HMGCLL1

Functionⁱ

Non-mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis, the products of which support energy production in nonhepatic animal tissues.2 Publications

Catalytic activityⁱ

(3S)-hydroxy-3-methylglutaryl-CoA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
acetoacetate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
acetyl-CoA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.5
  "Identification and characterization of an extramitochondrial human 3-Hydroxy-3-methylglutaryl-CoA lyase."
  Montgomery C., Pei Z., Watkins P.A., Miziorko H.M.
  J. Biol. Chem. 287:33227-33236(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
- Ref.6
  "Characterization of a novel HMG-CoA Lyase enzyme with a dual location in endoplasmic reticulum and cytosol."
  Arnedo M., Menao S., Puisac B., Teresa-Rodrigo M.E., Gil-Rodriguez M.C., Lopez-Vinas E., Gomez-Puertas P., Casals N., Casale C.H., Hegardt F.G., Pie J.
  J. Lipid Res. 53:2046-2056(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-86; LEU-237 AND HIS-278.
EC:
4.1.3.4
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.5
  "Identification and characterization of an extramitochondrial human 3-Hydroxy-3-methylglutaryl-CoA lyase."
  Montgomery C., Pei Z., Watkins P.A., Miziorko H.M.
  J. Biol. Chem. 287:33227-33236(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
- Ref.6
  "Characterization of a novel HMG-CoA Lyase enzyme with a dual location in endoplasmic reticulum and cytosol."
  Arnedo M., Menao S., Puisac B., Teresa-Rodrigo M.E., Gil-Rodriguez M.C., Lopez-Vinas E., Gomez-Puertas P., Casals N., Casale C.H., Hegardt F.G., Pie J.
  J. Lipid Res. 53:2046-2056(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-86; LEU-237 AND HIS-278.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
(3S)-hydroxy-3-methylglutaryl-CoA
zoom
=
acetoacetate
zoom
+
acetyl-CoA
zoom

Cofactorⁱ

a divalent metal cation1 Publication

Kineticsⁱ

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:

Hydroxymethylglutaryl-CoA lyase, mitochondrial (HMGCL), 3-hydroxy-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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	86	SubstrateBy similarity	1
Metal bindingⁱ	87	Divalent metal cationBy similarity	1
Metal bindingⁱ	278	Divalent metal cationBy similarity	1
Metal bindingⁱ	280	Divalent metal cationBy similarity	1
Active siteⁱ	311	By similarity	1
Metal bindingⁱ	320	Divalent metal cationBy similarity	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Ligand	Metal-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-77111 Synthesis of Ketone Bodies
SABIO-RKⁱ	Q8TB92
UniPathwayⁱ	UPA00896;UER00863

Chemistry databases

SwissLipidsⁱ	SLP:000001291 [Q8TB92-2]

SwissLipidsⁱ

SLP:000001291 [Q8TB92-2]

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic (EC:4.1.3.42 Publications) Alternative name(s): 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1 Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase1 Publication Short name: er-cHL1 Publication
Gene namesⁱ	Name:HMGCLL1
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 6

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:21359 HMGCLL1
neXtProtⁱ	NX_Q8TB92

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	2	G → A: Abolishes myristoylation and induces a subcellular location change. 1 Publication	1
Mutagenesisⁱ	86	R → Q: Abolishes catalytic activity. 1 Publication	1
Mutagenesisⁱ	237	L → S: Abolishes catalytic activity. 1 Publication	1
Mutagenesisⁱ	278	H → R: Abolishes catalytic activity. 1 Publication	1

Organism-specific databases

Open Targets More...OpenTargetsⁱ	ENSG00000146151
PharmGKBⁱ	PA134989971

Miscellaneous databases

Pharosⁱ	Q8TB92

Pharosⁱ

Q8TB92

Polymorphism and mutation databases

BioMutaⁱ	HMGCLL1
DMDMⁱ	189028466

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed
ChainⁱPRO_0000334669	2 – 370	3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmicAdd BLAST		369

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Lipidationⁱ	2	N-myristoyl glycine1 Publication		1

