Reviewed,
UniProtKB/Swiss-Prot Q28056 (ASPH_BOVIN)
Last modified
November 25, 2008.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aspartyl/asparaginyl beta-hydroxylase EC=1.14.11.16 Alternative name(s): Aspartate beta-hydroxylase Short name=ASP beta-hydroxylase Peptide-aspartate beta-dioxygenase | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 754 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins. |
| Catalytic activity | Peptide L-aspartate + 2-oxoglutarate + O(2) = peptide 3-hydroxy-L-aspartate + succinate + CO(2). |
| Cofactor | Iron. |
| Subunit structure | Monomer. |
| Subcellular location | Endoplasmic reticulum membrane; Single-pass type II membrane protein. |
| Post-translational modification | Might be processed to the 56 kDa (AA 289-754) or 52 kDa (AA 311-754) forms in the lumen of the endoplasmic reticulum. |
| Sequence similarities | Belongs to the aspartyl/asparaginyl beta-hydroxylase family. Contains 5 TPR repeats. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Repeat Signal-anchor TPR repeat Transmembrane |
| Ligand | Iron |
| Molecular function | Dioxygenase Oxidoreductase |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-amino acid modificationInferred from electronic annotation. Source: InterPro |
| Cellular component | integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred from electronic annotation. Source: UniProtKB-KW peptide-aspartate beta-dioxygenase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 754 | 754 | Aspartyl/asparaginyl beta-hydroxylase | PRO_0000064705 | |||||
Regions | |||||||||
| Topological domain | 1 – 56 | 56 | Cytoplasmic Potential | ||||||
| Transmembrane | 57 – 77 | 21 | Signal-anchor for type II membrane protein Potential | ||||||
| Topological domain | 78 – 754 | 677 | Lumenal Potential | ||||||
| Repeat | 337 – 370 | 34 | TPR 1 | ||||||
| Repeat | 378 – 411 | 34 | TPR 2 | ||||||
| Repeat | 450 – 483 | 34 | TPR 3 | ||||||
| Repeat | 485 – 517 | 33 | TPR 4 | ||||||
| Repeat | 521 – 553 | 33 | TPR 5 | ||||||
| Compositional bias | 9 – 12 | 4 | Poly-Gly | ||||||
| Compositional bias | 14 – 21 | 8 | Poly-Ser | ||||||
| Compositional bias | 311 – 352 | 42 | Lys-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 32 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 96 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 466 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 702 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-hydroxylase." Jia S., Vandusen W.J., Diehl R.E., Kohl N.E., Dixon R.A.F., Elliston K.O., Stern A.M., Friedman P.A. J. Biol. Chem. 267:14322-14327(1992) [PubMed: 1378441] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain and Liver. |
| [2] | "Bovine liver aspartyl beta-hydroxylase. Purification and characterization." Wang Q., Vandusen W.J., Petroski C.J., Garsky V.M., Stern A.M., Friedman P.A. J. Biol. Chem. 266:14004-14010(1991) [PubMed: 1856229] [Abstract] Cited for: PROTEIN SEQUENCE OF 289-385 AND 615-641. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| M91213 mRNA. Translation: AAA03563.1. | |
| PIR | BABOH. A42969. |
| RefSeq | NP_777182.1. |
| UniGene | Bt.46037 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAG00000026283. Bos taurus. [Contig view] |
| GeneID | 286771. |
| KEGG | bta:286771. |
Phylogenomic databases | |
| HOVERGEN | Q28056. |
Family and domain databases | |
| InterPro | IPR007943. Asp-B-hydro_N. IPR007803. Asp_Arg_Hydrox. IPR011990. TPR-like_helical. IPR013026. TPR_region. [Graphical view] |
| Gene3D | G3DSA:1.25.40.10. TPR-like_helical. 1 hit. |
| Pfam | PF05279. Asp-B-Hydro_N. 1 hit. PF05118. Asp_Arg_Hydrox. 1 hit. [Graphical view] |
| PROSITE | PS50005. TPR. 2 hits. PS50293. TPR_REGION. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASPH_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q28056 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


