Module number 788




Database revision : gnsdb28.10
Date : Tue Feb 25 17:12:03 2003
How to read this figure?



mHIS3:imidazoleglycerol-phosphate dehydratase,imidazoleglycerol-ph\nosphate dehydratase,Null mutant is viable and requires histi\ndine\n mVPS75:Unknown ,, Unknown\n mCEG1:mRNA guanylyltransferase (mRNA capping enzyme), alpha subuni\nt,mRNA capping enzyme alpha subunit , mRNA guanylyltransfera\nse,Null mutant is inviable\n mOAF1:transcription factor,transcription factor,\n mYLR404W:Unknown ,, Unknown\n mVAC14:Unknown ,, Unknown\n Cond711:t2+Vec\n mYJR097W:Unknown ,, Unknown\n GCR1.gcr1:Understanding the growth phenotype of the yeast gcr1 mutant \nin terms of global genomic expression patterns.  J Bacteriol\n. 2000 Sep;182(17):4970-8.\n mMUP3:methionine uptake,very low affinity methionine permease,\n mAZR1:MFS-MDR,,\n mYLR077W:Unknown ,, Unknown\n mCAF17:CCR4 associated factor,CCR4 transcriptional complex componen\nt,Null mutant is viable, shows petite phenotype\n mROT1:Reversal of tor2 lethality,membrane protein (putative),Null \nmutant is inviable; rot1 mutations can suppress tor2 mutatio\nns; synthetically lethal with rot2\n mYGR012W:Unknown ,, Unknown\n mYKR051W:Unknown ,, Unknown\n mHRT2:High level expression reduced Ty3 Transposition,,Null mutant\n is viable; over-expression results in reduced Ty3 transposi\ntion\n mXDJ1:Homolog of E. coli DnaJ, closely related to Ydj1p,,Null muta\nnt is viable, displays no detectable phenotype\n mPAP1:poly(A) polymerase,poly(A) polymerase,lethal\n mYML079W:Unknown ,, Unknown\n mMSK1:mitochondrial lysine-tRNA synthetase,lysine-tRNA ligase,An u\nncharacterized allele is respiratory deficient.\n mSSP120:secretory protein,,Null mutant is viable\n mKIN2:Serine/threonine protein kinase,,\n Cond724:t4+SSD1,H44\n mGSH2:Glutathione Synthetase,glutathione synthetase,Null mutant is\n viable, growth was poor under aerobic conditions in minimum\n medium\n mARH1:adrenodoxin oxidoreductase homolog,adrenodoxin oxidoreductas\ne homolog,Null mutant is inviable\n Cond713:t4+Vec\n COMP.:Functional classification via a compendium of knockouts. Hug\nes et.al., cell 2000.\n mTAF14:Protein required for actin cytoskeleton assembly or function\n,transcription initiation factor TFIIF small subunit,Null mu\ntant is viable but has a depolarized actin cytoskeleton.\n mSMM1:Suppressor of Mitochondrial Mutation in the tRNAasp gene; Di\nhydrouridine synthase 2,tRNA dihydrouridine synthase,Overexp\nression weakly suppresses a mutation affecting the maturatio\nn of mitochondrial tRNA-Asp.\n mCKB1:beta (38kDa) subunit of casein kinase II (CKII),casein kinas\ne II beta subunit,Null mutant is viable, exhibits salt sensi\ntivity specific to NaCl and LiCl\n mLSB6:LAs17 Binding protein,,\n Cond718:t4+SSD1wt\n mYDR061W:Unknown ,, Unknown\n Cond709:t0+Vec\n mCYC1:iso-1-cytochrome c,iso-1-cytochrome c,Cytochrome c deficienc\ny\n mCYC2:Involved in import of cytochrome c into mitochondria,cytochr\nome c mitochondrial import factor,Null mutant is viable. Del\netion of CYC2 leads to accumulation of apocytochrome c in th\ne cytoplasm; strains with deletions of CYC2 still import low\n levels of cytochrome c into mitochondria\n mYKR016W:Unknown ,, Unknown\n mPPG1:Serine/threonine protein phosphatase involved in glycogen ac\ncumulation,,Null mutant is viable but accumulates less glyco\ngen\n mYDR316W:Unknown ,, Unknown\n mCNE1:Functions in endoplasmic reticulum protein quality control,c\nalnexin and calreticulin homolog,Null mutant is viable, incr\nease of cell-surface expression of ste2-3p, increase in secr\netion of heterologously expressed mammalian alpha 1-antitryp\nsin\n mGAA1:ER protein essential for attaching GPI (glycosylphosphatidyl\ninositol) to protein,GPI:protein transamidase component (put\native),Null mutant is inviable; temperature-sensitive mutant\n, after shifting to restrictive temperature, does not attach\n GPI to protein; also defective in endocytosis and pheromone\n response\n mRHO4:ras homolog--GTP binding protein,GTP-binding protein , ras h\nomolog,Null mutant is viable; rho3 rho4 cells are inviable a\nt 30 degrees C\n mMRPL3:Mitochondrial ribosomal protein MRPL3 (YmL3),ribosomal prote\nin (YmL3),\n mYKR070W:Unknown ,, Unknown\n mMRPL4:essential for mitochondrial function and for proper cell gro\nwth under non-respiratory conditions,ribosomal protein 60S L\n4,Null mutant is viable, fails to grow on nonfermentable car\nbon sources, has growth defects on fermentable carbon source\ns\n mGLR1:converts oxidized glutathine and NADPH into two glutathiones\n and NADP+,glutathione oxidoreductase,Null mutant is viable\n mRAM2:CAAX farnesyltransferase alpha subunit,CAAX farnesyltransfer\nase alpha subunit,lethal\n mNUP53:Component of karyopherin docking complex of the nuclear pore\n complex,karyopherin docking complex component of the nuclea\nr pore complex,Null mutant is viable but disrupts Kap121 loc\nalization to the nuclear envelope.\n Cond717:t2-SSD1\n mYKL071W:Unknown ,, Unknown\n mAPG7:autophagy,,Null mutant is viable, defective in autophagy\n mREX3:RNA EXonuclease; member of 3'->5' exonuclease family. See Mo\nser et al. 1997 Nucleic acids Res. 25:5110-5118,,Mutants exh\nibit RNase MRP RNA processing defect; functions redundantly \nwith REX1 and REX2 in U5 snRNA and RNase P RNA processing\n Cond725:t4-SSD1,M31\n Cond708:t0+SSD1\n mYDR287W:Unknown ,, Unknown\n Cond906:(77i5)_S150-2B_YPD_NormInt\n mNUP2:Localizes to discrete spots in the nuclear envelope; probabl\ny functions in transport through nuclear pore,nuclear pore c\nomplex subunit,Null mutant is viable; some combinations of a\nlleles of nup1, nsp1 and nup2 are synthetically lethal\n mSNF12:73 kDa subunit of the SWI/SNF transcription activation compl\nex, homolog of Rsc6p subunit of the RSC chromatin remodeling\n complex,RSC chromatin remodeling complex Rsc6p subunit homo\nlog , SWI/SNF transcription activation complex 73 kDa subuni\nt,Null mutant is viable but is temperature-sensitive, fails \nto transcribe SWI/SNF-dependent genes such as SUC2 and INO1,\n sucrose non-fermenting, defective in transcriptional activa\ntion by the glucocorticoid receptor; snf12 mutants are insen\nsitive to expression of Adenovirus E1A protein\n mNUP170:Component of yeast nuclear pore complex; may play a role in \nlocalizing specific nucleoporins to nuclear pore complex; Hi\ngh identity with Sc nucleoporin NUP157 & to mammalian nucleo\nporin Nup155p. Complemented with Nup155p,nuclear pore comple\nx subunit,Null mutant is viable; synthetically lethal with n\nup157, nup188, and pom152; changing NUP170 expression causes\n morphological abnormalities in nuclear envelope\n SGD.GO:Functional classification via a compendium of knockouts. Hug\nes et.al., cell 2000.