Reviewed, UniProtKB/Swiss-Prot Q28056 (ASPH_BOVIN)

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)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 electronic annotation. Source: EC
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	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
	Modified residue	32	1	Phosphoserine By similarity
	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)
	Q28056-1 [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: 1378441] [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: 1856229] [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.
UniGene	Bt.46037
3D structure databases
SMR	Q28056. Positions 456-535, 618-738.
ModBase	Search...
Protein-protein interaction databases
STRING	Q28056.
Genome annotation databases
Ensembl	ENSBTAT00000021267; ENSBTAP00000021267; ENSBTAG00000026283; Bos taurus. [Genome view]
GeneID	286771.
KEGG	bta:286771.
Organism-specific databases
CTD	286771.
Phylogenomic databases
eggNOG	maNOG06588.
HOVERGEN	Q28056.
InParanoid	Q28056.
OMA	EKLRKRX.
OrthoDB	EOG954CHX.
Enzyme and pathway databases
BRENDA	1.14.11.16. 251.
Family and domain databases
InterPro	IPR007803. Asp_Arg_b-Hydrxlase. IPR013026. TPR-contain. IPR011990. TPR-like_helical. IPR019734. TPR_repeat. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
Pfam	PF05118. Asp_Arg_Hydrox. 1 hit. [Graphical view]
PROSITE	PS50005. TPR. 2 hits. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...

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:	February 9, 2010
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)