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RER2/YBR002C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrII: 242570 to 241710 CDS: 242570 - 241710 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
RER2	YBR002C		ORF, Verified	S000000206
Description
Cis-prenyltransferase involved in dolichol synthesis; participates in endoplasmic reticulum (ER) protein sorting

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By dehydrodolichyl diphosphate synthase activity Sato M, et al. (2001) Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6(6):495-506        IDA : Inferred from Direct Assay Assigned on 2005-07-08 SGD prenyltransferase activity Sato M, et al. (1999) The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol Cell Biol 19(1):471-83        IDA : Inferred from Direct Assay Assigned on 2002-03-07 SGD Poznanski J and Szkopinska A (2007) Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae. Biopolymers 86(2):155-64          IDA : Inferred from Direct Assay Assigned on 2007-03-12 SGD transferase activity GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0808 Assigned on 2009-03-04 UniProtKB transferase activity, transferring alkyl or aryl (other than methyl) groups DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR018520 , EBI:IPR001441 Assigned on 2009-03-04 UniProtKB
Biological Process Annotation(s) Reference(s) Evidence Assigned By ER to Golgi vesicle-mediated transport Belgareh-Touze N, et al. (2003) Yeast functional analysis: identification of two essential genes involved in ER to Golgi trafficking. Traffic 4(9):607-17        IMP : Inferred from Mutant Phenotype Assigned on 2005-07-12 SGD dolichol biosynthetic process Kato J, et al. (1999) The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis. J Bacteriol 181(9):2733-8        IDA : Inferred from Direct Assay Assigned on 2002-08-27 SGD protein amino acid glycosylation Sato M, et al. (1999) The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol Cell Biol 19(1):471-83        IMP : Inferred from Mutant Phenotype IDA : Inferred from Direct Assay Assigned on 2002-03-07 SGD
Cellular Component Annotation(s) Reference(s) Evidence Assigned By endoplasmic reticulum Sato M, et al. (1999) The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol Cell Biol 19(1):471-83        IDA : Inferred from Direct Assay Assigned on 2002-03-07 SGD Sato M, et al. (2001) Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6(6):495-506        IDA : Inferred from Direct Assay Assigned on 2002-03-07 SGD GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0256 Assigned on 2007-05-23 UniProtKB extrinsic to membrane GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-9903 Assigned on 2009-10-01 UniProtKB membrane GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0472 Assigned on 2007-05-23 UniProtKB

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for RER2/YBR002C for RER2 Dolichols are a class of polyisoprenoid alcohols with five or more isoprene units in which the C2-C3 bond is saturated. In yeast, dolichols with 14-18 isoprene units are the carrier molecules on which many of the steps in N-linked glycosylation, O-linked glycosylation, and GPI anchor synthesis occur on the membrane of the endoplasmic reticulum (ER) (reviewed in 1). In mammals, dolichols with 19-22 isoprene units are the carrier molecules on which these steps occur. RER2 encodes a cis-prenyltransferase that catalyzes the formation of dehydrodolichyl diphosphate, the committed step in dolichol synthesis, from farnesyl diphosphate and an isopentenyl pyrophosphate with 10-14 isoprene units. This results in the formation of a dolichol precursor with 14-18 isoprene units (2, 3). Rer2p is peripherally associated with the ER membrane (2, 3). RER2 is expressed in the early logarithmic phase (3). Overexpression of Erg20p, which synthesizes the Rer2p substrate farnesyl diphosphate, induces expression of RER2, SRT1, and DPM1. Originally isolated as a mutant defective in retaining certain proteins in the ER (2), rer2 cells also grow slowly (2, 4) have defects in N-linked and O-linked glycosylation (2, 5), and form clumps when grown in suspension (2). They accumulate excessive ER and Golgi membrane material and are sensitive to hygromycin B and resistant to sodium orthovanadate (2). Overexpression of the Rer2p homolog Srt1p, which synthesizes dolichol precursors with 19-22 isoprene units, suppresses deletion of RER2, but the resultant cells make only the longer-chain dolichols (2, 5). The rer2 srt1 double deletion is lethal (2). The RER2 human homolog (OMIM), called hCIT(6) or hds (7) complements its deletion in yeast. Last Updated: 2005-07-08

Basic References [TOP]

BASIC INFORMATION REFERENCES forRER2/YBR002C for RER2 1) Grabinska K and Palamarczyk G (2002) Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase. FEMS Yeast Res 2(3):259-65            2) Sato M, et al. (1999) The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol Cell Biol 19(1):471-83        3) Sato M, et al. (2001) Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6(6):495-506        4) Nishikawa S and Nakano A (1993) Identification of a gene required for membrane protein retention in the early secretory pathway. Proc Natl Acad Sci U S A 90(17):8179-83        5) Schenk B, et al. (2001) An alternative cis-isoprenyltransferase activity in yeast that produces polyisoprenols with chain lengths similar to mammalian dolichols. Glycobiology 11(1):89-98        6) Shridas P, et al. (2003) Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells. Biochem Biophys Res Commun 312(4):1349-56        7) Endo S, et al. (2003) Identification of human dehydrodolichyl diphosphate synthase gene. Biochim Biophys Acta 1625(3):291-5

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for RER2/YBR002C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for RER2/YBR002C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]
Protein Sequence Calculations from Predicted Full length Translation N-term METDSGI C-term LKEKKLN Length(aa) 286 MW(Da) 32,693 pI 7.79 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.003   Codon Adaptation Index 0.109   Frequency of Optimal Codons 0.400   Hydropathicity of Protein -0.315   Aromaticity Score 0.084	10 20 30 40 50 | | | | | METDSGIPGHSFVLKWTKNIFSRTLRASNCVPRHVGFIMDGNRRFARKKE MDVKEGHEAGFVSMSRILELCYEAGVDTATVFAFSIENFKRSSREVESLM TLARERIRQITERGELACKYGVRIKIIGDLSLLDKSLLEDVRVAVETTKN NKRATLNICFPYTGREEILHAMKETIVQHKKGAAIDESTLESHLYTAGVP PLDLLIRTSGVSRLSDFLIWQASSKGVRIELLDCLWPEFGPIRMAWILLK FSFHKSFLNKEYRLEEGDYDEETNGDPIDLKEKKLN*

Protein Structures from PDB: proteins of known structure with sequence similarity to RER2/YBR002C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to RER2 Homolog Source (per PDB) Protein Alignment: RER2 vs. Homolog External Links P-Value %Identical %Similar Alignment 2vg2 ( Chain: D, B, A, C) Rv2361 with ipp PDB_Info PDB_Structure Mycobacterium tuberculosis Chain D = 1.9e-26 37 25 View alignment SCOP MMDB CATH Chain B = 1.9e-26 37 25 View alignment Chain A = 1.9e-26 37 25 View alignment Chain C = 1.9e-26 37 25 View alignment 2vg3 ( Chain: D, B, C, A) Rv2361 with citronellyl pyrophosphate PDB_Info PDB_Structure Mycobacterium tuberculosis Chain D = 1.9e-26 37 25 View alignment SCOP MMDB CATH Chain B = 1.9e-26 37 25 View alignment Chain C = 1.9e-26 37 25 View alignment Chain A = 1.9e-26 37 25 View alignment 2vg4 ( Chain: A, B, C, D) Rv2361 native PDB_Info PDB_Structure Mycobacterium tuberculosis Chain A = 1.9e-26 37 25 View alignment SCOP MMDB CATH Chain B = 1.9e-26 37 25 View alignment Chain C = 1.9e-26 37 25 View alignment Chain D = 1.9e-26 37 25 View alignment 1x06 ( Chain: A) Crystal structure of undecaprenyl pyrophosphate synthase in complex with mg, ipp and fspp PDB_Info PDB_Structure Escherichia coli 3.3e-25 34 27 View alignment SCOP MMDB CATH 1x07 ( Chain: A) Crystal structure of undecaprenyl pyrophosphate synthase in complex with mg and ipp PDB_Info PDB_Structure Escherichia coli 3.3e-25 34 27 View alignment SCOP MMDB CATH 2e9c ( Chain: A, B) E. coli undecaprenyl pyrophosphate synthase in complex with bph-675 PDB_Info PDB_Structure Escherichia coli Chain A = 3.3e-25 34 27 View alignment SCOP MMDB CATH Chain B = 3.3e-25 34 27 View alignment 2e9a ( Chain: B, A) E. coli undecaprenyl pyrophosphate synthase in complex with bph-628 PDB_Info PDB_Structure Escherichia coli Chain B = 3.3e-25 34 27 View alignment SCOP MMDB CATH Chain A = 3.3e-25 34 27 View alignment 2e9d ( Chain: B, A) E. coli undecaprenyl pyrophosphate synthase in complex with bph-676 PDB_Info PDB_Structure Escherichia coli Chain B = 3.3e-25 34 27 View alignment SCOP MMDB CATH Chain A = 3.3e-25 34 27 View alignment 2e99 ( Chain: B, A) E. coli undecaprenyl pyrophosphate synthase in complex with bph-608 PDB_Info PDB_Structure Escherichia coli Chain B = 3.3e-25 34 27 View alignment SCOP MMDB CATH Chain A = 3.3e-25 34 27 View alignment 1ueh ( Chain: B, A) E. coli undecaprenyl pyrophosphate synthase in complex with triton x-100, magnesium and sulfate PDB_Info PDB_Structure Escherichia coli Chain B = 3.3e-25 34 27 View alignment SCOP MMDB CATH Chain A = 3.3e-25 34 27 View alignment 1jp3 ( Chain: A, B) Structure of e.coli undecaprenyl pyrophosphate synthase PDB_Info PDB_Structure Escherichia coli Chain A = 3.3e-25 34 27 View alignment SCOP MMDB CATH Chain B = 3.3e-25 34 27 View alignment 2e98 ( Chain: B, A) E. coli undecaprenyl pyrophosphate synthase in complex with bph-629 PDB_Info PDB_Structure Escherichia coli Chain B = 3.3e-25 34 27 View alignment SCOP MMDB CATH Chain A = 3.3e-25 34 27 View alignment 1v7u ( Chain: A, B) Crystal structure of undecaprenyl pyrophosphate synthase with farnesyl pyrophosphate PDB_Info PDB_Structure Escherichia coli Chain A = 3.3e-25 34 27 View alignment SCOP MMDB CATH Chain B = 3.3e-25 34 27 View alignment 1f75 ( Chain: A, B) Crystal structure of undecaprenyl diphosphate synthase from micrococcus luteus b-p 26 PDB_Info PDB_Structure Micrococcus luteus Chain A = 4.7e-25 35 28 View alignment SCOP MMDB CATH Chain B = 4.7e-25 35 28 View alignment 1x08 ( Chain: A) Crystal structure of d26a mutant upps in complex with mg, ipp and fspp PDB_Info PDB_Structure Escherichia coli 1.9e-24 33 27 View alignment SCOP MMDB CATH 1x09 ( Chain: A) Crystal structure of the d26a mutant upps in complex with magnesium and isopentenyl pyrophosphate PDB_Info PDB_Structure Escherichia coli 1.9e-24 33 27 View alignment SCOP MMDB CATH 2vg1 ( Chain: B, A) Rv1086 e,e-farnesyl diphosphate complex PDB_Info PDB_Structure Mycobacterium tuberculosis Chain B = 2.5e-23 33 32 View alignment SCOP MMDB CATH Chain A = 2.5e-23 33 32 View alignment 2vg0 ( Chain: B, A) Rv1086 citronelly pyrophosphate complex PDB_Info PDB_Structure Mycobacterium tuberculosis Chain B = 2.5e-23 33 32 View alignment SCOP MMDB CATH Chain A = 2.5e-23 33 32 View alignment 2vfw ( Chain: B, A) Rv1086 native PDB_Info PDB_Structure Mycobacterium tuberculosis Chain B = 2.5e-23 33 32 View alignment SCOP MMDB CATH Chain A = 2.5e-23 33 32 View alignment 2d2r ( Chain: A, B) Crystal structure of helicobacter pylori undecaprenyl pyrophosphate synthase PDB_Info PDB_Structure Helicobacter pylori Chain A = 3.0e-19 31 31 View alignment SCOP MMDB CATH Chain B = 3.0e-19 31 31 View alignment 2dtn ( Chain: A, B) Crystal structure of helicobacter pylori undecaprenyl pyrophosphate synthase complexed with pyrophosphate PDB_Info PDB_Structure Helicobacter pylori Chain A = 3.0e-19 31 31 View alignment SCOP MMDB CATH Chain B = 3.0e-19 31 31 View alignment

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
RER2	Nishikawa S and Nakano A (1993) Identification of a gene required for membrane protein retention in the early secretory pathway. Proc Natl Acad Sci U S A 90(17):8179-83

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YBR002C	SGD Systematic Sequence
852287	NCBI: Gene ID
NP_009556.1	NCBI: RefSeq protein version ID
NP_009556.1	NCBI: RefSeq protein version ID
6319474	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YeastRC Localization (Seattle) Organelle DB (UMich) YGAC Triples YPL.db at Uni Graz YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
26 curated references; 0 references not yet curated
Reviews	Kuranda K, et al. (2010) The isoprenoid pathway and transcriptional response to its inhibitors in the yeast Saccharomyces cerevisiae. FEMS Yeast Res 10(1):14-27	|COQ1 |COX10 |ERG10 |ERG12 |ERG13 |ERG20 |ERG8 |ERG9 |HMG1 |HMG2 |IDI1 |MOD5 |MVD1 |RAM1 |MORE
Mutants/Phenotypes	Ammar R, et al. (2009) A comparative analysis of DNA barcode microarray feature size. BMC Genomics 10:471	|ADO1 |ALG7 |BCK1 |COP1 |FYV8 |GET2 |HAC1 |IRE1 |PSE1 |RET2 |RPC31 |VPS25 |YER010C |YFL032W |MORE
Function/Process Regulation of	Kuranda K, et al. (2009) The YTA7 gene is involved in the regulation of the isoprenoid pathway in the yeast Saccharomyces cerevisiae. FEMS Yeast Res 9(3):381-90	|ABC1 |AZR1 |ERG20 |HAP1 |HIR1 |HIR3 |HMG1 |HMG2 |OPT2 |SRB4 |SRT1 |YTA7
Function/Process Regulation of	Kaliszewski P, et al. (2008) Rsp5p ubiquitin ligase and the transcriptional activators Spt23p and Mga2p are involved in co-regulation of biosynthesis of end products of the mevalonate pathway and triacylglycerol in yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1781(10):627-34	|MGA2 |RSP5 |SPT23 |SRT1
Genetic Interactions Mutants/Phenotypes Protein Processing/Modification/Regulation Strains/Constructs	Gorka-Niec W, et al. (2007) Protein glycosylation in pmt mutants of Saccharomyces cerevisiae. Influence of heterologously expressed cellobiohydrolase II of Trichoderma reesei and elevated levels of GDP-mannose and cis-prenyltransferase activity. Biochim Biophys Acta 1770(5):774-80	|PMT1 |PMT2 |PSA1
Genetic Interactions	Orlowski J, et al. (2007) Dissecting the role of dolichol in cell wall assembly in the yeast mutants impaired in early glycosylation reactions. Yeast 24(4):239-52	|DPM1 |GAS1 |ROT1 |SEC59 |SLT2 |SRT1
Function/Process Non-Fungal Related Genes/Proteins Protein Physical Properties Substrates/Ligands/Cofactors	Poznanski J and Szkopinska A (2007) Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae. Biopolymers 86(2):155-64	|SRT1
Cross-species Expression Function/Process	Perlinska-Lenart U, et al. (2006) Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation. Fungal Genet Biol 43(6):422-9	|DPM1 |PSA1
Function/Process Regulation of	Szkopinska A, et al. (2006) Interplay between the cis-prenyltransferases and polyprenol reductase in the yeast Saccharomyces cerevisiae. Biochimie 88(3-4):271-6	|ERG20 |ERG9 |SRT1
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Davierwala AP, et al. (2005) The synthetic genetic interaction spectrum of essential genes. Nat Genet 37(10):1147-52	|ABD1 |ACT1 |ALG13 |ALG14 |ALG7 |APC11 |ARL3 |ARP2 |ARP7 |ASK1 |AVO1 |BET3 |BET5 |BIM1 |MORE
Genetic Interactions Transcription	Grabinska K, et al. (2005) Functional relationships between the Saccharomyces cerevisiae cis-prenyltransferases required for dolichol biosynthesis. Acta Biochim Pol 52(1):221-32	|DPM1 |ERG20 |SRT1
