Reviewed, UniProtKB/Swiss-Prot Q12797 (ASPH_HUMAN)

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

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	758 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Tissue specificity	Detected in all tissues tested.
Sequence similarities	Belongs to the aspartyl/asparaginyl beta-hydroxylase family. Contains 4 TPR repeats.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal-anchor TPR repeat Transmembrane
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	muscle contraction Traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular function	calcium ion binding Traceable author statement. Source: ProtInc electron carrier activity Ref.1 Traceable author statement. Source: UniProtKB 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 Traceable author statement. Source: ProtInc structural constituent of muscle Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 758	758	Aspartyl/asparaginyl beta-hydroxylase		PRO_0000064706
Regions
	Topological domain	1 – 53	53	Cytoplasmic Potential
	Transmembrane	54 – 74	21	Signal-anchor for type II membrane protein Potential
	Topological domain	75 – 758	684	Lumenal Potential
	Repeat	341 – 374	34	TPR 1
	Repeat	454 – 487	34	TPR 2
	Repeat	489 – 521	33	TPR 3
	Repeat	525 – 557	33	TPR 4
	Compositional bias	9 – 29	21	Ser-rich
	Compositional bias	111 – 312	202	Glu-rich
	Compositional bias	323 – 332	10	Poly-Lys
Amino acid modifications
	Modified residue	29	1	Phosphoserine Ref.5
	Glycosylation	452	1	N-linked (GlcNAc...)
	Glycosylation	706	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	354	1	R → M: dbSNP rs6995412.		VAR_053781
Experimental info
	Sequence conflict	565	1	Y → I in AAA82108. Ref.1
	Sequence conflict	575 – 577	3	WWT → CG in AAA82108. Ref.1
	Sequence conflict	585	1	E → Q in AAA82108. Ref.1
	Sequence conflict	709	1	K → R in AAB50779. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q12797-1 [UniParc]. Last modified April 17, 2007. Version 3. Checksum: 4AE56D1D8DF0AF0C	FASTA	758	85,863
	10 20 30 40 50 60 MAQRKNAKSS GNSSSSGSGS GSTSAGSSSP GARRETKHGG HKNGRKGGLS GTSFFTWFMV 70 80 90 100 110 120 IALLGVWTSV AVVWFDLVDY EEVLGKLGIY DADGDGDFDV DDAKVLLGLK ERSTSEPAVP 130 140 150 160 170 180 PEEAEPHTEP EEQVPVEAEP QNIEDEAKEQ IQSLLHEMVH AEHVEGEDLQ QEDGPTGEPQ 190 200 210 220 230 240 QEDDEFLMAT DVDDRFETLE PEVSHEETEH SYHVEETVSQ DCNQDMEEMM SEQENPDSSE 250 260 270 280 290 300 PVVEDERLHH DTDDVTYQVY EEQAVYEPLE NEGIEITEVT APPEDNPVED SQVIVEEVSI 310 320 330 340 350 360 FPVEEQQEVP PETNRKTDDP EQKAKVKKKK PKLLNKFDKT IKAELDAAEK LRKRGKIEEA 370 380 390 400 410 420 VNAFKELVRK YPQSPRARYG KAQCEDDLAE KRRSNEVLRG AIETYQEVAS LPDVPADLLK 430 440 450 460 470 480 LSLKRRSDRQ QFLGHMRGSL LTLQRLVQLF PNDTSLKNDL GVGYLLIGDN DNAKKVYEEV 490 500 510 520 530 540 LSVTPNDGFA KVHYGFILKA QNKIAESIPY LKEGIESGDP GTDDGRFYFH LGDAMQRVGN 550 560 570 580 590 600 KEAYKWYELG HKRGHFASVW QRSLYNVNGL KAQPWWTPKE TGYTELVKSL ERNWKLIRDE 610 620 630 640 650 660 GLAVMDKAKG LFLPEDENLR EKGDWSQFTL WQQGRRNENA CKGAPKTCTL LEKFPETTGC 670 680 690 700 710 720 RRGQIKYSIM HPGTHVWPHT GPTNCRLRMH LGLVIPKEGC KIRCANETKT WEEGKVLIFD 730 740 750 DSFEHEVWQD ASSFRLIFIV DVWHPELTPQ QRRSLPAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase." Korioth F., Gieffers C., Frey J. Gene 150:395-399(1994) [PubMed: 7821814] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma." Lavaissiere L., Jia S., Nishiyama M., de la Monte S., Stern A.M., Wands J.R., Friedman P.A. J. Clin. Invest. 98:1313-1323(1996) [PubMed: 8823296] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed: 16421571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-452, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U03109 mRNA. Translation: AAA82108.1. S83325 mRNA. Translation: AAB50779.1. AC067881 Genomic DNA. No translation available. CH471068 Genomic DNA. Translation: EAW86848.1.
IPI	IPI00294834.
PIR	I38423.
RefSeq	NP_004309.2.
UniGene	Hs.622998
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q12797.
Proteomic databases
PRIDE	Q12797.
Genome annotation databases
Ensembl	ENSG00000198363. Homo sapiens. [Contig view]
GeneID	444.
KEGG	hsa:444.
Organism-specific databases
GeneCards	GC08M062578.
H-InvDB	HIX0034267.
HGNC	HGNC:757. ASPH.
MIM	600582. gene.
PharmGKB	PA25056.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q12797.
OMA	Q12797. TEHVEGE.
Enzyme and pathway databases
BRENDA	1.14.11.16. 247.
Gene expression databases
ArrayExpress	Q12797.
Bgee	Q12797.
CleanEx	HS_ASPH.
GermOnline	ENSG00000198363. Homo sapiens.
Family and domain databases
InterPro	IPR007943. Asp-B-hydro_N. IPR007803. Asp_Arg_b-Hydrxlase. IPR011990. TPR-like_helical. IPR013026. TPR_region. IPR019734. TPR_repeat. [Graphical view]
Gene3D	G3DSA:1.25.40.10. TPR-like_helical. 1 hit.
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 Resources
DrugBank	DB00128. L-Aspartic Acid. DB00139. Succinic acid.
NextBio	1859.
SOURCE	Search...

Entry information

Entry name

ASPH_HUMAN

Accession

Primary (citable) accession number: Q12797
Secondary accession number(s): A6NHI2, Q9Y4J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	April 17, 2007
Last modified:	June 16, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)