Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q16836 - HCDH_HUMAN

UniProt

Q16836 - HCDH_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

Gene

HADH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Lipid metabolism; fatty acid beta-oxidation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571NAD2 Publications
Binding sitei73 – 731Coenzyme A
Binding sitei80 – 801Coenzyme A
Binding sitei122 – 1221NAD2 Publications
Binding sitei127 – 1271NAD2 Publications
Binding sitei149 – 1491Coenzyme A
Binding sitei149 – 1491NAD2 Publications
Sitei170 – 1701Important for catalytic activityCurated
Binding sitei173 – 1731NAD2 Publications
Binding sitei305 – 3051NAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 396NAD2 Publications

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4799. HADH.

Subcellular locationi

Mitochondrion matrix

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

3-alpha-hydroxyacyl-CoA dehydrogenase deficiency1 Publication

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

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

See also OMIM:231530
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 41 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.

See also OMIM:609975
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-succinyllysineBy similarity
Modified residuei81 – 811N6-acetyllysine; alternateBy similarity
Modified residuei81 – 811N6-succinyllysine; alternateBy similarity
Modified residuei87 – 871N6-acetyllysine; alternateBy similarity
Modified residuei87 – 871N6-succinyllysine; alternateBy similarity
Modified residuei125 – 1251N6-acetyllysineBy similarity
Modified residuei136 – 1361N6-acetyllysine; alternateBy similarity
Modified residuei136 – 1361N6-succinyllysine; alternateBy similarity
Modified residuei179 – 1791N6-acetyllysineBy similarity
Modified residuei185 – 1851N6-acetyllysine; alternate1 Publication
Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
Modified residuei192 – 1921N6-acetyllysine; alternateBy similarity
Modified residuei192 – 1921N6-succinyllysine; alternateBy similarity
Modified residuei202 – 2021N6-acetyllysine; alternate1 Publication
Modified residuei202 – 2021N6-succinyllysine; alternateBy similarity
Modified residuei206 – 2061N6-succinyllysineBy similarity
Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity
Modified residuei241 – 2411N6-acetyllysine; alternate1 Publication
Modified residuei241 – 2411N6-succinyllysine; alternateBy similarity
Modified residuei312 – 3121N6-acetyllysine; alternate1 Publication
Modified residuei312 – 3121N6-succinyllysine; alternateBy similarity

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

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

BgeeiQ16836.
CleanExiHS_HADH.
ExpressionAtlasiQ16836. baseline and differential.
GenevestigatoriQ16836.

Organism-specific databases

HPAiHPA039588.
HPA043888.

Interactioni

Subunit structurei

Homodimer.2 Publications

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 – 335Combined sources
Helixi37 – 4812Combined sources
Beta strandi52 – 565Combined sources
Helixi60 – 7920Combined sources
Beta strandi82 – 843Combined sources
Helixi86 – 9813Combined sources
Beta strandi100 – 1045Combined sources
Helixi106 – 1094Combined sources
Helixi110 – 1123Combined sources
Beta strandi114 – 1185Combined sources
Helixi124 – 13411Combined sources
Turni135 – 1373Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi149 – 1513Combined sources
Helixi153 – 1575Combined sources
Helixi163 – 1653Combined sources
Beta strandi166 – 1716Combined sources
Turni175 – 1773Combined sources
Beta strandi180 – 1845Combined sources
Helixi191 – 20313Combined sources
Beta strandi207 – 2115Combined sources
Turni215 – 2184Combined sources
Helixi219 – 23517Combined sources
Helixi241 – 25212Combined sources
Helixi258 – 2658Combined sources
Helixi267 – 27913Combined sources
Turni280 – 2834Combined sources
Helixi285 – 2873Combined sources
Helixi291 – 2988Combined sources
Turni304 – 3074Combined sources
Beta strandi308 – 3125Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16836.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ16836.
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

        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]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

Experimental Info

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

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. 1 PublicationVSP_016551
Alternative sequencei236 – 2361R → RDFQTCGDSNSGLGFSLK in isoform 2 and isoform 3. 1 PublicationVSP_016552

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.
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]
uc010ilx.3. human.

Polymorphism databases

DMDMi311033442.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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.
CCDSiCCDS3678.1. [Q16836-1]
CCDS54790.1. [Q16836-3]
PIRiJC4879.
RefSeqiNP_001171634.2. NM_001184705.2.
NP_005318.3. NM_005327.4.
UniGeneiHs.438289.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ16836.

Polymorphism databases

DMDMi311033442.

2D gel databases

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

Proteomic databases

MaxQBiQ16836.
PaxDbiQ16836.
PRIDEiQ16836.

Protocols and materials databases

DNASUi3033.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309522; ENSP00000312288; ENSG00000138796. [Q16836-1]
ENST00000603302; ENSP00000474560; ENSG00000138796. [Q16836-3]
GeneIDi3033.
KEGGihsa:3033.
UCSCiuc003hyq.3. human. [Q16836-1]
uc010ilx.3. human.

Organism-specific databases

CTDi3033.
GeneCardsiGC04P108910.
GeneReviewsiHADH.
HGNCiHGNC:4799. HADH.
HPAiHPA039588.
HPA043888.
MIMi231530. phenotype.
601609. gene.
609975. phenotype.
neXtProtiNX_Q16836.
Orphaneti71212. Hyperinsulinism due to short chain 3-hydroxylacyl-CoA dehydrogenase deficiency.
PharmGKBiPA29173.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000141498.
HOVERGENiHBG000832.
InParanoidiQ16836.
KOiK00022.
OrthoDBiEOG7K3TMS.
PhylomeDBiQ16836.
TreeFamiTF300886.

Enzyme and pathway databases

UniPathwayiUPA00659.
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.

Miscellaneous databases

ChiTaRSiHADH. human.
EvolutionaryTraceiQ16836.
GeneWikiiHydroxyacyl-Coenzyme_A_dehydrogenase.
GenomeRNAii3033.
NextBioi12006.
PROiQ16836.
SOURCEiSearch...

Gene expression databases

BgeeiQ16836.
CleanExiHS_HADH.
ExpressionAtlasiQ16836. baseline and differential.
GenevestigatoriQ16836.

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]
ProtoNetiSearch...

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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 169 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

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 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.