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Q16836

- HCDH_HUMAN

UniProt

Q16836 - HCDH_HUMAN

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Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NAD
Binding sitei73 – 731Coenzyme A
Binding sitei80 – 801Coenzyme A
Binding sitei122 – 1221NAD
Binding sitei127 – 1271NAD
Binding sitei149 – 1491Coenzyme A
Binding sitei149 – 1491NAD
Sitei170 – 1701Important for catalytic activity Inferred
Binding sitei173 – 1731NAD
Binding sitei305 – 3051NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 396NAD

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: Reactome
  2. NAD+ binding Source: InterPro

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. fatty acid beta-oxidation Source: Reactome
  3. negative regulation of insulin secretion Source: Ensembl
  4. response to activity Source: Ensembl
  5. response to drug Source: Ensembl
  6. response to insulin Source: Ensembl
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS06563-MONOMER.
ReactomeiREACT_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_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
SABIO-RKQ16836.
UniPathwayiUPA00659.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4799. HADH.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. mitochondrial inner membrane Source: Ensembl
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: HPA
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

3-alpha-hydroxyacyl-CoA dehydrogenase deficiency (HADH deficiency) [MIM:231530]: A metabolic disorder with various clinical presentations including hypoglycemia, hepatoencephalopathy, myopathy or cardiomyopathy, and in some cases sudden death.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401A → T in HADH deficiency. 1 Publication
VAR_024079
Natural varianti57 – 571D → E in HADH deficiency. 1 Publication
VAR_024080
Familial hyperinsulinemic hypoglycemia 4 (HHF4) [MIM:609975]: Most 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti258 – 2581P → L in HHF4; loss of activity. 1 Publication
VAR_024081

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi231530. phenotype.
609975. phenotype.
Orphaneti71212. Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency.
PharmGKBiPA29173.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1212MitochondrionAdd
BLAST
Chaini13 – 314302Hydroxyacyl-coenzyme A dehydrogenase, mitochondrialPRO_0000007406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801N6-succinyllysine By similarity
Modified residuei81 – 811N6-acetyllysine; alternate By similarity
Modified residuei81 – 811N6-succinyllysine; alternate By similarity
Modified residuei87 – 871N6-acetyllysine; alternate By similarity
Modified residuei87 – 871N6-succinyllysine; alternate By similarity
Modified residuei125 – 1251N6-acetyllysine By similarity
Modified residuei136 – 1361N6-acetyllysine; alternate By similarity
Modified residuei136 – 1361N6-succinyllysine; alternate By similarity
Modified residuei179 – 1791N6-acetyllysine By similarity
Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
Modified residuei185 – 1851N6-succinyllysine; alternate By similarity
Modified residuei192 – 1921N6-acetyllysine; alternate By similarity
Modified residuei192 – 1921N6-succinyllysine; alternate By similarity
Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
Modified residuei202 – 2021N6-succinyllysine; alternate By similarity
Modified residuei206 – 2061N6-succinyllysine By similarity
Modified residuei212 – 2121N6-acetyllysine; alternate By similarity
Modified residuei212 – 2121N6-succinyllysine; alternate By similarity
Modified residuei241 – 2411N6-acetyllysine; alternate1 Publication
Modified residuei241 – 2411N6-succinyllysine; alternate By similarity
Modified residuei312 – 3121N6-acetyllysine; alternate1 Publication
Modified residuei312 – 3121N6-succinyllysine; alternate By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ16836.
PaxDbiQ16836.
PRIDEiQ16836.

2D gel databases

REPRODUCTION-2DPAGEIPI00298406.
UCD-2DPAGEO00324.
Q16836.

PTM databases

PhosphoSiteiQ16836.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ16836.
BgeeiQ16836.
CleanExiHS_HADH.
GenevestigatoriQ16836.

Organism-specific databases

HPAiHPA039588.
HPA043888.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi109283. 7 interactions.
IntActiQ16836. 3 interactions.
MINTiMINT-5004681.
STRINGi9606.ENSP00000312288.

Structurei

Secondary structure

1
314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 335
Helixi37 – 4812
Beta strandi52 – 565
Helixi60 – 7920
Beta strandi82 – 843
Helixi86 – 9813
Beta strandi100 – 1045
Helixi106 – 1094
Helixi110 – 1123
Beta strandi114 – 1185
Helixi124 – 13411
Turni135 – 1373
Beta strandi143 – 1464
Beta strandi149 – 1513
Helixi153 – 1575
Helixi163 – 1653
Beta strandi166 – 1716
Turni175 – 1773
Beta strandi180 – 1845
Helixi191 – 20313
Beta strandi207 – 2115
Turni215 – 2184
Helixi219 – 23517
Helixi241 – 25212
Helixi258 – 2658
Helixi267 – 27913
Turni280 – 2834
Helixi285 – 2873
Helixi291 – 2988
Turni304 – 3074
Beta strandi308 – 3125

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F0YX-ray1.80A/B13-314[»]
1F12X-ray2.40A/B13-314[»]
1F14X-ray2.30A/B13-314[»]
1F17X-ray2.30A/B13-314[»]
1IL0X-ray2.20A/B13-314[»]
1LSJX-ray2.50A/B13-314[»]
1LSOX-ray2.60A/B13-314[»]
1M75X-ray2.30A/B13-314[»]
1M76X-ray2.15A/B13-314[»]
2HDHX-ray2.20A/B24-314[»]
3HADX-ray2.00A/B13-314[»]
3RQSX-ray2.00A/B1-314[»]
ProteinModelPortaliQ16836.
SMRiQ16836. Positions 1-314.

Miscellaneous databases

EvolutionaryTraceiQ16836.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
KOiK00022.
OrthoDBiEOG7K3TMS.
PhylomeDBiQ16836.
TreeFamiTF300886.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR022694. 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_C-like.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000105. HCDH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

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

Isoform 1 (identifier: Q16836-1) [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

MAFVTRQFMR SVSSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG    50
HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI 100
ATSTDAASVV HSTDLVVEAI VENLKVKNEL FKRLDKFAAE HTIFASNTSS 150
LQITSIANAT TRQDRFAGLH FFNPVPVMKL VEVIKTPMTS QKTFESLVDF 200
SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERGDAS KEDIDTAMKL 250
GAGYPMGPFE LLDYVGLDTT KFIVDGWHEM DAENPLHQPS PSLNKLVAEN 300
KFGKKTGEGF YKYK 314
Length:314
Mass (Da):34,294
Last modified:November 2, 2010 - v3
Checksum:i0C6F7C01BBCE646A
GO
Isoform 2 (identifier: Q16836-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:390
Mass (Da):42,140
Checksum:i3C20D80AAC4EB142
GO
Isoform 3 (identifier: Q16836-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:331
Mass (Da):36,051
Checksum:i11B5646AD077A666
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401A → T in HADH deficiency. 1 Publication
VAR_024079
Natural varianti57 – 571D → E in HADH deficiency. 1 Publication
VAR_024080
Natural varianti86 – 861L → P.4 Publications
Corresponds to variant rs4956145 [ dbSNP | Ensembl ].
VAR_026764
Natural varianti152 – 1521Q → H.1 Publication
Corresponds to variant rs1051519 [ dbSNP | Ensembl ].
VAR_055701
Natural varianti258 – 2581P → L in HHF4; loss of activity. 1 Publication
VAR_024081

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGRAGLEAPPPPCGVTGTPG ARGLQGRVGPRPQSLAFRGC LPRASSLPGSPRCRRRCHTM in isoform 2. VSP_016551
Alternative sequencei236 – 2361R → RDFQTCGDSNSGLGFSLK in isoform 2 and isoform 3. VSP_016552

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: Q16836-2)
Sequence conflicti41 – 411L → P in AAB58153. 1 Publication
Sequence conflicti56 – 561R → H in AAB58153. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS3678.1. [Q16836-1]
CCDS54790.1. [Q16836-3]
PIRiJC4879.
RefSeqiNP_001171634.2. NM_001184705.2.
NP_005318.3. NM_005327.4.
UniGeneiHs.438289.

Genome annotation databases

EnsembliENST00000309522; ENSP00000312288; ENSG00000138796. [Q16836-1]
ENST00000603302; ENSP00000474560; ENSG00000138796. [Q16836-3]
GeneIDi3033.
KEGGihsa:3033.
UCSCiuc003hyq.3. human. [Q16836-1]

Polymorphism databases

DMDMi311033442.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109283. 7 interactions.
IntActi Q16836. 3 interactions.
MINTi MINT-5004681.
STRINGi 9606.ENSP00000312288.

Chemistry

DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei Q16836.

Polymorphism databases

DMDMi 311033442.

2D gel databases

REPRODUCTION-2DPAGE IPI00298406.
UCD-2DPAGE O00324.
Q16836.

Proteomic databases

MaxQBi Q16836.
PaxDbi Q16836.
PRIDEi Q16836.

Protocols and materials databases

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.3. human. [Q16836-1 ]

Organism-specific databases

CTDi 3033.
GeneCardsi GC04P108910.
GeneReviewsi HADH.
HGNCi HGNC:4799. HADH.
HPAi HPA039588.
HPA043888.
MIMi 231530. phenotype.
601609. gene.
609975. phenotype.
neXtProti NX_Q16836.
Orphaneti 71212. Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency.
PharmGKBi PA29173.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000141498.
HOVERGENi HBG000832.
KOi K00022.
OrthoDBi EOG7K3TMS.
PhylomeDBi Q16836.
TreeFami TF300886.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci MetaCyc:HS06563-MONOMER.
Reactomei 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_419. Beta oxidation of butanoyl-CoA to acetyl-CoA.
REACT_735. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
SABIO-RK Q16836.

Miscellaneous databases

ChiTaRSi HADH. human.
EvolutionaryTracei Q16836.
GeneWikii Hydroxyacyl-Coenzyme_A_dehydrogenase.
GenomeRNAii 3033.
NextBioi 12006.
PROi Q16836.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16836.
Bgeei Q16836.
CleanExi HS_HADH.
Genevestigatori Q16836.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProi 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_C-like.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000105. HCDH. 1 hit.
SUPFAMi SSF48179. SSF48179. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence."
    Vredendaal P.J.C.M., van den Berg I.E.T., Malingre H.E.M., Stroobants A.K., Oldeweghuis D.E.M., Berger R.
    Biochem. Biophys. Res. Commun. 223:718-723(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS PRO-86 AND HIS-152.
    Tissue: Liver.
  2. "Cloning of a L-3-hydroxyacyl CoA dehydrogenase that binds to GLUT4 glucose transporter cytoplasmic C-terminus: possible crosstalk between glucose transport and fatty acid metabolism."
    Shi Y., Samuel S.J., Lee W., Yu C.H., Zhang W., Lachaal M., Jung C.Y.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 7-314 (ISOFORM 1), VARIANT PRO-86.
    Tissue: Skeletal muscle.
  3. "Human short chain L-3-hydroxyacyl-CoA dehydrogenase."
    O'Brien L.K., Sims H.F., Strauss A.W.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-86.
  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. "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), VARIANT PRO-86.
    Tissue: Lung.
  6. "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-185; LYS-202; LYS-241 AND LYS-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism."
    Barycki J.J., O'Brien L.K., Bratt J.M., Zhang R., Sanishvili R., Strauss A.W., Banaszak L.J.
    Biochemistry 38:5786-5798(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
  9. "Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase."
    Barycki J.J., O'Brien L.K., Strauss A.W., Banaszak L.J.
    J. Biol. Chem. 275:27186-27196(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314 IN COMPLEX WITH SUBSTRATE AND NAD.
  10. "3-hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease."
    Yang S.-Y., He X.-Y., Schulz H.
    FEBS J. 272:4874-4883(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. "Fulminant hepatic failure associated with mutations in the medium and short chain L-3-hydroxyacyl-CoA dehydrogenase gene."
    O'Brien L.K., Rinaldo P., Sims H.F., Alonso E.M., Charrow J., Jones P.M., Bennett M.J., Barycki J.J., Banaszak L.J., Strauss A.W.
    J. Inherit. Metab. Dis. 23 Suppl. 1:127-127(2000)
    Cited for: VARIANTS HADH DEFICIENCY THR-40 AND GLU-57.
  12. "Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion."
    Clayton P.T., Eaton S., Aynsley-Green A., Edginton M., Hussain K., Krywawych S., Datta V., Malingre H.E.M., Berger R., van den Berg I.E.T.
    J. Clin. Invest. 108:457-465(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HHF4 LEU-258, CHARACTERIZATION OF VARIANT HHF4 LEU-258.

Entry informationi

Entry nameiHCDH_HUMAN
AccessioniPrimary (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 3, 2014
This is version 164 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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