Aspartate Beta-Hydroxylase (ASPH) Human Recombinant Protein

This gene is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of some proteins, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Other isoforms differ primarily in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum. Some of these isoforms are found in complexes with calsequestrin, triadin, and the ryanodine receptor, and have been shown to regulate calcium release from the sarcoplasmic reticulum. Some isoforms have been implicated in metastasis. [provided by RefSeq, Sep 2009]

ASPH: Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. Belongs to the aspartyl/asparaginyl beta-hydroxylase family. 9 isoforms of the human protein are produced by alternative splicing.

Protein type: Oxidoreductase; Membrane protein, integral; EC 1.14.11.16

Chromosomal Location of Human Ortholog: 8q12.1

Cellular Component: endoplasmic reticulum membrane; sarcoplasmic reticulum membrane; sarcoplasmic reticulum lumen; endoplasmic reticulum; integral to membrane; plasma membrane; integral to endoplasmic reticulum membrane

Molecular Function: protein binding; electron carrier activity; structural constituent of muscle; calcium ion binding; structural molecule activity; peptide-aspartate beta-dioxygenase activity

Biological Process: peptidyl-aspartic acid hydroxylation; negative regulation of cell proliferation; activation of store-operated calcium channel activity; muscle contraction; positive regulation of proteolysis; positive regulation of transcription, DNA-dependent; regulation of protein stability; regulation of inositol-1,4,5-triphosphate receptor activity; palate development; detection of calcium ion; pattern specification process; limb morphogenesis; response to ATP