ALAD Gene Summary [Human]
The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. Alternative splicing of this gene results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2015]
Details
| Type | Protein Coding |
| Official Symbol | ALAD |
| Official Name | aminolevulinate dehydratase [Source:HGNC Symbol;Acc:HGNC:395] |
| Ensembl ID | ENSG00000148218 |
| Bio databases IDs | |
| Aliases | aminolevulinate dehydratase, porphobilinogen synthase |
| Synonyms | ALADH, ALADR, aminolevulinate dehydratase, aminolevulinate, delta-, dehydratase, aminolevulinate, δ-, dehydratase, Dah, Lv, PBGS, δ aminolevulinate dehydratase |
| Species | Human, Homo sapiens |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in human ALAD often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- Delta-aminolevulinic acid dehydratase
- ALAD_PBGS
- binding protein
- zinc ion binding
- porphobilinogen synthase
- enzyme
- identical protein binding
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- nodular basal cell carcinoma
- susceptibility to lead poisoning
- recurrent ovarian cancer
- metaplastic breast cancer
- skin neoplasm
- delta-aminolevulinate dehydratase porphyria
- breast ductal carcinoma in situ
- mucinous breast cancer
- superficial basal cell carcinoma
- actinic keratosis of the face and scalp
regulates
- FAS
- heme
- heme a
role in cell
- response by
- alternative splicing in
- response
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Cytoplasm
- membrane fraction
- secretory granule lumen
- ficolin-1-rich granule lumen
- Extracellular Space
- cell periphery
- cytosol
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the human ALAD gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- response to aluminum ion
- response to zinc ion
- response to amino acid stimulus
- heme biosynthetic process
- heme a biosynthetic process
- response to xenobiotic stimulus
- protoporphyrinogen IX biosynthetic process
- response to herbicide
- heme b biosynthetic process
- response to ethanol
- response to oxidative stress
- response to hypoxia
- response to arsenic-containing substance
- response to platinum ion
- response to glucocorticoid stimulus
- cellular response to interleukin-4
- response to iron ion
- response to cobalt ion
- response to fatty acid
- response to ionizing radiation
- response to vitamin E
- protein homooligomerization
- response to mercury ion
- response to cadmium ion
- cellular response to lead ion
- heme O biosynthetic process
- response to methylmercury
- response to selenium ion
- response to lipopolysaccharide
- response to activity
- response to vitamin B1
Cellular Component
Where in the cell the gene product is active
- nucleus
- extracellular vesicular exosome
- cytosol
- secretory granule lumen
- extracellular region
Molecular Function
What the gene product does at the molecular level
- porphobilinogen synthase activity
- identical protein binding
- zinc ion binding
- catalytic activity