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Q13825

- AUHM_HUMAN

UniProt

Q13825 - AUHM_HUMAN

Protein

Methylglutaconyl-CoA hydratase, mitochondrial

Gene

AUH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. enoyl-CoA hydratase activity Source: UniProtKB
    2. methylglutaconyl-CoA hydratase activity Source: Reactome
    3. mRNA 3'-UTR binding Source: UniProtKB

    GO - Biological processi

    1. branched-chain amino acid catabolic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. leucine catabolic process Source: UniProtKB-UniPathway
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Branched-chain amino acid catabolism

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07490-MONOMER.
    BRENDAi4.2.1.18. 2681.
    ReactomeiREACT_197. Branched-chain amino acid catabolism.
    SABIO-RKQ13825.
    UniPathwayiUPA00363; UER00862.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:AUH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:890. AUH.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    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).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti240 – 2401A → V in MGA1. 1 Publication
    VAR_016911

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi105 – 1051K → N: Abolishes RNA-binding; when associated with E-109 and Q-113. 1 Publication
    Mutagenesisi109 – 1091K → E: Abolishes RNA-binding; when associated with N-105 and Q-113. 1 Publication
    Mutagenesisi113 – 1131K → Q: Abolishes RNA-binding; when associated with N-105 and E-109. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi250950. phenotype.
    Orphaneti67046. 3-methylglutaconic aciduria type 1.
    PharmGKBiPA25181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6767Mitochondrion1 PublicationAdd
    BLAST
    Chaini68 – 339272Methylglutaconyl-CoA hydratase, mitochondrialPRO_0000007415Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei100 – 1001N6-acetyllysine; alternateBy similarity
    Modified residuei100 – 1001N6-succinyllysine; alternateBy similarity
    Modified residuei109 – 1091N6-succinyllysineBy similarity
    Modified residuei113 – 1131N6-acetyllysine; alternateBy similarity
    Modified residuei113 – 1131N6-succinyllysine; alternateBy similarity
    Modified residuei144 – 1441N6-acetyllysine; alternateBy similarity
    Modified residuei144 – 1441N6-succinyllysine; alternateBy similarity
    Modified residuei148 – 1481N6-succinyllysineBy similarity
    Modified residuei160 – 1601N6-succinyllysineBy similarity
    Modified residuei204 – 2041N6-acetyllysine; alternateBy similarity
    Modified residuei204 – 2041N6-succinyllysine; alternateBy similarity
    Modified residuei211 – 2111N6-acetyllysine; alternateBy similarity
    Modified residuei211 – 2111N6-succinyllysine; alternateBy similarity
    Modified residuei329 – 3291N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ13825.
    PaxDbiQ13825.
    PRIDEiQ13825.

    PTM databases

    PhosphoSiteiQ13825.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13825.
    BgeeiQ13825.
    CleanExiHS_AUH.
    GenevestigatoriQ13825.

    Organism-specific databases

    HPAiHPA004171.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    BioGridi107030. 3 interactions.
    STRINGi9606.ENSP00000364883.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi76 – 816
    Helixi84 – 863
    Beta strandi89 – 946
    Helixi97 – 993
    Helixi107 – 12014
    Beta strandi125 – 1339
    Beta strandi135 – 1384
    Helixi143 – 1464
    Helixi151 – 16919
    Beta strandi175 – 18410
    Helixi186 – 1938
    Beta strandi194 – 2007
    Beta strandi204 – 2063
    Helixi209 – 2124
    Helixi220 – 2289
    Helixi230 – 23910
    Beta strandi242 – 2443
    Helixi245 – 2506
    Beta strandi255 – 2584
    Helixi266 – 27611
    Turni277 – 2804
    Helixi283 – 29715
    Helixi301 – 31313
    Turni314 – 3174
    Helixi319 – 32810
    Turni329 – 3313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ13825.
    SMRiQ13825. Positions 74-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13825.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni105 – 11915RNA-bindingAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1024.
    HOGENOMiHOG000027939.
    HOVERGENiHBG106714.
    InParanoidiQ13825.
    KOiK05607.
    OMAiNRPAAKN.
    OrthoDBiEOG7NPFV3.
    PhylomeDBiQ13825.
    TreeFamiTF314276.

    Family and domain databases

    Gene3Di1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13825-1) [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

    MAAAVAAAPG ALGSLHAGGA RLVAACSAWL CPGLRLPGSL AGRRAGPAIW    50
    AQGWVPAAGG PAPKRGYSSE MKTEDELRVR HLEEENRGIV VLGINRAYGK 100
    NSLSKNLIKM LSKAVDALKS DKKVRTIIIR SEVPGIFCAG ADLKERAKMS 150
    SSEVGPFVSK IRAVINDIAN LPVPTIAAID GLALGGGLEL ALACDIRVAA 200
    SSAKMGLVET KLAIIPGGGG TQRLPRAIGM SLAKELIFSA RVLDGKEAKA 250
    VGLISHVLEQ NQEGDAAYRK ALDLAREFLP QGPVAMRVAK LAINQGMEVD 300
    LVTGLAIEEA CYAQTIPTKD RLEGLLAFKE KRPPRYKGE 339
    Length:339
    Mass (Da):35,609
    Last modified:November 1, 1996 - v1
    Checksum:iE04FEB95933FB30B
    GO
    Isoform 2 (identifier: Q13825-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         140-168: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:310
    Mass (Da):32,508
    Checksum:i24B4C6983AFED47F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti240 – 2401A → V in MGA1. 1 Publication
    VAR_016911

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei140 – 16829Missing in isoform 2. 1 PublicationVSP_008336Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS6689.1. [Q13825-1]
    PIRiI37195.
    RefSeqiNP_001689.1. NM_001698.2. [Q13825-1]
    XP_005252125.1. XM_005252068.1. [Q13825-2]
    UniGeneiHs.175905.

    Genome annotation databases

    EnsembliENST00000303617; ENSP00000307334; ENSG00000148090. [Q13825-2]
    ENST00000375731; ENSP00000364883; ENSG00000148090. [Q13825-1]
    GeneIDi549.
    KEGGihsa:549.
    UCSCiuc004arf.4. human. [Q13825-1]
    uc004arg.4. human. [Q13825-2]

    Polymorphism databases

    DMDMi37076898.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS6689.1. [Q13825-1 ]
    PIRi I37195.
    RefSeqi NP_001689.1. NM_001698.2. [Q13825-1 ]
    XP_005252125.1. XM_005252068.1. [Q13825-2 ]
    UniGenei Hs.175905.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HZD X-ray 2.20 A/B/C/D/E/F 68-339 [» ]
    2ZQQ X-ray 2.20 A/B/C/D/E/F 68-339 [» ]
    2ZQR X-ray 2.50 A/B/C/D/E/F 68-339 [» ]
    ProteinModelPortali Q13825.
    SMRi Q13825. Positions 74-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107030. 3 interactions.
    STRINGi 9606.ENSP00000364883.

    PTM databases

    PhosphoSitei Q13825.

    Polymorphism databases

    DMDMi 37076898.

    Proteomic databases

    MaxQBi Q13825.
    PaxDbi Q13825.
    PRIDEi Q13825.

    Protocols and materials databases

    DNASUi 549.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303617 ; ENSP00000307334 ; ENSG00000148090 . [Q13825-2 ]
    ENST00000375731 ; ENSP00000364883 ; ENSG00000148090 . [Q13825-1 ]
    GeneIDi 549.
    KEGGi hsa:549.
    UCSCi uc004arf.4. human. [Q13825-1 ]
    uc004arg.4. human. [Q13825-2 ]

    Organism-specific databases

    CTDi 549.
    GeneCardsi GC09M093976.
    HGNCi HGNC:890. AUH.
    HPAi HPA004171.
    MIMi 250950. phenotype.
    600529. gene.
    neXtProti NX_Q13825.
    Orphaneti 67046. 3-methylglutaconic aciduria type 1.
    PharmGKBi PA25181.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1024.
    HOGENOMi HOG000027939.
    HOVERGENi HBG106714.
    InParanoidi Q13825.
    KOi K05607.
    OMAi NRPAAKN.
    OrthoDBi EOG7NPFV3.
    PhylomeDBi Q13825.
    TreeFami TF314276.

    Enzyme and pathway databases

    UniPathwayi UPA00363 ; UER00862 .
    BioCyci MetaCyc:HS07490-MONOMER.
    BRENDAi 4.2.1.18. 2681.
    Reactomei REACT_197. Branched-chain amino acid catabolism.
    SABIO-RK Q13825.

    Miscellaneous databases

    EvolutionaryTracei Q13825.
    GenomeRNAii 549.
    NextBioi 2269.
    PROi Q13825.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13825.
    Bgeei Q13825.
    CleanExi HS_AUH.
    Genevestigatori Q13825.

    Family and domain databases

    Gene3Di 1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view ]
    Pfami PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 1 hit.
    PROSITEi PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. Cited for: VARIANT MGA1 VAL-240, FUNCTION.

    Entry informationi

    Entry nameiAUHM_HUMAN
    AccessioniPrimary (citable) accession number: Q13825
    Secondary accession number(s): B1ALV7, B1ALV8, Q8WUE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 141 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3