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Protein

Hydroxymethylglutaryl-CoA lyase, mitochondrial

Gene

HMGCL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key enzyme in ketogenesis (ketone body formation). Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism.3 Publications

Catalytic activityi

(S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate.PROSITE-ProRule annotation2 Publications

Cofactori

a divalent metal cation1 Publication

Enzyme regulationi

Stimulated by reducing agents such as dithiothreitol (DTT).1 Publication

Kineticsi

  1. KM=200 µM for magnesium ion2 Publications
  2. KM=48 µM for HMG-CoA2 Publications
  1. Vmax=191 µmol/min/mg enzyme2 Publications

Pathwayi: (S)-3-hydroxy-3-methylglutaryl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Hydroxymethylglutaryl-CoA lyase, mitochondrial (HMGCL), 3-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmic (HMGCLL1)
This subpathway is part of the pathway (S)-3-hydroxy-3-methylglutaryl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA, the pathway (S)-3-hydroxy-3-methylglutaryl-CoA degradation and in Metabolic intermediate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei41Substrate1
Metal bindingi42Divalent metal cation1
Metal bindingi233Divalent metal cation1
Metal bindingi235Divalent metal cation1
Active sitei266PROSITE-ProRule annotation1
Metal bindingi275Divalent metal cation1

GO - Molecular functioni

  • carboxylic acid binding Source: Ensembl
  • fatty-acyl-CoA binding Source: Ensembl
  • hydroxymethylglutaryl-CoA lyase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • metal ion binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

  • acyl-CoA metabolic process Source: Ensembl
  • ketone body biosynthetic process Source: UniProtKB
  • leucine catabolic process Source: UniProtKB
  • lipid metabolic process Source: BHF-UCL
  • liver development Source: Ensembl
  • mitochondrion organization Source: Ensembl
  • protein tetramerization Source: UniProtKB
  • response to fatty acid Source: Ensembl
  • response to nutrient Source: Ensembl
  • response to starvation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS04116-MONOMER.
ZFISH:HS04116-MONOMER.
BRENDAi4.1.3.4. 2681.
ReactomeiR-HSA-77111. Synthesis of Ketone Bodies.
SABIO-RKP35914.
UniPathwayiUPA00896; UER00863.

Chemistry databases

SwissLipidsiSLP:000001292. [P35914-1]

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxymethylglutaryl-CoA lyase, mitochondrial (EC:4.1.3.4)
Short name:
HL
Short name:
HMG-CoA lyase
Alternative name(s):
3-hydroxy-3-methylglutarate-CoA lyase
Gene namesi
Name:HMGCL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:5005. HMGCL.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Ensembl
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

