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Q8BSY0 (ASPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length741 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 + O2 = peptide 3-hydroxy-L-aspartate + succinate + CO2.

Cofactor

Iron By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.

Post-translational modification

Might be processed to the 56 kDa (AA 274-757) or 52 kDa (AA 315-757) forms in the lumen of the endoplasmic reticulum By similarity.

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
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 mutant phenotype PubMed 11773073. Source: MGI

limb morphogenesis

Inferred from mutant phenotype PubMed 11773073. Source: MGI

negative regulation of cell proliferation

Inferred from genetic interaction PubMed 11773073. Source: MGI

palate development

Inferred from mutant phenotype PubMed 11773073. Source: MGI

pattern specification process

Inferred from mutant phenotype PubMed 11773073. Source: MGI

peptidyl-aspartic acid hydroxylation

Inferred from direct assay PubMed 11773073. Source: MGI

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 direct assay PubMed 22123818. Source: BHF-UCL

regulation of protein stability

Inferred from direct assay PubMed 22123818. Source: BHF-UCL

response to ATP

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcortical endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 22123818. Source: BHF-UCL

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from sequence or structural similarity Ref.1. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionpeptide-aspartate beta-dioxygenase activity

Inferred from sequence or structural similarity Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 741741Aspartyl/asparaginyl beta-hydroxylase
PRO_0000254161

Regions

Topological domain1 – 6262Cytoplasmic Potential
Transmembrane63 – 8321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain84 – 741658Lumenal Potential
Repeat324 – 35734TPR 1
Repeat365 – 39834TPR 2
Repeat437 – 47034TPR 3
Repeat472 – 50433TPR 4
Repeat508 – 54033TPR 5
Region671 – 67332-oxoglutarate binding By similarity
Compositional bias9 – 6153Gly-rich
Compositional bias14 – 3825Ser-rich
Compositional bias310 – 3156Poly-Lys

Sites

Metal binding6621Iron By similarity
Metal binding7081Iron By similarity
Binding site60812-oxoglutarate By similarity
Binding site65112-oxoglutarate By similarity
Binding site71812-oxoglutarate By similarity

Amino acid modifications

Glycosylation4531N-linked (GlcNAc...) Potential
Glycosylation6891N-linked (GlcNAc...) Potential
Disulfide bond624 ↔ 631 By similarity

Experimental info

Sequence conflict131 – 1322Missing in AAG40808. Ref.1
Sequence conflict131 – 1322Missing in AAG40809. Ref.1
Sequence conflict2791A → E in AAG40808. Ref.1
Sequence conflict2791A → E in AAG40809. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BSY0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0660A6A5E34418C8

FASTA74183,042
        10         20         30         40         50         60 
MAPRKNAKGG GGNSSSSGSG SGSGSGSPST GSSGSSSSPG ARREAKHGGH KNGRRGGISG 

        70         80         90        100        110        120 
GSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLGKLGVYD ADGDGDFDVD DAKVLLGLKE 

       130        140        150        160        170        180 
RSPSERTFPP EEEAETHAEL EEQAPEGADI QNVEDEVKEQ IQSLLQESVH TDHDLEADGL 

       190        200        210        220        230        240 
AGEPQPEVED FLTVTDSDDR FEDLEPGTVH EEIEDTYHVE DTASQNHPND MEEMTNEQEN 

       250        260        270        280        290        300 
SDPSEAVTDA GVLLPHAEEV RHQDYDEPVY EPSEHEGVAI SDNTIDDSSI ISEEINVASV 

       310        320        330        340        350        360 
EEQQDTPPVK KKKPKLLNKF DKTIKAELDA AEKLRKRGKI EEAVNAFEEL VRKYPQSPRA 

       370        380        390        400        410        420 
RYGKAQCEDD LAEKQRSNEV LRRAIETYQE AADLPDAPTD LVKLSLKRRS ERQQFLGHMR 

       430        440        450        460        470        480 
GSLLTLQRLV QLFPSDTTLK NDLGVGYLLL GDNDSAKKVY EEVLNVTPND GFAKVHYGFI 

       490        500        510        520        530        540 
LKAQNKISES IPYLKEGIES GDPGTDDGRF YFHLGDAMQR VGNKEAYKWY ELGHKRGHFA 

       550        560        570        580        590        600 
SVWQRSLYNV NGLKAQPWWT PRETGYTELV KSLERNWKLI RDEGLMVMDK AKGLFLPEDE 

       610        620        630        640        650        660 
NLREKGDWSQ FTLWQQGRKN ENACKGAPKT CALLEKFSET TGCRRGQIKY SIMHPGTHVW 

       670        680        690        700        710        720 
PHTGPTNCRL RMHLGLVIPK EGCKIRCANE TRTWEEGKVL IFDDSFEHEV WQDASSFRLI 

       730        740 
FIVDVWHPEL TPQQRRSLPA I 

« Hide

References

« Hide 'large scale' references
[1]"Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin."
Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J., O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F., Friedman P.A.
J. Biol. Chem. 275:39543-39554(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF289486 mRNA. Translation: AAG40808.1.
AF289487 mRNA. Translation: AAG40809.1.
AK030293 mRNA. Translation: BAC26882.1.
RefSeqNP_001171321.1. NM_001177850.1.
NP_001171323.1. NM_001177852.1.
NP_001171324.1. NM_001177853.1.
NP_001171325.1. NM_001177854.1.
NP_001171326.1. NM_001177855.1.
NP_075553.2. NM_023066.3.
UniGeneMm.222206.
Mm.412008.

3D structure databases

ProteinModelPortalQ8BSY0.
SMRQ8BSY0. Positions 328-376, 405-522, 545-741.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211167. 2 interactions.
IntActQ8BSY0. 5 interactions.
MINTMINT-4112262.

PTM databases

PhosphoSiteQ8BSY0.

Proteomic databases

PaxDbQ8BSY0.
PRIDEQ8BSY0.

Protocols and materials databases

DNASU65973.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000078139; ENSMUSP00000077273; ENSMUSG00000028207.
GeneID65973.
KEGGmmu:65973.
UCSCuc008ryf.2. mouse.

Organism-specific databases

CTD444.
MGIMGI:1914186. Asph.

Phylogenomic databases

eggNOGCOG3555.
GeneTreeENSGT00530000063281.
HOGENOMHOG000231625.
HOVERGENHBG004290.
InParanoidQ8BSY0.
KOK00476.
OMARNENACK.
OrthoDBEOG715Q44.
PhylomeDBQ8BSY0.
TreeFamTF312799.

Gene expression databases

ArrayExpressQ8BSY0.
BgeeQ8BSY0.
CleanExMM_ASPH.
GenevestigatorQ8BSY0.

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.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PROSITEPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio320434.
PROQ8BSY0.
SOURCESearch...

Entry information

Entry nameASPH_MOUSE
AccessionPrimary (citable) accession number: Q8BSY0
Secondary accession number(s): Q9EPA6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 101 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot