Sequence information
Variant position: 129 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 579 The length of the canonical sequence.
Location on the sequence:
KGTNCVTSYLADCETQLSQA
P RQGLLYGVPVSLKECFTYKG
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human KGTNCVTSYLADCETQLSQAP RQG--------LLYGVPVSLKECFTYKG
Mouse KGTNCVTSYLTDCETQLSQAP RQG--------LLYGVPVSL
Rat KGTNCVTSYLTDCETQLSQAP RQG--------LLYGVPVSL
Pig RGTNCVTTYLADCEAQLCQAP GQG--------LLYGVPVSL
Caenorhabditis elegans EKTNAVTCFILDAERQAEELD EQAKLPYYVKPPLFGVPLSL
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
1 – 579
Fatty-acid amide hydrolase 1
Topological domain
30 – 403
Cytoplasmic
Active site
142 – 142
Charge relay system
Literature citations
Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT THR-129;
Submission
Mural R.J.; Istrail S.; Sutton G.G.; Florea L.; Halpern A.L.; Mobarry C.M.; Lippert R.; Walenz B.; Shatkay H.; Dew I.; Miller J.R.; Flanigan M.J.; Edwards N.J.; Bolanos R.; Fasulo D.; Halldorsson B.V.; Hannenhalli S.; Turner R.; Yooseph S.; Lu F.; Nusskern D.R.; Shue B.C.; Zheng X.H.; Zhong F.; Delcher A.L.; Huson D.H.; Kravitz S.A.; Mouchard L.; Reinert K.; Remington K.A.; Clark A.G.; Waterman M.S.; Eichler E.E.; Adams M.D.; Hunkapiller M.W.; Myers E.W.; Venter J.C.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT THR-129;
A missense mutation in human fatty acid amide hydrolase associated with problem drug use.
Sipe J.C.; Chiang K.; Gerber A.L.; Beutler E.; Cravatt B.F.;
Proc. Natl. Acad. Sci. U.S.A. 99:8394-8399(2002)
Cited for: POLYMORPHISM; ASSOCIATION OF VARIANT THR-129 WITH SUSCEPTIBILITY TO POLYSUBSTANCE ABUSE; CHARACTERIZATION OF VARIANT THR-129;
Reduced cellular expression and activity of the P129T mutant of human fatty acid amide hydrolase: evidence for a link between defects in the endocannabinoid system and problem drug use.
Chiang K.P.; Gerber A.L.; Sipe J.C.; Cravatt B.F.;
Hum. Mol. Genet. 13:2113-2119(2004)
Cited for: CHARACTERIZATION OF VARIANT THR-129;
The fatty acid amide hydrolase 385 A/A (P129T) variant: haplotype analysis of an ancient missense mutation and validation of risk for drug addiction.
Flanagan J.M.; Gerber A.L.; Cadet J.L.; Beutler E.; Sipe J.C.;
Hum. Genet. 120:581-588(2006)
Cited for: ASSOCIATION OF VARIANT THR-129 WITH SUSCEPTIBILITY TO POLYSUBSTANCE ABUSE;
Association of a functional FAAH polymorphism with methamphetamine-induced symptoms and dependence in a Malaysian population.
Sim M.S.; Hatim A.; Reynolds G.P.; Mohamed Z.;
Pharmacogenomics 14:505-514(2013)
Cited for: ASSOCIATION OF VARIANT THR-129 WITH SUSCEPTIBILITY TO METHAMPHETAMINE DEPENDENCE;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.