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P40939 (ECHA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trifunctional enzyme subunit alpha, mitochondrial
Alternative name(s):
78 kDa gastrin-binding protein
TP-alpha

Including the following 2 domains:

  1. Long-chain enoyl-CoA hydratase
    EC=4.2.1.17
  2. Long chain 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.211
Gene names
Name:HADHA
Synonyms:HADH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length763 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional subunit.

Catalytic activity

(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.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits. Ref.8

Subcellular location

Mitochondrion.

Involvement in disease

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.

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.

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. Ref.12

Sequence similarities

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.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandNAD
   Molecular functionLyase
Oxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processcardiolipin acyl-chain remodeling

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation

Traceable author statement. Source: Reactome

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

response to drug

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial fatty acid beta-oxidation multienzyme complex

Inferred from electronic annotation. Source: Ensembl

mitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial nucleoid

Inferred from direct assay PubMed 18063578. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

   Molecular_function3-hydroxyacyl-CoA dehydrogenase activity

Traceable author statement Ref.1. Source: ProtInc

NAD binding

Inferred from electronic annotation. Source: Ensembl

acetyl-CoA C-acetyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

enoyl-CoA hydratase activity

Traceable author statement Ref.1. Source: ProtInc

fatty-acyl-CoA binding

Inferred from electronic annotation. Source: Ensembl

long-chain-3-hydroxyacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

long-chain-enoyl-CoA hydratase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 20562859. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P40939-1)

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.
Isoform 2 (identifier: P40939-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3636Mitochondrion Potential
Chain37 – 763727Trifunctional enzyme subunit alpha, mitochondrial
PRO_0000007403

Sites

Site1511Important for catalytic activity By similarity
Site1731Important for catalytic activity By similarity

Amino acid modifications

Modified residue461N6-acetyllysine; alternate By similarity
Modified residue461N6-succinyllysine; alternate By similarity
Modified residue601N6-acetyllysine; alternate By similarity
Modified residue601N6-succinyllysine; alternate By similarity
Modified residue1291N6-acetyllysine By similarity
Modified residue1661N6-acetyllysine; alternate By similarity
Modified residue1661N6-succinyllysine; alternate By similarity
Modified residue2131N6-succinyllysine By similarity
Modified residue2141N6-acetyllysine; alternate By similarity
Modified residue2141N6-succinyllysine; alternate By similarity
Modified residue2301N6-succinyllysine By similarity
Modified residue2491N6-acetyllysine; alternate By similarity
Modified residue2491N6-succinyllysine; alternate By similarity
Modified residue2891N6-acetyllysine By similarity
Modified residue2951N6-acetyllysine Ref.9
Modified residue3031N6-acetyllysine; alternate Ref.9
Modified residue3031N6-succinyllysine; alternate By similarity
Modified residue3261N6-acetyllysine; alternate By similarity
Modified residue3261N6-succinyllysine; alternate By similarity
Modified residue3341N6-acetyllysine; alternate By similarity
Modified residue3341N6-succinyllysine; alternate By similarity
Modified residue3501N6-acetyllysine; alternate By similarity
Modified residue3501N6-succinyllysine; alternate By similarity
Modified residue3531N6-acetyllysine By similarity
Modified residue4061N6-acetyllysine; alternate Ref.9
Modified residue4061N6-succinyllysine; alternate By similarity
Modified residue4111N6-acetyllysine; alternate By similarity
Modified residue4111N6-succinyllysine; alternate By similarity
Modified residue4151N6-succinyllysine By similarity
Modified residue4401N6-succinyllysine By similarity
Modified residue4601N6-acetyllysine; alternate By similarity
Modified residue4601N6-succinyllysine; alternate By similarity
Modified residue5051N6-acetyllysine; alternate Ref.9
Modified residue5051N6-succinyllysine; alternate By similarity
Modified residue5191N6-acetyllysine; alternate By similarity
Modified residue5191N6-succinyllysine; alternate By similarity
Modified residue5401N6-acetyllysine Ref.9
Modified residue5691N6-acetyllysine; alternate By similarity
Modified residue5691N6-succinyllysine; alternate By similarity
Modified residue6341N6-succinyllysine By similarity
Modified residue6441N6-acetyllysine; alternate Ref.9
Modified residue6441N6-succinyllysine; alternate By similarity
Modified residue6461N6-succinyllysine By similarity
Modified residue6641N6-acetyllysine; alternate By similarity
Modified residue6641N6-succinyllysine; alternate By similarity
Modified residue7281N6-acetyllysine; alternate By similarity
Modified residue7281N6-succinyllysine; alternate By similarity
Modified residue7351N6-acetyllysine By similarity
Modified residue7591N6-acetyllysine; alternate By similarity
Modified residue7591N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence1 – 1818MVACR…SAFRI → MESKGMWQLFELTLPIQS in isoform 2.
VSP_054358
Alternative sequence19 – 10587Missing in isoform 2.
VSP_054359
Alternative sequence326 – 34722KFGEL…YHGQV → VNLFPFNVLLSVKGKLKIQS SV in isoform 2.
VSP_054360
Alternative sequence348 – 763416Missing in isoform 2.
VSP_054361
Natural variant2821V → D in TFP deficiency; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. Ref.15
VAR_021125
Natural variant3051I → N in TFP deficiency; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy. Ref.15
VAR_021126
Natural variant3421L → P in LCHAD deficiency. Ref.14
VAR_021127
Natural variant3581Q → K.
Corresponds to variant rs10200182 [ dbSNP | Ensembl ].
VAR_048908
Natural variant5101E → Q in AFLP and LCHAD deficiency; loss of activity. Ref.11 Ref.12 Ref.13 Ref.14
Corresponds to variant rs137852769 [ dbSNP | Ensembl ].
VAR_002273

Experimental info

Sequence conflict1461L → V in BAA03941. Ref.1
Sequence conflict1521V → L in AAA56664. Ref.2
Sequence conflict1711T → A in AAA56664. Ref.2
Sequence conflict1781A → I in AAA56664. Ref.2
Sequence conflict197 – 1982AL → VF in AAA56664. Ref.2
Sequence conflict2061S → N in AAA56664. Ref.2
Sequence conflict2111R → S in AAA56664. Ref.2
Sequence conflict5761T → P in AAA56664. Ref.2
Sequence conflict6941L → S in BAA03941. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2002. Version 2.
Checksum: 247FF7B4E48FB484

FASTA76383,000
        10         20         30         40         50         60 
MVACRAIGIL SRFSAFRILR SRGYICRNFT GSSALLTRTH INYGVKGDVA VVRINSPNSK 

        70         80         90        100        110        120 
VNTLSKELHS EFSEVMNEIW ASDQIRSAVL ISSKPGCFIA GADINMLAAC KTLQEVTQLS 

       130        140        150        160        170        180 
QEAQRIVEKL EKSTKPIVAA INGSCLGGGL EVAISCQYRI ATKDRKTVLG TPEVLLGALP 

       190        200        210        220        230        240 
GAGGTQRLPK MVGVPAALDM MLTGRSIRAD RAKKMGLVDQ LVEPLGPGLK PPEERTIEYL 

       250        260        270        280        290        300 
EEVAITFAKG LADKKISPKR DKGLVEKLTA YAMTIPFVRQ QVYKKVEEKV RKQTKGLYPA 

       310        320        330        340        350        360 
PLKIIDVVKT GIEQGSDAGY LCESQKFGEL VMTKESKALM GLYHGQVLCK KNKFGAPQKD 

       370        380        390        400        410        420 
VKHLAILGAG LMGAGIAQVS VDKGLKTILK DATLTALDRG QQQVFKGLND KVKKKALTSF 

       430        440        450        460        470        480 
ERDSIFSNLT GQLDYQGFEK ADMVIEAVFE DLSLKHRVLK EVEAVIPDHC IFASNTSALP 

       490        500        510        520        530        540 
ISEIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTEKTSKD TSASAVAVGL KQGKVIIVVK 

       550        560        570        580        590        600 
DGPGFYTTRC LAPMMSEVIR ILQEGVDPKK LDSLTTSFGF PVGAATLVDE VGVDVAKHVA 

       610        620        630        640        650        660 
EDLGKVFGER FGGGNPELLT QMVSKGFLGR KSGKGFYIYQ EGVKRKDLNS DMDSILASLK 

       670        680        690        700        710        720 
LPPKSEVSSD EDIQFRLVTR FVNEAVMCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF 

       730        740        750        760 
VDLYGAQKIV DRLKKYEAAY GKQFTPCQLL ADHANSPNKK FYQ 

« Hide

Isoform 2 [UniParc].

Checksum: BA756450F59E9B8E
Show »

FASTA26028,367

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1721.1.
PIRJC2108.
RefSeqNP_000173.2. NM_000182.4. [P40939-1]
UniGeneHs.516032.

3D structure databases

ProteinModelPortalP40939.
SMRP40939. Positions 45-763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109280. 47 interactions.
IntActP40939. 31 interactions.
MINTMINT-1159893.
STRING9606.ENSP00000370023.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP40939.

Polymorphism databases

DMDM20141376.

2D gel databases

REPRODUCTION-2DPAGEIPI00031522.
UCD-2DPAGEP40939.

Proteomic databases

MaxQBP40939.
PaxDbP40939.
PeptideAtlasP40939.
PRIDEP40939.

Protocols and materials databases

DNASU3030.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380649; ENSP00000370023; ENSG00000084754.
ENST00000457468; ENSP00000405344; ENSG00000084754.
GeneID3030.
KEGGhsa:3030.
UCSCuc002rgy.3. human. [P40939-1]

Organism-specific databases

CTD3030.
GeneCardsGC02M026413.
HGNCHGNC:4801. HADHA.
HPAHPA015536.
HPA056070.
MIM600890. gene.
609015. phenotype.
609016. phenotype.
neXtProtNX_P40939.
Orphanet243367. Acute fatty liver of pregnancy.
5. Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency.
746. Mitochondrial trifunctional protein deficiency.
PharmGKBPA29175.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
HOVERGENHBG005557.
InParanoidP40939.
KOK07515.
OMAFYVYQEG.
OrthoDBEOG7P2XRF.
PhylomeDBP40939.
TreeFamTF352288.

Enzyme and pathway databases

BioCycMetaCyc:HS01481-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP40939.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressP40939.
BgeeP40939.
CleanExHS_HADH.
HS_HADHA.
GenevestigatorP40939.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProIPR006180. 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]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR02441. fa_ox_alpha_mit. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHADHA. human.
GenomeRNAi3030.
NextBio11996.
PROP40939.
SOURCESearch...

Entry information

Entry nameECHA_HUMAN
AccessionPrimary (citable) accession number: P40939
Secondary accession number(s): B2R7L4 expand/collapse secondary AC list , B4DYP2, Q16679, Q53T69, Q53TA2, Q96GT7, Q9UQC5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 3, 2002
Last modified: July 9, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM