HADH

Functionⁱ

Plays an essential role in the mitochondrial beta-oxidation of short chain fatty acids. Exerts it highest activity toward 3-hydroxybutyryl-CoA.

Catalytic activityⁱ

(S)-3-hydroxyacyl-CoA + NAD⁺ = 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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	57	NAD2 Publications	1
Binding siteⁱ	73	Coenzyme A	1
Binding siteⁱ	80	Coenzyme A	1
Binding siteⁱ	122	NAD2 Publications	1
Binding siteⁱ	127	NAD2 Publications	1
Binding siteⁱ	149	Coenzyme A	1
Binding siteⁱ	149	NAD2 Publications	1
Siteⁱ	170	Important for catalytic activityCurated	1
Binding siteⁱ	173	NAD2 Publications	1
Binding siteⁱ	305	NAD2 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	34 – 39	NAD2 Publications		6

GO - Molecular functionⁱ

3-hydroxyacyl-CoA dehydrogenase activity Source: Reactome
NAD+ binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

fatty acid beta-oxidation Source: Reactome
negative regulation of insulin secretion Source: Ensembl
positive regulation of cold-induced thermogenesis
Source: YuBioLab
Inferred from sequence or structural similarityⁱ
- 21990309
response to activity Source: Ensembl
response to drug Source: Ensembl
response to insulin Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Fatty acid metabolism, Lipid metabolism
Ligand	NAD

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS06563-MONOMER
BRENDAⁱ	1.1.1.35 2681
Reactomeⁱ	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 R-HSA-77352 Beta oxidation of butanoyl-CoA to acetyl-CoA
SABIO-RKⁱ	Q16836
UniPathwayⁱ	UPA00659

Chemistry databases

SwissLipidsⁱ	SLP:000001250

SwissLipidsⁱ

SLP:000001250

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial (EC:1.1.1.35) Short name: HCDH Alternative name(s): Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase Short-chain 3-hydroxyacyl-CoA dehydrogenase
Gene namesⁱ	Name:HADH Synonyms:HAD, HADHSC, SCHAD
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 4

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000138796.15
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4799 HADH
MIMⁱ	601609 gene
neXtProtⁱ	NX_Q16836

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

3-alpha-hydroxyacyl-CoA dehydrogenase deficiency (HADH deficiency)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive, metabolic disorder with various clinical presentations including hypoglycemia, hepatoencephalopathy, myopathy or cardiomyopathy, and in some cases sudden death.

Familial hyperinsulinemic hypoglycemia 4 (HHF4)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionMost common cause of persistent hypoglycemia in infancy. Unless early and aggressive intervention is undertaken, brain damage from recurrent episodes of hypoglycemia may occur. HHF4 should be easily recognizable by analysis of acylcarnitine species and that this disorder responds well to treatment with diazoxide. It provides the first 'experiment of nature' that links impaired fatty acid oxidation to hyperinsulinism and that provides support for the concept that a lipid signaling pathway is implicated in the control of insulin secretion.

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_024081	258	P → L in HHF4; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs137853103EnsemblClinVar.		1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3033
GeneReviewsⁱ	HADH
MalaCards human disease database More...MalaCardsⁱ	HADH
MIMⁱ	231530 phenotype 609975 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000138796
Orphanetⁱ	71212 Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency
PharmGKBⁱ	PA29173

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB03612 3-Hydroxybutyryl-Coenzyme A DB03059 Acetoacetyl-Coenzyme A DB00157 NADH

DrugBankⁱ

DB03612 3-Hydroxybutyryl-Coenzyme A
DB03059 Acetoacetyl-Coenzyme A
DB00157 NADH

Polymorphism and mutation databases

BioMutaⁱ	HADH
DMDMⁱ	311033442

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 12	MitochondrionAdd BLAST		12
ChainⁱPRO_0000007406	13 – 314	Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialAdd BLAST		302

