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P40939

- ECHA_HUMAN

UniProt

P40939 - ECHA_HUMAN

Protein

Trifunctional enzyme subunit alpha, mitochondrial

Gene

HADHA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (03 Apr 2002)
      Previous versions | rss
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    Functioni

    Bifunctional subunit.

    Catalytic activityi

    (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
    A long-chain (S)-3-hydroxyacyl-CoA + NAD+ = a long-chain 3-oxoacyl-CoA + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei151 – 1511Important for catalytic activityBy similarity
    Sitei173 – 1731Important for catalytic activityBy similarity

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: ProtInc
    2. acetyl-CoA C-acetyltransferase activity Source: ProtInc
    3. enoyl-CoA hydratase activity Source: ProtInc
    4. fatty-acyl-CoA binding Source: Ensembl
    5. long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
    6. long-chain-enoyl-CoA hydratase activity Source: Ensembl
    7. NAD binding Source: Ensembl
    8. protein binding Source: IntAct

    GO - Biological processi

    1. cardiolipin acyl-chain remodeling Source: Reactome
    2. cellular lipid metabolic process Source: Reactome
    3. fatty acid beta-oxidation Source: Reactome
    4. glycerophospholipid biosynthetic process Source: Reactome
    5. phospholipid metabolic process Source: Reactome
    6. response to drug Source: Ensembl
    7. response to insulin Source: Ensembl
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01481-MONOMER.
    ReactomeiREACT_121006. Acyl chain remodeling of CL.
    REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_2025. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
    REACT_2108. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
    REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
    SABIO-RKP40939.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trifunctional enzyme subunit alpha, mitochondrial
    Alternative name(s):
    78 kDa gastrin-binding protein
    TP-alpha
    Including the following 2 domains:
    Long-chain enoyl-CoA hydratase (EC:4.2.1.17)
    Long chain 3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.211)
    Gene namesi
    Name:HADHA
    Synonyms:HADH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4801. HADHA.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial fatty acid beta-oxidation multienzyme complex Source: Ensembl
    2. mitochondrial inner membrane Source: Reactome
    3. mitochondrial nucleoid Source: BHF-UCL
    4. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Trifunctional protein deficiency (TFP deficiency) [MIM:609015]: The clinical manifestations are very variable and include hypoglycemia, cardiomyopathy and sudden death. Phenotypes with mainly hepatic and neuromyopathic involvement can also be distinguished. Biochemically, TFP deficiency is defined by the loss of all three enzyme activities of the TFP complex.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti282 – 2821V → D in TFP deficiency; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. 1 Publication
    VAR_021125
    Natural varianti305 – 3051I → N in TFP deficiency; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. 1 Publication
    VAR_021126
    Long-chain 3-hydroxyl-CoA dehydrogenase deficiency (LCHAD deficiency) [MIM:609016]: The clinical features are very similar to TFP deficiency. Biochemically, LCHAD deficiency is characterized by reduced long-chain 3-hydroxyl-CoA dehydrogenase activity, while the other enzyme activities of the TFP complex are normal or only slightly reduced.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti342 – 3421L → P in LCHAD deficiency. 1 Publication
    VAR_021127
    Natural varianti510 – 5101E → Q in AFLP and LCHAD deficiency; loss of activity. 3 Publications
    Corresponds to variant rs137852769 [ dbSNP | Ensembl ].
    VAR_002273
    Maternal acute fatty liver of pregnancy (AFLP) [MIM:609016]: Severe maternal illness occurring during pregnancies with affected fetuses. This disease is associated with LCHAD deficiency and characterized by sudden unexplained infant death or hypoglycemia and abnormal liver enzymes (Reye-like syndrome).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti510 – 5101E → Q in AFLP and LCHAD deficiency; loss of activity. 3 Publications
    Corresponds to variant rs137852769 [ dbSNP | Ensembl ].
    VAR_002273

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi609015. phenotype.
    609016. phenotype.
    Orphaneti243367. Acute fatty liver of pregnancy.
    5. Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency.
    746. Mitochondrial trifunctional protein deficiency.
    PharmGKBiPA29175.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3636MitochondrionSequence AnalysisAdd
    BLAST
    Chaini37 – 763727Trifunctional enzyme subunit alpha, mitochondrialPRO_0000007403Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461N6-acetyllysine; alternateBy similarity
    Modified residuei46 – 461N6-succinyllysine; alternateBy similarity
    Modified residuei60 – 601N6-acetyllysine; alternateBy similarity
    Modified residuei60 – 601N6-succinyllysine; alternateBy similarity
    Modified residuei129 – 1291N6-acetyllysineBy similarity
    Modified residuei166 – 1661N6-acetyllysine; alternateBy similarity
    Modified residuei166 – 1661N6-succinyllysine; alternateBy similarity
    Modified residuei213 – 2131N6-succinyllysineBy similarity
    Modified residuei214 – 2141N6-acetyllysine; alternateBy similarity
    Modified residuei214 – 2141N6-succinyllysine; alternateBy similarity
    Modified residuei230 – 2301N6-succinyllysineBy similarity
    Modified residuei249 – 2491N6-acetyllysine; alternateBy similarity
    Modified residuei249 – 2491N6-succinyllysine; alternateBy similarity
    Modified residuei289 – 2891N6-acetyllysineBy similarity
    Modified residuei295 – 2951N6-acetyllysine1 Publication
    Modified residuei303 – 3031N6-acetyllysine; alternate1 Publication
    Modified residuei303 – 3031N6-succinyllysine; alternateBy similarity
    Modified residuei326 – 3261N6-acetyllysine; alternateBy similarity
    Modified residuei326 – 3261N6-succinyllysine; alternateBy similarity
    Modified residuei334 – 3341N6-acetyllysine; alternateBy similarity
    Modified residuei334 – 3341N6-succinyllysine; alternateBy similarity
    Modified residuei350 – 3501N6-acetyllysine; alternateBy similarity
    Modified residuei350 – 3501N6-succinyllysine; alternateBy similarity
    Modified residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei406 – 4061N6-acetyllysine; alternate1 Publication
    Modified residuei406 – 4061N6-succinyllysine; alternateBy similarity
    Modified residuei411 – 4111N6-acetyllysine; alternateBy similarity
    Modified residuei411 – 4111N6-succinyllysine; alternateBy similarity
    Modified residuei415 – 4151N6-succinyllysineBy similarity
    Modified residuei440 – 4401N6-succinyllysineBy similarity
    Modified residuei460 – 4601N6-acetyllysine; alternateBy similarity
    Modified residuei460 – 4601N6-succinyllysine; alternateBy similarity
    Modified residuei505 – 5051N6-acetyllysine; alternate1 Publication
    Modified residuei505 – 5051N6-succinyllysine; alternateBy similarity
    Modified residuei519 – 5191N6-acetyllysine; alternateBy similarity
    Modified residuei519 – 5191N6-succinyllysine; alternateBy similarity
    Modified residuei540 – 5401N6-acetyllysine1 Publication
    Modified residuei569 – 5691N6-acetyllysine; alternateBy similarity
    Modified residuei569 – 5691N6-succinyllysine; alternateBy similarity
    Modified residuei634 – 6341N6-succinyllysineBy similarity
    Modified residuei644 – 6441N6-acetyllysine; alternate1 Publication
    Modified residuei644 – 6441N6-succinyllysine; alternateBy similarity
    Modified residuei646 – 6461N6-succinyllysineBy similarity
    Modified residuei664 – 6641N6-acetyllysine; alternateBy similarity
    Modified residuei664 – 6641N6-succinyllysine; alternateBy similarity
    Modified residuei728 – 7281N6-acetyllysine; alternateBy similarity
    Modified residuei728 – 7281N6-succinyllysine; alternateBy similarity
    Modified residuei735 – 7351N6-acetyllysineBy similarity
    Modified residuei759 – 7591N6-acetyllysine; alternateBy similarity
    Modified residuei759 – 7591N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP40939.
    PaxDbiP40939.
    PeptideAtlasiP40939.
    PRIDEiP40939.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00031522.
    UCD-2DPAGEP40939.

    PTM databases

    PhosphoSiteiP40939.

    Expressioni

    Gene expression databases

    ArrayExpressiP40939.
    BgeeiP40939.
    CleanExiHS_HADH.
    HS_HADHA.
    GenevestigatoriP40939.

    Organism-specific databases

    HPAiHPA015536.
    HPA056070.

    Interactioni

    Subunit structurei

    Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPO951665EBI-356720,EBI-712001
    GABARAPL1Q9H0R84EBI-356720,EBI-746969
    GABARAPL2P605204EBI-356720,EBI-720116
    MAP1LC3BQ9GZQ84EBI-356720,EBI-373144

    Protein-protein interaction databases

    BioGridi109280. 48 interactions.
    IntActiP40939. 31 interactions.
    MINTiMINT-1159893.
    STRINGi9606.ENSP00000370023.

    Structurei

    3D structure databases

    ProteinModelPortaliP40939.
    SMRiP40939. Positions 45-763.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
    In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261346.
    HOVERGENiHBG005557.
    InParanoidiP40939.
    KOiK07515.
    OMAiFYVYQEG.
    OrthoDBiEOG7P2XRF.
    PhylomeDBiP40939.
    TreeFamiTF352288.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR012803. Fa_ox_alpha_mit.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 2 hits.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    TIGRFAMsiTIGR02441. fa_ox_alpha_mit. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    PS00166. 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: P40939-1) [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

    MVACRAIGIL SRFSAFRILR SRGYICRNFT GSSALLTRTH INYGVKGDVA    50
    VVRINSPNSK VNTLSKELHS EFSEVMNEIW ASDQIRSAVL ISSKPGCFIA 100
    GADINMLAAC KTLQEVTQLS QEAQRIVEKL EKSTKPIVAA INGSCLGGGL 150
    EVAISCQYRI ATKDRKTVLG TPEVLLGALP GAGGTQRLPK MVGVPAALDM 200
    MLTGRSIRAD RAKKMGLVDQ LVEPLGPGLK PPEERTIEYL EEVAITFAKG 250
    LADKKISPKR DKGLVEKLTA YAMTIPFVRQ QVYKKVEEKV RKQTKGLYPA 300
    PLKIIDVVKT GIEQGSDAGY LCESQKFGEL VMTKESKALM GLYHGQVLCK 350
    KNKFGAPQKD VKHLAILGAG LMGAGIAQVS VDKGLKTILK DATLTALDRG 400
    QQQVFKGLND KVKKKALTSF ERDSIFSNLT GQLDYQGFEK ADMVIEAVFE 450
    DLSLKHRVLK EVEAVIPDHC IFASNTSALP ISEIAAVSKR PEKVIGMHYF 500
    SPVDKMQLLE IITTEKTSKD TSASAVAVGL KQGKVIIVVK DGPGFYTTRC 550
    LAPMMSEVIR ILQEGVDPKK LDSLTTSFGF PVGAATLVDE VGVDVAKHVA 600
    EDLGKVFGER FGGGNPELLT QMVSKGFLGR KSGKGFYIYQ EGVKRKDLNS 650
    DMDSILASLK LPPKSEVSSD EDIQFRLVTR FVNEAVMCLQ EGILATPAEG 700
    DIGAVFGLGF PPCLGGPFRF VDLYGAQKIV DRLKKYEAAY GKQFTPCQLL 750
    ADHANSPNKK FYQ 763
    Length:763
    Mass (Da):83,000
    Last modified:April 3, 2002 - v2
    Checksum:i247FF7B4E48FB484
    GO
    Isoform 2 (identifier: P40939-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MVACRAIGILSRFSAFRI → MESKGMWQLFELTLPIQS
         19-105: Missing.
         326-347: KFGELVMTKESKALMGLYHGQV → VNLFPFNVLLSVKGKLKIQSSV
         348-763: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:260
    Mass (Da):28,367
    Checksum:iBA756450F59E9B8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461L → V in BAA03941. (PubMed:8135828)Curated
    Sequence conflicti152 – 1521V → L in AAA56664. (PubMed:7918661)Curated
    Sequence conflicti171 – 1711T → A in AAA56664. (PubMed:7918661)Curated
    Sequence conflicti178 – 1781A → I in AAA56664. (PubMed:7918661)Curated
    Sequence conflicti197 – 1982AL → VF in AAA56664. (PubMed:7918661)Curated
    Sequence conflicti206 – 2061S → N in AAA56664. (PubMed:7918661)Curated
    Sequence conflicti211 – 2111R → S in AAA56664. (PubMed:7918661)Curated
    Sequence conflicti576 – 5761T → P in AAA56664. (PubMed:7918661)Curated
    Sequence conflicti694 – 6941L → S in BAA03941. (PubMed:8135828)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti282 – 2821V → D in TFP deficiency; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. 1 Publication
    VAR_021125
    Natural varianti305 – 3051I → N in TFP deficiency; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. 1 Publication
    VAR_021126
    Natural varianti342 – 3421L → P in LCHAD deficiency. 1 Publication
    VAR_021127
    Natural varianti358 – 3581Q → K.
    Corresponds to variant rs10200182 [ dbSNP | Ensembl ].
    VAR_048908
    Natural varianti510 – 5101E → Q in AFLP and LCHAD deficiency; loss of activity. 3 Publications
    Corresponds to variant rs137852769 [ dbSNP | Ensembl ].
    VAR_002273

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1818MVACR…SAFRI → MESKGMWQLFELTLPIQS in isoform 2. 1 PublicationVSP_054358Add
    BLAST
    Alternative sequencei19 – 10587Missing in isoform 2. 1 PublicationVSP_054359Add
    BLAST
    Alternative sequencei326 – 34722KFGEL…YHGQV → VNLFPFNVLLSVKGKLKIQS SV in isoform 2. 1 PublicationVSP_054360Add
    BLAST
    Alternative sequencei348 – 763416Missing in isoform 2. 1 PublicationVSP_054361Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16480 mRNA. Translation: BAA03941.1.
    U04627 mRNA. Translation: AAA56664.1.
    AK302532 mRNA. Translation: BAG63804.1.
    AK313027 mRNA. Translation: BAG35861.1.
    AC010896 Genomic DNA. Translation: AAY14643.1.
    AC011742 Genomic DNA. Translation: AAX93141.1.
    CH471053 Genomic DNA. Translation: EAX00703.1.
    BC009235 mRNA. Translation: AAH09235.1.
    AB020811 Genomic DNA. Translation: BAA76735.1.
    CCDSiCCDS1721.1. [P40939-1]
    PIRiJC2108.
    RefSeqiNP_000173.2. NM_000182.4. [P40939-1]
    UniGeneiHs.516032.

    Genome annotation databases

    EnsembliENST00000380649; ENSP00000370023; ENSG00000084754. [P40939-1]
    GeneIDi3030.
    KEGGihsa:3030.
    UCSCiuc002rgy.3. human. [P40939-1]

    Polymorphism databases

    DMDMi20141376.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16480 mRNA. Translation: BAA03941.1 .
    U04627 mRNA. Translation: AAA56664.1 .
    AK302532 mRNA. Translation: BAG63804.1 .
    AK313027 mRNA. Translation: BAG35861.1 .
    AC010896 Genomic DNA. Translation: AAY14643.1 .
    AC011742 Genomic DNA. Translation: AAX93141.1 .
    CH471053 Genomic DNA. Translation: EAX00703.1 .
    BC009235 mRNA. Translation: AAH09235.1 .
    AB020811 Genomic DNA. Translation: BAA76735.1 .
    CCDSi CCDS1721.1. [P40939-1 ]
    PIRi JC2108.
    RefSeqi NP_000173.2. NM_000182.4. [P40939-1 ]
    UniGenei Hs.516032.

    3D structure databases

    ProteinModelPortali P40939.
    SMRi P40939. Positions 45-763.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109280. 48 interactions.
    IntActi P40939. 31 interactions.
    MINTi MINT-1159893.
    STRINGi 9606.ENSP00000370023.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P40939.

    Polymorphism databases

    DMDMi 20141376.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00031522.
    UCD-2DPAGE P40939.

    Proteomic databases

    MaxQBi P40939.
    PaxDbi P40939.
    PeptideAtlasi P40939.
    PRIDEi P40939.

    Protocols and materials databases

    DNASUi 3030.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380649 ; ENSP00000370023 ; ENSG00000084754 . [P40939-1 ]
    GeneIDi 3030.
    KEGGi hsa:3030.
    UCSCi uc002rgy.3. human. [P40939-1 ]

    Organism-specific databases

    CTDi 3030.
    GeneCardsi GC02M026413.
    HGNCi HGNC:4801. HADHA.
    HPAi HPA015536.
    HPA056070.
    MIMi 600890. gene.
    609015. phenotype.
    609016. phenotype.
    neXtProti NX_P40939.
    Orphaneti 243367. Acute fatty liver of pregnancy.
    5. Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency.
    746. Mitochondrial trifunctional protein deficiency.
    PharmGKBi PA29175.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261346.
    HOVERGENi HBG005557.
    InParanoidi P40939.
    KOi K07515.
    OMAi FYVYQEG.
    OrthoDBi EOG7P2XRF.
    PhylomeDBi P40939.
    TreeFami TF352288.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci MetaCyc:HS01481-MONOMER.
    Reactomei REACT_121006. Acyl chain remodeling of CL.
    REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
    REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
    REACT_1887. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
    REACT_2025. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
    REACT_2108. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
    REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
    SABIO-RK P40939.

    Miscellaneous databases

    ChiTaRSi HADHA. human.
    GenomeRNAii 3030.
    NextBioi 11996.
    PROi P40939.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P40939.
    Bgeei P40939.
    CleanExi HS_HADH.
    HS_HADHA.
    Genevestigatori P40939.

    Family and domain databases

    Gene3Di 1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR012803. Fa_ox_alpha_mit.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00725. 3HCDH. 2 hits.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    TIGRFAMsi TIGR02441. fa_ox_alpha_mit. 1 hit.
    PROSITEi PS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural analysis of cDNAs for subunits of human mitochondrial fatty acid beta-oxidation trifunctional protein."
      Kamijo T., Aoyama T., Komiyama A., Hashimoto T.
      Biochem. Biophys. Res. Commun. 199:818-825(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structures of the human cDNA and gene encoding the 78 kDa gastrin-binding protein and of a related pseudogene."
      Zhang Q.X., Baldwin G.S.
      Biochim. Biophys. Acta 1219:567-575(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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: Amygdala and Testis.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lymph.
    7. "Genes for the human mitochondrial trifunctional protein alpha- and beta-subunits are divergently transcribed from a common promoter region."
      Orii K.E., Orii K.O., Souri M., Orii T., Kondo N., Hashimoto T., Aoyama T.
      J. Biol. Chem. 274:8077-8084(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    8. "Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients."
      Kamijo T., Wanders R.J., Saudubray J.-M., Aoyama T., Komiyama A., Hashimoto T.
      J. Clin. Invest. 93:1740-1747(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295; LYS-303; LYS-406; LYS-505; LYS-540 AND LYS-644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of the major disease-causing mutation in the alpha-subunit of the mitochondrial trifunctional protein."
      Ijlst L., Wanders R.J.A., Ushikubo S., Kamijo T., Hashimoto T.
      Biochim. Biophys. Acta 1215:347-350(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LCHAD DEFICIENCY GLN-510.
    12. "The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy."
      Sims H.F., Brackett J.C., Powell C.K., Treem W.R., Hale D.E., Bennett M.J., Gibson B., Shapiro S., Strauss A.W.
      Proc. Natl. Acad. Sci. U.S.A. 92:841-845(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AFLP GLN-510.
    13. "Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein alpha subunit gene."
      Ijlst L., Ruiter J.P.N., Hoovers J.M.N., Jakobs M.E., Wanders R.J.A.
      J. Clin. Invest. 98:1028-1033(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT LCHAD DEFICIENCY GLN-510.
    14. "Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of two new mutations."
      Ijlst L., Oostheim W., Ruiter J.P.N., Wanders R.J.A.
      J. Inherit. Metab. Dis. 20:420-422(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LCHAD DEFICIENCY PRO-342 AND GLN-510.
    15. "Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation."
      Ibdah J.A., Tein I., Dionisi-Vici C., Bennett M.J., Ijlst L., Gibson B., Wanders R.J.A., Strauss A.W.
      J. Clin. Invest. 102:1193-1199(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TFP DEFICIENCY ASP-282 AND ASN-305.

    Entry informationi

    Entry nameiECHA_HUMAN
    AccessioniPrimary (citable) accession number: P40939
    Secondary accession number(s): B2R7L4
    , B4DYP2, Q16679, Q53T69, Q53TA2, Q96GT7, Q9UQC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: April 3, 2002
    Last modified: October 1, 2014
    This is version 169 of the entry and version 2 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3