A0A0A6YY92 · A0A0A6YY92_HUMAN
- ProteinAdenylosuccinate lyase
- GeneADSL
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids498 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.
Catalytic activity
- (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate
Pathway
Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity | |
Molecular Function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylosuccinate lyase
- EC number
- Short namesASL
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A0A6YY92
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 621 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 253 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 348 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 448 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 391-475 | Adenylosuccinate lyase C-terminal | ||||
Sequence: LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFL |
Sequence similarities
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length498
- Mass (Da)56,217
- Last updated2015-02-04 v1
- Checksum05811B5D4843DDEF
Computationally mapped potential isoform sequences
There are 18 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P30566 | PUR8_HUMAN | ADSL | 484 | ||
A0A096LNY4 | A0A096LNY4_HUMAN | ADSL | 164 | ||
A0A096LNY5 | A0A096LNY5_HUMAN | ADSL | 381 | ||
A0A096LNY6 | A0A096LNY6_HUMAN | ADSL | 498 | ||
A0A096LNT0 | A0A096LNT0_HUMAN | ADSL | 81 | ||
A0A096LPA2 | A0A096LPA2_HUMAN | ADSL | 133 | ||
A0A096LP92 | A0A096LP92_HUMAN | ADSL | 273 | ||
A0A096LP72 | A0A096LP72_HUMAN | ADSL | 149 | ||
A0A096LP76 | A0A096LP76_HUMAN | ADSL | 102 | ||
A0A7P0T8E4 | A0A7P0T8E4_HUMAN | ADSL | 469 | ||
A0A7P0T9A7 | A0A7P0T9A7_HUMAN | ADSL | 513 | ||
A0A1B0GTJ7 | A0A1B0GTJ7_HUMAN | ADSL | 480 | ||
A0A1B0GTG9 | A0A1B0GTG9_HUMAN | ADSL | 467 | ||
A0A1B0GWJ0 | A0A1B0GWJ0_HUMAN | ADSL | 480 | ||
A0A1B0GWF8 | A0A1B0GWF8_HUMAN | ADSL | 403 | ||
B4DEP1 | B4DEP1_HUMAN | ADSL | 127 | ||
V9GY96 | V9GY96_HUMAN | ADSL | 57 | ||
A0A7P0Z472 | A0A7P0Z472_HUMAN | ADSL | 526 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL022238 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |