEKQSS- HHHHHHCCCCHHCC- | 32.65 | 22468782 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of FAAH1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FAAH1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of FAAH1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NT2NL_HUMAN | NOTCH2NL | physical | 25416956 |
loading...
Phosphorylation | |
Reference | PubMed |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-329 AND TYR-335, ANDMASS SPECTROMETRY. |