protein
Isoform 7 of Aspartyl/asparaginyl beta-hydroxylase
Gene
ASPH
Organism
Homo sapiens(9606)
Length
203 aa
Mass
21,963 Da
Aspartyl/asparaginyl beta-hydroxylase (ASPH), isoform 7, is a 203-amino-acid protein encoded by the *ASPH* gene in humans (UniProt: Q12797-7). This enzyme catalyzes post-translational hydroxylation of aspartyl and asparaginyl residues in target proteins, a modification important for protein folding and stability in the endoplasmic reticulum and secretory pathway.
ASPH is broadly distributed across tissues and participates in protein quality control mechanisms. While UniProt records no specific disease associations for this isoform, the protein has been implicated in various cellular processes related to protein maturation and secretion.
In Alzheimer's disease, ASPH isoform 7 shows reduced expression in post-mortem AD brain relative to age-matched controls, with a mean log2 fold-change of −0.44 across analyzed subcellular fractions (Chaparral AD proteomics). This modest downregulation suggests a potential role in the pathophysiology of neurodegeneration, though the functional significance of reduced ASPH levels in AD remains to be elucidated.
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
↓ Down in ADP3
not detected
P2
not detected
S2
not detected
S3
-0.442
Mean log₂FC across detected fractions: -0.4422 (1 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
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Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Sources
Last updated 5/8/2026, 6:29:14 AM