Pathology & Biotechi

Involvement in diseasei

3-hydroxy-3-methylglutaryl-CoA lyase deficiency (HMGCLD)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disease affecting ketogenesis and L-leucine catabolism. The disease usually appears in the first year of life after a fasting period and its clinical acute symptoms include vomiting, seizures, metabolic acidosis, hypoketotic hypoglycemia and lethargy. These symptoms sometimes progress to coma, with fatal outcome in some cases.
See also OMIM:246450
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05844037E → K in HMGCLD; activity lower than 5% respect to the wild-type. 1 Publication1
Natural variantiVAR_00374441R → Q in HMGCLD; loss of activity and of proton exchange. 2 PublicationsCorresponds to variant rs121964997dbSNPEnsembl.1
Natural variantiVAR_00374542D → E in HMGCLD; reduced activity. 1 Publication1
Natural variantiVAR_00374642D → G in HMGCLD; loss of activity. 2 Publications1
Natural variantiVAR_00374742D → H in HMGCLD; loss of activity. 1 Publication1
Natural variantiVAR_05844148K → N in HMGCLD; abolishes almost all enzymatic activity. 1 Publication1
Natural variantiVAR_00374870V → L in HMGCLD. Corresponds to variant rs121964996dbSNPEnsembl.1
Natural variantiVAR_05844275S → R in HMGCLD. 1 Publication1
Natural variantiVAR_058443142S → F in HMGCLD; activity lower than 5% respect to the wild-type. 1 Publication1
Natural variantiVAR_065453165R → Q in HMGCLD. 1 PublicationCorresponds to variant rs199587895dbSNPEnsembl.1
Natural variantiVAR_058444174C → Y in HMGCLD; activity lower than 5% respect to the wild-type. 1 PublicationCorresponds to variant rs765475941dbSNPEnsembl.1
Natural variantiVAR_058445192F → S in HMGCLD; activity lower than 5% respect to the wild-type. 1 Publication1
Natural variantiVAR_058446200I → F in HMGCLD; activity lower than 5% respect to the wild-type. 1 Publication1
Natural variantiVAR_058447201S → Y in HMGCLD. 1 PublicationCorresponds to variant rs760106433dbSNPEnsembl.1
Natural variantiVAR_058448203G → E in HMGCLD; complete loss of activity. 1 Publication1
Natural variantiVAR_058449204D → N in HMGCLD. 1 Publication1
Natural variantiVAR_003749233H → R in HMGCLD; loss of activity. 3 PublicationsCorresponds to variant rs727503963dbSNPEnsembl.1
Natural variantiVAR_058450263L → P in HMGCLD. 1 Publication1
Natural variantiVAR_014202279E → K in HMGCLD. 1 PublicationCorresponds to variant rs28934894dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi37E → D: Normal activity. 1 Publication1
Mutagenesisi41R → M: Reduced activity, and loss of proton exchange. 1 Publication1
Mutagenesisi42D → A or N: Loss of activity, and reduced proton exchange rate. 2 Publications1
Mutagenesisi72E → A: Loss of activity, and reduced affinity for metal cofactor and substrate. 1 Publication1
Mutagenesisi204D → A: Reduced activity, and reduced affinity for metal cofactor and substrate. 1 Publication1
Mutagenesisi233H → A: Loss of activity, and reduced proton exchange rate. 2 Publications1
Mutagenesisi266C → A: Loss of activity. 1
Mutagenesisi279E → A: Reduced thermal stability, but normal activity. 1 Publication1
Mutagenesisi280D → A: Normal activity. 1 Publication1
Mutagenesisi323C → S: Abolishes interchain homodimerization. Exhibits no DTT stimulated activity. 2 Publications1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3155.
MalaCardsiHMGCL.
MIMi246450. phenotype.
OpenTargetsiENSG00000117305.
Orphaneti20. 3-hydroxy-3-methylglutaric aciduria.
PharmGKBiPA29336.

Polymorphism and mutation databases

BioMutaiHMGCL.
DMDMi24418852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 27MitochondrionAdd BLAST27
ChainiPRO_000001347828 – 325Hydroxymethylglutaryl-CoA lyase, mitochondrialAdd BLAST298

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48N6-acetyllysine; alternateCombined sources1
Modified residuei48N6-succinyllysine; alternateBy similarity1
Modified residuei111N6-acetyllysineBy similarity1
Modified residuei137N6-acetyllysine; alternateBy similarity1
Modified residuei137N6-succinyllysine; alternateBy similarity1
Modified residuei179N6-acetyllysine; alternateBy similarity1
Modified residuei179N6-succinyllysine; alternateBy similarity1
Disulfide bondi323Interchain1 Publication
Modified residuei324N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiP35914.
PaxDbiP35914.
PeptideAtlasiP35914.
PRIDEiP35914.

PTM databases

iPTMnetiP35914.
PhosphoSitePlusiP35914.

Expressioni

Tissue specificityi

Highest expression in liver. Expressed in pancreas, kidney, intestine, testis, fibroblasts and lymphoblasts. Very low expression in brain and skeletal muscle. The relative expression of isoform 2 (at mRNA level) is highest in heart (30%), skeletal muscle (22%), and brain (14%).1 Publication

Gene expression databases

BgeeiENSG00000117305.
CleanExiHS_HMGCL.
ExpressionAtlasiP35914. baseline and differential.
GenevisibleiP35914. HS.

Organism-specific databases

HPAiHPA004727.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Can also form homotetramers.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109398. 22 interactors.
IntActiP35914. 9 interactors.
MINTiMINT-3014127.
STRINGi9606.ENSP00000363614.

