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Protein Overview: HMG1

General Information:
Name(s) found: HMG1 / YML075C [SGD]
Description(s) found:
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  • pir||A30239 hydroxymethylglutaryl-CoA reductase (EC 1.1.1.88) I - yeast (Saccharomyces cerevisiae) [NCBI NR]
  • gi|6323565|ref|NP_013636.1| One of two isozymes of HMG-CoA reductase that catalyzes the conversion of HMG-CoA to mevalonate, which is a rate-limiting step in sterol biosynthesis; localizes to the nuclear envelope; overproduction induces the formation of k [NCBI NR]
  • gi|587536|emb|CAA86503.1| HMG1 [Saccharomyces cerevisiae] [NCBI NR]
  • gi|171686|gb|AAA34676.1| 3-hydroxy-3-methyl-glutaryl coenzyme A reductase [NCBI NR]
  • gi|123336|sp|P12683.1|HMDH1_YEAST RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 1; Short=HMG-CoA reductase 1 [NCBI NR]
  • 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 OS=Saccharomyces cerevisiae GN=HMG1 PE=1 SV=1 [Swiss-Prot]
  • (P12683) 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 (EC 1.1.1.34) (HMG-CoA reductase 1) [Swiss-Prot]
  • HMG1 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 [mips]
  • One of two isozymes of HMG-CoA reductase that catalyzes the conversion of HMG-CoA to mevalonate, which is a rate-limiting step in sterol biosynthesis; localizes to the nuclear envelope; overproduction induces the formation of karmellae [SGD]
  • HMG1, Chr XIII from 115734-118898, reverse complement [yeast_orfs2]
  • Chr XIII from 115734-118898, reverse complement [yeastorf3.fasta]
  • Chr XIII from 118898-115734, reverse complement [yeastorf5.fasta]
  • HMG1 SGDID:S0004540, Chr XIII from 118898-115734, reverse complement, Verified ORF [yeastflysequest.fasta]
  • Hmg1p [Saccharomyces cerevisiae]gi|587536|emb|CAA86503.1| HMG1 [Saccharomyces cerevisiae]gi|123336|sp|P12683|HMD1_YEAST 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 (HMG-CoA reductase 1)gi|83081|pir||A30239 hydroxymethylglutaryl-CoA reductase (EC [nrdb_11152004_Chlamydomonas]
  • HMG1 SGDID:S000004540, Chr XIII from 118898-115734, reverse complement, Verified ORF, "One of two isozymes of HMG-CoA reductase that catalyzes the conversion of HMG-CoA to mevalonate, which is a rate-limiting step in sterol biosynthesis; localizes to the [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
  • One of two isozymes of HMG-CoA reductase that catalyzes the conversion of HMG-CoA to mevalonate, which is a rate-limiting step in sterol biosynthesis; localizes to the nuclear envelope; overproduction induces the formation of karmellae; Hmg1p [Saccharomyc [nr-271106-contam.fasta]
  • HMG1 [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • 3-hydroxy-3-methyl-glutaryl coenzyme A reductase [nr-271106-contam.fasta]
  • 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 (HMG-CoA reductase 1) [nr-271106-contam.fasta]
  • HMG1 SGDID:S000004540, Chr XIII from 118898-115734, reverse complement, Verified ORF, "One of two isozymes of HMG-CoA reductase that catalyzes the conversion of HMG-CoA to mevalonate, which is a rate-limiting step in sterol biosynthesis; localizes to the nuclear envelope; overproduction induces the formation of karmellae" [yeast-bovrabprots.fasta]
  • [chemostatdb.fasta]
  • 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=HMG1 PE=1 SV=1 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
  • HMG1 SGDID:S000004540, Chr XIII from 118898-115734, Genome Release 64-1-1, reverse complement, Verified ORF, "One of two isozymes of HMG-CoA reductase that catalyzes the conversion of HMG-CoA to mevalonate, which is a rate-limiting step in sterol biosynthesis; localizes to the nuclear envelope; overproduction induces the formation of karmellae" [yeast-030211-contam.fasta]
  • HMG1 SGDID:S000004540, Chr XIII from 118898-115734, Genome Release 64-2-1, reverse complement, Verified ORF, "HMG-CoA reductase; catalyzes the conversion of HMG-CoA to mevalonate, which is a rate-limiting step in sterol biosynthesis; one of two isozymes; localizes to the nuclear envelope; overproduction induces the formation of karmellae; forms foci at the nuclear periphery upon DNA replication stress; HMG1 has a paralog, HMG2, that arose from the whole genome duplication" [20141208_orf_trans.fasta]
  • YML075C SGDID:S000004540, Chr XIII from 118898-115734, Genome Release 64-1-1, reverse complement, Verified ORF, "One of two isozymes of HMG-CoA reductase that catalyzes the conversion of HMG-CoA to mevalonate, which is a rate-limiting step in sterol biosynthesis; localizes to the nuclear envelope; overproduction induces the formation of karmellae" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
    • Organism: Saccharomyces cerevisiae
    Length: 1054 amino acids

