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P54868

- HMCS2_HUMAN

UniProt

P54868 - HMCS2_HUMAN

Protein

Hydroxymethylglutaryl-CoA synthase, mitochondrial

Gene

HMGCS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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 intermediate1 PublicationPROSITE-ProRule annotation
    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

    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

    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.3 Publications
    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 – 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 residuei437 – 4371N6-acetyllysineBy similarity
    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

    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

    HPAiHPA027423.
    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54868.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HMG-CoA synthase family.Curated

    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

    Experimental Info

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

    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:
    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...
    MobiDBi 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-2DPAGE 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-InvDB 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

    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: October 1, 2014
    This is version 143 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