Q6ICH7 (ASPH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate beta-hydroxylase domain-containing protein 2
EC=1.14.11.-

Gene names

Name:

ASPHD2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Subcellular location	Membrane; Single-pass type II membrane protein Potential.
Sequence similarities	Belongs to the aspartyl/asparaginyl beta-hydroxylase family.
Sequence caution	The sequence AAH36753.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAG37570.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-amino acid modification Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Aspartate beta-hydroxylase domain-containing protein 2		PRO_0000254162
Regions
	Topological domain	1 – 58	58	Cytoplasmic Potential
	Transmembrane	59 – 79	21	Helical; Potential
	Topological domain	80 – 369	290	Lumenal Potential
Amino acid modifications
	Glycosylation	211	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	235	1	N → S. Corresponds to variant rs34902186 [ dbSNP | Ensembl ].		VAR_060123

Sequences

	Sequence		Length	Mass (Da)
	Q6ICH7 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: AE28ED71AC770ACF	FASTA	369	41,699
	10 20 30 40 50 60 MVWAPLGPPR TDCLTLLHTP SKDSPKMSLE WLVAWSWSLD GLRDCIATGI QSVRDCDTTA 70 80 90 100 110 120 VITVACLLVL FVWYCYHVGR EQPRPYVSVN SLMQAADANG LQNGYVYCQS PECVRCTHNE 130 140 150 160 170 180 GLNQKLYHNL QEYAKRYSWS GMGRIHKGIR EQGRYLNSRP SIQKPEVFFL PDLPTTPYFS 190 200 210 220 230 240 RDAQKHDVEV LERNFQTILC EFETLYKAFS NCSLPQGWKM NSTPSGEWFT FYLVNQGVCV 250 260 270 280 290 300 PRNCRKCPRT YRLLGSLRTC IGNNVFGNAC ISVLSPGTVI TEHYGPTNIR IRCHLGLKTP 310 320 330 340 350 360 NGCELVVGGE PQCWAEGRCL LFDDSFLHAA FHEGSAEDGP RVVFMVDLWH PNVAAAERQA LDFIFAPGR

References

[1]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-369. Tissue: Amygdala.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR456391 mRNA. Translation: CAG30277.1. AK315112 mRNA. Translation: BAG37570.1. Different initiation. Z99714 Genomic DNA. Translation: CAI17879.1. BC036753 mRNA. Translation: AAH36753.1. Different initiation. AL161993 mRNA. Translation: CAB82325.1.
IPI	IPI00465237.
PIR	T47148.
RefSeq	NP_065170.2. NM_020437.4.
UniGene	Hs.567547.
3D structure databases
ProteinModelPortal	Q6ICH7.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000215906.
PTM databases
PhosphoSite	Q6ICH7.
Polymorphism databases
DMDM	74757726.
Proteomic databases
PaxDb	Q6ICH7.
PRIDE	Q6ICH7.
Protocols and materials databases
DNASU	57168.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000215906; ENSP00000215906; ENSG00000128203.
GeneID	57168.
KEGG	hsa:57168.
UCSC	uc003acg.2. human.
Organism-specific databases
CTD	57168.
GeneCards	GC22P026825.
HGNC	HGNC:30437. ASPHD2.
HPA	HPA000820.
neXtProt	NX_Q6ICH7.
PharmGKB	PA143485314.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3555.
HOGENOM	HOG000233597.
HOVERGEN	HBG079419.
InParanoid	Q6ICH7.
OMA	NSLMQGA.
OrthoDB	EOG4GTKDM.
Gene expression databases
ArrayExpress	Q6ICH7.
Bgee	Q6ICH7.
CleanEx	HS_ASPHD2.
Genevestigator	Q6ICH7.
GermOnline	ENSG00000128203. Homo sapiens.
Family and domain databases
InterPro	IPR007803. Asp_Arg_b-Hydrxlase. [Graphical view]
Pfam	PF05118. Asp_Arg_Hydrox. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	57168.
NextBio	63181.

Entry information

Entry name

ASPH2_HUMAN

Accession

Primary (citable) accession number: Q6ICH7
Secondary accession number(s): B2RCH3, Q7L0W3, Q9NSN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.