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P54868

- HMCS2_HUMAN

UniProt

P54868 - HMCS2_HUMAN

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Protein
Hydroxymethylglutaryl-CoA synthase, mitochondrial
Gene
HMGCS2
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801Substrate
Active sitei132 – 1321Proton donor/acceptor Inferred
Active sitei166 – 1661Acyl-thioester intermediate1 Publication
Binding sitei204 – 2041Substrate
Binding sitei258 – 2581Substrate
Active sitei301 – 3011Proton donor/acceptor Inferred
Binding sitei380 – 3801Substrate

GO - Molecular functioni

  1. hydroxymethylglutaryl-CoA synthase activity Source: UniProtKB-EC
Complete GO annotation...

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: 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) [MIM:605911]: Affected 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.
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 – 3737Mitochondrion Inferred
Add
BLAST
Chaini38 – 508471Hydroxymethylglutaryl-CoA synthase, mitochondrial
PRO_0000013483Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP54868.
PaxDbiP54868.
PeptideAtlasiP54868.
PRIDEiP54868.

2D gel databases

REPRODUCTION-2DPAGEiIPI00008934.

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

HPAiHPA027423.
HPA027442.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP54868.

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA synthase family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3425.
HOGENOMiHOG000012351.
HOVERGENiHBG051912.
InParanoidiP54868.
KOiK01641.
OMAiVDGKYSS.
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. Align

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

MQRLLTPVKR ILQLTRAVQE TSLTPARLLP VAHQRFSTAS AVPLAKTDTW    50
PKDVGILALE VYFPAQYVDQ TDLEKYNNVE AGKYTVGLGQ TRMGFCSVQE 100
DINSLCLTVV QRLMERIQLP WDSVGRLEVG TETIIDKSKA VKTVLMELFQ 150
DSGNTDIEGI DTTNACYGGT ASLFNAANWM ESSSWDGRYA MVVCGDIAVY 200
PSGNARPTGG AGAVAMLIGP KAPLALERGL RGTHMENVYD FYKPNLASEY 250
PIVDGKLSIQ CYLRALDRCY TSYRKKIQNQ WKQAGSDRPF TLDDLQYMIF 300
HTPFCKMVQK SLARLMFNDF LSASSDTQTS LYKGLEAFGG LKLEDTYTNK 350
DLDKALLKAS QDMFDKKTKA SLYLSTHNGN MYTSSLYGCL ASLLSHHSAQ 400
ELAGSRIGAF SYGSGLAASF FSFRVSQDAA PGSPLDKLVS STSDLPKRLA 450
SRKCVSPEEF TEIMNQREQF YHKVNFSPPG DTNSLFPGTW YLERVDEQHR 500
RKYARRPV 508
Length:508
Mass (Da):56,635
Last modified:October 1, 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

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.
VSP_042892Add
BLAST
Alternative sequencei229 – 28355Missing in isoform 3.
VSP_047445Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341H → Y in CAG33131. 1 Publication
Sequence conflicti385 – 3851S → T in CAG33131. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53353.1. [P54868-2 ]
CCDS905.1. [P54868-1 ]
PIRi S71623.
RefSeqi NP_001159579.1. NM_001166107.1. [P54868-2 ]
NP_005509.1. NM_005518.3. [P54868-1 ]
UniGenei Hs.59889.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WYA X-ray 1.70 A/B/C/D 51-508 [» ]
ProteinModelPortali P54868.
SMRi P54868. Positions 51-508.
ModBasei Search...

Protein-protein interaction databases

BioGridi 109401. 3 interactions.
IntActi P54868. 1 interaction.
STRINGi 9606.ENSP00000358414.

PTM databases

PhosphoSitei P54868.

Polymorphism databases

DMDMi 1708234.

2D gel databases

REPRODUCTION-2DPAGEi IPI00008934.

Proteomic databases

MaxQBi P54868.
PaxDbi P54868.
PeptideAtlasi P54868.
PRIDEi P54868.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369406 ; ENSP00000358414 ; ENSG00000134240 . [P54868-1 ]
ENST00000544913 ; ENSP00000439495 ; ENSG00000134240 . [P54868-2 ]
GeneIDi 3158.
KEGGi hsa:3158.
UCSCi uc001eid.3. human. [P54868-1 ]
uc010oxj.2. human. [P54868-2 ]

Organism-specific databases

CTDi 3158.
GeneCardsi GC01M120290.
H-InvDBi HIX0160007.
HGNCi HGNC:5008. HMGCS2.
HPAi HPA027423.
HPA027442.
MIMi 600234. gene.
605911. phenotype.
neXtProti NX_P54868.
Orphaneti 35701. 3-hydroxy-3-methylglutaryl-CoA synthase deficiency.
PharmGKBi PA29338.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3425.
HOGENOMi HOG000012351.
HOVERGENi HBG051912.
InParanoidi P54868.
KOi K01641.
OMAi VDGKYSS.
OrthoDBi EOG741Z1W.
PhylomeDBi P54868.
TreeFami TF105361.

Enzyme and pathway databases

UniPathwayi UPA00058 ; UER00102 .
BioCyci MetaCyc:HS05836-MONOMER.
BRENDAi 2.3.3.10. 2681.
Reactomei REACT_116145. PPARA activates gene expression.
REACT_1464. Synthesis of Ketone Bodies.

Miscellaneous databases

EvolutionaryTracei P54868.
GenomeRNAii 3158.
NextBioi 12510.
PROi P54868.
SOURCEi Search...

Gene expression databases

Bgeei P54868.
CleanExi HS_HMGCS2.
Genevestigatori P54868.

Family and domain databases

Gene3Di 3.40.47.10. 1 hit.
InterProi IPR000590. 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 ]
Pfami PF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 3 hits.
TIGRFAMsi TIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEi PS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1995) [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(1997) [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 (AUG-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(2004) [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(2006) [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(2004) [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(1994) [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(2012) [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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 51-508, SUBUNIT, ACTIVE SITE, SUBSTRATE-BINDING SITES.
  12. Cited for: VARIANTS HMGCS DEFICIENCY ARG-212 AND HIS-500.
  13. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HMGCS DEFICIENCY LEU-174, CHARACTERIZATION OF VARIANT HMGCS DEFICIENCY LEU-174.
  14. "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(2003) [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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 142 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

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