Structurei

Secondary structure

1325
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 37Combined sources4
Turni39 – 41Combined sources3
Helixi42 – 45Combined sources4
Helixi53 – 65Combined sources13
Beta strandi69 – 71Combined sources3
Turni79 – 81Combined sources3
Helixi83 – 85Combined sources3
Helixi88 – 94Combined sources7
Helixi110 – 118Combined sources9
Beta strandi122 – 130Combined sources9
Helixi132 – 139Combined sources8
Helixi143 – 159Combined sources17
Beta strandi163 – 169Combined sources7
Turni170 – 172Combined sources3
Turni175 – 177Combined sources3
Helixi182 – 194Combined sources13
Beta strandi198 – 204Combined sources7
Helixi211 – 224Combined sources14
Helixi227 – 229Combined sources3
Beta strandi230 – 235Combined sources6
Helixi241 – 250Combined sources10
Beta strandi255 – 259Combined sources5
Helixi278 – 288Combined sources11
Helixi296 – 309Combined sources14
Helixi317 – 322Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CW6X-ray2.10A/B/C/D/E/F28-325[»]
3MP3X-ray2.40A/B/C/D/E/F28-325[»]
3MP4X-ray2.20A/B/C/D/E/F28-325[»]
3MP5X-ray2.25A/B/C/D/E/F28-325[»]
ProteinModelPortaliP35914.
SMRiP35914.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35914.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 300Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST268

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi323 – 325Microbody targeting signalSequence analysis3

Sequence similaritiesi

Belongs to the HMG-CoA lyase family.Curated
Contains 1 pyruvate carboxyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2368. Eukaryota.
COG0119. LUCA.
GeneTreeiENSGT00390000017690.
HOGENOMiHOG000219757.
HOVERGENiHBG064656.
InParanoidiP35914.
KOiK01640.
OMAiEAFAQKN.
OrthoDBiEOG091G0DA9.
PhylomeDBiP35914.
TreeFamiTF105363.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR030020. HL.
IPR000138. HMG_CoA_lyase_AS.
IPR000891. PYR_CT.
[Graphical view]
PANTHERiPTHR10277:SF35. PTHR10277:SF35. 1 hit.
PfamiPF00682. HMGL-like. 1 hit.
[Graphical view]
PROSITEiPS01062. HMG_COA_LYASE. 1 hit.
PS50991. PYR_CT. 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. AlignAdd to basket

Isoform 1 (identifier: P35914-1) [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
MAAMRKALPR RLVGLASLRA VSTSSMGTLP KRVKIVEVGP RDGLQNEKNI
60 70 80 90 100
VSTPVKIKLI DMLSEAGLSV IETTSFVSPK WVPQMGDHTE VLKGIQKFPG
110 120 130 140 150
INYPVLTPNL KGFEAAVAAG AKEVVIFGAA SELFTKKNIN CSIEESFQRF
160 170 180 190 200
DAILKAAQSA NISVRGYVSC ALGCPYEGKI SPAKVAEVTK KFYSMGCYEI
210 220 230 240 250
SLGDTIGVGT PGIMKDMLSA VMQEVPLAAL AVHCHDTYGQ ALANTLMALQ
260 270 280 290 300
MGVSVVDSSV AGLGGCPYAQ GASGNLATED LVYMLEGLGI HTGVNLQKLL
310 320
EAGNFICQAL NRKTSSKVAQ ATCKL
Length:325
Mass (Da):34,360
Last modified:October 25, 2002 - v2
Checksum:iB82B2488A10D6980
GO
Isoform 2 (identifier: P35914-2) [UniParc]FASTAAdd to basket
Also known as: HMGCS2delta5,6

The sequence of this isoform differs from the canonical sequence as follows:
     117-187: Missing.

Note: The transcript is not translated, but would result in a catalytically impaired product if it was.
Show »
Length:254
Mass (Da):26,910
Checksum:iFAD9D90A1A62F3AD
GO
Isoform 3 (identifier: P35914-3) [UniParc]FASTAAdd to basket
Also known as: HMGCS2delta5,6,7

The sequence of this isoform differs from the canonical sequence as follows:
     117-187: Missing.
     188-250: Missing.

