SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q13825

- AUHM_HUMAN

UniProt

Q13825 - AUHM_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Methylglutaconyl-CoA hydratase, mitochondrial
Gene
AUH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

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).
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 Publication
Add
BLAST
Chaini68 – 339272Methylglutaconyl-CoA hydratase, mitochondrial
PRO_0000007415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001N6-acetyllysine; alternate By similarity
Modified residuei100 – 1001N6-succinyllysine; alternate By similarity
Modified residuei109 – 1091N6-succinyllysine By similarity
Modified residuei113 – 1131N6-acetyllysine; alternate By similarity
Modified residuei113 – 1131N6-succinyllysine; alternate By similarity
Modified residuei144 – 1441N6-acetyllysine; alternate By similarity
Modified residuei144 – 1441N6-succinyllysine; alternate By similarity
Modified residuei148 – 1481N6-succinyllysine By similarity
Modified residuei160 – 1601N6-succinyllysine By similarity
Modified residuei204 – 2041N6-acetyllysine; alternate By similarity
Modified residuei204 – 2041N6-succinyllysine; alternate By similarity
Modified residuei211 – 2111N6-acetyllysine; alternate By similarity
Modified residuei211 – 2111N6-succinyllysine; alternate By similarity
Modified residuei329 – 3291N6-succinyllysine By 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.1 Publication

Protein-protein interaction databases

BioGridi107030. 3 interactions.
STRINGi9606.ENSP00000364883.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ13825.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 11915RNA-binding
Add
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.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 140 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

Similar proteinsi