Recombinant Human Aspartyl/asparaginyl beta-hydroxylase

Uniprot Id

Q12797

Target Species

Human

Target Name

ASPH

Target Full Name

Aspartyl/asparaginyl beta-hydroxylase

Target Function

specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.; 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.

Target Involvement

Facial dysmorphism, lens dislocation, anterior segment abnormalities, and spontaneous filtering blebs (FDLAB)

Target Subcellular Location

[Isoform 1]: Endoplasmic reticulum membrane; Single-pass type II membrane protein.; [Isoform 4]: Sarcoplasmic reticulum membrane; Single-pass type II membrane protein.; [Isoform 8]: Endoplasmic reticulum membrane; Single-pass type II membrane protein.

Target Protein Families

Aspartyl/asparaginyl beta-hydroxylase family

Target Tissue Specificity

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).

Target Research Area

Signal Transduction

Target Synonyms

ASPH; BAHAspartyl/asparaginyl beta-hydroxylase; EC 1.14.11.16; Aspartate beta-hydroxylase; ASP beta-hydroxylase; Peptide-aspartate beta-dioxygenase

Target Background

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.