D
IPR007943

Aspartyl beta-hydroxylase/Triadin domain

InterPro entry
Short nameAsp-B-hydro/Triadin_dom

Description

This domain is found in members of the junctin, junctate and aspartyl beta-hydroxylase protein families. Junctate is an integral ER/SR membrane calcium binding protein, which comes from an alternatively spliced form of the same gene that generates aspartyl beta-hydroxylase and junctin
[1]
. Aspartyl beta-hydroxylase catalyses the post-translational hydroxylation of aspartic acid or asparagine residues contained within epidermal growth factor (EGF) domains of proteins
[2]
.

This domain is also found in several eukaryotic triadin proteins. Triadin is a ryanodine receptor and calsequestrin binding protein located in junctional sarcoplasmic reticulum of striated muscles
[3]
.

References

1.Molecular cloning and characterization of mouse cardiac junctate isoforms. Hong CS, Kwak YG, Ji JH, Chae SW, Kim DH. Biochem. Biophys. Res. Commun. 289, 882-7, (2001). View articlePMID: 11735129

2.Absence of post-translational aspartyl beta-hydroxylation of epidermal growth factor domains in mice leads to developmental defects and an increased incidence of intestinal neoplasia. Dinchuk JE, Focht RJ, Kelley JA, Henderson NL, Zolotarjova NI, Wynn R, Neff NT, Link J, Huber RM, Burn TC, Rupar MJ, Cunningham MR, Selling BH, Ma J, Stern AA, Hollis GF, Stein RB, Friedman PA. J. Biol. Chem. 277, 12970-7, (2002). View articlePMID: 11773073

3.Molecular cloning and characterization of mouse cardiac triadin isoforms. Hong CS, Ji JH, Kim JP, Jung DH, Kim DH. Gene 278, 193-9, (2001). View articlePMID: 11707337

GO terms

biological process

  • None

molecular function

  • None

cellular component

Cross References

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