FAAH1_HUMAN - dbPTM
FAAH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
88PhosphorylationQLVQKLHSRELAPEA
HHHHHHHHCCCCCCC
37.58-
99PhosphorylationAPEAVLFTYVGKAWE
CCCCEEEEEECCCEE
17.0920058876
241PhosphorylationLGTDIGGSIRFPSSF
CCCCCCCCEECCCCC
12.8412060782
289PhosphorylationPMARDVESLALCLRA
CCCCCHHHHHHHHHH
20.8424667141
329PhosphorylationSQPLRVGYYETDNYT
CCCEEEEEEECCCCC
8.6922817900
330PhosphorylationQPLRVGYYETDNYTM
CCEEEEEEECCCCCC
13.3624043423
332PhosphorylationLRVGYYETDNYTMPS
EEEEEEECCCCCCCC
17.2724043423
335PhosphorylationGYYETDNYTMPSPAM
EEEECCCCCCCCHHH
13.7622817900
336PhosphorylationYYETDNYTMPSPAMR
EEECCCCCCCCHHHH
28.9424043423
339PhosphorylationTDNYTMPSPAMRRAV
CCCCCCCCHHHHHHH
17.9224043423
406PhosphorylationPCLGDLVSILKLPQW
HHHHHHHHHHHHHHH
29.5124719451
423UbiquitinationGLLAFLVKPLLPRLS
HHHHHHHHHHHHHHH
31.90-
430PhosphorylationKPLLPRLSAFLSNMK
HHHHHHHHHHHHHCC
20.46-
434PhosphorylationPRLSAFLSNMKSRSA
HHHHHHHHHCCCCCC
28.55-
440PhosphorylationLSNMKSRSAGKLWEL
HHHCCCCCCHHHHHH
48.76-
454PhosphorylationLQHEIEVYRKTVIAQ
HHHHHHHHHHHHHHH
8.13-
488PhosphorylationLNAPGRATGAVSYTM
CCCCCCCCCCCCHHH
25.0622210691
493PhosphorylationRATGAVSYTMLYNCL
CCCCCCCHHHHHHHH
6.9222210691
513PhosphorylationVVPVTTVTAEDEAQM
EEEEEEEECCHHHHH
23.4122210691
573PhosphorylationREVERLMTPEKQSS-
HHHHHHCCCCHHCC-
32.6522468782

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAAH1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NT2NL_HUMANNOTCH2NLphysical
25416956

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00818Propofol
DB00599Thiopental
Regulatory Network of FAAH1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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