Keywords - PTMⁱ

Lipoprotein, Myristate

Proteomic databases

jPOSTⁱ	Q8TB92
MassIVEⁱ	Q8TB92
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q8TB92
PaxDbⁱ	Q8TB92
PeptideAtlas More...PeptideAtlasⁱ	Q8TB92
PRIDEⁱ	Q8TB92
ProteomicsDBⁱ	29914 73974 [Q8TB92-1] 73975 [Q8TB92-2] 73976 [Q8TB92-4]

PTM databases

iPTMnetⁱ	Q8TB92
PhosphoSitePlusⁱ	Q8TB92

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000146151 Expressed in 138 organ(s), highest expression level in forebrain
ExpressionAtlasⁱ	Q8TB92 baseline and differential
Genevisibleⁱ	Q8TB92 HS

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	120006, 2 interactors
IntActⁱ	Q8TB92, 2 interactors
STRINGⁱ	9606.ENSP00000381654

Structureⁱ

3D structure databases

SMRⁱ	Q8TB92
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	78 – 345	Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST		268

Sequence similaritiesⁱ

Belongs to the HMG-CoA lyase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG2368 Eukaryota COG0119 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000159467
HOGENOMⁱ	HOG000219757
InParanoidⁱ	Q8TB92
KEGG Orthology (KO) More...KOⁱ	K01640
OMAⁱ	IHEVGAR
Database of Orthologous Groups More...OrthoDBⁱ	1029775at2759
PhylomeDBⁱ	Q8TB92
TreeFamⁱ	TF105363

Family and domain databases

Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR030021 ER-cHL IPR000891 PYR_CT
PANTHERⁱ	PTHR42738:SF5 PTHR42738:SF5, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00682 HMGL-like, 1 hit
PROSITEⁱ	View protein in PROSITE PS50991 PYR_CT, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q8TB92-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MGNVPSAVKH CLSYQQLLRE HLWIGDSVAG ALDPAQTSLL TNLHCFQPDV 
        60         70         80         90        100
SGFSVSLAGT VACIHWETSQ LSGLPEFVKI VEVGPRDGLQ NEKVIVPTDI 
       110        120        130        140        150
KIEFINRLSQ TGLSVIEVTS FVSSRWVPQM ADHTEVMKGI HQYPGVRYPV 
       160        170        180        190        200
LTPNLQGFHH AVAAGATEIS VFGAASESFS KKNINCSIEE SMGKFEEVVK 
       210        220        230        240        250
SARHMNIPAR GYVSCALGCP YEGSITPQKV TEVSKRLYGM GCYEISLGDT 
       260        270        280        290        300
IGVGTPGSMK RMLESVMKEI PPGALAVHCH DTYGQALANI LTALQMGINV 
       310        320        330        340        350
VDSAVSGLGG CPYAKGASGN VATEDLIYML NGLGLNTGVN LYKVMEAGDF 
       360        370
ICKAVNKTTN SKVAQASFNA

Length:370

Mass (Da):39,514

Last modified:May 20, 2008 - v3

Checksum:ⁱ7DDEE81555E092A1

GO

Isoform 2 (identifier: Q8TB92-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
37-66: Missing.

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        10         20         30         40         50
MGNVPSAVKH CLSYQQLLRE HLWIGDSVAG ALDPAQETSQ LSGLPEFVKI 
        60         70         80         90        100
VEVGPRDGLQ NEKVIVPTDI KIEFINRLSQ TGLSVIEVTS FVSSRWVPQM 
       110        120        130        140        150
ADHTEVMKGI HQYPGVRYPV LTPNLQGFHH AVAAGATEIS VFGAASESFS 
       160        170        180        190        200
KKNINCSIEE SMGKFEEVVK SARHMNIPAR GYVSCALGCP YEGSITPQKV 
       210        220        230        240        250
TEVSKRLYGM GCYEISLGDT IGVGTPGSMK RMLESVMKEI PPGALAVHCH 
       260        270        280        290        300
DTYGQALANI LTALQMGINV VDSAVSGLGG CPYAKGASGN VATEDLIYML 
       310        320        330        340
NGLGLNTGVN LYKVMEAGDF ICKAVNKTTN SKVAQASFNA

Show »

Length:340

Mass (Da):36,328

Checksum:ⁱ6F175387821614CC

GO

Isoform 3 (identifier: Q8TB92-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
37-53: TSLLTNLHCFQPDVSGF → ELQSVMLMLHHGPLRKP
54-370: Missing.