Non-Fungal Related Genes/Proteins	Jones J, et al. (2005) Polyprenyl lipid synthesis in mammalian cells expressing human cis-prenyl transferase. Biochem Biophys Res Commun 331(2):379-83
Function/Process Mutants/Phenotypes Strains/Constructs	Davydenko SG, et al. (2004) Screening for novel essential genes of Saccharomyces cerevisiae involved in protein secretion. Yeast 21(6):463-71	|HSP150 |NOG2 |NOP15 |RPN5 |RRP40 |SDA1 |USE1
Function/Process Mutants/Phenotypes Strains/Constructs	Belgareh-Touze N, et al. (2003) Yeast functional analysis: identification of two essential genes involved in ER to Golgi trafficking. Traffic 4(9):607-17	|USE1
Cross-species Expression Non-Fungal Related Genes/Proteins Strains/Constructs	Endo S, et al. (2003) Identification of human dehydrodolichyl diphosphate synthase gene. Biochim Biophys Acta 1625(3):291-5	|SRT1
Cross-species Expression Function/Process Mutants/Phenotypes Non-Fungal Related Genes/Proteins Strains/Constructs	Shridas P, et al. (2003) Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells. Biochem Biophys Res Commun 312(4):1349-56	|SEC59
Function/Process Reviews	Grabinska K and Palamarczyk G (2002) Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase. FEMS Yeast Res 2(3):259-65	|ERG20 |HMG1 |HMG2 |SRT1 |YTA7
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Strains/Constructs Substrates/Ligands/Cofactors	Sato M, et al. (2001) Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6(6):495-506	|ERG6 |SRT1
Function/Process Fungal Related Genes/Proteins Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins Strains/Constructs	Schenk B, et al. (2001) An alternative cis-isoprenyltransferase activity in yeast that produces polyisoprenols with chain lengths similar to mammalian dolichols. Glycobiology 11(1):89-98	|SRT1
Genetic Interactions	Cullen PJ, et al. (2000) Defects in protein glycosylation cause SHO1-dependent activation of a STE12 signaling pathway in yeast. Genetics 155(3):1005-18	|ALG1 |DPM1 |FUS1 |HOG1 |KSS1 |MNN10 |OCH1 |PGI1 |PMI40 |PSA1 |SHO1 |SPT14 |STE11 |STE12 |MORE
Non-Fungal Related Genes/Proteins	Oh SK, et al. (2000) Molecular cloning, expression, and functional analysis of a cis-prenyltransferase from Arabidopsis thaliana. Implications in rubber biosynthesis. J Biol Chem 275(24):18482-8
Non-Fungal Related Genes/Proteins	Apfel CM, et al. (1999) Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene. J Bacteriol 181(2):483-92	|SRT1
Cellular Location DNA/RNA Sequence Features Function/Process Mutants/Phenotypes Non-Fungal Related Genes/Proteins Strains/Constructs	Kato J, et al. (1999) The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis. J Bacteriol 181(9):2733-8
Function/Process Fungal Related Genes/Proteins Mutants/Phenotypes Non-Fungal Related Genes/Proteins Strains/Constructs	Sato M, et al. (1999) The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol Cell Biol 19(1):471-83	|SEC12 |SEC59 |SRT1
DNA/RNA Sequence Features Mapping	Wolfe KH and Lohan AJ (1994) Sequence around the centromere of Saccharomyces cerevisiae chromosome II: similarity of CEN2 to CEN4. Yeast 10 Suppl A:S41-6	|CEN2 |CEN4 |COQ1 |HTA1 |HTA2 |NTH1 |NTH2
Mutants/Phenotypes Strains/Constructs	Nishikawa S and Nakano A (1993) Identification of a gene required for membrane protein retention in the early secretory pathway. Proc Natl Acad Sci U S A 90(17):8179-83	|KAR2 |RER1 |SEC12

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