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Q13825 (AUHM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylglutaconyl-CoA hydratase, mitochondrial

EC=4.2.1.18
Alternative name(s):
AU-specific RNA-binding enoyl-CoA hydratase
Short name=AU-binding protein/enoyl-CoA hydratase
Gene names
Name:AUH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of 3-methylglutaconyl-CoA to 3-hydroxy-3-methylglutaryl-CoA. Has very low enoyl-CoA hydratase activity. Was originally identified as RNA-binding protein that binds in vitro to clustered 5'-AUUUA-3' motifs. Ref.1 Ref.5 Ref.7 Ref.8

Catalytic activity

(S)-3-hydroxy-3-methylglutaryl-CoA = trans-3-methylglutaconyl-CoA + H2O.

Pathway

Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 3/3.

Subunit structure

Homohexamer. Ref.7

Subcellular location

Mitochondrion By similarity.

Involvement in disease

3-methylglutaconic aciduria 1 (MGA1) [MIM:250950]: An inborn error of leucine metabolism. It leads to an autosomal recessive syndrome with variable clinical phenotype, ranging from delayed speech development to severe psychomotor retardation, coma, failure to thrive, metabolic acidosis and dystonia. MGA1 can be distinguished from other forms of MGA by the pattern of metabolite excretion: 3-methylglutaconic acid levels are higher than those detected in other forms, whereas methylglutaric acid levels are usually only slightly elevated and there is a high level of 3-hydroxyisovaleric acid excretion (not present in other MGA forms).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.8

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13825-1)

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.
Isoform 2 (identifier: Q13825-2)

The sequence of this isoform differs from the canonical sequence as follows:
     140-168: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6767Mitochondrion Ref.1
Chain68 – 339272Methylglutaconyl-CoA hydratase, mitochondrial
PRO_0000007415

Regions

Region105 – 11915RNA-binding

Amino acid modifications

Modified residue1001N6-acetyllysine; alternate By similarity
Modified residue1001N6-succinyllysine; alternate By similarity
Modified residue1091N6-succinyllysine By similarity
Modified residue1131N6-acetyllysine; alternate By similarity
Modified residue1131N6-succinyllysine; alternate By similarity
Modified residue1441N6-acetyllysine; alternate By similarity
Modified residue1441N6-succinyllysine; alternate By similarity
Modified residue1481N6-succinyllysine By similarity
Modified residue1601N6-succinyllysine By similarity
Modified residue2041N6-acetyllysine; alternate By similarity
Modified residue2041N6-succinyllysine; alternate By similarity
Modified residue2111N6-acetyllysine; alternate By similarity
Modified residue2111N6-succinyllysine; alternate By similarity
Modified residue3291N6-succinyllysine By similarity

Natural variations

Alternative sequence140 – 16829Missing in isoform 2.
VSP_008336
Natural variant2401A → V in MGA1. Ref.8
VAR_016911

Experimental info

Mutagenesis1051K → N: Abolishes RNA-binding; when associated with E-109 and Q-113. Ref.7
Mutagenesis1091K → E: Abolishes RNA-binding; when associated with N-105 and Q-113. Ref.7
Mutagenesis1131K → Q: Abolishes RNA-binding; when associated with N-105 and E-109. Ref.7

Secondary structure

................................................ 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E04FEB95933FB30B

FASTA33935,609
        10         20         30         40         50         60 
MAAAVAAAPG ALGSLHAGGA RLVAACSAWL CPGLRLPGSL AGRRAGPAIW AQGWVPAAGG 

        70         80         90        100        110        120 
PAPKRGYSSE MKTEDELRVR HLEEENRGIV VLGINRAYGK NSLSKNLIKM LSKAVDALKS 

       130        140        150        160        170        180 
DKKVRTIIIR SEVPGIFCAG ADLKERAKMS SSEVGPFVSK IRAVINDIAN LPVPTIAAID 

       190        200        210        220        230        240 
GLALGGGLEL ALACDIRVAA SSAKMGLVET KLAIIPGGGG TQRLPRAIGM SLAKELIFSA 

       250        260        270        280        290        300 
RVLDGKEAKA VGLISHVLEQ NQEGDAAYRK ALDLAREFLP QGPVAMRVAK LAINQGMEVD 

       310        320        330 
LVTGLAIEEA CYAQTIPTKD RLEGLLAFKE KRPPRYKGE 

« Hide

Isoform 2 [UniParc].

