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protein coding gene - hcs1 (SPAC4F8.14c) - 3-hydroxy-3-methylglutaryl-CoA synthase

Gene summary

Standard name
hcs1
Systematic ID
SPAC4F8.14c
Product
3-hydroxy-3-methylglutaryl-CoA synthase
Organism
Schizosaccharomyces pombe (fission yeast)
Synonyms
hcs
UniProt ID
P54874
ORFeome ID
24/24F06
Characterisation status
biological role published
Feature type
mRNA gene
Genomic location
chromosome I: 2643524..2645254 forward strand

Annotation

Disease association

MONDO:0011614 - 3-hydroxy-3-methylglutaryl-CoA synthase deficiency

References:

GO biological process

GO:0006084 - acetyl-CoA metabolic process

References:

GO:0006696 - ergosterol biosynthetic process

References:

GO:0010142 - farnesyl diphosphate biosynthetic process, mevalonate pathway

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GO cellular component

GO:0005829 - cytosol

References:

GO:0005783 - endoplasmic reticulum

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GO:0005634 - nucleus

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GO molecular function

GO:0004421 - hydroxymethylglutaryl-CoA synthase activity

References:

Modification

MOD:00046 - O-phospho-L-serine

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MOD:00047 - O-phospho-L-threonine

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MOD:00048 - O4'-phospho-L-tyrosine

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MOD:01148 - ubiquitinylated lysine

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Qualitative gene expression

PomGeneEx:0000019 - protein level decreased

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PomGeneEx:0000012 - RNA level decreased

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Quantitative gene expression

PBO:0006310 - protein level

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PBO:0011963 - RNA level

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Single locus phenotype

FYPO:0007327 - DNA content decreased during G0

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Genotypes:

FYPO:0001327 - increased protein level during vegetative growth

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Genotypes:

FYPO:0001042 - inviable after spore germination, single or double cell division

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Genotypes:

FYPO:0000313 - inviable after spore germination, without cell division, with abnormal germ tube morphology

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Genotypes:

FYPO:0002061 - inviable vegetative cell population

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Genotypes:

FYPO:0006518 - loss of viability in G0

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Genotypes:

FYPO:0000075 - resistance to lovastatin

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Genotypes:

Taxonomic conservation

PBO:0011067 - conserved in bacteria

PBO:0011065 - conserved in eukaryotes

PBO:0011064 - conserved in fungi

PBO:0011069 - conserved in metazoa

PBO:0011070 - conserved in vertebrates

PBO:0006222 - predominantly single copy (one to one)

Protein features

IDNameInterPro nameDB name
PF08540HMG_CoA_synt_CHMG_CoA_synt_C_domPFAM
PF01154HMG_CoA_synt_NHMG_CoA_synth_NPFAM
cd00827init_cond_enzymesCDD
PS01226HMG_COA_SYNTHASEHMG_CoA_synt_ASPROSITE_PATTERNS
G3DSA:3.40.47.10:FF:000008FUNFAM
SSF53901Thiolase-likeThiolase-likeSUPERFAMILY
G3DSA:3.40.47.10Thiolase-likeGENE3D
PTHR433233-HYDROXY-3-METHYLGLUTARYL COENZYME A SYNTHASEPANTHER
TIGR01833HMG-CoA-S_eukHMG_CoA_synthase_eukNCBIFAM

Orthologs

References / Literature

PMID:37970674 - SUMOylation regulates Lem2 function in centromere clustering and silencing.
Strachan J et al. J Cell Sci 2023 Dec 01;136(23)
PMID:24763107 - Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).
Carpy A et al. Mol Cell Proteomics 2014 Aug;13(8):1925-36
PMID:8896278 - Molecular, functional and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe.
Lum PY et al. Yeast 1996 Sep 15;12(11):1107-24
GO_REF:0000033 - Annotation inferences using phylogenetic trees
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
PMID:23697806 - A genome-wide resource of cell cycle and cell shape genes of fission yeast.
Hayles J et al. Open Biol 2013 May 22;3(5):130053
PMID:39367033 - Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast Schizosaccharomyces pombe.
Sivakova B et al. Sci Rep 2024 Oct 04;14(1):23105
PMID:31626996 - Multiplexed proteome profiling of carbon source perturbations in two yeast species with SL-SP3-TMT.
Paulo JA et al. J Proteomics 2020 Jan 06;210:103531
PB_REF:0000006 - Disease associations from Monarch via human-pombe orthologs
PMID:18257517 - Phosphoproteome analysis of fission yeast.
Wilson-Grady JT et al. J Proteome Res 2008 Mar;7(3):1088-97
PMID:8750242 - Molecular cloning and sequencing of the hcs gene, which encodes 3-hydroxy-3-methylglutaryl coenzyme A synthase of Schizosaccharomyces pombe.
Katayama S et al. Yeast 1995 Dec;11(15):1533-7
PMID:33823663 - A TOR (target of rapamycin) and nutritional phosphoproteome of fission yeast reveals novel targets in networks conserved in humans.
Halova L et al. Open Biol 2021 Apr;11(4):200405
PMID:39476757 - Characterization of Ksg1 protein kinase-dependent phosphoproteome in the fission yeast S. pombe.
Cipak L et al. Biochem Biophys Res Commun 2024 Oct 25;736:150895
PMID:20473289 - Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
Kim DU et al. Nat Biotechnol 2010 Jun;28(6):617-623
PMID:25720772 - Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.
Kettenbach AN et al. Mol Cell Proteomics 2015 May;14(5):1275-87
PMID:39705284 - Proteomic and phosphoproteomic analyses reveal that TORC1 is reactivated by pheromone signaling during sexual reproduction in fission yeast.
Bérard M et al. PLoS Biol 2024 Dec 20;22(12):e3002963
PMID:16823372 - ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
Matsuyama A et al. Nat Biotechnol 2006 Jul;24(7):841-7
PMID:19366728 - Genetic control of cellular quiescence in S. pombe.
Sajiki K et al. J Cell Sci 2009 May 01;122(Pt 9):1418-29
PMID:30726745 - Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.
Tay YD et al. Cell Rep 2019 Feb 05;26(6):1654-1667.e7
PMID:27984744 - Survival in Quiescence Requires the Euchromatic Deployment of Clr4/SUV39H by Argonaute-Associated Small RNAs.
Joh RI et al. Mol Cell 2016 Dec 15;64(6):1088-1101
PMID:23101633 - Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.
Marguerat S et al. Cell 2012 Oct 26;151(3):671-83
PMID:15797383 - SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast.
Hughes AL et al. Cell 2005 Mar 25;120(6):831-42