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Q8JZK9

- HMCS1_MOUSE

UniProt

Q8JZK9 - HMCS1_MOUSE

Protein

Hydroxymethylglutaryl-CoA synthase, cytoplasmic

Gene

Hmgcs1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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.By similarity

    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
    Active sitei95 – 951Proton donor/acceptorPROSITE-ProRule annotation
    Active sitei129 – 1291Acyl-thioester intermediatePROSITE-ProRule annotation
    Active sitei264 – 2641Proton donor/acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. drug binding Source: Ensembl
    2. hydroxymethylglutaryl-CoA synthase activity Source: UniProtKB-EC
    3. isomerase activity Source: Ensembl
    4. organic acid binding Source: Ensembl

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cellular response to cholesterol Source: Ensembl
    3. cellular response to follicle-stimulating hormone stimulus Source: Ensembl
    4. cholesterol biosynthetic process Source: UniProtKB-KW
    5. isoprenoid biosynthetic process Source: InterPro
    6. liver development Source: Ensembl
    7. male gonad development Source: Ensembl
    8. response to acid chemical Source: Ensembl
    9. response to drug Source: Ensembl
    10. response to lipoprotein particle Source: Ensembl
    11. response to low light intensity stimulus Source: Ensembl
    12. response to purine-containing compound Source: Ensembl
    13. response to tellurium ion Source: Ensembl
    14. response to vitamin E Source: Ensembl

    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

    ReactomeiREACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_208531. Cholesterol biosynthesis.
    UniPathwayiUPA00058; UER00102.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxymethylglutaryl-CoA synthase, cytoplasmic (EC:2.3.3.10)
    Short name:
    HMG-CoA synthase
    Alternative name(s):
    3-hydroxy-3-methylglutaryl coenzyme A synthase
    Gene namesi
    Name:Hmgcs1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:107592. Hmgcs1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. nucleus Source: Ensembl
    3. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 520520Hydroxymethylglutaryl-CoA synthase, cytoplasmicPRO_0000213748Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41PhosphoserineBy similarity
    Modified residuei46 – 461N6-acetyllysineBy similarity
    Modified residuei273 – 2731N6-acetyllysineBy similarity
    Modified residuei495 – 4951Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8JZK9.
    PaxDbiQ8JZK9.
    PRIDEiQ8JZK9.

    2D gel databases

    REPRODUCTION-2DPAGEQ8JZK9.

    PTM databases

    PhosphoSiteiQ8JZK9.

    Expressioni

    Gene expression databases

    BgeeiQ8JZK9.
    CleanExiMM_HMGCS1.
    GenevestigatoriQ8JZK9.

    Interactioni

    Protein-protein interaction databases

    IntActiQ8JZK9. 2 interactions.
    MINTiMINT-1869354.
    STRINGi10090.ENSMUSP00000097858.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8JZK9.
    SMRiQ8JZK9. Positions 16-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HMG-CoA synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG3425.
    GeneTreeiENSGT00390000006096.
    HOGENOMiHOG000012351.
    HOVERGENiHBG051912.
    InParanoidiQ8JZK9.
    KOiK01641.
    OMAiRDFTLND.
    OrthoDBiEOG741Z1W.
    PhylomeDBiQ8JZK9.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q8JZK9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGSLPLNAE ACWPKDVGIV ALEIYFPSQY VDQAELEKYD GVDAGKYTIG    50
    LGQARMGFCT DREDINSLCL TVVQKLMERH SLSYDCIGRL EVGTETIIDK 100
    SKSVKSNLMQ LFEESGNTDI EGIDTTNACY GGTAAVFNAV NWVESSSWDG 150
    RYALVVAGDI AIYATGNARP TGGVGAVALL IGPNAPLIFD RGLRGTHMQH 200
    AYDFYKPDML SEYPVVDGKL SIQCYLSALD RCYSVYRKKI RAQWQKEGKD 250
    KDFTLNDFGF MIFHSPYCKL VQKSLARMFL NDFLNDQNRD KNSIYSGLEA 300
    FGDVKLEDTY FDRDVEKAFM KASSELFNQK TKASLLVSNQ NGNMYTSSVY 350
    GSLASVLAQY SPQQLAGKRV GVFSYGSGLA ATLYSLKVTQ DATPGSALDK 400
    ITASLCDLKS RLDSRTCVAP DVFAENMKLR EDTHHLANYI PQCSIDSLFE 450
    GTWYLVRVDE KHRRTYARRP FTNDHSLDEG MGLVHSNTAT EHIPSPAKKV 500
    PRLPATSAES ESAVISNGEH 520
    Length:520
    Mass (Da):57,569
    Last modified:October 1, 2002 - v1
    Checksum:iE28F8772CF64D85C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC023851 mRNA. Translation: AAH23851.1.
    BC029693 mRNA. Translation: AAH29693.1.
    BC034317 mRNA. Translation: AAH34317.1.
    AK031297 mRNA. Translation: BAC27338.1.
    AK044835 mRNA. Translation: BAC32112.1.
    AK045094 mRNA. Translation: BAC32218.1.
    AK135551 mRNA. Translation: BAE22579.1.
    CCDSiCCDS56901.1.
    RefSeqiNP_001278368.1. NM_001291439.1.
    NP_666054.2. NM_145942.5.
    XP_006517641.1. XM_006517578.1.
    UniGeneiMm.61526.

    Genome annotation databases

    EnsembliENSMUST00000179869; ENSMUSP00000136944; ENSMUSG00000093930.
    GeneIDi208715.
    KEGGimmu:208715.
    UCSCiuc007rzv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC023851 mRNA. Translation: AAH23851.1 .
    BC029693 mRNA. Translation: AAH29693.1 .
    BC034317 mRNA. Translation: AAH34317.1 .
    AK031297 mRNA. Translation: BAC27338.1 .
    AK044835 mRNA. Translation: BAC32112.1 .
    AK045094 mRNA. Translation: BAC32218.1 .
    AK135551 mRNA. Translation: BAE22579.1 .
    CCDSi CCDS56901.1.
    RefSeqi NP_001278368.1. NM_001291439.1.
    NP_666054.2. NM_145942.5.
    XP_006517641.1. XM_006517578.1.
    UniGenei Mm.61526.

    3D structure databases

    ProteinModelPortali Q8JZK9.
    SMRi Q8JZK9. Positions 16-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8JZK9. 2 interactions.
    MINTi MINT-1869354.
    STRINGi 10090.ENSMUSP00000097858.

    PTM databases

    PhosphoSitei Q8JZK9.

    2D gel databases

    REPRODUCTION-2DPAGE Q8JZK9.

    Proteomic databases

    MaxQBi Q8JZK9.
    PaxDbi Q8JZK9.
    PRIDEi Q8JZK9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000179869 ; ENSMUSP00000136944 ; ENSMUSG00000093930 .
    GeneIDi 208715.
    KEGGi mmu:208715.
    UCSCi uc007rzv.1. mouse.

    Organism-specific databases

    CTDi 3157.
    MGIi MGI:107592. Hmgcs1.

    Phylogenomic databases

    eggNOGi COG3425.
    GeneTreei ENSGT00390000006096.
    HOGENOMi HOG000012351.
    HOVERGENi HBG051912.
    InParanoidi Q8JZK9.
    KOi K01641.
    OMAi RDFTLND.
    OrthoDBi EOG741Z1W.
    PhylomeDBi Q8JZK9.
    TreeFami TF105361.

    Enzyme and pathway databases

    UniPathwayi UPA00058 ; UER00102 .
    Reactomei REACT_198602. PPARA activates gene expression.
    REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_208531. Cholesterol biosynthesis.

    Miscellaneous databases

    NextBioi 372391.
    PROi Q8JZK9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8JZK9.
    CleanExi MM_HMGCS1.
    Genevestigatori Q8JZK9.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Muellerian duct and Testis.
    2. "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].
      Strain: FVB/N and FVB/N-3.
      Tissue: Eye and Mammary tumor.
    3. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 47-75; 90-100; 220-231; 278-289; 292-313; 322-330; 370-409; 416-428 AND 469-498, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiHMCS1_MOUSE
    AccessioniPrimary (citable) accession number: Q8JZK9
    Secondary accession number(s): Q3UXI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3