P13798 · ACPH_HUMAN
- ProteinAcylamino-acid-releasing enzyme
- GeneAPEH
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids732 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus (PubMed:10719179, PubMed:1740429, PubMed:2006156).
It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity).
Also, involved in the degradation of oxidized and glycated proteins (PubMed:10719179).
It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity).
Also, involved in the degradation of oxidized and glycated proteins (PubMed:10719179).
Catalytic activity
Activity regulation
Homotetramerization is required for activity. Tetramerization results in the formation of a gated channel which is involved in substrate selection and substrate access to the catalytic sites.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 587 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 675 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 707 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular region | |
Cellular Component | ficolin-1-rich granule lumen | |
Cellular Component | nuclear membrane | |
Molecular Function | identical protein binding | |
Molecular Function | omega peptidase activity | |
Molecular Function | RNA binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | amyloid-beta metabolic process | |
Biological Process | proteolysis | |
Biological Process | translational termination |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAcylamino-acid-releasing enzyme
- EC number
- Short namesAARE
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP13798
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_051580 | 541 | in dbSNP:rs3816877 | |||
Sequence: T → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 758 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000122430 | 1-732 | UniProt | Acylamino-acid-releasing enzyme | |||
Sequence: MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGQYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGGTGPGEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVAEKKRPKAESFFQTKALDVSASDDEIARLKKPDQAIKGDQFVFYEDWGENMVSKSIPVLCVLDVESGNISVLEGVPENVSPGQAFWAPGDAGVVFVGWWHEPFRLGIRFCTNRRSALYYVDLIGGKCELLSDDSLAVSSPRLSPDQCRIVYLQYPSLIPHHQCSQLCLYDWYTKVTSVVVDVVPRQLGENFSGIYCSLLPLGCWSADSQRVVFDSAQRSRQDLFAVDTQVGTVTSLTAGGSGGSWKLLTIDQDLMVAQFSTPSLPPTLKVGFLPSAGKEQSVLWVSLEEAEPIPDIHWGIRVLQPPPEQENVQYAGLDFEAILLQPGSPPDKTQVPMVVMPHGGPHSSFVTAWMLFPAMLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGHQDVKDVQFAVEQVLQEEHFDASHVALMGGSHGGFISCHLIGQYPETYRACVARNPVINIASMLGSTDIPDWCVVEAGFPFSSDCLPDLSVWAEMLDKSPIRYIPQVKTPLLLMLGQEDRRVPFKQGMEYYRALKTRNVPVRLLLYPKSTHALSEVEVESDSFMNAVLWLRTHLGS | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 185 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 185 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 187 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 187 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in erythrocytes (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P13798 | APEH P13798 | 6 | EBI-723792, EBI-723792 | |
BINARY | P13798 | IST1 P53990 | 5 | EBI-723792, EBI-945994 | |
BINARY | P13798 | IST1 P53990-3 | 3 | EBI-723792, EBI-12188567 | |
BINARY | P13798 | LGALS8 O00214 | 4 | EBI-723792, EBI-740058 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length732
- Mass (Da)81,225
- Last updated2003-11-07 v4
- ChecksumA2C370516324D851
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 101 | in Ref. 1; BAA07476 | ||||
Sequence: T → S | ||||||
Sequence conflict | 137 | in Ref. 1; BAA07476 | ||||
Sequence: A → V | ||||||
Sequence conflict | 168 | in Ref. 1; BAA07476 | ||||
Sequence: K → R | ||||||
Sequence conflict | 200 | in Ref. 1; BAA07476 | ||||
Sequence: A → P | ||||||
Sequence conflict | 403 | in Ref. 2; AAF37321 | ||||
Sequence: A → V |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D38441 EMBL· GenBank· DDBJ | BAA07476.1 EMBL· GenBank· DDBJ | mRNA | ||
AF141383 EMBL· GenBank· DDBJ | AAF37321.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000362 EMBL· GenBank· DDBJ | AAH00362.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001499 EMBL· GenBank· DDBJ | AAH01499.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001826 EMBL· GenBank· DDBJ | AAH01826.1 EMBL· GenBank· DDBJ | mRNA | ||
J03068 EMBL· GenBank· DDBJ | AAA35769.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |