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Protein

Trifunctional enzyme subunit alpha, mitochondrial

Gene

HADHA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei151Important for catalytic activityBy similarity1
Sitei173Important for catalytic activityBy similarity1

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydrogenase activity Source: ProtInc
  • acetyl-CoA C-acetyltransferase activity Source: ProtInc
  • enoyl-CoA hydratase activity Source: ProtInc
  • fatty-acyl-CoA binding Source: Ensembl
  • long-chain-3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
  • long-chain-enoyl-CoA hydratase activity Source: Ensembl
  • NAD binding Source: Ensembl

GO - Biological processi

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.
ZFISH:HS01481-MONOMER.
ReactomeiR-HSA-1482798. Acyl chain remodeling of CL.
R-HSA-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-HSA-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-HSA-77305. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
R-HSA-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-HSA-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
SABIO-RKP40939.
UniPathwayiUPA00659.

Chemistry databases

SwissLipidsiSLP:000000247.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:4801. HADHA.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: BHF-UCL
  • mitochondrial fatty acid beta-oxidation multienzyme complex Source: Ensembl
  • mitochondrial inner membrane Source: Reactome
  • mitochondrial nucleoid Source: BHF-UCL
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Mitochondrial trifunctional protein deficiency (MTPD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease biochemically characterized by loss of all enzyme activities of the mitochondrial trifunctional protein complex. Variable clinical manifestations include hypoglycemia, cardiomyopathy, delayed psychomotor development, sensorimotor axonopathy, generalized weakness, hepatic dysfunction, respiratory failure. Sudden infant death may occur. Most patients die from heart failure.
See also OMIM:609015
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021125282V → D in MTPD; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. 1 PublicationCorresponds to variant rs137852773dbSNPEnsembl.1
Natural variantiVAR_021126305I → N in MTPD; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. 1 PublicationCorresponds to variant rs137852774dbSNPEnsembl.1
Long-chain 3-hydroxyl-CoA dehydrogenase deficiency (LCHAD deficiency)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionThe 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.
See also OMIM:609016
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021127342L → P in LCHAD deficiency. 1 PublicationCorresponds to variant rs137852772dbSNPEnsembl.1
Natural variantiVAR_002273510E → Q in AFLP and LCHAD deficiency; loss of activity. 4 PublicationsCorresponds to variant rs137852769dbSNPEnsembl.1
Maternal acute fatty liver of pregnancy (AFLP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSevere 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).
See also OMIM:609016
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_002273510E → Q in AFLP and LCHAD deficiency; loss of activity. 4 PublicationsCorresponds to variant rs137852769dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3030.
MalaCardsiHADHA.
MIMi609015. phenotype.
609016. phenotype.
OpenTargetsiENSG00000084754.
Orphaneti243367. Acute fatty liver of pregnancy.
5. Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency.
746. Mitochondrial trifunctional protein deficiency.
PharmGKBiPA29175.

Polymorphism and mutation databases

BioMutaiHADHA.
DMDMi20141376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 36MitochondrionSequence analysisAdd BLAST36
ChainiPRO_000000740337 – 763Trifunctional enzyme subunit alpha, mitochondrialAdd BLAST727

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46N6-acetyllysine; alternateBy similarity1
Modified residuei46N6-succinyllysine; alternateBy similarity1
Modified residuei60N6-acetyllysine; alternateBy similarity1
Modified residuei60N6-succinyllysine; alternateBy similarity1
Modified residuei129N6-acetyllysineBy similarity1
Modified residuei166N6-acetyllysine; alternateBy similarity1
Modified residuei166N6-succinyllysine; alternateBy similarity1
Modified residuei213N6-succinyllysineBy similarity1
Modified residuei214N6-acetyllysine; alternateBy similarity1
Modified residuei214N6-succinyllysine; alternateBy similarity1
Modified residuei230N6-succinyllysineBy similarity1
Modified residuei249N6-acetyllysine; alternateBy similarity1
Modified residuei249N6-succinyllysine; alternateBy similarity1
Modified residuei289N6-acetyllysineBy similarity1
Modified residuei295N6-acetyllysineCombined sources1
Modified residuei303N6-acetyllysine; alternateCombined sources1
Modified residuei303N6-succinyllysine; alternateBy similarity1
Modified residuei316PhosphoserineBy similarity1
Modified residuei326N6-acetyllysine; alternateBy similarity1
Modified residuei326N6-succinyllysine; alternateBy similarity1
Modified residuei334N6-acetyllysine; alternateBy similarity1
Modified residuei334N6-succinyllysine; alternateBy similarity1
Modified residuei350N6-acetyllysine; alternateBy similarity1
Modified residuei350N6-succinyllysine; alternateBy similarity1
Modified residuei353N6-acetyllysineBy similarity1
Modified residuei395PhosphothreonineCombined sources1
Modified residuei399Omega-N-methylarginineBy similarity1
Modified residuei406N6-acetyllysine; alternateCombined sources1
Modified residuei406N6-succinyllysine; alternateBy similarity1
Modified residuei411N6-acetyllysine; alternateBy similarity1
Modified residuei411N6-succinyllysine; alternateBy similarity1
Modified residuei415N6-succinyllysineBy similarity1
Modified residuei419PhosphoserineBy similarity1
Modified residuei440N6-succinyllysineBy similarity1
Modified residuei460N6-acetyllysine; alternateBy similarity1
Modified residuei460N6-succinyllysine; alternateBy similarity1
Modified residuei505N6-acetyllysine; alternateCombined sources1
Modified residuei505N6-succinyllysine; alternateBy similarity1
Modified residuei519N6-acetyllysine; alternateBy similarity1
Modified residuei519N6-succinyllysine; alternateBy similarity1
Modified residuei540N6-acetyllysineCombined sources1
Modified residuei569N6-acetyllysine; alternateBy similarity1
Modified residuei569N6-succinyllysine; alternateBy similarity1
Modified residuei634N6-succinyllysineBy similarity1
Modified residuei644N6-acetyllysine; alternateCombined sources1
Modified residuei644N6-succinyllysine; alternateBy similarity1
Modified residuei646N6-succinyllysineBy similarity1
Modified residuei650PhosphoserineBy similarity1
Modified residuei664N6-acetyllysine; alternateBy similarity1
Modified residuei664N6-succinyllysine; alternateBy similarity1
Modified residuei728N6-acetyllysine; alternateBy similarity1
Modified residuei728N6-succinyllysine; alternateBy similarity1
Modified residuei735N6-acetyllysineBy similarity1
Modified residuei756PhosphoserineCombined sources1
Modified residuei759N6-acetyllysine; alternateBy similarity1
Modified residuei759N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP40939.
MaxQBiP40939.
PaxDbiP40939.
PeptideAtlasiP40939.
PRIDEiP40939.

2D gel databases

REPRODUCTION-2DPAGEIPI00031522.
UCD-2DPAGEP40939.

PTM databases

iPTMnetiP40939.
PhosphoSitePlusiP40939.
SwissPalmiP40939.

Expressioni

Gene expression databases

BgeeiENSG00000084754.
CleanExiHS_HADH.
HS_HADHA.
ExpressionAtlasiP40939. baseline and differential.
GenevisibleiP40939. HS.

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. 79 interactors.
IntActiP40939. 45 interactors.
MINTiMINT-1159893.
STRINGi9606.ENSP00000370023.

Structurei

3D structure databases

ProteinModelPortaliP40939.
SMRiP40939.
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

eggNOGiKOG1683. Eukaryota.
COG1024. LUCA.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261346.
HOVERGENiHBG005557.
InParanoidiP40939.
KOiK07515.
OMAiMMMLNEA.
OrthoDBiEOG091G02LF.
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.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
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. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MVACRAIGIL SRFSAFRILR SRGYICRNFT GSSALLTRTH INYGVKGDVA
60 70 80 90 100
VVRINSPNSK VNTLSKELHS EFSEVMNEIW ASDQIRSAVL ISSKPGCFIA
110 120 130 140 150
GADINMLAAC KTLQEVTQLS QEAQRIVEKL EKSTKPIVAA INGSCLGGGL
160 170 180 190 200
EVAISCQYRI ATKDRKTVLG TPEVLLGALP GAGGTQRLPK MVGVPAALDM
210 220 230 240 250
MLTGRSIRAD RAKKMGLVDQ LVEPLGPGLK PPEERTIEYL EEVAITFAKG
260 270 280 290 300
LADKKISPKR DKGLVEKLTA YAMTIPFVRQ QVYKKVEEKV RKQTKGLYPA
310 320 330 340 350
PLKIIDVVKT GIEQGSDAGY LCESQKFGEL VMTKESKALM GLYHGQVLCK
360 370 380 390 400
KNKFGAPQKD VKHLAILGAG LMGAGIAQVS VDKGLKTILK DATLTALDRG
410 420 430 440 450
QQQVFKGLND KVKKKALTSF ERDSIFSNLT GQLDYQGFEK ADMVIEAVFE
460 470 480 490 500
DLSLKHRVLK EVEAVIPDHC IFASNTSALP ISEIAAVSKR PEKVIGMHYF
510 520 530 540 550
SPVDKMQLLE IITTEKTSKD TSASAVAVGL KQGKVIIVVK DGPGFYTTRC
560 570 580 590 600
LAPMMSEVIR ILQEGVDPKK LDSLTTSFGF PVGAATLVDE VGVDVAKHVA
610 620 630 640 650
EDLGKVFGER FGGGNPELLT QMVSKGFLGR KSGKGFYIYQ EGVKRKDLNS
660 670 680 690 700
DMDSILASLK LPPKSEVSSD EDIQFRLVTR FVNEAVMCLQ EGILATPAEG
710 720 730 740 750
DIGAVFGLGF PPCLGGPFRF VDLYGAQKIV DRLKKYEAAY GKQFTPCQLL
760
ADHANSPNKK FYQ
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)DescriptionActionsGraphical viewLength
Sequence conflicti146L → V in BAA03941 (PubMed:8135828).Curated1
Sequence conflicti152V → L in AAA56664 (PubMed:7918661).Curated1
Sequence conflicti171T → A in AAA56664 (PubMed:7918661).Curated1
Sequence conflicti178A → I in AAA56664 (PubMed:7918661).Curated1
Sequence conflicti197 – 198AL → VF in AAA56664 (PubMed:7918661).Curated2
Sequence conflicti206S → N in AAA56664 (PubMed:7918661).Curated1
Sequence conflicti211R → S in AAA56664 (PubMed:7918661).Curated1
Sequence conflicti576T → P in AAA56664 (PubMed:7918661).Curated1
Sequence conflicti694L → S in BAA03941 (PubMed:8135828).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021125282V → D in MTPD; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. 1 PublicationCorresponds to variant rs137852773dbSNPEnsembl.1
Natural variantiVAR_021126305I → N in MTPD; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. 1 PublicationCorresponds to variant rs137852774dbSNPEnsembl.1
Natural variantiVAR_021127342L → P in LCHAD deficiency. 1 PublicationCorresponds to variant rs137852772dbSNPEnsembl.1
Natural variantiVAR_048908358Q → K.Corresponds to variant rs10200182dbSNPEnsembl.1
Natural variantiVAR_002273510E → Q in AFLP and LCHAD deficiency; loss of activity. 4 PublicationsCorresponds to variant rs137852769dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0543581 – 18MVACR…SAFRI → MESKGMWQLFELTLPIQS in isoform 2. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_05435919 – 105Missing in isoform 2. 1 PublicationAdd BLAST87
Alternative sequenceiVSP_054360326 – 347KFGEL…YHGQV → VNLFPFNVLLSVKGKLKIQS SV in isoform 2. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_054361348 – 763Missing in isoform 2. 1 PublicationAdd BLAST416

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP40939.
SMRiP40939.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109280. 79 interactors.
IntActiP40939. 45 interactors.
MINTiMINT-1159893.
STRINGi9606.ENSP00000370023.

Chemistry databases

SwissLipidsiSLP:000000247.

PTM databases

iPTMnetiP40939.
PhosphoSitePlusiP40939.
SwissPalmiP40939.

Polymorphism and mutation databases

BioMutaiHADHA.
DMDMi20141376.

2D gel databases

REPRODUCTION-2DPAGEIPI00031522.
UCD-2DPAGEP40939.

Proteomic databases

EPDiP40939.
MaxQBiP40939.
PaxDbiP40939.
PeptideAtlasiP40939.
PRIDEiP40939.

Protocols and materials databases

DNASUi3030.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3030.
DisGeNETi3030.
GeneCardsiHADHA.
HGNCiHGNC:4801. HADHA.
HPAiHPA015536.
HPA056070.
MalaCardsiHADHA.
MIMi600890. gene.
609015. phenotype.
609016. phenotype.
neXtProtiNX_P40939.
OpenTargetsiENSG00000084754.
Orphaneti243367. Acute fatty liver of pregnancy.
5. Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency.
746. Mitochondrial trifunctional protein deficiency.
PharmGKBiPA29175.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1024. LUCA.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261346.
HOVERGENiHBG005557.
InParanoidiP40939.
KOiK07515.
OMAiMMMLNEA.
OrthoDBiEOG091G02LF.
PhylomeDBiP40939.
TreeFamiTF352288.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:HS01481-MONOMER.
ZFISH:HS01481-MONOMER.
ReactomeiR-HSA-1482798. Acyl chain remodeling of CL.
R-HSA-77285. Beta oxidation of myristoyl-CoA to lauroyl-CoA.
R-HSA-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-HSA-77305. Beta oxidation of palmitoyl-CoA to myristoyl-CoA.
R-HSA-77310. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
R-HSA-77350. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
SABIO-RKP40939.

Miscellaneous databases

ChiTaRSiHADHA. human.
GenomeRNAii3030.
PROiP40939.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000084754.
CleanExiHS_HADH.
HS_HADHA.
ExpressionAtlasiP40939. baseline and differential.
GenevisibleiP40939. HS.

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.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
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. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02441. fa_ox_alpha_mit. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 192 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.