Q9NUJ1 (ABHDA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mycophenolic acid acyl-glucuronide esterase, mitochondrial
EC=3.1.1.93

Alternative name(s):
Alpha/beta hydrolase domain-containing protein 10
Short name=Abhydrolase domain-containing protein 10

Gene names

Name:

ABHD10

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	306 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, a metabolite of the immunosuppressant drug mycophenolate. Ref.6
Catalytic activity	Mycophenolic acid O-acyl-glucuronide + H2O = mycophenolate + D-glucuronate. Ref.6
Subcellular location	Mitochondrion Potential.
Sequence similarities	Belongs to the AB hydrolase superfamily.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucuronoside catabolic process Inferred from direct assay Ref.6. Source: BHF-UCL
Cellular_component	cytosol Inferred from direct assay Ref.6. Source: BHF-UCL mitochondrion Inferred from direct assay. Source: LIFEdb
Molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from direct assay Ref.6. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 52	52	Mitochondrion Potential
	Chain	53 – 306	254	Mycophenolic acid acyl-glucuronide esterase, mitochondrial		PRO_0000280733
Sites
	Active site	152	1	Charge relay system By similarity
	Active site	249	1	Charge relay system By similarity
	Active site	279	1	Charge relay system By similarity
Natural variations
	Natural variant	251	1	I → V. Corresponds to variant rs17429033 [ dbSNP | Ensembl ].		VAR_031194

Sequences

	Sequence		Length	Mass (Da)
	Q9NUJ1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E41139D5C22A83FE	FASTA	306	33,933
	10 20 30 40 50 60 MAVARLAAVA AWVPCRSWGW AAVPFGPHRG LSVLLARIPQ RAPRWLPACR QKTSLSFLNR 70 80 90 100 110 120 PDLPNLAYKK LKGKSPGIIF IPGYLSYMNG TKALAIEEFC KSLGHACIRF DYSGVGSSDG 130 140 150 160 170 180 NSEESTLGKW RKDVLSIIDD LADGPQILVG SSLGGWLMLH AAIARPEKVV ALIGVATAAD 190 200 210 220 230 240 TLVTKFNQLP VELKKEVEMK GVWSMPSKYS EEGVYNVQYS FIKEAEHHCL LHSPIPVNCP 250 260 270 280 290 300 IRLLHGMKDD IVPWHTSMQV ADRVLSTDVD VILRKHSDHR MREKADIQLL VYTIDDLIDK LSTIVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Placenta.
[2]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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]. Tissue: Ovary.
[4]	"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 73-306. Tissue: Melanoma.
[5]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]	"Human alpha/beta hydrolase domain containing 10 (ABHD10) is responsible enzyme for deglucuronidation of mycophenolic acid acyl-glucuronide in liver." Iwamura A., Fukami T., Higuchi R., Nakajima M., Yokoi T. J. Biol. Chem. 287:9240-9249(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK002204 mRNA. Translation: BAA92133.1. CH471052 Genomic DNA. Translation: EAW79688.1. CH471052 Genomic DNA. Translation: EAW79689.1. BC014516 mRNA. Translation: AAH14516.1. AL713726 mRNA. Translation: CAD28516.2.
IPI	IPI00020075.
RefSeq	NP_060864.1. NM_018394.3.
UniGene	Hs.477115.
3D structure databases
ProteinModelPortal	Q9NUJ1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NUJ1. 2 interactions.
STRING	9606.ENSP00000273359.
Protein family/group databases
MEROPS	S09.062.
PTM databases
PhosphoSite	Q9NUJ1.
Polymorphism databases
DMDM	74734347.
Proteomic databases
PaxDb	Q9NUJ1.
PeptideAtlas	Q9NUJ1.
PRIDE	Q9NUJ1.
Protocols and materials databases
DNASU	55347.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000273359; ENSP00000273359; ENSG00000144827.
GeneID	55347.
KEGG	hsa:55347.
UCSC	uc003dyk.4. human.
Organism-specific databases
CTD	55347.
GeneCards	GC03P111697.
HGNC	HGNC:25656. ABHD10.
HPA	HPA036992.
neXtProt	NX_Q9NUJ1.
PharmGKB	PA134978569.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0596.
HOGENOM	HOG000139902.
HOVERGEN	HBG080562.
InParanoid	Q9NUJ1.
KO	K13702.
OMA	FDYSGHG.
OrthoDB	EOG476K0X.
PhylomeDB	Q9NUJ1.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000144827-MONOMER.
Gene expression databases
ArrayExpress	Q9NUJ1.
Bgee	Q9NUJ1.
CleanEx	HS_ABHD10.
Genevestigator	Q9NUJ1.
Family and domain databases
ProtoNet	Search...
Other
GenomeRNAi	55347.
NextBio	59687.

Entry information

Entry name

ABHDA_HUMAN

Accession

Primary (citable) accession number: Q9NUJ1
Secondary accession number(s): D3DN63, Q8TCF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 97 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.