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	80	N6-succinyllysineBy similarity	1
Modified residueⁱ	81	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	81	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	87	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	87	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	125	N6-acetyllysineBy similarity	1
Modified residueⁱ	136	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	136	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	179	N6-acetyllysineBy similarity	1
Modified residueⁱ	185	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	185	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	192	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	192	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	202	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	202	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	206	N6-succinyllysineBy similarity	1
Modified residueⁱ	212	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	212	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	241	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	241	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	312	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	312	N6-succinyllysine; alternateBy similarity	1

Post-translational modificationⁱ

Succinylation at Lys-81, adjacent to a coenzyme A binding site. Desuccinylated by SIRT5 (By similarity).By similarity

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	Q16836
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q16836
PeptideAtlas More...PeptideAtlasⁱ	Q16836
PRIDEⁱ	Q16836
ProteomicsDBⁱ	61096 61097 [Q16836-2]
TopDownProteomicsⁱ	Q16836-1 [Q16836-1]

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00298406
UCD-2DPAGEⁱ	Q16836

PTM databases

iPTMnetⁱ	Q16836
PhosphoSitePlusⁱ	Q16836

Expressionⁱ

Tissue specificityⁱ

Expressed in liver, kidney, pancreas, heart and skeletal muscle.

Gene expression databases

Bgeeⁱ	ENSG00000138796 Expressed in 233 organ(s), highest expression level in parietal pleura
CleanExⁱ	HS_HADH
ExpressionAtlasⁱ	Q16836 baseline and differential
Genevisibleⁱ	Q16836 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA039588 HPA043888

HPAⁱ

HPA039588
HPA043888

Interactionⁱ

Subunit structureⁱ

Homodimer.2 Publications

Protein-protein interaction databases

BioGridⁱ	109283, 23 interactors
IntActⁱ	Q16836, 5 interactors

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	1 – 11	Combined sources	11
Helixⁱ	14 – 22	Combined sources	9
Beta strandⁱ	29 – 33	Combined sources	5
Helixⁱ	37 – 48	Combined sources	12
Beta strandⁱ	52 – 56	Combined sources	5
Helixⁱ	60 – 79	Combined sources	20
Beta strandⁱ	82 – 84	Combined sources	3
Helixⁱ	86 – 98	Combined sources	13
Beta strandⁱ	100 – 104	Combined sources	5
Helixⁱ	106 – 109	Combined sources	4
Helixⁱ	110 – 112	Combined sources	3
Beta strandⁱ	114 – 118	Combined sources	5
Helixⁱ	124 – 134	Combined sources	11
Turnⁱ	135 – 137	Combined sources	3
Beta strandⁱ	143 – 146	Combined sources	4
Beta strandⁱ	149 – 151	Combined sources	3
Helixⁱ	153 – 157	Combined sources	5
Helixⁱ	163 – 165	Combined sources	3
Beta strandⁱ	166 – 171	Combined sources	6
Turnⁱ	175 – 177	Combined sources	3
Beta strandⁱ	180 – 184	Combined sources	5
Helixⁱ	191 – 203	Combined sources	13
Beta strandⁱ	207 – 211	Combined sources	5
Turnⁱ	215 – 218	Combined sources	4
Helixⁱ	219 – 235	Combined sources	17
Helixⁱ	241 – 252	Combined sources	12
Helixⁱ	258 – 265	Combined sources	8
Helixⁱ	267 – 279	Combined sources	13
Turnⁱ	280 – 283	Combined sources	4
Helixⁱ	285 – 287	Combined sources	3
Helixⁱ	291 – 298	Combined sources	8
Turnⁱ	304 – 307	Combined sources	4
Beta strandⁱ	308 – 312	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	Q16836
SMRⁱ	Q16836
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q16836

