PAM Gene Summary [Human]
This gene encodes a multifunctional protein. The encoded preproprotein is proteolytically processed to generate the mature enzyme. This enzyme includes two domains with distinct catalytic activities, a peptidylglycine alpha-hydroxylating monooxygenase (PHM) domain and a peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain. These catalytic domains work sequentially to catalyze the conversion of neuroendocrine peptides to active alpha-amidated products. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Jan 2016]
Details
| Type | Protein Coding |
| Official Symbol | PAM |
| Official Name | peptidylglycine alpha-amidating monooxygenase [Source:HGNC Symbol;Acc:HGNC:8596] |
| Ensembl ID | ENSG00000145730 |
| Bio databases IDs | |
| Aliases | peptidylglycine alpha-amidating monooxygenase, peptidyl-alpha-hydroxyglycine alpha-amidating lyase, peptidylglycine alpha-hydroxylating monooxygenase |
| Synonyms | LOC102553671, PAL, PAM-1, peptidylglycine alpha-amidating monooxygenase, peptidylglycine α-amidating monooxygenase, PHM |
| 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 PAM often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- Copper type II ascorbate-dependent monooxygenase, C-terminal domain
- protein kinase binding
- signal response domain
- calcium ion binding
- chromatin binding
- enzyme
- protein binding
- NHL repeat unit of beta-propeller proteins
- identical protein binding
- peptidylamidoglycolate lyase
- internalization targeting signal
- copper ion binding
- cytoplasmic domain
- zinc ion binding
- peptidylglycine monooxygenase
- NHL repeat
- lumenal domain
- transmembrane domain
- Copper type II ascorbate-dependent monooxygenase, N-terminal domain
- pro domain
- targeting signal
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- non-insulin-dependent diabetes mellitus
- diabetic retinopathy
- insomnia
- COVID-19
- systemic lupus erythematosus
- obesity
- diabetes mellitus
- androgenic alopecia
- acute myeloid leukemia
- edema
role in cell
- expression in
- production in
- accumulation in
- morphology
- response
- formation
- organization
- branching
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Plasma Membrane
- soluble fraction
- membrane fraction
- Cytoplasm
- cell surface
- Golgi region
- Extracellular Space
- perinuclear region
- cellular membrane
- endosomes
- vesicles
- secretory granule membrane
- cytosol
- trans Golgi network
- chromosome
- perinuclear vesicles
- secretory granules
- chromatin
- perikaryon
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the human PAM gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- response to zinc ion
- peptide amidation
Cellular Component
Where in the cell the gene product is active
- secretory granule membrane
- extracellular vesicular exosome
- transport vesicle membrane
- membrane
- extracellular region
Molecular Function
What the gene product does at the molecular level
- L-ascorbic acid binding
- zinc ion binding
- peptidylglycine monooxygenase activity
- protein binding
- copper ion binding
- calcium ion binding
- peptidylamidoglycolate lyase activity