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UniProtKB/Swiss-Prot entry P24814


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GRR1_YEAST
Primary accession number P24814
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on March 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 87)
Name and origin of the protein
Protein name SCF E3 ubiquitin ligase complex F-box protein GRR1
Synonyms F-box and leucine-rich repeat protein GRR1
F-box/LRR-repeat protein GRR1
Gene name
Name: GRR1
Synonyms: CAT80, COT2
OrderedLocusNames: YJR090C
ORFNames: J1885
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND LEUCINE-RICH REPEATS.
PubMed=1922034 [NCBI, ExPASy, EBI, Israel, Japan]
Flick J.S., Johnston M.;
"GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats.";
Mol. Cell. Biol. 11:5101-5112(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/(SICI)1097-0061(199607)12:9<869::AID-YEA964>3.3.CO;2-T; PubMed=8840504 [NCBI, ExPASy, EBI, Israel, Japan]
Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
"Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI.";
Yeast 12:869-875(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
[4]
FUNCTION IN UBIQUITINATION OF CLN1 AND CLN2.
PubMed=7883165 [NCBI, ExPASy, EBI, Israel, Japan]
Barral Y., Jentsch S., Mann C.;
"G1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast.";
Genes Dev. 9:399-409(1995).
[5]
FUNCTION IN UBIQUITINATION OF GIC2.
DOI=10.1093/emboj/17.18.5360; PubMed=9736614 [NCBI, ExPASy, EBI, Israel, Japan]
Jaquenoud M., Gulli M.P., Peter K., Peter M.;
"The Cdc42p effector Gic2p is targeted for ubiquitin-dependent degradation by the SCFGrr1 complex.";
EMBO J. 17:5360-5373(1998).
[6]
IDENTIFICATION IN SCF COMPLEX, AND FUNCTION IN UBIQUITINATION OF CLN1.
DOI=10.1126/science.284.5414.662; PubMed=10213692 [NCBI, ExPASy, EBI, Israel, Japan]
Skowyra D., Koepp D.M., Kamura T., Conrad M.N., Conaway R.C., Conaway J.W., Elledge S.J., Harper J.W.;
"Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1.";
Science 284:662-665(1999).
[7]
INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(GRR1) COMPLEX.
DOI=10.1002/prot.10620; PubMed=14747994 [NCBI, ExPASy, EBI, Israel, Japan]
Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
"Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro.";
Proteins 54:455-467(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-300, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
  • FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. Probably constitutes the primary response element required for the generation or interpretation of the signal that induces glucose repression.
  • PATHWAY: Protein modification; protein ubiquitination.
  • SUBUNIT: Interacts with SKP1. Component of the probable SCF(GRR1) complex containing CDC53, SKP1, RBX1 and GRR1.
  • INTERACTION:
    P52286:SKP1; NbExp=2; IntAct=EBI-7898, EBI-4090;
  • SUBCELLULAR LOCATION: Membrane. Note=Associated with the particulate fraction. Probably forms a complex by protein-protein interactions via its leucine-rich segment.
  • INDUCTION: Expressed constitutively at low levels.
  • SIMILARITY: Contains 1 F-box domain.
  • SIMILARITY: Contains 12 LRR (leucine-rich) repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M59247; AAA34652.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49590; CAA89617.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L47993; AAB39313.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41529; A41529.
RefSeq NP_012623.1; -.
3D structure databases
ModBase P24814.
Protein-protein interaction databases
DIP DIP:1626N; -.
IntAct P24814; -.
Organism-specific databases
CYGD YJR090c; -.
SGD S000003850; GRR1.
Yeast-GFP YJR090C.
Gene expression databases
ArrayExpress P24814; -.
GermOnline YJR090C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0000142; Cellular component: cellular bud neck contractile ring (inferred from direct assay from SGD).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0019005; Cellular component: SCF ubiquitin ligase complex (inferred from mutant phenotype from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (traceable author statement from SGD).
GO:0000751; Biological process: cell cycle arrest in response to pheromone (inferred from mutant phenotype from SGD).
GO:0000082; Biological process: G1/S transition of mitotic cell cycle (traceable author statement from SGD).
GO:0006006; Biological process: glucose metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0016567; Biological process: protein ubiquitination (inferred from genetic interaction from SGD).
GO:0006974; Biological process: response to DNA damage stimulus (inferred from mutant phenotype from SGD).
GO:0031146; Biological process: SCF-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from physical interaction from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001810; F-box.
IPR001611; LRR.
Graphical view of domain structure.
Pfam PF00646; F-box; 1.
PF00560; LRR_1; 1.
Pfam graphical view of domain structure.
SMART SM00256; FBOX; 1.
SMART graphical view of domain structure.
PROSITE PS50181; FBOX; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P24814.
ProtoNet P24814.
Proteomic databases
PeptideAtlas P24814; -.
Genome annotation databases
Ensembl YJR090C; Saccharomyces cerevisiae. [Contig view]
GeneID 853552; -.
GenomeReviews Y13136_GR; YJR090C.
KEGG sce:YJR090C; -.
NMPDR fig|4932.3.peg.3597; -.
Phylogenomic databases
HOGENOM P24814; -.
Other
LinkHub P24814; -.
NextBio 974287; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Complete proteome; Glucose metabolism; Leucine-rich repeat; Membrane; Phosphoprotein; Repeat; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1151  1151     SCF E3 ubiquitin ligase complex F-box protein GRR1. PRO_0000119968
DOMAIN   314    361  48     F-box. 
REPEAT   409    434  26     LRR 1. 
REPEAT   435    460  26     LRR 2. 
REPEAT   461    486  26     LRR 3. 
REPEAT   487    512  26     LRR 4. 
REPEAT   513    548  36     LRR 5. 
REPEAT   549    567  19     LRR 6. 
REPEAT   568    593  26     LRR 7. 
REPEAT   594    619  26     LRR 8. 
REPEAT   620    645  26     LRR 9. 
REPEAT   646    670  25     LRR 10. 
REPEAT   671    699  29     LRR 11. 
REPEAT   700    726  27     LRR 12. 
COMPBIAS   38     49  12     Poly-Asn. 
COMPBIAS   1045   1124  80     Asn-rich. 
MOD_RES   199    199        Phosphoserine. 
MOD_RES   300    300        Phosphoserine. 
Sequence information
Length: 1151 AA [This is the length of the unprocessed precursor] Molecular weight: 132734 Da [This is the MW of the unprocessed precursor] CRC64: 6BB6C46611E6F825 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDQDNNNHND SNRLHPPDIH PNLGPQLWLN SSGDFDDNNN NNNNNNNNNS TRPQMPSRTR 