Note: Very low expression. The transcript is not translated, but would result in a catalytically inactive product if it was.
Show »
Length:191
Mass (Da):20,222
Checksum:iD5540BECDB75D854
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti243A → T in AAA92733 (PubMed:8440722).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05844037E → K in HMGCLD; activity lower than 5% respect to the wild-type. 1 Publication1
Natural variantiVAR_00374441R → Q in HMGCLD; loss of activity and of proton exchange. 2 PublicationsCorresponds to variant rs121964997dbSNPEnsembl.1
Natural variantiVAR_00374542D → E in HMGCLD; reduced activity. 1 Publication1
Natural variantiVAR_00374642D → G in HMGCLD; loss of activity. 2 Publications1
Natural variantiVAR_00374742D → H in HMGCLD; loss of activity. 1 Publication1
Natural variantiVAR_05844148K → N in HMGCLD; abolishes almost all enzymatic activity. 1 Publication1
Natural variantiVAR_00374870V → L in HMGCLD. Corresponds to variant rs121964996dbSNPEnsembl.1
Natural variantiVAR_05844275S → R in HMGCLD. 1 Publication1
Natural variantiVAR_058443142S → F in HMGCLD; activity lower than 5% respect to the wild-type. 1 Publication1
Natural variantiVAR_065453165R → Q in HMGCLD. 1 PublicationCorresponds to variant rs199587895dbSNPEnsembl.1
Natural variantiVAR_058444174C → Y in HMGCLD; activity lower than 5% respect to the wild-type. 1 PublicationCorresponds to variant rs765475941dbSNPEnsembl.1
Natural variantiVAR_058445192F → S in HMGCLD; activity lower than 5% respect to the wild-type. 1 Publication1
Natural variantiVAR_058446200I → F in HMGCLD; activity lower than 5% respect to the wild-type. 1 Publication1
Natural variantiVAR_058447201S → Y in HMGCLD. 1 PublicationCorresponds to variant rs760106433dbSNPEnsembl.1
Natural variantiVAR_058448203G → E in HMGCLD; complete loss of activity. 1 Publication1
Natural variantiVAR_058449204D → N in HMGCLD. 1 Publication1
Natural variantiVAR_003749233H → R in HMGCLD; loss of activity. 3 PublicationsCorresponds to variant rs727503963dbSNPEnsembl.1
Natural variantiVAR_058450263L → P in HMGCLD. 1 Publication1
Natural variantiVAR_014202279E → K in HMGCLD. 1 PublicationCorresponds to variant rs28934894dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_047444117 – 187Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST71
Alternative sequenceiVSP_043788188 – 250Missing in isoform 3. 1 PublicationAdd BLAST63

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07033 mRNA. Translation: AAA92733.1.
AK300733 mRNA. Translation: BAG62406.1.
AK313869 mRNA. Translation: BAG36597.1.
BT009792 mRNA. Translation: AAP88794.1.
CR456884 mRNA. Translation: CAG33165.1.
AL031295 Genomic DNA. No translation available.
AL590728 Genomic DNA. No translation available.
CH471134 Genomic DNA. Translation: EAW95094.1.
BC010570 mRNA. Translation: AAH10570.1.
AH003700 Genomic DNA. Translation: AAB19099.1.
FJ472654 mRNA. Translation: ACK58684.1.
GU433941 mRNA. Translation: ADD21697.1.
CCDSiCCDS243.1. [P35914-1]
CCDS53279.1. [P35914-2]
PIRiA45470.
RefSeqiNP_000182.2. NM_000191.2. [P35914-1]
NP_001159531.1. NM_001166059.1. [P35914-2]
UniGeneiHs.533444.

Genome annotation databases

EnsembliENST00000374490; ENSP00000363614; ENSG00000117305. [P35914-1]
ENST00000436439; ENSP00000389281; ENSG00000117305. [P35914-2]
GeneIDi3155.
KEGGihsa:3155.
UCSCiuc001bib.4. human. [P35914-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07033 mRNA. Translation: AAA92733.1.
AK300733 mRNA. Translation: BAG62406.1.
AK313869 mRNA. Translation: BAG36597.1.
BT009792 mRNA. Translation: AAP88794.1.
CR456884 mRNA. Translation: CAG33165.1.
AL031295 Genomic DNA. No translation available.
AL590728 Genomic DNA. No translation available.
CH471134 Genomic DNA. Translation: EAW95094.1.
BC010570 mRNA. Translation: AAH10570.1.
AH003700 Genomic DNA. Translation: AAB19099.1.
FJ472654 mRNA. Translation: ACK58684.1.
GU433941 mRNA. Translation: ADD21697.1.
CCDSiCCDS243.1. [P35914-1]
CCDS53279.1. [P35914-2]
PIRiA45470.
RefSeqiNP_000182.2. NM_000191.2. [P35914-1]
NP_001159531.1. NM_001166059.1. [P35914-2]
UniGeneiHs.533444.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CW6X-ray2.10A/B/C/D/E/F28-325[»]
3MP3X-ray2.40A/B/C/D/E/F28-325[»]
3MP4X-ray2.20A/B/C/D/E/F28-325[»]
3MP5X-ray2.25A/B/C/D/E/F28-325[»]
ProteinModelPortaliP35914.
SMRiP35914.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109398. 22 interactors.
IntActiP35914. 9 interactors.
MINTiMINT-3014127.
STRINGi9606.ENSP00000363614.

Chemistry databases

SwissLipidsiSLP:000001292. [P35914-1]

PTM databases

iPTMnetiP35914.
PhosphoSitePlusiP35914.

Polymorphism and mutation databases

BioMutaiHMGCL.
DMDMi24418852.

Proteomic databases

EPDiP35914.
PaxDbiP35914.
PeptideAtlasiP35914.
PRIDEiP35914.

Protocols and materials databases

DNASUi3155.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374490; ENSP00000363614; ENSG00000117305. [P35914-1]
ENST00000436439; ENSP00000389281; ENSG00000117305. [P35914-2]
GeneIDi3155.
KEGGihsa:3155.
UCSCiuc001bib.4. human. [P35914-1]

Organism-specific databases

CTDi3155.
DisGeNETi3155.
GeneCardsiHMGCL.
HGNCiHGNC:5005. HMGCL.
HPAiHPA004727.
MalaCardsiHMGCL.
MIMi246450. phenotype.
613898. gene.
neXtProtiNX_P35914.
OpenTargetsiENSG00000117305.
Orphaneti20. 3-hydroxy-3-methylglutaric aciduria.
PharmGKBiPA29336.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2368. Eukaryota.
COG0119. LUCA.
GeneTreeiENSGT00390000017690.
HOGENOMiHOG000219757.
HOVERGENiHBG064656.
InParanoidiP35914.
KOiK01640.
OMAiEAFAQKN.
OrthoDBiEOG091G0DA9.
PhylomeDBiP35914.
TreeFamiTF105363.

Enzyme and pathway databases

UniPathwayiUPA00896; UER00863.
BioCyciMetaCyc:HS04116-MONOMER.
ZFISH:HS04116-MONOMER.
BRENDAi4.1.3.4. 2681.
ReactomeiR-HSA-77111. Synthesis of Ketone Bodies.
SABIO-RKP35914.

Miscellaneous databases

ChiTaRSiHMGCL. human.
EvolutionaryTraceiP35914.
GenomeRNAii3155.
PROiP35914.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117305.
CleanExiHS_HMGCL.
ExpressionAtlasiP35914. baseline and differential.
GenevisibleiP35914. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR030020. HL.
IPR000138. HMG_CoA_lyase_AS.
IPR000891. PYR_CT.
[Graphical view]
PANTHERiPTHR10277:SF35. PTHR10277:SF35. 1 hit.
PfamiPF00682. HMGL-like. 1 hit.
[Graphical view]
PROSITEiPS01062. HMG_COA_LYASE. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHMGCL_HUMAN
AccessioniPrimary (citable) accession number: P35914
Secondary accession number(s): B4DUP4
, B7UCC6, D3Y5K7, Q6IBC0, Q96FP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 25, 2002
Last modified: November 2, 2016
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

Similar proteinsi

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