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Protein

Hydroxymethylglutaryl-CoA synthase, mitochondrial

Gene

HMGCS2

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

Functioni

This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.

Catalytic activityi

Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801Substrate
Active sitei132 – 1321Proton donor/acceptor1 Publication
Active sitei166 – 1661Acyl-thioester intermediatePROSITE-ProRule annotation1 Publication
Binding sitei204 – 2041Substrate
Binding sitei258 – 2581Substrate
Active sitei301 – 3011Proton donor/acceptor1 Publication
Binding sitei380 – 3801Substrate

GO - Molecular functioni

  1. hydroxymethylglutaryl-CoA synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular ketone body metabolic process Source: Reactome
  2. cellular lipid metabolic process Source: Reactome
  3. cholesterol biosynthetic process Source: UniProtKB-KW
  4. isoprenoid biosynthetic process Source: InterPro
  5. ketone body biosynthetic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS05836-MONOMER.
BRENDAi2.3.3.10. 2681.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_1464. Synthesis of Ketone Bodies.
UniPathwayiUPA00058; UER00102.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxymethylglutaryl-CoA synthase, mitochondrial (EC:2.3.3.10)
Short name:
HMG-CoA synthase
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene namesi
Name:HMGCS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:5008. HMGCS2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Ensembl
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

HMG-CoA synthase deficiency (HMGCS deficiency)3 Publications

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

Disease descriptionAffected individuals present with severe hypoketotic hypoglycemia, mild hepatomegaly, or fatty liver, and a nondiagnostic pattern of urinary organic acids with increase of medium and short chain dicarboxylic acids.

See also OMIM:605911
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541V → M in HMGCS deficiency. 1 Publication
Corresponds to variant rs28937320 [ dbSNP | Ensembl ].
VAR_032757
Natural varianti167 – 1671Y → C in HMGCS deficiency. 1 Publication
VAR_032758
Natural varianti174 – 1741F → L in HMGCS deficiency; reduced peptide level; no enzymatic activity. 1 Publication
VAR_032711
Natural varianti212 – 2121G → R in HMGCS deficiency. 1 Publication
VAR_032759
Natural varianti500 – 5001R → H in HMGCS deficiency. 1 Publication
VAR_032760

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi605911. phenotype.
Orphaneti35701. 3-hydroxy-3-methylglutaryl-CoA synthase deficiency.
PharmGKBiPA29338.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionCuratedAdd
BLAST
Chaini38 – 508471Hydroxymethylglutaryl-CoA synthase, mitochondrialPRO_0000013483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521N6-succinyllysineBy similarity
Modified residuei83 – 831N6-acetyllysine; alternateBy similarity
Modified residuei83 – 831N6-succinyllysine; alternateBy similarity
Modified residuei221 – 2211N6-succinyllysineBy similarity
Modified residuei243 – 2431N6-acetyllysineBy similarity
Modified residuei256 – 2561N6-acetyllysine; alternateBy similarity
Modified residuei256 – 2561N6-succinyllysine; alternateBy similarity
Modified residuei306 – 3061N6-acetyllysineBy similarity
Modified residuei310 – 3101N6-acetyllysine; alternateBy similarity
Modified residuei310 – 3101N6-succinyllysine; alternateBy similarity
Modified residuei333 – 3331N6-succinyllysineBy similarity
Modified residuei342 – 3421N6-acetyllysine; alternateBy similarity
Modified residuei342 – 3421N6-succinyllysine; alternateBy similarity
Modified residuei350 – 3501N6-acetyllysine; alternateBy similarity
Modified residuei350 – 3501N6-succinyllysine; alternateBy similarity
Modified residuei354 – 3541N6-acetyllysine; alternateBy similarity
Modified residuei354 – 3541N6-succinyllysine; alternateBy similarity
Modified residuei358 – 3581N6-acetyllysine; alternateBy similarity
Modified residuei358 – 3581N6-succinyllysine; alternateBy similarity
Modified residuei433 – 4331Phosphoserine1 Publication
Modified residuei437 – 4371N6-acetyllysineBy similarity
Modified residuei440 – 4401Phosphoserine1 Publication
Modified residuei447 – 4471N6-acetyllysine; alternateBy similarity
Modified residuei447 – 4471N6-succinyllysine; alternateBy similarity
Modified residuei473 – 4731N6-acetyllysine; alternateBy similarity
Modified residuei473 – 4731N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP54868.
PaxDbiP54868.
PeptideAtlasiP54868.
PRIDEiP54868.

2D gel databases

REPRODUCTION-2DPAGEIPI00008934.

PTM databases

PhosphoSiteiP54868.

Expressioni

Tissue specificityi

Expression in liver is 200-fold higher than in any other tissue. Low expression in colon, kidney, testis, and pancreas. Very low expression in heart and skeletal muscle. Not detected in brain. The relative expression of isoform 3 (at mRNA level) is highest in heart (70%) and skeletal muscle (60%).3 Publications

Gene expression databases

BgeeiP54868.
CleanExiHS_HMGCS2.
GenevestigatoriP54868.

Organism-specific databases

HPAiCAB032906.
HPA027423.
HPA027442.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi109401. 3 interactions.
IntActiP54868. 1 interaction.
STRINGi9606.ENSP00000358414.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi55 – 628Combined sources
Beta strandi65 – 695Combined sources
Helixi70 – 767Combined sources
Helixi83 – 886Combined sources
Beta strandi92 – 943Combined sources
Helixi102 – 11716Combined sources
Helixi121 – 1233Combined sources
Beta strandi124 – 1307Combined sources
Beta strandi137 – 1393Combined sources
Helixi141 – 1455Combined sources
Helixi146 – 1483Combined sources
Helixi150 – 1523Combined sources
Beta strandi161 – 1644Combined sources
Helixi165 – 1673Combined sources
Helixi168 – 18013Combined sources
Beta strandi189 – 19810Combined sources
Helixi206 – 2083Combined sources
Beta strandi210 – 22112Combined sources
Beta strandi223 – 2264Combined sources
Beta strandi232 – 2354Combined sources
Beta strandi240 – 2423Combined sources
Helixi255 – 28329Combined sources
Helixi292 – 2943Combined sources
Beta strandi296 – 3005Combined sources
Helixi305 – 32218Combined sources
Helixi325 – 3317Combined sources
Helixi333 – 3386Combined sources
Helixi343 – 3475Combined sources
Helixi350 – 36718Combined sources
Helixi369 – 3724Combined sources
Helixi373 – 3786Combined sources
Helixi382 – 3843Combined sources
Helixi385 – 39612Combined sources
Helixi399 – 4024Combined sources
Beta strandi406 – 4138Combined sources
Turni414 – 4163Combined sources
Beta strandi417 – 4259Combined sources
Helixi434 – 4407Combined sources
Turni441 – 4444Combined sources
Helixi445 – 4506Combined sources
Beta strandi452 – 4554Combined sources
Helixi457 – 47014Combined sources
Helixi482 – 4843Combined sources
Beta strandi490 – 4956Combined sources
Beta strandi501 – 5055Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WYAX-ray1.70A/B/C/D51-508[»]
ProteinModelPortaliP54868.
SMRiP54868. Positions 51-508.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54868.

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3425.
GeneTreeiENSGT00390000006096.
HOGENOMiHOG000012351.
HOVERGENiHBG051912.
InParanoidiP54868.
KOiK01641.
OMAiRIQLPWD.
OrthoDBiEOG741Z1W.
PhylomeDBiP54868.
TreeFamiTF105361.

Family and domain databases

Gene3Di3.40.47.10. 1 hit.
InterProiIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 3 hits.
TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEiPS01226. HMG_COA_SYNTHASE. 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: P54868-1) [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
MQRLLTPVKR ILQLTRAVQE TSLTPARLLP VAHQRFSTAS AVPLAKTDTW
60 70 80 90 100
PKDVGILALE VYFPAQYVDQ TDLEKYNNVE AGKYTVGLGQ TRMGFCSVQE
110 120 130 140 150
DINSLCLTVV QRLMERIQLP WDSVGRLEVG TETIIDKSKA VKTVLMELFQ
160 170 180 190 200
DSGNTDIEGI DTTNACYGGT ASLFNAANWM ESSSWDGRYA MVVCGDIAVY
210 220 230 240 250
PSGNARPTGG AGAVAMLIGP KAPLALERGL RGTHMENVYD FYKPNLASEY
260 270 280 290 300
PIVDGKLSIQ CYLRALDRCY TSYRKKIQNQ WKQAGSDRPF TLDDLQYMIF
310 320 330 340 350
HTPFCKMVQK SLARLMFNDF LSASSDTQTS LYKGLEAFGG LKLEDTYTNK
360 370 380 390 400
DLDKALLKAS QDMFDKKTKA SLYLSTHNGN MYTSSLYGCL ASLLSHHSAQ
410 420 430 440 450
ELAGSRIGAF SYGSGLAASF FSFRVSQDAA PGSPLDKLVS STSDLPKRLA
460 470 480 490 500
SRKCVSPEEF TEIMNQREQF YHKVNFSPPG DTNSLFPGTW YLERVDEQHR

RKYARRPV
Length:508
Mass (Da):56,635
Last modified:September 30, 1996 - v1
Checksum:iBD362D631F7C3C80
GO
Isoform 2 (identifier: P54868-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     187-228: Missing.

Note: No experimental confirmation available.

Show »
Length:466
Mass (Da):52,482
Checksum:i9D3C527559B74618
GO
Isoform 3 (identifier: P54868-3) [UniParc]FASTAAdd to basket

Also known as: HMGCS2delta4

The sequence of this isoform differs from the canonical sequence as follows:
     229-283: Missing.

Show »
Length:453
Mass (Da):50,050
Checksum:i80C1D1EBB7403EC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341H → Y in CAG33131 (Ref. 3) Curated
Sequence conflicti385 – 3851S → T in CAG33131 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541V → M in HMGCS deficiency. 1 Publication
Corresponds to variant rs28937320 [ dbSNP | Ensembl ].
VAR_032757
Natural varianti167 – 1671Y → C in HMGCS deficiency. 1 Publication
VAR_032758
Natural varianti174 – 1741F → L in HMGCS deficiency; reduced peptide level; no enzymatic activity. 1 Publication
VAR_032711
Natural varianti212 – 2121G → R in HMGCS deficiency. 1 Publication
VAR_032759
Natural varianti500 – 5001R → H in HMGCS deficiency. 1 Publication
VAR_032760

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei187 – 22842Missing in isoform 2. 1 PublicationVSP_042892Add
BLAST
Alternative sequencei229 – 28355Missing in isoform 3. 1 PublicationVSP_047445Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83618 mRNA. Translation: CAA58593.1.
U81859
, U81851, U81852, U81853, U81854, U81855, U81856, U81857, U81858 Genomic DNA. Translation: AAB72036.1.
CR456850 mRNA. Translation: CAG33131.1.
AK303777 mRNA. Translation: BAH14049.1.
AL589734 Genomic DNA. Translation: CAI22408.1.
CH471122 Genomic DNA. Translation: EAW56709.1.
BC044217 mRNA. Translation: AAH44217.1.
U12788 mRNA. Translation: AAA92673.1.
U12789 mRNA. Translation: AAA92674.1.
GU433940 mRNA. Translation: ADD21696.1.
CCDSiCCDS53353.1. [P54868-2]
CCDS905.1. [P54868-1]
PIRiS71623.
RefSeqiNP_001159579.1. NM_001166107.1. [P54868-2]
NP_005509.1. NM_005518.3. [P54868-1]
UniGeneiHs.59889.

Genome annotation databases

EnsembliENST00000369406; ENSP00000358414; ENSG00000134240. [P54868-1]
ENST00000544913; ENSP00000439495; ENSG00000134240. [P54868-2]
GeneIDi3158.
KEGGihsa:3158.
UCSCiuc001eid.3. human. [P54868-1]
uc010oxj.2. human. [P54868-2]

Polymorphism databases

DMDMi1708234.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83618 mRNA. Translation: CAA58593.1.
U81859
, U81851, U81852, U81853, U81854, U81855, U81856, U81857, U81858 Genomic DNA. Translation: AAB72036.1.
CR456850 mRNA. Translation: CAG33131.1.
AK303777 mRNA. Translation: BAH14049.1.
AL589734 Genomic DNA. Translation: CAI22408.1.
CH471122 Genomic DNA. Translation: EAW56709.1.
BC044217 mRNA. Translation: AAH44217.1.
U12788 mRNA. Translation: AAA92673.1.
U12789 mRNA. Translation: AAA92674.1.
GU433940 mRNA. Translation: ADD21696.1.
CCDSiCCDS53353.1. [P54868-2]
CCDS905.1. [P54868-1]
PIRiS71623.
RefSeqiNP_001159579.1. NM_001166107.1. [P54868-2]
NP_005509.1. NM_005518.3. [P54868-1]
UniGeneiHs.59889.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WYAX-ray1.70A/B/C/D51-508[»]
ProteinModelPortaliP54868.
SMRiP54868. Positions 51-508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109401. 3 interactions.
IntActiP54868. 1 interaction.
STRINGi9606.ENSP00000358414.

PTM databases

PhosphoSiteiP54868.

Polymorphism databases

DMDMi1708234.

2D gel databases

REPRODUCTION-2DPAGEIPI00008934.

Proteomic databases

MaxQBiP54868.
PaxDbiP54868.
PeptideAtlasiP54868.
PRIDEiP54868.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369406; ENSP00000358414; ENSG00000134240. [P54868-1]
ENST00000544913; ENSP00000439495; ENSG00000134240. [P54868-2]
GeneIDi3158.
KEGGihsa:3158.
UCSCiuc001eid.3. human. [P54868-1]
uc010oxj.2. human. [P54868-2]

Organism-specific databases

CTDi3158.
GeneCardsiGC01M120290.
H-InvDBHIX0160007.
HGNCiHGNC:5008. HMGCS2.
HPAiCAB032906.
HPA027423.
HPA027442.
MIMi600234. gene.
605911. phenotype.
neXtProtiNX_P54868.
Orphaneti35701. 3-hydroxy-3-methylglutaryl-CoA synthase deficiency.
PharmGKBiPA29338.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3425.
GeneTreeiENSGT00390000006096.
HOGENOMiHOG000012351.
HOVERGENiHBG051912.
InParanoidiP54868.
KOiK01641.
OMAiRIQLPWD.
OrthoDBiEOG741Z1W.
PhylomeDBiP54868.
TreeFamiTF105361.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00102.
BioCyciMetaCyc:HS05836-MONOMER.
BRENDAi2.3.3.10. 2681.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_1464. Synthesis of Ketone Bodies.

Miscellaneous databases

EvolutionaryTraceiP54868.
GenomeRNAii3158.
NextBioi12510.
PROiP54868.
SOURCEiSearch...

Gene expression databases

BgeeiP54868.
CleanExiHS_HMGCS2.
GenevestigatoriP54868.

Family and domain databases

Gene3Di3.40.47.10. 1 hit.
InterProiIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 3 hits.
TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEiPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and tissue expression of human mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase."
    Mascaro C., Buesa C., Ortiz J.A., Haro D., Hegardt F.G.
    Arch. Biochem. Biophys. 317:385-390(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "Cloning and characterization of the human mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase gene."
    Boukaftane Y., Mitchell G.A.
    Gene 195:121-126(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution."
    Boukaftane Y., Duncan A., Wang S., Labuda D., Robert M.-F., Sarrazin J., Schappert K.T., Mitchell G.A.
    Genomics 23:552-559(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-508 (ISOFORM 1).
    Tissue: Liver.
  9. "Characterization of splice variants of the genes encoding human mitochondrial HMG-CoA lyase and HMG-CoA synthase, the main enzymes of the ketogenesis pathway."
    Puisac B., Ramos M., Arnedo M., Menao S., Gil-Rodriguez M.C., Teresa-Rodrigo M.E., Pie A., de Karam J.C., Wesselink J.J., Gimenez I., Ramos F.J., Casals N., Gomez-Puertas P., Hegardt F.G., Pie J.
    Mol. Biol. Rep. 39:4777-4785(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-316 (ISOFORM 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  10. "Ketogenic HMGCS2 Is a c-Myc target gene expressed in differentiated cells of human colonic epithelium and down-regulated in colon cancer."
    Camarero N., Mascaro C., Mayordomo C., Vilardell F., Haro D., Marrero P.F.
    Mol. Cancer Res. 4:645-653(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Crystal structures of human HMG-CoA synthase isoforms provide insights into inherited ketogenesis disorders and inhibitor design."
    Shafqat N., Turnbull A., Zschocke J., Oppermann U., Yue W.W.
    J. Mol. Biol. 398:497-506(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 51-508, SUBUNIT, ACTIVE SITE, SUBSTRATE-BINDING SITES.
  13. Cited for: VARIANTS HMGCS DEFICIENCY ARG-212 AND HIS-500.
  14. "Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase deficiency: clinical course and description of causal mutations in two patients."
    Bouchard L., Robert M.-F., Vinarov D., Stanley C.A., Thompson G.N., Morris A., Leonard J.V., Quant P., Hsu B.Y.L., Boneh A., Boukaftane Y., Ashmarina L., Wang S., Miziorko H., Mitchell G.A.
    Pediatr. Res. 49:326-331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HMGCS DEFICIENCY LEU-174, CHARACTERIZATION OF VARIANT HMGCS DEFICIENCY LEU-174.
  15. "Mitochondrial HMG-CoA synthase deficiency: identification of two further patients carrying two novel mutations."
    Wolf N.I., Rahman S., Clayton P.T., Zschocke J.
    Eur. J. Pediatr. 162:279-280(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HMGCS DEFICIENCY MET-54 AND CYS-167.

Entry informationi

Entry nameiHMCS2_HUMAN
AccessioniPrimary (citable) accession number: P54868
Secondary accession number(s): B7Z8R3
, D3Y5K6, Q5SZU2, Q6IBF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: September 30, 1996
Last modified: March 3, 2015
This is version 146 of the entry and version 1 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

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.