ASPH Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. Isoform 8: membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells. Belongs to the aspartyl/asparaginyl beta-hydroxylase family. Isoform 1 is detected in all tissues tested. Isoform 8 is mainly expressed in pancreas, heart, brain, kidney and liver. Isoform 8 is expressed in kidney (at protein level). 11 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: EC 1.14.11.16; Membrane protein, integral; Oxidoreductase
Chromosomal Location of human Ortholog: 8q12.3
Cellular Component:  cortical endoplasmic reticulum; endoplasmic reticulum; endoplasmic reticulum membrane; plasma membrane; sarcoplasmic reticulum membrane
Molecular Function:  calcium ion binding; electron transfer activity; peptidyl-aspartic acid 3-dioxygenase activity; protein binding; structural constituent of muscle; structural molecule activity
Biological Process:  activation of cysteine-type endopeptidase activity; cell population proliferation; electron transport chain; face morphogenesis; limb morphogenesis; muscle contraction; negative regulation of cell population proliferation; pattern specification process; peptidyl-aspartic acid hydroxylation; positive regulation of proteolysis; regulation of protein depolymerization; regulation of protein stability; roof of mouth development
Reference #:  Q12797 (UniProtKB)
Alt. Names/Synonyms: A beta H-J-J; AAH; ASP beta-hydroxylase; Aspartate beta-hydroxylase; Aspartyl/asparaginyl beta-hydroxylase; aspartyl/asparaginyl-beta-hydroxylase; ASPH; BAH; cardiac junctin; CASQ2BP1; FDLAB; HAAH; humbug; JCTN; junctate; junctin; Peptide-aspartate beta-dioxygenase
Gene Symbols: ASPH
Molecular weight: 85,863 Da
Basal Isoelectric point: 4.92  Predict pI for various phosphorylation states
Select Structure to View Below

ASPH

Protein Structure Not Found.


Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  CCLE  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB  |  Ensembl Protein