Q8BSY0 (ASPH_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	741 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 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 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: 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 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: Compara
Cellular_component	cortical endoplasmic reticulum Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 22123818. Source: BHF-UCL integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from sequence or structural similarity Ref.1. Source: MGI 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 sequence or structural similarity Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 741	741	Aspartyl/asparaginyl beta-hydroxylase		PRO_0000254161
Regions
	Topological domain	1 – 62	62	Cytoplasmic Potential
	Transmembrane	63 – 83	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	84 – 741	658	Lumenal Potential
	Repeat	324 – 357	34	TPR 1
	Repeat	365 – 398	34	TPR 2
	Repeat	437 – 470	34	TPR 3
	Repeat	472 – 504	33	TPR 4
	Repeat	508 – 540	33	TPR 5
	Compositional bias	9 – 61	53	Gly-rich
	Compositional bias	14 – 38	25	Ser-rich
	Compositional bias	310 – 315	6	Poly-Lys
Amino acid modifications
	Glycosylation	453	1	N-linked (GlcNAc...) Potential
	Glycosylation	689	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	131 – 132	2	Missing in AAG40808. Ref.1
	Sequence conflict	131 – 132	2	Missing in AAG40809. Ref.1
	Sequence conflict	279	1	A → E in AAG40808. Ref.1
	Sequence conflict	279	1	A → E in AAG40809. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BSY0 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 0660A6A5E34418C8	FASTA	741	83,042
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00624896.
RefSeq	NP_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.
UniGene	Mm.222206. Mm.412008.
3D structure databases
ProteinModelPortal	Q8BSY0.
SMR	Q8BSY0. Positions 437-537, 545-741.
ModBase	Search...
PTM databases
PhosphoSite	Q8BSY0.
Proteomic databases
PaxDb	Q8BSY0.
PRIDE	Q8BSY0.
Protocols and materials databases
DNASU	65973.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000078139; ENSMUSP00000077273; ENSMUSG00000028207.
GeneID	65973.
KEGG	mmu:65973.
Organism-specific databases
CTD	444.
MGI	MGI:1914186. Asph.
Phylogenomic databases
eggNOG	COG3555.
GeneTree	ENSGT00530000063281.
HOGENOM	HOG000231625.
HOVERGEN	HBG004290.
InParanoid	Q8BSY0.
KO	K00476.
OMA	FPNDTSL.
OrthoDB	EOG42FSK2.
Gene expression databases
ArrayExpress	Q8BSY0.
Bgee	Q8BSY0.
CleanEx	MM_ASPH.
Genevestigator	Q8BSY0.
GermOnline	ENSMUSG00000028207. Mus musculus.
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. IPR013105. TPR_2. IPR019734. TPR_repeat. [Graphical view]
Pfam	PF05279. Asp-B-Hydro_N. 1 hit. PF05118. Asp_Arg_Hydrox. 1 hit. PF07719. TPR_2. 1 hit. [Graphical view]
PROSITE	PS50005. TPR. 2 hits. PS50293. TPR_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	320434.
SOURCE	Search...

Entry information

Entry name

ASPH_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program