Checksum: 24B4C6983AFED47F
Show »

FASTA31032,508

References

« Hide 'large scale' references
[1]"AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity."
Nakagawa J., Waldner H.P., Meyer-Monard S., Hofsteenge J., Jenoe P., Moroni C.
Proc. Natl. Acad. Sci. U.S.A. 92:2051-2055(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 68-87; 213-215; 235-241; 251-268 AND 278-286, FUNCTION, RNA-BINDING.
Tissue: Neuroblastoma.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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. expand/collapse author list , 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].
[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 2).
Tissue: Testis.
[5]"3-methylglutaconic aciduria type I is caused by mutations in AUH."
Ijlst L., Loupatty F.J., Ruiter J.P.N., Duran M., Lehnert W., Wanders R.J.A.
Am. J. Hum. Genet. 71:1463-1466(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, FUNCTION.
[6]"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].
[7]"Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase."
Kurimoto K., Fukai S., Nureki O., Muto Y., Yokoyama S.
Structure 9:1253-1263(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 75-339, HEXAMERIZATION, FUNCTION, MUTAGENESIS OF LYS-105; LYS-109 AND LYS-113.
[8]"Mutations in the AUH gene cause 3-methylglutaconic aciduria type I."
Ly T.B.N., Peters V., Gibson K.M., Liesert M., Buckel W., Wilcken B., Carpenter K., Ensenauer R., Hoffmann G.F., Mack M., Zschocke J.
Hum. Mutat. 21:401-407(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MGA1 VAL-240, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79888 mRNA. Translation: CAA56260.1.
AL158071, AL353645, AL513353 Genomic DNA. Translation: CAH72265.1.
AL158071, AL353645, AL513353 Genomic DNA. Translation: CAH72266.1.
AL513353, AL158071, AL353645 Genomic DNA. Translation: CAH72310.1.
AL513353, AL158071, AL353645 Genomic DNA. Translation: CAH72311.1.
AL353645, AL158071, AL513353 Genomic DNA. Translation: CAH73894.1.
AL353645, AL158071, AL513353 Genomic DNA. Translation: CAH73895.1.
CH471089 Genomic DNA. Translation: EAW62794.1.
CH471089 Genomic DNA. Translation: EAW62795.1.
BC020722 mRNA. Translation: AAH20722.1.
CCDSCCDS6689.1. [Q13825-1]
PIRI37195.
RefSeqNP_001689.1. NM_001698.2. [Q13825-1]
XP_005252125.1. XM_005252068.1. [Q13825-2]
UniGeneHs.175905.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HZDX-ray2.20A/B/C/D/E/F68-339[»]
2ZQQX-ray2.20A/B/C/D/E/F68-339[»]
2ZQRX-ray2.50A/B/C/D/E/F68-339[»]
ProteinModelPortalQ13825.
SMRQ13825. Positions 74-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107030. 3 interactions.
STRING9606.ENSP00000364883.

PTM databases

PhosphoSiteQ13825.

Polymorphism databases

DMDM37076898.

Proteomic databases

MaxQBQ13825.
PaxDbQ13825.
PRIDEQ13825.

Protocols and materials databases

DNASU549.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303617; ENSP00000307334; ENSG00000148090. [Q13825-2]
ENST00000375731; ENSP00000364883; ENSG00000148090. [Q13825-1]
GeneID549.
KEGGhsa:549.
UCSCuc004arf.4. human. [Q13825-1]
uc004arg.4. human. [Q13825-2]

Organism-specific databases

CTD549.
GeneCardsGC09M093976.
HGNCHGNC:890. AUH.
HPAHPA004171.
MIM250950. phenotype.
600529. gene.
neXtProtNX_Q13825.
Orphanet67046. 3-methylglutaconic aciduria type 1.
PharmGKBPA25181.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1024.
HOGENOMHOG000027939.
HOVERGENHBG106714.
InParanoidQ13825.
KOK05607.
OMANRPAAKN.
OrthoDBEOG7NPFV3.
PhylomeDBQ13825.
TreeFamTF314276.

Enzyme and pathway databases

BioCycMetaCyc:HS07490-MONOMER.
BRENDA4.2.1.18. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ13825.
UniPathwayUPA00363; UER00862.

Gene expression databases

ArrayExpressQ13825.
BgeeQ13825.
CleanExHS_AUH.
GenevestigatorQ13825.

Family and domain databases

Gene3D1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF52096. SSF52096. 1 hit.
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13825.
GenomeRNAi549.
NextBio2269.
PROQ13825.
SOURCESearch...

Entry information

Entry nameAUHM_HUMAN
AccessionPrimary (citable) accession number: Q13825
Secondary accession number(s): B1ALV7, B1ALV8, Q8WUE4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM