ASPH

From Wikipedia, the free encyclopedia

Aspartate beta-hydroxylase

Identifiers

ASPH; BAH; CASQ2BP1; HAAH; JCTN; junctin

External IDs

OMIM: 600582 MGI: 1914186 HomoloGene: 20910

Gene ontology
Molecular Function:	• peptide-aspartate beta-dioxygenase activity • binding • iron ion binding • calcium ion binding • structural constituent of muscle • electron carrier activity • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
Cellular Component:	• endoplasmic reticulum • endoplasmic reticulum membrane • membrane • integral to membrane • integral to endoplasmic reticulum membrane
Biological Process:	• muscle contraction • biological_process • peptidyl-amino acid modification

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004318 (mRNA)
NP_004309 (protein)

NM_023066 (mRNA)
NP_075553 (protein)

Location

Chr 8: 62.58 - 62.79 Mb

Chr 4: 9.38 - 9.6 Mb

Pubmed search

[1]

[2]

Aspartate beta-hydroxylase, also known as ASPH, is a human gene.^[1]

This gene is thought to play an important role in calcium homeostasis. Alternative splicing of this gene results in five transcript variants which vary in protein translation, the coding of catalytic domains, and tissue expression. Variation among these transcripts impacts their functions which involve roles in the calcium storage and release process in the endoplasmic and sarcoplasmic reticulum as well as hydroxylation of aspartic acid and asparagine in epidermal growth factor-like domains of various proteins.^[1]

[edit] References

^ ^a ^b Entrez Gene: ASPH aspartate beta-hydroxylase.

[edit] Further reading

Hirota K, Semenza GL (2005). "Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases.". Biochem. Biophys. Res. Commun. 338 (1): 610–6. doi:10.1016/j.bbrc.2005.08.193. PMID 16154531.
Korioth F, Gieffers C, Frey J (1995). "Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase.". Gene 150 (2): 395–9. PMID 7821814.
Lavaissiere L, Jia S, Nishiyama M, et al. (1996). "Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma.". J. Clin. Invest. 98 (6): 1313–23. PMID 8823296.
Zhang L, Kelley J, Schmeisser G, et al. (1997). "Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane.". J. Biol. Chem. 272 (37): 23389–97. PMID 9287354.
Wetzel GT, Ding S, Chen F (2000). "Molecular cloning of junctin from human and developing rabbit heart.". Mol. Genet. Metab. 69 (3): 252–8. doi:10.1006/mgme.2000.2966. PMID 10767180.
Dinchuk JE, Henderson NL, Burn TC, et al. (2001). "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin.". J. Biol. Chem. 275 (50): 39543–54. doi:10.1074/jbc.M006753200. PMID 10956665.
Lim KY, Hong CS, Kim DH (2000). "cDNA cloning and characterization of human cardiac junctin.". Gene 255 (1): 35–42. PMID 10974562.
Treves S, Feriotto G, Moccagatta L, et al. (2001). "Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane.". J. Biol. Chem. 275 (50): 39555–68. doi:10.1074/jbc.M005473200. PMID 11007777.
Kirchhefer U, Neumann J, Baba HA, et al. (2001). "Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1.". J. Biol. Chem. 276 (6): 4142–9. doi:10.1074/jbc.M006443200. PMID 11069905.
Sepe PS, Lahousse SA, Gemelli B, et al. (2002). "Role of the aspartyl-asparaginyl-beta-hydroxylase gene in neuroblastoma cell motility.". Lab. Invest. 82 (7): 881–91. PMID 12118090.
Ho SP, Scully MS, Krauthauser CM, et al. (2002). "Antisense oligonucleotides selectively regulate aspartyl beta-hydroxylase and its truncated protein isoform in vitro but distribute poorly into A549 tumors in vivo.". J. Pharmacol. Exp. Ther. 302 (2): 795–803. PMID 12130746.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Maeda T, Sepe P, Lahousse S, et al. (2004). "Antisense oligodeoxynucleotides directed against aspartyl (asparaginyl) beta-hydroxylase suppress migration of cholangiocarcinoma cells.". J. Hepatol. 38 (5): 615–22. PMID 12713872.
Treves S, Franzini-Armstrong C, Moccagatta L, et al. (2004). "Junctate is a key element in calcium entry induced by activation of InsP3 receptors and/or calcium store depletion.". J. Cell Biol. 166 (4): 537–48. doi:10.1083/jcb.200404079. PMID 15302852.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
Xian ZH, Zhang SH, Cong WM, et al. (2006). "Expression of aspartyl beta-hydroxylase and its clinicopathological significance in hepatocellular carcinoma.". Mod. Pathol. 19 (2): 280–6. doi:10.1038/modpathol.3800530. PMID 16341145.
de la Monte SM, Tamaki S, Cantarini MC, et al. (2006). "Aspartyl-(asparaginyl)-beta-hydroxylase regulates hepatocellular carcinoma invasiveness.". J. Hepatol. 44 (5): 971–83. doi:10.1016/j.jhep.2006.01.038. PMID 16564107.
Feldmann G, Nattermann J, Nischalke HD, et al. (2006). "Detection of human aspartyl (asparaginyl) beta-hydroxylase and homeobox B7 mRNA in brush cytology specimens from patients with bile duct cancer.". Endoscopy 38 (6): 604–9. doi:10.1055/s-2006-925065. PMID 16673309.
Gundogan F, Elwood G, Greco D, et al. (2007). "Role of aspartyl-(asparaginyl) beta-hydroxylase in placental implantation: Relevance to early pregnancy loss.". Hum. Pathol. 38 (1): 50–9. doi:10.1016/j.humpath.2006.06.005. PMID 16949909.