Q28056 (ASPH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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

Name:

ASPH

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	754 AA.
Sequence status	Complete.
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 + O2 = peptide 3-hydroxy-L-aspartate + succinate + CO2.
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 Transmembrane helix
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of store-operated calcium channel activity Inferred from electronic annotation. Source: Compara calcium ion transmembrane transport Inferred from electronic annotation. Source: Compara cellular response to calcium ion Inferred from electronic annotation. Source: Compara face morphogenesis Inferred from electronic annotation. Source: Compara limb morphogenesis Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara palate development Inferred from electronic annotation. Source: Compara pattern specification process Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of intracellular protein transport Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Inferred from electronic annotation. Source: Compara response to ATP Inferred from electronic annotation. Source: Compara
Cellular_component	cortical endoplasmic reticulum Inferred from electronic annotation. Source: Compara integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen 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 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	Helical; 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
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	466	1	N-linked (GlcNAc...) Potential
	Glycosylation	702	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q28056 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 369593A1F0B558C8	FASTA	754	84,999
	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

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. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M91213 mRNA. Translation: AAA03563.1.
IPI	IPI00697843.
PIR	BABOH. A42969.
RefSeq	NP_777182.1. NM_174757.2.
UniGene	Bt.46037.
3D structure databases
ProteinModelPortal	Q28056.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000021267.
Proteomic databases
PaxDb	Q28056.
PRIDE	Q28056.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000021267; ENSBTAP00000021267; ENSBTAG00000026283.
GeneID	286771.
KEGG	bta:286771.
Organism-specific databases
CTD	444.
Phylogenomic databases
eggNOG	COG3555.
GeneTree	ENSGT00530000063281.
HOGENOM	HOG000231625.
HOVERGEN	HBG004290.
InParanoid	Q28056.
KO	K00476.
OMA	FPNDTSL.
OrthoDB	EOG42FSK2.
Gene expression databases
ArrayExpress	Q28056.
Family and domain databases
Gene3D	1.25.40.10. 1 hit.
InterPro	IPR007943. Asp-B-hydro/Triadin_dom. IPR007803. Asp_Arg_b-Hydrxlase. IPR013026. TPR-contain_dom. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
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...
Other
NextBio	20806432.

Entry information

Entry name

ASPH_BOVIN

Accession

Primary (citable) accession number: Q28056

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program