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        10         20         30         40         50
MGNVPSAVKH CLSYQQLLRE HLWIGDSVAG ALDPAQELQS VMLMLHHGPL 

RKP

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Show »

Length:53

Mass (Da):5,874

Checksum:ⁱ16F3265215AF8A2A

GO

Isoform 4 (identifier: Q8TB92-5) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
37-66: Missing.
130-161: Missing.

« Hide

        10         20         30         40         50
MGNVPSAVKH CLSYQQLLRE HLWIGDSVAG ALDPAQETSQ LSGLPEFVKI 
        60         70         80         90        100
VEVGPRDGLQ NEKVIVPTDI KIEFINRLSQ TGLSVIEVTS FVSSRWVPQV 
       110        120        130        140        150
AAGATEISVF GAASESFSKK NINCSIEESM GKFEEVVKSA RHMNIPARGY 
       160        170        180        190        200
VSCALGCPYE GSITPQKVTE VSKRLYGMGC YEISLGDTIG VGTPGSMKRM 
       210        220        230        240        250
LESVMKEIPP GALAVHCHDT YGQALANILT ALQMGINVVD SAVSGLGGCP 
       260        270        280        290        300
YAKGASGNVA TEDLIYMLNG LGLNTGVNLY KVMEAGDFIC KAVNKTTNSK 

VAQASFNA

Note: No experimental confirmation available.

Show »

Length:308

Mass (Da):32,701

Checksum:ⁱ49ED9FE7EC8038BB

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

B7Z212	B7Z212_HUMAN	3-hydroxy-3-methylglutaryl-CoA lyas... 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic (cDNA FLJ57919)	HMGCLL1	237	Annotation score:
B7Z4D4	B7Z4D4_HUMAN	3-hydroxy-3-methylglutaryl-CoA lyas... 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic (cDNA FLJ57397)	HMGCLL1	174	Annotation score:
G5E9S9	G5E9S9_HUMAN	3-hydroxy-3-methylglutaryl-CoA lyas... 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic (3-hydroxymethyl-3-methylglutaryl-Coenzyme A lyase-like 1, isoform CRA_d)	HMGCLL1 hCG_2001183	151	Annotation score:
D6RHJ2	D6RHJ2_HUMAN	3-hydroxy-3-methylglutaryl-CoA lyas... 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic	HMGCLL1	39	Annotation score:

Sequence cautionⁱ

The sequence BAC87045 differs from that shown. Reason: Frameshift.Curated

The sequence BAG51462 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	99	D → G in BAH11613 (PubMed:14702039).Curated		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_033752	37 – 66	Missing in isoform 2 and isoform 4. 2 PublicationsAdd BLAST	30
Alternative sequenceⁱVSP_038021	37 – 53	TSLLT…DVSGF → ELQSVMLMLHHGPLRKP in isoform 3. 1 PublicationAdd BLAST	17
Alternative sequenceⁱVSP_038022	54 – 370	Missing in isoform 3. 1 PublicationAdd BLAST	317
Alternative sequenceⁱVSP_044324	130 – 161	Missing in isoform 4. 1 PublicationAdd BLAST	32

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK055075 mRNA Translation: BAG51462.1 Sequence problems. AK127587 mRNA Translation: BAC87045.1 Frameshift. AK293856 mRNA Translation: BAH11613.1 AL590290 Genomic DNA No translation available. AL590406 Genomic DNA No translation available. CH471081 Genomic DNA Translation: EAX04442.1 CH471081 Genomic DNA Translation: EAX04444.1 BC024194 mRNA Translation: AAH24194.2
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS43474.1 [Q8TB92-2] CCDS43475.1 [Q8TB92-1] CCDS75473.1 [Q8TB92-5]
NCBI Reference Sequences More...RefSeqⁱ	NP_001035865.1, NM_001042406.1 [Q8TB92-2] NP_001274670.1, NM_001287741.1 [Q8TB92-5] NP_001274675.1, NM_001287746.1 NP_061909.2, NM_019036.2 [Q8TB92-1]

Genome annotation databases

Ensemblⁱ	ENST00000274901; ENSP00000274901; ENSG00000146151 [Q8TB92-2] ENST00000308161; ENSP00000309737; ENSG00000146151 [Q8TB92-5] ENST00000370852; ENSP00000359889; ENSG00000146151 [Q8TB92-4] ENST00000398661; ENSP00000381654; ENSG00000146151 [Q8TB92-1]
GeneIDⁱ	54511
KEGGⁱ	hsa:54511
UCSC genome browser More...UCSCⁱ	uc003pcn.4 human [Q8TB92-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins	Species	Length	Source
Q8TB92-2	3-hydroxymethyl-3-methylglutaryl-CoA lyase like 1	PANTR	340	UniRef100_A0A2I3RD22
Q8TB92-4	HMGCLL1 isoform 3	PANTR	53	UniRef100_A0A2J8P161
Q8TB92-5	3-hydroxymethyl-3-methylglutaryl-CoA lyase like 1	PANTR	308	UniRef100_A0A2I3RGS7

Protein	Similar proteins		Species	Score	Length	Source
Q8TB92	HMGCLL1 isoform 2		PONAB		370	UniRef90_Q8TB92
3-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmic isoform X1		TARSY		370
3-hydroxymethyl-3-methylglutaryl-CoA lyase like 1		SAIBB		370
Pyruvate carboxyltransferase domain-containing protein		MACMU		370
Pyruvate carboxyltransferase domain-containing protein		MACFA		370
+78
Q8TB92-4	HMGCLL1 isoform 3		PONAB		53	UniRef90_A0A2J8SSP3
HMGCLL1 isoform 3		PANTR		53
Q8TB92-5	Pyruvate carboxyltransferase domain-containing protein		MACMU		308	UniRef90_F7CUT0
Pyruvate carboxyltransferase domain-containing protein		PAPAN		308
Pyruvate carboxyltransferase domain-containing protein		MANLE		308
Pyruvate carboxyltransferase domain-containing protein		MACFA		308
Pyruvate carboxyltransferase domain-containing protein		MACNE		308
+40

Protein	Similar proteins		Species	Score	Length	Source
Q8TB92	3-hydroxymethyl-3-methylglutaryl-CoA lyase like 1		PANTR		370	UniRef50_Q8TB92
3-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmic isoform X1		TARSY		370
Pyruvate carboxyltransferase domain-containing protein		AOTNA		370
Pyruvate carboxyltransferase domain-containing protein		PAPAN		370
Pyruvate carboxyltransferase domain-containing protein		MACMU		370
+178
Q8TB92-4	HMGCLL1 isoform 3		PONAB		53	UniRef50_A0A2J8SSP3
HMGCLL1 isoform 3		PANTR		53
Q8TB92-5	Pyruvate carboxyltransferase domain-containing protein		MACMU		308	UniRef50_F7CUT0
Pyruvate carboxyltransferase domain-containing protein		PAPAN		308
Pyruvate carboxyltransferase domain-containing protein		MANLE		308
Pyruvate carboxyltransferase domain-containing protein		MACFA		308
Pyruvate carboxyltransferase domain-containing protein		MACNE		308
+170

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AK055075 mRNA Translation: BAG51462.1 Sequence problems. AK127587 mRNA Translation: BAC87045.1 Frameshift. AK293856 mRNA Translation: BAH11613.1 AL590290 Genomic DNA No translation available. AL590406 Genomic DNA No translation available. CH471081 Genomic DNA Translation: EAX04442.1 CH471081 Genomic DNA Translation: EAX04444.1 BC024194 mRNA Translation: AAH24194.2
CCDSⁱ	CCDS43474.1 [Q8TB92-2] CCDS43475.1 [Q8TB92-1] CCDS75473.1 [Q8TB92-5]
RefSeqⁱ	NP_001035865.1, NM_001042406.1 [Q8TB92-2] NP_001274670.1, NM_001287741.1 [Q8TB92-5] NP_001274675.1, NM_001287746.1 NP_061909.2, NM_019036.2 [Q8TB92-1]

