|Institutional Source||Beutler Lab|
|Gene Name||aminoadipate-semialdehyde synthase|
|Is this an essential gene?||Possibly non essential (E-score: 0.325)|
|Stock #||R0546 (G1)|
|Chromosomal Location||23072173-23132986 bp(-) (GRCm38)|
|Type of Mutation||critical splice donor site (2 bp from exon)|
|DNA Base Change (assembly)||A to G at 23077077 bp|
|Amino Acid Change|
|Ref Sequence||ENSEMBL: ENSMUSP00000031707 (fasta)|
|Gene Model||predicted gene model for transcript(s): [ENSMUST00000031707]|
|Predicted Effect||probably null
|Meta Mutation Damage Score||0.456|
|Coding Region Coverage||
|Validation Efficiency||99% (74/75)|
|MGI Phenotype||FUNCTION: This gene encodes a bifunctional mitochondrial protein that catalyzes the first two steps in the lysine degradation pathway. The N-terminus contains lysine-ketoglutarate reductase activity and converts lysine to saccharopine, whereas the C-terminus contains saccharopine dehydrogenase activity and converts saccharopine to alpha-aminoadipate semialdehyde. Mutations in a human gene encoding a highly similar protein are associated with familial hyperlysinemia. [provided by RefSeq, Jul 2008]|
|Allele List at MGI|
|Other mutations in this stock||
|Other mutations in Aass||
(F):5'- GGCATGACTTCCCCATTGTTCAGG -3'
(R):5'- GGGCAGGGGCTGTAAAATTCATTTG -3'
(F):5'- CCCATTGTTCAGGGAATGATCC -3'
(R):5'- AGGGGCTGTAAAATTCATTTGTCTTC -3'
|Protein Function and Prediction|
In lysine metabolism, the first two steps of the lysine-degradation pathway are catalyzed by lysine-ketoglutarate reducase (LKR) and saccharopine dehydrogenase (SDH), respectively. AASS is a bifunctional protein that contains both LKR and SDH activity (1). AASS was detected in all human tissues examined by Northern blot analysis; highest expression was observed in the liver (1).
Mutations in AASS are linked to hyperlysinemia (OMIM: #238700) and saccaropinuria (OMIM: %268700). Patients with hyperlysinemia are often mentally retarded and exhibit convulsions, have impaired sexual development, lax ligaments and muscles, and mild anemia (2). Patients with saccharopinuria exhibit moderate retardation and EEG abnormalities (3).
1. Sacksteder, K. A., Biery, B. J., Morrell, J. C., Goodman, B. K., Geisbrecht, B. V., Cox, R. P., Gould, S. J., and Geraghty, M. T. (2000) Identification of the Alpha-Aminoadipic Semialdehyde Synthase Gene, which is Defective in Familial Hyperlysinemia. Am J Hum Genet. 66, 1736-1743.
|Science Writer||Anne Murray|