Details of Protein
General Information of Protein (ID: PRT001698) | |||||
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Name | Argininosuccinate synthase (ASS1) | ||||
Synonyms |
Click to Show/Hide Synonyms of This Protein
Citrulline-aspartate ligase; ASS
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Gene Name | ASS1 | Gene ID | |||
UniProt ID | |||||
Family | Ligases (EC 6) | ||||
EC Number | EC: 6.3.4.5 (Click to Show/Hide the Complete EC Tree) | ||||
Click to Show/Hide the Molecular/Functional Data (Sequence/Structure/Function) of This Protein | |||||
Sequence |
MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVF
IEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATG KGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWS MDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKD GTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAF TMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYI LGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK |
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Structure | |||||
Function | One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues. | ||||
Regulatory Network | |||||
Full List of Metabolite(s) Regulating This Protein | ||||||
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Organic acids and derivatives | ||||||
Arginine | Click to Show/Hide the Full List of Regulating Pair(s): 1 Pair(s) | |||||
Detailed Information |
Metabo Info
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Regulating Pair |
Experim Info
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[1] | ||||
Introduced Variation | Arginine decrease (24 hours) | |||||
Induced Change | ASS1 protein expression levels: increase | |||||
Summary | Introduced Variation
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Disease Status | Leiomyosarcoma [ICD-11: 2B58] | |||||
Details | It is reported that arginine decrease causes the increase of ASS1 protein expression compared with control group. | |||||
References | |||||
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1 | Systems level profiling of arginine starvation reveals MYC and ERK adaptive metabolic reprogramming. Cell Death Dis. 2020 Aug 20;11(8):662. |
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