\n Cond712:t4+SSD1\n mYBR159W:Unknown ,, Unknown\n mSSL1:Component of RNA polymerase transcription factor TFIIH,RNA p\nolymerase transcription factor TFIIH component,Null mutant i\ns inviable; temperature-sensitive mutants are UV-sensitive a\nnd deficient in nucleotide excision repair.\n mPSR2:Plasma membrane Sodium Response 2,,Mutant is sensitive to so\ndium ions.\n Cond723:t2-SSD1,M31\n mRFC3:RFC is a DNA binding protein and ATPase that acts as a proce\nssivity factor for DNA polymerases delta and epsilon and loa\nds proliferating cell nuclear antigen (PCNA) on DNA,replicat\nion factor C subunit 3 , similar to human RFC 36 kDa subunit\n,Null mutant is inviable\n mSLY1:Hydrophilic suppressor of ypt1 involved in vesicle trafficki\nng between ER and Golgi,,Null mutant is inviable; SLY1-20, w\nhich differs from wild-type SLY1 by a single amino acid, is \na single copy suppressor of loss of YPT1\n mRFC5:RFC is a multisubunit DNA binding protein and ATPase that ac\nts as a processivity factor for DNA polymerases delta and ep\nsilon and loads proliferating cell nuclear antigen (PCNA) on\n DNA,replication factor C subunit 5 , similar to human RFC 3\n8 kDa subunit,Null mutant is inviable\n mYMR040W:Unknown ,, Unknown\n mCBK1:cell wall biosynthesis kinase,protein kinase,Null mutation i\ns viable; shows alpha factor resistance; in liquid culture l\narge aggregates of cells are formed\n mMRP1:shows allele-specific genetic interactions with pet122 and p\net123,37 kDa mitochondrial ribosomal protein,defective mitoc\nhondrial protein synthesis; absence of a and b type cytochro\nmes; reduced levels of mitochondrial 15 S rRNA; defective pr\nocessing of apocytochrome b intron; convert to rho- and rho0\n at high frequency\n mSEH1:Nuclear pore protein, homologous to sec13,,\n mIMP2:Inner membrane protease (mitochondrial protein),protease,\n mMRP4:Involved in mitochondrial protein synthesis,mitochondrial ri\nbosomal protein , mitochondrial ribosome 37 S subunit compon\nent , similar to E. coli ribosomal protein S2,Null mutant is\n viable\n mKTR3:Putative alpha-1,2-mannosyltransferase,alpha-1,2-mannosyltra\nnsferase (putative),\n mOSM1:osmotic growth protein,osmotic growth protein,Null mutant is\n viable, sensitive to hypertonic medium\n mTAH11:Product of gene unknown,,tah11-1 mutant is hypersensitive to\n hydroxyurea, camptothecin when overexpressing wild-type TOP\n1\n Cond721:t0-SSD1,M31\n mCUE1:Cue1p assembles with Ubc7p. Cue1p recruits Ubc7p to the cyto\nsolic surface of the endoplasmic reticulum. Assembly with Cu\ne1p is a prerequisite for the function of Ubc7p,Ubc7p bindin\ng and recruitment protein,Null mutant is viable and shows st\nabilization of ER degradation substrates\n mMSB4:Multicopy Suppressor of Bud Emergence,,Null mutant is viable\n. msb3/msb4 double mutant exhibits slow growth and disorgani\nzed actin cytoskeleton\n mDID4:Hypothetical ORF,class E vacuolar-protein sorting and endocy\ntosis factor,secretion of vacuolar proteins; canavanine-hype\nrsensitive; temperature-sensitive; suppresses defects associ\nated with loss of Doa4\n mAOS1:along with Uba2p forms a heterodimeric activating enzyme for\n Smt3p,,Null mutant is inviable\n mCUE5:Unknown ,, Unknown\n mPTP1:phosphotyrosine-specific protein phosphatase,phosphotyrosine\n-specific protein phosphatase,viable\n Cond710:t2+SSD1\n mAPE2:Removal of intron fused YKL158W and YKL157W,aminopeptidase y\nscII,Null mutant is viable\n mRFC5 mRFC3

this is an automaticly generated SAMBA report
Computational Genomics Lab, Tel-Aviv uniresity