EvolutionaryTraceⁱ

Q16836

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00880000137923
HOGENOMⁱ	HOG000141498
HOVERGENⁱ	HBG000832
InParanoidⁱ	Q16836
KEGG Orthology (KO) More...KOⁱ	K00022
PhylomeDBⁱ	Q16836
TreeFamⁱ	TF300886

Family and domain databases

Gene3Dⁱ	1.10.1040.10, 1 hit
InterProⁱ	View protein in InterPro IPR022694 3-OHacyl-CoA_DH IPR006180 3-OHacyl-CoA_DH_CS IPR006176 3-OHacyl-CoA_DH_NAD-bd IPR006108 3HC_DH_C IPR008927 6-PGluconate_DH-like_C_sf IPR013328 6PGD_dom2 IPR036291 NAD(P)-bd_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00725 3HCDH, 1 hit PF02737 3HCDH_N, 1 hit
PIRSFⁱ	PIRSF000105 HCDH, 1 hit
SUPFAMⁱ	SSF48179 SSF48179, 1 hit SSF51735 SSF51735, 1 hit
PROSITEⁱ	View protein in PROSITE PS00067 3HCDH, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 12 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q16836-1) [UniParc]FASTA Add 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
MAFVTRQFMR SVSSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG 
        60         70         80         90        100
HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI 
       110        120        130        140        150
ATSTDAASVV HSTDLVVEAI VENLKVKNEL FKRLDKFAAE HTIFASNTSS 
       160        170        180        190        200
LQITSIANAT TRQDRFAGLH FFNPVPVMKL VEVIKTPMTS QKTFESLVDF 
       210        220        230        240        250
SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERGDAS KEDIDTAMKL 
       260        270        280        290        300
GAGYPMGPFE LLDYVGLDTT KFIVDGWHEM DAENPLHQPS PSLNKLVAEN 
       310 
KFGKKTGEGF YKYK

Length:314

Mass (Da):34,294

Last modified:November 2, 2010 - v3

Checksum:ⁱ0C6F7C01BBCE646A

GO

Isoform 2 (identifier: Q16836-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MGRAGLEAPPPPCGVTGTPGARGLQGRVGPRPQSLAFRGCLPRASSLPGSPRCRRRCHTM
236-236: R → RDFQTCGDSNSGLGFSLK

« Hide

        10         20         30         40         50
MGRAGLEAPP PPCGVTGTPG ARGLQGRVGP RPQSLAFRGC LPRASSLPGS 
        60         70         80         90        100
PRCRRRCHTM AFVTRQFMRS VSSSSTASAS AKKIIVKHVT VIGGGLMGAG 
       110        120        130        140        150
IAQVAAATGH TVVLVDQTED ILAKSKKGIE ESLRKVAKKK FAENLKAGDE 
       160        170        180        190        200
FVEKTLSTIA TSTDAASVVH STDLVVEAIV ENLKVKNELF KRLDKFAAEH 
       210        220        230        240        250
TIFASNTSSL QITSIANATT RQDRFAGLHF FNPVPVMKLV EVIKTPMTSQ 
       260        270        280        290        300
KTFESLVDFS KALGKHPVSC KDTPGFIVNR LLVPYLMEAI RLYERDFQTC 
       310        320        330        340        350
GDSNSGLGFS LKGDASKEDI DTAMKLGAGY PMGPFELLDY VGLDTTKFIV 
       360        370        380        390
DGWHEMDAEN PLHQPSPSLN KLVAENKFGK KTGEGFYKYK

Show »

Length:390

Mass (Da):42,140

Checksum:ⁱ3C20D80AAC4EB142

GO

Isoform 3 (identifier: Q16836-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
236-236: R → RDFQTCGDSNSGLGFSLK

« Hide

        10         20         30         40         50
MAFVTRQFMR SVSSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG 
        60         70         80         90        100
HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI 
       110        120        130        140        150
ATSTDAASVV HSTDLVVEAI VENLKVKNEL FKRLDKFAAE HTIFASNTSS 
       160        170        180        190        200
LQITSIANAT TRQDRFAGLH FFNPVPVMKL VEVIKTPMTS QKTFESLVDF 
       210        220        230        240        250
SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERDFQT CGDSNSGLGF 
       260        270        280        290        300
SLKGDASKED IDTAMKLGAG YPMGPFELLD YVGLDTTKFI VDGWHEMDAE 
       310        320        330 
NPLHQPSPSL NKLVAENKFG KKTGEGFYKY K

Note: No experimental confirmation available.

Show »

Length:331

Mass (Da):36,051

Checksum:ⁱ11B5646AD077A666

GO

Computationally mapped potential isoform sequencesⁱ

There are 12 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	A0A0A0MSE2	A0A0A0MSE2_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	317	Annotation score:
	E9PF18	E9PF18_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	390	Annotation score:
	A0A0D9SFP2	A0A0D9SFP2_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	318	Annotation score:
	A0A1W2PQV5	A0A1W2PQV5_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	245	Annotation score:
	A0A1W2PNM1	A0A1W2PNM1_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	267	Annotation score:
	A0A1W2PQ78	A0A1W2PQ78_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	176	Annotation score:
	A0A1W2PQC2	A0A1W2PQC2_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	165	Annotation score:
	A0A1W2PP40	A0A1W2PP40_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	145	Annotation score:
	A0A1W2PRT2	A0A1W2PRT2_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	183	Annotation score:
	A0A1W2PQ55	A0A1W2PQ55_HUMAN	Hydroxyacyl-coenzyme A dehydrogenas... Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	HADH	100	Annotation score:
There are more potential isoformsShow all

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Isoform 2 (identifier: Q16836-2)
Sequence conflictⁱ	41	L → P in AAB58153 (Ref. 2) Curated	1
Sequence conflictⁱ	56	R → H in AAB58153 (Ref. 2) Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_024079	40	A → T in HADH deficiency. 1 PublicationCorresponds to variant dbSNP:rs137853101EnsemblClinVar.	1
Natural variantⁱVAR_024080	57	D → E in HADH deficiency. 1 PublicationCorresponds to variant dbSNP:rs137853102EnsemblClinVar.	1
Natural variantⁱVAR_026764	86	L → P4 PublicationsCorresponds to variant dbSNP:rs4956145Ensembl.	1
Natural variantⁱVAR_055701	152	Q → H1 PublicationCorresponds to variant dbSNP:rs1051519EnsemblClinVar.	1
Natural variantⁱVAR_024081	258	P → L in HHF4; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs137853103EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_016551	1	M → MGRAGLEAPPPPCGVTGTPG ARGLQGRVGPRPQSLAFRGC LPRASSLPGSPRCRRRCHTM in isoform 2. 1 Publication		1
Alternative sequenceⁱVSP_016552	236	R → RDFQTCGDSNSGLGFSLK in isoform 2 and isoform 3. 1 Publication		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X96752 mRNA Translation: CAA65528.1 AF001902 mRNA Translation: AAB54008.1 AF001903 mRNA Translation: AAB54009.1 AF001904 Genomic DNA Translation: AAB58153.1 AF095703 Genomic DNA Translation: AAD13581.1 AC114733 Genomic DNA Translation: AAY41050.1 AC118062 Genomic DNA No translation available. BC000306 mRNA Translation: AAH00306.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS3678.1 [Q16836-1] CCDS54790.1 [Q16836-3]
PIRⁱ	JC4879
NCBI Reference Sequences More...RefSeqⁱ	NP_001171634.2, NM_001184705.2 NP_005318.3, NM_005327.4
UniGeneⁱ	Hs.438289

Genome annotation databases

Ensemblⁱ	ENST00000309522; ENSP00000312288; ENSG00000138796 [Q16836-1] ENST00000603302; ENSP00000474560; ENSG00000138796 [Q16836-3]
GeneIDⁱ	3033
KEGGⁱ	hsa:3033
UCSC genome browser More...UCSCⁱ	uc003hyq.4 human [Q16836-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q16836	Testis secretory sperm-binding protein Li 203a		HUMAN		314	UniRef100_Q16836
Q16836-3	Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial		HUMAN		390	UniRef100_E9PF18

Protein	Similar proteins		Species	Score	Length	Source
Q16836	Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	)	PIG		314	UniRef90_Q16836
Testis secretory sperm-binding protein Li 203a		HUMAN		314
Uncharacterized protein		MACFA		390
Uncharacterized protein		PAPAN		374
Uncharacterized protein		MACMU		372
+73
Q16836-2	Uncharacterized protein		PANPA		452	UniRef90_Q16836-2
Hydroxyacyl-CoA dehydrogenase		PANTR		314
Hydroxyacyl-CoA dehydrogenase		GORGO		390
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial		HUMAN		390
Uncharacterized protein		NOMLE		390
+14
Q16836-3	Isoform 2 of Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial		HUMAN		390	UniRef90_Q16836-2
Uncharacterized protein		PANPA		452
Hydroxyacyl-CoA dehydrogenase		PANTR		314
Hydroxyacyl-CoA dehydrogenase		GORGO		390
Uncharacterized protein		NOMLE		390
+14

Protein	Similar proteins		Species	Score	Length	Source
Q16836	Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial	)	PIG		314	UniRef50_Q16836
Testis secretory sperm-binding protein Li 203a		HUMAN		314
Uncharacterized protein		MACFA		390
Uncharacterized protein		PAPAN		374
Uncharacterized protein		MACMU		372
+120

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X96752 mRNA Translation: CAA65528.1 AF001902 mRNA Translation: AAB54008.1 AF001903 mRNA Translation: AAB54009.1 AF001904 Genomic DNA Translation: AAB58153.1 AF095703 Genomic DNA Translation: AAD13581.1 AC114733 Genomic DNA Translation: AAY41050.1 AC118062 Genomic DNA No translation available. BC000306 mRNA Translation: AAH00306.1
CCDSⁱ	CCDS3678.1 [Q16836-1] CCDS54790.1 [Q16836-3]
PIRⁱ	JC4879
RefSeqⁱ	NP_001171634.2, NM_001184705.2 NP_005318.3, NM_005327.4
UniGeneⁱ	Hs.438289

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1F0Y	X-ray	1.80	A/B	13-314	[»]
	1F12	X-ray	2.40	A/B	13-314	[»]
	1F14	X-ray	2.30	A/B	13-314	[»]
	1F17	X-ray	2.30	A/B	13-314	[»]
	1IL0	X-ray	2.20	A/B	13-314	[»]
	1LSJ	X-ray	2.50	A/B	13-314	[»]
	1LSO	X-ray	2.60	A/B	13-314	[»]
	1M75	X-ray	2.30	A/B	13-314	[»]
	1M76	X-ray	2.15	A/B	13-314	[»]
	2HDH	X-ray	2.20	A/B	24-314	[»]
	3HAD	X-ray	2.00	A/B	13-314	[»]
	3RQS	X-ray	2.00	A/B	1-314	[»]
ProteinModelPortalⁱ	Q16836
SMRⁱ	Q16836
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109283, 23 interactors
IntActⁱ	Q16836, 5 interactors

Chemistry databases

DrugBankⁱ	DB03612 3-Hydroxybutyryl-Coenzyme A DB03059 Acetoacetyl-Coenzyme A DB00157 NADH
SwissLipidsⁱ	SLP:000001250

PTM databases

iPTMnetⁱ	Q16836
PhosphoSitePlusⁱ	Q16836

Polymorphism and mutation databases

BioMutaⁱ	HADH
DMDMⁱ	311033442

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00298406
UCD-2DPAGEⁱ	Q16836

Proteomic databases

EPDⁱ	Q16836
MaxQBⁱ	Q16836
PeptideAtlasⁱ	Q16836
PRIDEⁱ	Q16836
ProteomicsDBⁱ	61096 61097 [Q16836-2]
TopDownProteomicsⁱ	Q16836-1 [Q16836-1]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	3033
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000309522; ENSP00000312288; ENSG00000138796 [Q16836-1] ENST00000603302; ENSP00000474560; ENSG00000138796 [Q16836-3]
GeneIDⁱ	3033
KEGGⁱ	hsa:3033
UCSCⁱ	uc003hyq.4 human [Q16836-1]

Organism-specific databases

CTDⁱ	3033
DisGeNETⁱ	3033
EuPathDBⁱ	HostDB:ENSG00000138796.15
GeneCardsⁱ	HADH
GeneReviewsⁱ	HADH
HGNCⁱ	HGNC:4799 HADH
HPAⁱ	HPA039588 HPA043888
MalaCardsⁱ	HADH
MIMⁱ	231530 phenotype 601609 gene 609975 phenotype
neXtProtⁱ	NX_Q16836
OpenTargetsⁱ	ENSG00000138796
Orphanetⁱ	71212 Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency
PharmGKBⁱ	PA29173
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

GeneTreeⁱ	ENSGT00880000137923
HOGENOMⁱ	HOG000141498
HOVERGENⁱ	HBG000832
InParanoidⁱ	Q16836
KOⁱ	K00022
PhylomeDBⁱ	Q16836
TreeFamⁱ	TF300886

Enzyme and pathway databases

UniPathwayⁱ	UPA00659
BioCycⁱ	MetaCyc:HS06563-MONOMER
BRENDAⁱ	1.1.1.35 2681
Reactomeⁱ	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 R-HSA-77352 Beta oxidation of butanoyl-CoA to acetyl-CoA
SABIO-RKⁱ	Q16836

Miscellaneous databases

ChiTaRSⁱ	HADH human
EvolutionaryTraceⁱ	Q16836
GeneWikiⁱ	Hydroxyacyl-Coenzyme_A_dehydrogenase
GenomeRNAiⁱ	3033
Protein Ontology More...PROⁱ	PR:Q16836
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000138796 Expressed in 233 organ(s), highest expression level in parietal pleura
CleanExⁱ	HS_HADH
ExpressionAtlasⁱ	Q16836 baseline and differential
Genevisibleⁱ	Q16836 HS

Family and domain databases

Gene3Dⁱ	1.10.1040.10, 1 hit
InterProⁱ	View protein in InterPro IPR022694 3-OHacyl-CoA_DH IPR006180 3-OHacyl-CoA_DH_CS IPR006176 3-OHacyl-CoA_DH_NAD-bd IPR006108 3HC_DH_C IPR008927 6-PGluconate_DH-like_C_sf IPR013328 6PGD_dom2 IPR036291 NAD(P)-bd_dom_sf
Pfamⁱ	View protein in Pfam PF00725 3HCDH, 1 hit PF02737 3HCDH_N, 1 hit
PIRSFⁱ	PIRSF000105 HCDH, 1 hit
SUPFAMⁱ	SSF48179 SSF48179, 1 hit SSF51735 SSF51735, 1 hit
PROSITEⁱ	View protein in PROSITE PS00067 3HCDH, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HCDH_HUMAN
Accessionⁱ	Q16836Primary (citable) accession number: Q16836 Secondary accession number(s): J3KQ17 , O00324, O00397, O00753, Q4W5B4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	November 2, 2010
	Last modified:	September 12, 2018
	This is version 198 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
PATHWAY comments
Index of metabolic and biosynthesis pathways
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q16836 (HCDH_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid beta-oxidation

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Mitochondrion

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Your basket is currently empty. ⁱ

Functionⁱ

Pathwayⁱ: fatty acid beta-oxidation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