Aspartyl/asparaginyl beta-hydroxylase

Details

Name
Aspartyl/asparaginyl beta-hydroxylase
Synonyms
  • 1.14.11.16
  • ASP beta-hydroxylase
  • Aspartate beta-hydroxylase
  • BAH
  • Peptide-aspartate beta-dioxygenase
Gene Name
ASPH
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037038|Aspartyl/asparaginyl beta-hydroxylase
MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMV
IALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVP
PEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQ
QEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSE
PVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSI
FPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEA
VNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLK
LSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEV
LSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGN
KEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKETGYTELVKSLERNWKLIRDE
GLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGC
RRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFD
DSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
Number of residues
758
Molecular Weight
85862.095
Theoretical pI
4.67
GO Classification
Functions
calcium ion binding / electron carrier activity / ion channel binding / peptide-aspartate beta-dioxygenase activity / structural constituent of muscle / structural molecule activity
Processes
activation of cysteine-type endopeptidase activity / activation of store-operated calcium channel activity / calcium ion transmembrane transport / cellular response to calcium ion / detection of calcium ion / face morphogenesis / ion transmembrane transport / limb morphogenesis / muscle contraction / negative regulation of cell proliferation / palate development / pattern specification process / peptidyl-aspartic acid hydroxylation / positive regulation of calcium ion transport into cytosol / positive regulation of intracellular protein transport / positive regulation of proteolysis / positive regulation of ryanodine-sensitive calcium-release channel activity / positive regulation of transcription, DNA-templated / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of cell communication by electrical coupling / regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity / regulation of protein depolymerization / regulation of protein stability / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / regulation of ryanodine-sensitive calcium-release channel activity / response to ATP / transmembrane transport
Components
calcium channel complex / cortical endoplasmic reticulum / endoplasmic reticulum / endoplasmic reticulum membrane / integral component of endoplasmic reticulum membrane / integral component of membrane / junctional sarcoplasmic reticulum membrane / plasma membrane / sarcoplasmic reticulum lumen / sarcoplasmic reticulum membrane
General Function
Structural molecule activity
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
54-74
Cellular Location
Endoplasmic reticulum membrane
Gene sequence
>lcl|BSEQ0020468|Aspartyl/asparaginyl beta-hydroxylase (ASPH)
ATGGCTGAAGATAAAGAGACAAAGCATGGAGGACACAAGAATGGGAGGAAAGGCGGACTC
TCAGGAACTTCATTCTTCACGTGGTTTATGGTGATTGCATTGCTGGGCGTCTGGACATCT
GTAGCTGTCGTTTGGTTTGATCTTGTTGACTATGAGGAAGTTCTAGGAAAACTAGGAATC
TATGATGCTGATGGTGATGGAGATTTTGATGTGGATGATGCCAAAGTTTTATTAGGACTT
AAAGAGAGATCTACTTCAGAGCCAGCAGTCCCGCCAGAAGAGGCTGAGCCACACACTGAG
CCCGAGGAGCAGGTTCCTGTGGAGGCAGAACCCCAGAATATCGAAGATGAAGCAAAAGAA
CAAATTCAGTCCCTTCTCCATGAAATGGTACACGCAGAACATGTTGAGGGAGAAGACTTG
CAACAAGAAGATGGACCCACAGGAGAACCACAACAAGAGGATGATGAGTTTCTTATGGCG
ACTGATGTAGATGATAGATTTGAGACCCTGGAACCTGAAGTATCTCATGAAGAAACCGAG
CATAGTTACCACGTGGAAGAGACAGTTTCACAAGACTGTAATCAGGATATGGAAGAGATG
ATGTCTGAGCAGGAAAATCCAGATTCCAGTGAACCAGTAGTAGAAGATGAAAGATTGCAC
CATGATACAGATGATGTAACATACCAAGTCTATGAGGAACAAGCAGTATATGAACCTCTA
GAAAATGAAGGGATAGAAATCACAGAAGTAACTGCTCCCCCTGAGGATAATCCTGTAGAA
GATTCACAGGTAATTGTAGAAGAAGTAAGCATTTTTCCTGTGGAAGAACAGCAGGAAGTA
CCACCAGAAACAAATAGAAAAACAGATGATCCAGAACAAAAAGCAAAAGTTAAGAAAAAG
AAGCCTAAACTTTTAAATAAATTTGATAAGACTATTAAAGCTGAACTTGATGCTGCAGAA
AAACTCCGTAAAAGGGGAAAAATTGAGGAAGCAGTGAATGCATTTAAAGAACTAGTACGC
AAATACCCTCAGAGTCCACGAGCAAGATATGGGAAGGCGCAGTGTGAGGATGATTTGGCT
GAGAAGAGGAGAAGTAATGAGGTGCTACGTGGAGCCATCGAGACCTACCAAGAGGTGGCC
AGCCTACCTGATGTCCCTGCAGACCTGCTGAAGCTGAGTTTGAAGCGTCGCTCAGACAGG
CAACAATTTCTAGGTCATATGAGAGGTTCCCTGCTTACCCTGCAGAGATTAGTTCAACTA
TTTCCCAATGATACTTCCTTAAAAAATGACCTTGGCGTGGGATACCTCTTGATAGGAGAT
AATGACAATGCAAAGAAAGTTTATGAAGAGGTGCTGAGTGTGACACCTAATGATGGCTTT
GCTAAAGTCCATTATGGCTTCATCCTGAAGGCACAGAACAAAATTGCTGAGAGCATCCCA
TATTTAAAGGAAGGAATAGAATCCGGAGATCCTGGCACTGATGATGGGAGATTTTATTTC
CACCTGGGGGATGCCATGCAGAGGGTTGGGAACAAAGAGGCATATAAGTGGTATGAGCTT
GGGCACAAGAGAGGACACTTTGCATCTGTCTGGCAACGCTCACTCTACAATGTGAATGGA
CTGAAAGCACAGCCTTGGTGGACCCCAAAAGAAACGGGCTACACAGAGTTAGTAAAGTCT
TTAGAAAGAAACTGGAAGTTAATCCGAGATGAAGGCCTTGCAGTGATGGATAAAGCCAAA
GGTCTCTTCCTGCCTGAGGATGAAAACCTGAGGGAAAAAGGGGACTGGAGCCAGTTCACG
CTGTGGCAGCAAGGAAGAAGAAATGAAAATGCCTGCAAAGGAGCTCCTAAAACCTGTACC
TTACTAGAAAAGTTCCCCGAGACAACAGGATGCAGAAGAGGACAGATCAAATATTCCATC
ATGCACCCCGGGACTCACGTGTGGCCGCACACAGGGCCCACAAACTGCAGGCTCCGAATG
CACCTGGGCTTGGTGATTCCCAAGGAAGGCTGCAAGATTCGATGTGCCAACGAGACCAAG
ACCTGGGAGGAAGGCAAGGTGCTCATCTTTGATGACTCCTTTGAGCACGAGGTATGGCAG
GATGCCTCATCTTTCCGGCTGATATTCATCGTGGATGTGTGGCATCCGGAACTGACACCA
CAGCAGAGACGCAGCCTTCCAGCAATTTAG
Chromosome Location
8
Locus
8q12.1
External Identifiers
ResourceLink
UniProtKB IDQ12797
UniProtKB Entry NameASPH_HUMAN
GenBank Protein ID458032
GenBank Gene IDU03109
GenAtlas IDASPH
HGNC IDHGNC:757
General References
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  2. Lavaissiere L, Jia S, Nishiyama M, de la Monte S, Stern AM, Wands JR, Friedman PA: Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma. J Clin Invest. 1996 Sep 15;98(6):1313-23. [Article]
  3. Lim KY, Hong CS, Kim DH: cDNA cloning and characterization of human cardiac junctin. Gene. 2000 Sep 5;255(1):35-42. [Article]
  4. Dinchuk JE, Henderson NL, Burn TC, Huber R, Ho SP, Link J, O'Neil KT, Focht RJ, Scully MS, Hollis JM, Hollis GF, Friedman PA: Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin. J Biol Chem. 2000 Dec 15;275(50):39543-54. [Article]
  5. Treves S, Feriotto G, Moccagatta L, Gambari R, Zorzato F: 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. 2000 Dec 15;275(50):39555-68. [Article]
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  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  10. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
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  12. Srikanth S, Jew M, Kim KD, Yee MK, Abramson J, Gwack Y: Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 (STIM1). Proc Natl Acad Sci U S A. 2012 May 29;109(22):8682-7. doi: 10.1073/pnas.1200667109. Epub 2012 May 14. [Article]
  13. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [Article]
  14. Houle TD, Ram ML, Cala SE: Calsequestrin mutant D307H exhibits depressed binding to its protein targets and a depressed response to calcium. Cardiovasc Res. 2004 Nov 1;64(2):227-33. [Article]
  15. 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: 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. J Biol Chem. 2002 Apr 12;277(15):12970-7. Epub 2001 Dec 31. [Article]
  16. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  17. Patel N, Khan AO, Mansour A, Mohamed JY, Al-Assiri A, Haddad R, Jia X, Xiong Y, Megarbane A, Traboulsi EI, Alkuraya FS: Mutations in ASPH cause facial dysmorphism, lens dislocation, anterior-segment abnormalities, and spontaneous filtering blebs, or Traboulsi syndrome. Am J Hum Genet. 2014 May 1;94(5):755-9. doi: 10.1016/j.ajhg.2014.04.002. Epub 2014 Apr 24. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00128Aspartic acidapproved, nutraceuticalunknownDetails
DB00139Succinic acidapproved, nutraceuticalunknownproduct ofDetails