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Q28056 (ASPH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:ASPH
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length754 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.2

Catalytic activity

Peptide L-aspartate + 2-oxoglutarate + O2 = peptide 3-hydroxy-L-aspartate + succinate + CO2. Ref.2

Cofactor

Iron. Ref.2

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 componentEndoplasmic reticulum
Membrane
   DomainRepeat
Signal-anchor
TPR repeat
Transmembrane
Transmembrane helix
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

activation of store-operated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

calcium ion transmembrane transport

Inferred from electronic annotation. Source: Ensembl

cellular response to calcium ion

Inferred from electronic annotation. Source: Ensembl

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from electronic annotation. Source: Ensembl

pattern specification process

Inferred from electronic annotation. Source: Ensembl

peptidyl-aspartic acid hydroxylation

Inferred from direct assay PubMed 92332546. Source: UniProtKB

positive regulation of calcium ion transport into cytosol

Inferred from electronic annotation. Source: Ensembl

positive regulation of intracellular protein transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from electronic annotation. Source: Ensembl

regulation of protein depolymerization

Inferred from electronic annotation. Source: Ensembl

regulation of protein stability

Inferred from electronic annotation. Source: Ensembl

response to ATP

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcortical endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptide-aspartate beta-dioxygenase activity

Inferred from direct assay PubMed 92332546. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 754754Aspartyl/asparaginyl beta-hydroxylase
PRO_0000064705

Regions

Topological domain1 – 5656Cytoplasmic Potential
Transmembrane57 – 7721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain78 – 754677Lumenal Potential
Repeat337 – 37034TPR 1
Repeat378 – 41134TPR 2
Repeat450 – 48334TPR 3
Repeat485 – 51733TPR 4
Repeat521 – 55333TPR 5
Region684 – 68632-oxoglutarate binding By similarity
Compositional bias9 – 124Poly-Gly
Compositional bias14 – 218Poly-Ser
Compositional bias311 – 35242Lys-rich

Sites

Metal binding6751Iron By similarity
Metal binding7211Iron By similarity
Binding site62112-oxoglutarate By similarity
Binding site66412-oxoglutarate By similarity
Binding site73112-oxoglutarate By similarity

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation7021N-linked (GlcNAc...) Potential
Disulfide bond637 ↔ 644 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28056 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 369593A1F0B558C8

FASTA75484,999
        10         20         30         40         50         60 
MAPRKNAKGG GGNSSSSSSG SPTGCTSGGS SSPGARRETK QGGLKNGRKG GLSGSSFFTW 

        70         80         90        100        110        120 
FMVIALLGVW TSVAVVWFDL VDYEEVLAKA KDFRYNLSEV LQGKLGIYDA DGDGDFDVDD 

       130        140        150        160        170        180 
AKVLLGLKEK PAPKPTVPPE EADMYPWLED QVLESPGRQN IEDEVYEQVQ SLDETVYSEP 

       190        200        210        220        230        240 
GENLPQEPEG PAEELQPDDH VFVGSDADDR YEPMGTGAVH EETEDSYHIE ETASPAYSQD 

       250        260        270        280        290        300 
MEDMMYEQEN PDSSEPVVVD DAERTYQETD DVTYRDYDEQ DHAVDNSNTI LEEPHMPPAE 

       310        320        330        340        350        360 
EQQEVPPETN KKADEPGKKG KVKKKKPKLL NKFDKTIKAE LDAAEKLRKR GKIEEAVNAF 

       370        380        390        400        410        420 
EELVRKYPQS PGARYGKAQC EDDLAEKRRS NEILRRAIET YQEAASLPDA PTDLVKLSLK 

       430        440        450        460        470        480 
RRSDRQQFLG HMRGSLLTLQ KLVQLFPDDT ALKNDLGVGY LLIGDNDSAK KVYEEVLSVT 

       490        500        510        520        530        540 
PNDGFAKVHY GFILKAQNKI AESIPYLKEG IESGDPGTDD GRFYFHLGDA MQRVGNKEAY 

       550        560        570        580        590        600 
RWYELGHQRG HFASVWQRSL YNVQGLKAQP WWTPKETGYT ELVKSLERNW KLIRDEGLAA 

       610        620        630        640        650        660 
MDRTHGLFLP EDENLREKGD WSQFTLWQQG RKNENACKGA PKTCSLLDKF PETTGCRRGQ 

       670        680        690        700        710        720 
IKYSIMHPGT HVWPHTGPTN CRLRMHLGLV IPKEGCKIRC ANETRTWEEG KVLIFDDSFE 

       730        740        750 
HEVWQDAASF RLIFIVDVWH PELTPHQRRS LPAI 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 289-385 AND 615-641, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M91213 mRNA. Translation: AAA03563.1.
PIRBABOH. A42969.
RefSeqNP_777182.1. NM_174757.2.
UniGeneBt.46037.

3D structure databases

ProteinModelPortalQ28056.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000021267.

Proteomic databases

PaxDbQ28056.
PRIDEQ28056.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000021267; ENSBTAP00000021267; ENSBTAG00000026283.
GeneID286771.
KEGGbta:286771.

Organism-specific databases

CTD444.

Phylogenomic databases

eggNOGCOG3555.
GeneTreeENSGT00530000063281.
HOGENOMHOG000231625.
HOVERGENHBG004290.
InParanoidQ28056.
KOK00476.
OMARNENACK.
OrthoDBEOG715Q44.
TreeFamTF312799.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
2.60.120.330. 1 hit.
InterProIPR007943. Asp-B-hydro/Triadin_dom.
IPR007803. Asp_Arg_Pro-Hydrxlase.
IPR027443. IPNS-like.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view]
PROSITEPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20806432.

Entry information

Entry nameASPH_BOVIN
AccessionPrimary (citable) accession number: Q28056
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families