3D structure databases

SMRⁱ	Q8TB92
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	120006, 2 interactors
IntActⁱ	Q8TB92, 2 interactors
STRINGⁱ	9606.ENSP00000381654

Chemistry databases

SwissLipidsⁱ	SLP:000001291 [Q8TB92-2]

SwissLipidsⁱ

SLP:000001291 [Q8TB92-2]

PTM databases

iPTMnetⁱ	Q8TB92
PhosphoSitePlusⁱ	Q8TB92

Polymorphism and mutation databases

BioMutaⁱ	HMGCLL1
DMDMⁱ	189028466

Proteomic databases

jPOSTⁱ	Q8TB92
MassIVEⁱ	Q8TB92
MaxQBⁱ	Q8TB92
PaxDbⁱ	Q8TB92
PeptideAtlasⁱ	Q8TB92
PRIDEⁱ	Q8TB92
ProteomicsDBⁱ	29914 73974 [Q8TB92-1] 73975 [Q8TB92-2] 73976 [Q8TB92-4]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	54511

DNASUⁱ

54511

Genome annotation databases

Ensemblⁱ	ENST00000274901; ENSP00000274901; ENSG00000146151 [Q8TB92-2] ENST00000308161; ENSP00000309737; ENSG00000146151 [Q8TB92-5] ENST00000370852; ENSP00000359889; ENSG00000146151 [Q8TB92-4] ENST00000398661; ENSP00000381654; ENSG00000146151 [Q8TB92-1]
GeneIDⁱ	54511
KEGGⁱ	hsa:54511
UCSCⁱ	uc003pcn.4 human [Q8TB92-1]

Organism-specific databases

CTDⁱ	54511
GeneCardsⁱ	HMGCLL1
HGNCⁱ	HGNC:21359 HMGCLL1
neXtProtⁱ	NX_Q8TB92
OpenTargetsⁱ	ENSG00000146151
PharmGKBⁱ	PA134989971
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2368 Eukaryota COG0119 LUCA
GeneTreeⁱ	ENSGT00940000159467
HOGENOMⁱ	HOG000219757
InParanoidⁱ	Q8TB92
KOⁱ	K01640
OMAⁱ	IHEVGAR
OrthoDBⁱ	1029775at2759
PhylomeDBⁱ	Q8TB92
TreeFamⁱ	TF105363

Enzyme and pathway databases

UniPathwayⁱ	UPA00896;UER00863
Reactomeⁱ	R-HSA-77111 Synthesis of Ketone Bodies
SABIO-RKⁱ	Q8TB92

Miscellaneous databases

ChiTaRSⁱ	HMGCLL1 human
GenomeRNAiⁱ	54511
Pharosⁱ	Q8TB92
Protein Ontology More...PROⁱ	PR:Q8TB92

Gene expression databases

Bgeeⁱ	ENSG00000146151 Expressed in 138 organ(s), highest expression level in forebrain
ExpressionAtlasⁱ	Q8TB92 baseline and differential
Genevisibleⁱ	Q8TB92 HS

Family and domain databases

Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR030021 ER-cHL IPR000891 PYR_CT
PANTHERⁱ	PTHR42738:SF5 PTHR42738:SF5, 1 hit
Pfamⁱ	View protein in Pfam PF00682 HMGL-like, 1 hit
PROSITEⁱ	View protein in PROSITE PS50991 PYR_CT, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HMGC2_HUMAN
Accessionⁱ	Q8TB92Primary (citable) accession number: Q8TB92 Secondary accession number(s): B1AQ42 , B3KNV0, B7Z1S7, F8W793, Q6ZSA9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
	Last sequence update:	May 20, 2008
	Last modified:	October 16, 2019
	This is version 140 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

Complete proteome, Reference proteome

Documents

Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM
SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways

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Supporting data

UniProtKB - Q8TB92 (HMGC2_HUMAN)

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3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic

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<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 catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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

Sites

<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

Endoplasmic reticulum

Cytosol

Cytosol

Endoplasmic reticulum

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

Mutagenesis

Organism-specific databases

Miscellaneous 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

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

<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

3D structure 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

Domains and Repeats

<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

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

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

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

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

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

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