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Protein

Aspartyl/asparaginyl beta-hydroxylase

Gene

ASPH

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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 + CO2.2 Publications

Cofactori

Fe cation1 Publication

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi108 – 12013By similarityAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • peptide-aspartate beta-dioxygenase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Calcium, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.161 Publication)
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 Componenti: Chromosome 14

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5656CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei57 – 7721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini78 – 754677LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 754754Aspartyl/asparaginyl beta-hydroxylasePRO_0000064705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineBy similarity
Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi637 ↔ 644By similarity
Glycosylationi702 – 7021N-linked (GlcNAc...)Sequence Analysis

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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ28056.
PRIDEiQ28056.

Expressioni

Gene expression databases

ExpressionAtlasiQ28056. baseline and differential.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021267.

Structurei

3D structure databases

ProteinModelPortaliQ28056.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

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

Compositional bias

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

Sequence similaritiesi

Contains 5 TPR repeats.PROSITE-ProRule annotation

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_dom.
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

« Hide

        10         20         30         40         50
MAPRKNAKGG GGNSSSSSSG SPTGCTSGGS SSPGARRETK QGGLKNGRKG
60 70 80 90 100
GLSGSSFFTW FMVIALLGVW TSVAVVWFDL VDYEEVLAKA KDFRYNLSEV
110 120 130 140 150
LQGKLGIYDA DGDGDFDVDD AKVLLGLKEK PAPKPTVPPE EADMYPWLED
160 170 180 190 200
QVLESPGRQN IEDEVYEQVQ SLDETVYSEP GENLPQEPEG PAEELQPDDH
210 220 230 240 250
VFVGSDADDR YEPMGTGAVH EETEDSYHIE ETASPAYSQD MEDMMYEQEN
260 270 280 290 300
PDSSEPVVVD DAERTYQETD DVTYRDYDEQ DHAVDNSNTI LEEPHMPPAE
310 320 330 340 350
EQQEVPPETN KKADEPGKKG KVKKKKPKLL NKFDKTIKAE LDAAEKLRKR
360 370 380 390 400
GKIEEAVNAF EELVRKYPQS PGARYGKAQC EDDLAEKRRS NEILRRAIET
410 420 430 440 450
YQEAASLPDA PTDLVKLSLK RRSDRQQFLG HMRGSLLTLQ KLVQLFPDDT
460 470 480 490 500
ALKNDLGVGY LLIGDNDSAK KVYEEVLSVT PNDGFAKVHY GFILKAQNKI
510 520 530 540 550
AESIPYLKEG IESGDPGTDD GRFYFHLGDA MQRVGNKEAY RWYELGHQRG
560 570 580 590 600
HFASVWQRSL YNVQGLKAQP WWTPKETGYT ELVKSLERNW KLIRDEGLAA
610 620 630 640 650
MDRTHGLFLP EDENLREKGD WSQFTLWQQG RKNENACKGA PKTCSLLDKF
660 670 680 690 700
PETTGCRRGQ IKYSIMHPGT HVWPHTGPTN CRLRMHLGLV IPKEGCKIRC
710 720 730 740 750
ANETRTWEEG KVLIFDDSFE HEVWQDAASF RLIFIVDVWH PELTPHQRRS

LPAI
Length:754
Mass (Da):84,999
Last modified:November 1, 1997 - v1
Checksum:i369593A1F0B558C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
M91213 mRNA. Translation: AAA03563.1.
PIRiA42969. BABOH.
RefSeqiNP_777182.1. NM_174757.2.
UniGeneiBt.46037.

3D structure databases

ProteinModelPortaliQ28056.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021267.

Proteomic databases

PaxDbiQ28056.
PRIDEiQ28056.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi444.

Phylogenomic databases

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

Miscellaneous databases

NextBioi20806432.

Gene expression databases

ExpressionAtlasiQ28056. baseline and differential.

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_dom.
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]
ProtoNetiSearch...

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], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    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, SUBUNIT.
    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: March 4, 2015
This is version 109 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.