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Q28056

- ASPH_BOVIN

UniProt

Q28056 - ASPH_BOVIN

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Protein
Aspartyl/asparaginyl beta-hydroxylase
Gene
ASPH
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.1 Publication

Catalytic activityi

Peptide L-aspartate + 2-oxoglutarate + O2 = peptide 3-hydroxy-L-aspartate + succinate + CO2.1 Publication

Cofactori

Iron.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei621 – 62112-oxoglutarate By similarity
Binding sitei664 – 66412-oxoglutarate By similarity
Metal bindingi675 – 6751Iron By similarity
Metal bindingi721 – 7211Iron By similarity
Binding sitei731 – 73112-oxoglutarate By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. peptide-aspartate beta-dioxygenase activity Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity Source: Ensembl
  2. activation of store-operated calcium channel activity Source: Ensembl
  3. calcium ion transmembrane transport Source: Ensembl
  4. cellular response to calcium ion Source: Ensembl
  5. face morphogenesis Source: Ensembl
  6. limb morphogenesis Source: Ensembl
  7. negative regulation of cell proliferation Source: Ensembl
  8. palate development Source: Ensembl
  9. pattern specification process Source: Ensembl
  10. peptidyl-aspartic acid hydroxylation Source: UniProtKB
  11. positive regulation of calcium ion transport into cytosol Source: Ensembl
  12. positive regulation of intracellular protein transport Source: Ensembl
  13. positive regulation of proteolysis Source: Ensembl
  14. positive regulation of transcription, DNA-templated Source: Ensembl
  15. regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: Ensembl
  16. regulation of protein depolymerization Source: Ensembl
  17. regulation of protein stability Source: Ensembl
  18. response to ATP Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:ASPH
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 14

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5656Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei57 – 7721Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini78 – 754677Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cortical endoplasmic reticulum Source: Ensembl
  2. integral component of endoplasmic reticulum membrane Source: Ensembl
  3. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 754754Aspartyl/asparaginyl beta-hydroxylase
PRO_0000064705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi96 – 961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi466 – 4661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi637 ↔ 644 By similarity
Glycosylationi702 – 7021N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Might be processed to the 56 kDa (AA 289-754) or 52 kDa (AA 311-754) forms in the lumen of the endoplasmic reticulum.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ28056.
PRIDEiQ28056.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021267.

Structurei

3D structure databases

ProteinModelPortaliQ28056.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati337 – 37034TPR 1
Add
BLAST
Repeati378 – 41134TPR 2
Add
BLAST
Repeati450 – 48334TPR 3
Add
BLAST
Repeati485 – 51733TPR 4
Add
BLAST
Repeati521 – 55333TPR 5
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni684 – 68632-oxoglutarate binding By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 124Poly-Gly
Compositional biasi14 – 218Poly-Ser
Compositional biasi311 – 35242Lys-rich
Add
BLAST

Sequence similaritiesi

Contains 5 TPR repeats.

Keywords - Domaini

Repeat, Signal-anchor, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3555.
GeneTreeiENSGT00530000063281.
HOGENOMiHOG000231625.
HOVERGENiHBG004290.
InParanoidiQ28056.
KOiK00476.
OMAiRNENACK.
OrthoDBiEOG715Q44.
TreeFamiTF312799.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.60.120.330. 1 hit.
InterProiIPR007943. 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]
PfamiPF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view]
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q28056-1 [UniParc]FASTAAdd to Basket

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MAPRKNAKGG GGNSSSSSSG SPTGCTSGGS SSPGARRETK QGGLKNGRKG    50
GLSGSSFFTW FMVIALLGVW TSVAVVWFDL VDYEEVLAKA KDFRYNLSEV 100
LQGKLGIYDA DGDGDFDVDD AKVLLGLKEK PAPKPTVPPE EADMYPWLED 150
QVLESPGRQN IEDEVYEQVQ SLDETVYSEP GENLPQEPEG PAEELQPDDH 200
VFVGSDADDR YEPMGTGAVH EETEDSYHIE ETASPAYSQD MEDMMYEQEN 250
PDSSEPVVVD DAERTYQETD DVTYRDYDEQ DHAVDNSNTI LEEPHMPPAE 300
EQQEVPPETN KKADEPGKKG KVKKKKPKLL NKFDKTIKAE LDAAEKLRKR 350
GKIEEAVNAF EELVRKYPQS PGARYGKAQC EDDLAEKRRS NEILRRAIET 400
YQEAASLPDA PTDLVKLSLK RRSDRQQFLG HMRGSLLTLQ KLVQLFPDDT 450
ALKNDLGVGY LLIGDNDSAK KVYEEVLSVT PNDGFAKVHY GFILKAQNKI 500
AESIPYLKEG IESGDPGTDD GRFYFHLGDA MQRVGNKEAY RWYELGHQRG 550
HFASVWQRSL YNVQGLKAQP WWTPKETGYT ELVKSLERNW KLIRDEGLAA 600
MDRTHGLFLP EDENLREKGD WSQFTLWQQG RKNENACKGA PKTCSLLDKF 650
PETTGCRRGQ IKYSIMHPGT HVWPHTGPTN CRLRMHLGLV IPKEGCKIRC 700
ANETRTWEEG KVLIFDDSFE HEVWQDAASF RLIFIVDVWH PELTPHQRRS 750
LPAI 754
Length:754
Mass (Da):84,999
Last modified:November 1, 1997 - v1
Checksum:i369593A1F0B558C8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M91213 mRNA. Translation: AAA03563.1.
PIRiA42969. BABOH.
RefSeqiNP_777182.1. NM_174757.2.
UniGeneiBt.46037.

Genome annotation databases

EnsembliENSBTAT00000021267; ENSBTAP00000021267; ENSBTAG00000026283.
GeneIDi286771.
KEGGibta:286771.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M91213 mRNA. Translation: AAA03563.1 .
PIRi A42969. BABOH.
RefSeqi NP_777182.1. NM_174757.2.
UniGenei Bt.46037.

3D structure databases

ProteinModelPortali Q28056.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000021267.

Proteomic databases

PaxDbi Q28056.
PRIDEi Q28056.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000021267 ; ENSBTAP00000021267 ; ENSBTAG00000026283 .
GeneIDi 286771.
KEGGi bta:286771.

Organism-specific databases

CTDi 444.

Phylogenomic databases

eggNOGi COG3555.
GeneTreei ENSGT00530000063281.
HOGENOMi HOG000231625.
HOVERGENi HBG004290.
InParanoidi Q28056.
KOi K00476.
OMAi RNENACK.
OrthoDBi EOG715Q44.
TreeFami TF312799.

Miscellaneous databases

NextBioi 20806432.

Family and domain databases

Gene3Di 1.25.40.10. 1 hit.
2.60.120.330. 1 hit.
InterProi IPR007943. 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 ]
Pfami PF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view ]
PROSITEi PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiASPH_BOVIN
AccessioniPrimary (citable) accession number: Q28056
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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