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Showing Protein Aspartyl/asparaginyl beta-hydroxylase (HMDBP01022)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 6 metabolites
Identification
HMDB Protein ID HMDBP01022
Secondary Accession Numbers
  • 6310
Name Aspartyl/asparaginyl beta-hydroxylase
Synonyms
  1. ASP beta-hydroxylase
  2. Aspartate beta-hydroxylase
  3. Peptide-aspartate beta-dioxygenase
Gene Name ASPH
Protein Type Unknown
Biological Properties
General Function Involved in peptide-aspartate beta-dioxygenase 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.
Pathways Not Available
Reactions
Peptide L-aspartate + Oxoglutaric acid + Oxygen → peptide 3-hydroxy-L-aspartate + Succinic acid + CO(2) details
GO Classification
Biological Process
cellular response to calcium ion
activation of store-operated calcium channel activity
calcium ion transmembrane transport
face morphogenesis
limb morphogenesis
muscle contraction
negative regulation of ryanodine-sensitive calcium-release channel activity
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 ryanodine-sensitive calcium-release channel activity
regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity
regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
response to ATP
positive regulation of transcription, DNA-dependent
negative regulation of cell proliferation
Cellular Component
integral to endoplasmic reticulum membrane
plasma membrane
cortical endoplasmic reticulum
junctional sarcoplasmic reticulum membrane
Component
membrane
cell part
membrane part
intrinsic to membrane
intrinsic to organelle membrane
intrinsic to endoplasmic reticulum membrane
integral to endoplasmic reticulum membrane
Function
binding
catalytic activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
peptide-aspartate beta-dioxygenase activity
oxidoreductase activity
Molecular Function
electron carrier activity
peptide-aspartate beta-dioxygenase activity
structural constituent of muscle
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
calcium ion binding
Process
metabolic process
macromolecule metabolic process
macromolecule modification
protein modification process
oxidation reduction
peptidyl-amino acid modification
Cellular Location
  1. Single-pass type II membrane protein
  2. Isoform 1:Endoplasmic reticulum membrane
Gene Properties
Chromosome Location 8
Locus 8q12.1
SNPs ASPH
Gene Sequence 
>2277 bp
ATGGCCCAGCGTAAGAATGCCAAGAGCAGCGGCAACAGCAGCAGCAGCGGCTCCGGCAGC
GGTAGCACGAGTGCGGGCAGCAGCAGCCCCGGGGCCCGGAGAGAGACAAAGCATGGAGGA
CACAAGAATGGGAGGAAAGGCGGACTCTCAGGAACTTCATTCTTCACGTGGTTTATGGTG
ATTGCATTGCTGGGCGTCTGGACATCTGTAGCTGTCGTTTGGTTTGATCTTGTTGACTAT
GAGGAAGTTCTAGGAAAACTAGGAATCTATGATGCTGATGGTGATGGAGATTTTGATGTG
GATGATGCCAAAGTTTTATTAGGACTTAAAGAGAGATCTACTTCAGAGCCAGCAGTCCCG
CCAGAAGAGGCTGAGCCACACACTGAGCCCGAGGAGCAGGTTCCTGTGGAGGCAGAACCC
CAGAATATCGAAGATGAAGCAAAAGAACAAATTCAGTCCCTTCTCCATGAAATGGTACAC
GCAGAACATGTTGAGGGAGAAGACTTGCAACAAGAAGATGGACCCACAGGAGAACCACAA
CAAGAGGATGATGAGTTTCTTATGGCGACTGATGTAGATGATAGATTTGAGACCCTGGAA
CCTGAAGTATCTCATGAAGAAACCGAGCATAGTTACCACGTGGAAGAGACAGTTTCACAA
GACTGTAATCAGGATATGGAAGAGATGATGTCTGAGCAGGAAAATCCAGATTCCAGTGAA
CCAGTAGTAGAAGATGAAAGATTGCACCATGATACAGATGATGTAACATACCAAGTCTAT
GAGGAACAAGCAGTATATGAACCTCTAGAAAATGAAGGGATAGAAATCACAGAAGTAACT
GCTCCCCCTGAGGATAATCCTGTAGAAGATTCACAGGTAATTGTAGAAGAAGTAAGCATT
TTTCCTGTGGAAGAACAGCAGGAAGTACCACCAGAAACAAATAGAAAAACAGATGATCCA
GAACAAAAAGCAAAAGTTAAGAAAAAGAAGCCTAAACTTTTAAATAAATTTGATAAGACT
ATTAAAGCTGAACTTGATGCTGCAGAAAAACTCCGTAAAAGGGGAAAAATTGAGGAAGCA
GTGAATGCATTTAAAGAACTAGTACGCAAATACCCTCAGAGTCCACGAGCAAGATATGGG
AAGGCGCAGTGTGAGGATGATTTGGCTGAGAAGAGGAGAAGTAATGAGGTGCTACGTGGA
GCCATCGAGACCTACCAAGAGGTGGCCAGCCTACCTGATGTCCCTGCAGACCTGCTGAAG
CTGAGTTTGAAGCGTCGCTCAGACAGGCAACAATTTCTAGGTCATATGAGAGGTTCCCTG
CTTACCCTGCAGAGATTAGTTCAACTATTTCCCAATGATACTTCCTTAAAAAATGACCTT
GGCGTGGGATACCTCTTGATAGGAGATAATGACAATGCAAAGAAAGTTTATGAAGAGGTG
CTGAGTGTGACACCTAATGATGGCTTTGCTAAAGTCCATTATGGCTTCATCCTGAAGGCA
CAGAACAAAATTGCTGAGAGCATCCCATATTTAAAGGAAGGAATAGAATCCGGAGATCCT
GGCACTGATGATGGGAGATTTTATTTCCACCTGGGGGATGCCATGCAGAGGGTTGGGAAC
AAAGAGGCATATAAGTGGTATGAGCTTGGGCACAAGAGAGGACACTTTGCATCTGTCTGG
CAACGCTCACTCTACAATGTGAATGGACTGAAAGCACAGCCTTGGTGGACCCCAAAAGAA
ACGGGCTACACAGAGTTAGTAAAGTCTTTAGAAAGAAACTGGAAGTTAATCCGAGATGAA
GGCCTTGCAGTGATGGATAAAGCCAAAGGTCTCTTCCTGCCTGAGGATGAAAACCTGAGG
GAAAAAGGGGACTGGAGCCAGTTCACGCTGTGGCAGCAAGGAAGAAGAAATGAAAATGCC
TGCAAAGGAGCTCCTAAAACCTGTACCTTACTAGAAAAGTTCCCCGAGACAACAGGATGC
AGAAGAGGACAGATCAAATATTCCATCATGCACCCCGGGACTCACGTGTGGCCGCACACA
GGGCCCACAAACTGCAGGCTCCGAATGCACCTGGGCTTGGTGATTCCCAAGGAAGGCTGC
AAGATTCGATGTGCCAACGAGACCAAGACCTGGGAGGAAGGCAAGGTGCTCATCTTTGAT
GACTCCTTTGAGCACGAGGTATGGCAGGATGCCTCATCTTTCCGGCTGATATTCATCGTG
GATGTGTGGCATCCGGAACTGACACCACAGCAGAGACGCAGCCTTCCAGCAATTTAG
Protein Properties
Number of Residues 758
Molecular Weight 83267.47
Theoretical pI 4.914
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Aspartyl/asparaginyl beta-hydroxylase
MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMV
IALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVP
PEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQ
QEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSE
PVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSI
FPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEA
VNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLK
LSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEV
LSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGN
KEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKETGYTELVKSLERNWKLIRDE
GLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGC
RRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFD
DSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
GenBank ID Protein 14589866
UniProtKB/Swiss-Prot ID Q12797
UniProtKB/Swiss-Prot Entry Name ASPH_HUMAN
PDB IDs
GenBank Gene ID NM_004318.3
GeneCard ID ASPH
GenAtlas ID ASPH
HGNC ID HGNC:757
References
General References
  1. 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. [PubMed:19159218 ]
  2. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed:16421571 ]
  5. Korioth F, Gieffers C, Frey J: Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase. Gene. 1994 Dec 15;150(2):395-9. [PubMed:7821814 ]
  6. 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. [PubMed:8823296 ]
  7. Lim KY, Hong CS, Kim DH: cDNA cloning and characterization of human cardiac junctin. Gene. 2000 Sep 5;255(1):35-42. [PubMed:10974562 ]
  8. 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. [PubMed:10956665 ]
  9. Wetzel GT, Ding S, Chen F: Molecular cloning of junctin from human and developing rabbit heart. Mol Genet Metab. 2000 Mar;69(3):252-8. [PubMed:10767180 ]