        70         80         90        100        110        120 
ETATSERNAS EVRDATLNNI FRFDSIQRET LLPTNNGQPL NQNFSLTFQP QQQTNALNGI 

       130        140        150        160        170        180 
DINTVNTNLM NGVNVQIDQL NRLLPNLPEE ERKQIHEFKL IVGKKIQEFL VVIEKRRKKI 

       190        200        210        220        230        240 
LNEIELDNLK LKELRIDNSP QAISYLHKLQ RMRLRALETE NMEIRNLRLK ILTIIEEYKK 

       250        260        270        280        290        300 
SLYAYCHSKL RGQQVENPTD NFIIWINSID TTESSDLKEG LQDLSRYSRQ FINNVLSNPS 

       310        320        330        340        350        360 
NQNICTSVTR RSPVFALNML PSEILHLILD KLNQKYDIVK FLTVSKLWAE IIVKILYYRP 

       370        380        390        400        410        420 
HINKKSQLDL FLRTMKLTSE ETVFNYRLMI KRLNFSFVGD YMHDTELNYF VGCKNLERLT 

       430        440        450        460        470        480 
LVFCKHITSV PISAVLRGCK FLQSVDITGI RDVSDDVFDT LATYCPRVQG FYVPQARNVT 

       490        500        510        520        530        540 
FDSLRNFIVH SPMLKRIKIT ANNNMNDELV ELLANKCPLL VEVDITLSPN VTDSSLLKLL 

       550        560        570        580        590        600 
TRLVQLREFR ITHNTNITDN LFQELSKVVD DMPSLRLIDL SGCENITDKT IESIVNLAPK 

       610        620        630        640        650        660 
LRNVFLGKCS RITDASLFQL SKLGKNLQTV HFGHCFNITD NGVRALFHSC TRIQYVDFAC 

       670        680        690        700        710        720 
CTNLTNRTLY ELADLPKLKR IGLVKCTQMT DEGLLNMVSL RGRNDTLERV HLSYCSNLTI 

       730        740        750        760        770        780 
YPIYELLMSC PRLSHLSLTA VPSFLRPDIT MYCRPAPSDF SENQRQIFCV FSGKGVHKLR 

       790        800        810        820        830        840 
HYLVNLTSPA FGPHVDVNDV LTKYIRSKNL IFNGETLEDA LRRIITDLNQ DSAAIIAATG 

       850        860        870        880        890        900 
LNQINGLNND FLFQNINFER IDEVFSWYLN TFDGIRMSSE EVNSLLLQVN KTFCEDPFSD 

       910        920        930        940        950        960 
VDDDQDYVVA PGVNREINSE MCHIVRKFHE LNDHIDDFEV NVASLVRVQF QFTGFLLHEM 

       970        980        990       1000       1010       1020 
TQTYMQMIEL NRQICLVQKT VQESGNIDYQ KGLLIWRLLF IDKFIMVVQK YKLSTVVLRL 

      1030       1040       1050       1060       1070       1080 
YLKDNITLLT RQRELLIAHQ RSAWNNNNDN DANRNANNIV NIVSDAGAND TSNNETNNGN 

      1090       1100       1110       1120       1130       1140 
DDNETENPNF WRQFGNRMQI SPDQMRNLQM GLRNQNMVRN NNNNTIDESM PDTAIDSQMD 

      1150 
EASGTPDEDM L 

P24814 in FASTA format

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