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P40939

- ECHA_HUMAN

UniProt

P40939 - ECHA_HUMAN

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Protein

Trifunctional enzyme subunit alpha, mitochondrial

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

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 activity By similarity
Sitei173 – 1731Important for catalytic activity By 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
Complete GO annotation...

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
Complete GO annotation...

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.
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.
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. 4 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).
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti510 – 5101E → Q in AFLP and LCHAD deficiency; loss of activity. 4 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 – 3636Mitochondrion Reviewed predictionAdd
BLAST
Chaini37 – 763727Trifunctional enzyme subunit alpha, mitochondrialPRO_0000007403Add
BLAST

Amino acid modifications

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

Family & Domainsi

Sequence similaritiesi

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

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

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. 4 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. VSP_054358Add
BLAST
Alternative sequencei19 – 10587Missing in isoform 2. VSP_054359Add
BLAST
Alternative sequencei326 – 34722KFGEL…YHGQV → VNLFPFNVLLSVKGKLKIQS SV in isoform 2. VSP_054360Add
BLAST
Alternative sequencei348 – 763416Missing in isoform 2. VSP_054361Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461L → V in BAA03941. 1 Publication
Sequence conflicti152 – 1521V → L in AAA56664. 1 Publication
Sequence conflicti171 – 1711T → A in AAA56664. 1 Publication
Sequence conflicti178 – 1781A → I in AAA56664. 1 Publication
Sequence conflicti197 – 1982AL → VF in AAA56664. 1 Publication
Sequence conflicti206 – 2061S → N in AAA56664. 1 Publication
Sequence conflicti211 – 2111R → S in AAA56664. 1 Publication
Sequence conflicti576 – 5761T → P in AAA56664. 1 Publication
Sequence conflicti694 – 6941L → S in BAA03941. 1 Publication

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.
ENST00000457468; ENSP00000405344; ENSG00000084754.
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 .
ENST00000457468 ; ENSP00000405344 ; ENSG00000084754 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 168 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

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