    Gene Ontology:
    Cellular Component: nuclear envelope [IDALink to PubMed article]
    endoplasmic reticulum membrane [IDALink to PubMed article]
    mitochondrial matrix [TAS]
    Biological Process: ergosterol biosynthetic process [TAS]
    Molecular Function: hydroxymethylglutaryl-CoA reductase (NADPH) activity [TAS]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MPPLFKGLKQ MAKPIAYVSR FSAKRPIHII LFSLIISAFA YLSVIQYYFN GWQLDSNSVF  60
   61 ETAPNKDSNT LFQECSHYYR DSSLDGWVSI TAHEASELPA PHHYYLLNLN FNSPNETDSI 120
  121 PELANTVFEK DNTKYILQED LSVSKEISST DGTKWRLRSD RKSLFDVKTL AYSLYDVFSE 180
  181 NVTQADPFDV LIMVTAYLMM FYTIFGLFND MRKTGSNFWL SASTVVNSAS SLFLALYVTQ 240
  241 CILGKEVSAL TLFEGLPFIV VVVGFKHKIK IAQYALEKFE RVGLSKRITT DEIVFESVSE 300
  301 EGGRLIQDHL LCIFAFIGCS MYAHQLKTLT NFCILSAFIL IFELILTPTF YSAILALRLE 360
  361 MNVIHRSTII KQTLEEDGVV PSTARIISKA EKKSVSSFLN LSVVVIIMKL SVILLFVFIN 420
  421 FYNFGANWVN DAFNSLYFDK ERVSLPDFIT SNASENFKEQ AIVSVTPLLY YKPIKSYQRI 480
  481 EDMVLLLLRN VSVAIRDRFV SKLVLSALVC SAVINVYLLN AARIHTSYTA DQLVKTEVTK 540
  541 KSFTAPVQKA STPVLTNKTV ISGSKVKSLS SAQSSSSGPS SSSEEDDSRD IESLDKKIRP 600
  601 LEELEALLSS GNTKQLKNKE VAALVIHGKL PLYALEKKLG DTTRAVAVRR KALSILAEAP 660
  661 VLASDRLPYK NYDYDRVFGA CCENVIGYMP LPVGVIGPLV IDGTSYHIPM ATTEGCLVAS 720
  721 AMRGCKAINA GGGATTVLTK DGMTRGPVVR FPTLKRSGAC KIWLDSEEGQ NAIKKAFNST 780
  781 SRFARLQHIQ TCLAGDLLFM RFRTTTGDAM GMNMISKGVE YSLKQMVEEY GWEDMEVVSV 840
  841 SGNYCTDKKP AAINWIEGRG KSVVAEATIP GDVVRKVLKS DVSALVELNI AKNLVGSAMA 900
  901 GSVGGFNAHA ANLVTAVFLA LGQDPAQNVE SSNCITLMKE VDGDLRISVS MPSIEVGTIG 960
  961 GGTVLEPQGA MLDLLGVRGP HATAPGTNAR QLARIVACAV LAGELSLCAA LAAGHLVQSH1020
 1021 MTHNRKPAEP TKPNNLDATD INRLKDGSVT CIKS

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Gavin AC, et al. (2006) HMG1 RAD51 RPL27B
    View Details Qiu et al. (2008) HMG1 HMG2

    Mass Spectrometry Data

    The following runs contain data for this protein:

      BAIT COMMENTS PUBLICATION
    View Run CEP3 sample cbf3 from feb 2005 Sandall S, et all (2006)
    View Run RPA135 No Comments Schneider, DA, et al. (2006)
    View Run VAM3 Sample: HX11 - both fusion and trans-SNARE complex formation take place. Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX12 - trans-SNARE complex formation and fusion are inhibited (control). Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX13 - trans-SNARE complex forms but fusion is blocked. Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX14 - mixture in detergent (control). Hao Xu, et al. (2010)
    View Run MLP2 #03 Alpha Factor Prep1-TiO2 Flowthrough Keck JM, et al. (2011)
    View Run None Entered #17 Mitotic Prep3-TiO2 Phosphopeptide enrichment Keck JM, et al. (2011)

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

      BAIT PREY HITS PUBLICATION
    View Screen HMG1 PET494 2 Unpublished Fields Lab Data
    View Screen HMG1 POL32 2 Unpublished Fields Lab Data
    View Screen HMG1 RNP1 2 Unpublished Fields Lab Data
    View Screen HMG1 HSM3 2 Unpublished Fields Lab Data
    View Screen HMG1 PET494 2 Unpublished Fields Lab Data

    Microscopy / Localization Data

    New Feature: Upload Your Own Microscopy Data

      PROTEIN(S) PUBLICATION
    View Data HMG1 and NIC96 Huh WK, et al. (2003)
    View Data HMG1 Huh WK, et al. (2003)

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..524] MSA 100.381995 View MSA. No confident structure predictions are available.
    2 View Details [525..577] deduced N/A No confident structure predictions are available.
    3 View Details [578..689] PSI-BLAST 2420.0 NAD-binding domain of HMG-CoA reductase; Substrate-binding domain of HMG-CoA reductase
    4 View Details [690..743]
    [846..1054]    		 PSI-BLAST 2420.0 NAD-binding domain of HMG-CoA reductase; Substrate-binding domain of HMG-CoA reductase
    5 View Details [744..845] PSI-BLAST 2420.0 NAD-binding domain of HMG-CoA reductase; Substrate-binding domain of HMG-CoA reductase


    Reference: Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076


    Philius Transmembrane Prediction:

    [View Details]
    Source: Reynolds et al. 2008. Manuscript submitted Philius confidence legend
    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle