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Protein

Mycophenolic acid acyl-glucuronide esterase, mitochondrial

Gene

ABHD10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the deglucuronidation of mycophenolic acid acyl-glucuronide, a metabolite of the immunosuppressant drug mycophenolate.1 Publication

Catalytic activityi

Mycophenolic acid O-acyl-glucuronide + H2O = mycophenolate + D-glucuronate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521Charge relay systemBy similarity
Active sitei249 – 2491Charge relay systemBy similarity
Active sitei279 – 2791Charge relay systemBy similarity

GO - Molecular functioni

  • hydrolase activity, hydrolyzing O-glycosyl compounds Source: BHF-UCL

GO - Biological processi

  • glucuronoside catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000144827-MONOMER.
BRENDAi3.1.1.93. 2681.

Protein family/group databases

ESTHERihuman-ABHD10. AlphaBeta_hydrolase.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ABHD10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:25656. ABHD10.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: BHF-UCL
  • mitochondrion Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134978569.

Polymorphism and mutation databases

DMDMi74734347.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252MitochondrionSequence AnalysisAdd
BLAST
Chaini53 – 306254Mycophenolic acid acyl-glucuronide esterase, mitochondrialPRO_0000280733Add
BLAST

Proteomic databases

MaxQBiQ9NUJ1.
PaxDbiQ9NUJ1.
PeptideAtlasiQ9NUJ1.
PRIDEiQ9NUJ1.

PTM databases

PhosphoSiteiQ9NUJ1.

Expressioni

Gene expression databases

BgeeiQ9NUJ1.
CleanExiHS_ABHD10.
ExpressionAtlasiQ9NUJ1. baseline and differential.
GenevisibleiQ9NUJ1. HS.

Organism-specific databases

HPAiHPA036991.
HPA036992.

Interactioni

Protein-protein interaction databases

BioGridi120628. 5 interactions.
IntActiQ9NUJ1. 2 interactions.
STRINGi9606.ENSP00000273359.

Structurei

3D structure databases

ProteinModelPortaliQ9NUJ1.
SMRiQ9NUJ1. Positions 76-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00390000017765.
HOGENOMiHOG000139902.
HOVERGENiHBG080562.
InParanoidiQ9NUJ1.
KOiK13702.
OMAiTISRWLE.
PhylomeDBiQ9NUJ1.
TreeFamiTF329757.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NUJ1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAVARLAAVA AWVPCRSWGW AAVPFGPHRG LSVLLARIPQ RAPRWLPACR
60 70 80 90 100
QKTSLSFLNR PDLPNLAYKK LKGKSPGIIF IPGYLSYMNG TKALAIEEFC
110 120 130 140 150
KSLGHACIRF DYSGVGSSDG NSEESTLGKW RKDVLSIIDD LADGPQILVG
160 170 180 190 200
SSLGGWLMLH AAIARPEKVV ALIGVATAAD TLVTKFNQLP VELKKEVEMK
210 220 230 240 250
GVWSMPSKYS EEGVYNVQYS FIKEAEHHCL LHSPIPVNCP IRLLHGMKDD
260 270 280 290 300
IVPWHTSMQV ADRVLSTDVD VILRKHSDHR MREKADIQLL VYTIDDLIDK

LSTIVN
Length:306
Mass (Da):33,933
Last modified:October 1, 2000 - v1
Checksum:iE41139D5C22A83FE
GO
Isoform 2 (identifier: Q9NUJ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.

Note: No experimental confirmation available.
Show »
Length:149
Mass (Da):16,910
Checksum:iBB6B75027A2FD486
GO
Isoform 3 (identifier: Q9NUJ1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     193-205: LKKEVEMKGVWSM → DSGRKNYISLHSA
     206-306: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:205
Mass (Da):22,141
Checksum:i8EDC2A7F6446189B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti251 – 2511I → V.
Corresponds to variant rs17429033 [ dbSNP | Ensembl ].
VAR_031194

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 157157Missing in isoform 2. 1 PublicationVSP_056093Add
BLAST
Alternative sequencei193 – 20513LKKEV…GVWSM → DSGRKNYISLHSA in isoform 3. CuratedVSP_056742Add
BLAST
Alternative sequencei206 – 306101Missing in isoform 3. CuratedVSP_056743Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002204 mRNA. Translation: BAA92133.1.
AK300018 mRNA. Translation: BAH13194.1.
AC060225 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79688.1.
CH471052 Genomic DNA. Translation: EAW79689.1.
BC014516 mRNA. Translation: AAH14516.1.
AL713726 mRNA. Translation: CAD28516.2.
CCDSiCCDS2963.1. [Q9NUJ1-1]
CCDS63718.1. [Q9NUJ1-3]
RefSeqiNP_001258998.1. NM_001272069.1. [Q9NUJ1-3]
NP_060864.1. NM_018394.3. [Q9NUJ1-1]
XP_011511262.1. XM_011512960.1. [Q9NUJ1-3]
UniGeneiHs.477115.

Genome annotation databases

EnsembliENST00000273359; ENSP00000273359; ENSG00000144827.
ENST00000494817; ENSP00000418973; ENSG00000144827. [Q9NUJ1-3]
GeneIDi55347.
KEGGihsa:55347.
UCSCiuc003dyk.5. human. [Q9NUJ1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002204 mRNA. Translation: BAA92133.1.
AK300018 mRNA. Translation: BAH13194.1.
AC060225 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79688.1.
CH471052 Genomic DNA. Translation: EAW79689.1.
BC014516 mRNA. Translation: AAH14516.1.
AL713726 mRNA. Translation: CAD28516.2.
CCDSiCCDS2963.1. [Q9NUJ1-1]
CCDS63718.1. [Q9NUJ1-3]
RefSeqiNP_001258998.1. NM_001272069.1. [Q9NUJ1-3]
NP_060864.1. NM_018394.3. [Q9NUJ1-1]
XP_011511262.1. XM_011512960.1. [Q9NUJ1-3]
UniGeneiHs.477115.

3D structure databases

ProteinModelPortaliQ9NUJ1.
SMRiQ9NUJ1. Positions 76-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120628. 5 interactions.
IntActiQ9NUJ1. 2 interactions.
STRINGi9606.ENSP00000273359.

Protein family/group databases

ESTHERihuman-ABHD10. AlphaBeta_hydrolase.

PTM databases

PhosphoSiteiQ9NUJ1.

Polymorphism and mutation databases

DMDMi74734347.

Proteomic databases

MaxQBiQ9NUJ1.
PaxDbiQ9NUJ1.
PeptideAtlasiQ9NUJ1.
PRIDEiQ9NUJ1.

Protocols and materials databases

DNASUi55347.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000273359; ENSP00000273359; ENSG00000144827.
ENST00000494817; ENSP00000418973; ENSG00000144827. [Q9NUJ1-3]
GeneIDi55347.
KEGGihsa:55347.
UCSCiuc003dyk.5. human. [Q9NUJ1-1]

Organism-specific databases

CTDi55347.
GeneCardsiGC03P111697.
HGNCiHGNC:25656. ABHD10.
HPAiHPA036991.
HPA036992.
neXtProtiNX_Q9NUJ1.
PharmGKBiPA134978569.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00390000017765.
HOGENOMiHOG000139902.
HOVERGENiHBG080562.
InParanoidiQ9NUJ1.
KOiK13702.
OMAiTISRWLE.
PhylomeDBiQ9NUJ1.
TreeFamiTF329757.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000144827-MONOMER.
BRENDAi3.1.1.93. 2681.

Miscellaneous databases

GenomeRNAii55347.
NextBioi35479922.
PROiQ9NUJ1.

Gene expression databases

BgeeiQ9NUJ1.
CleanExiHS_ABHD10.
ExpressionAtlasiQ9NUJ1. baseline and differential.
GenevisibleiQ9NUJ1. HS.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 1 AND 2).
    Tissue: Placenta.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] (ISOFORM 1).
    Tissue: Ovary.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-306 (ISOFORM 1).
    Tissue: Melanoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiABHDA_HUMAN
AccessioniPrimary (citable) accession number: Q9NUJ1
Secondary accession number(s): B7Z6A8
, C9IZX5, D3DN63, Q8TCF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.