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P01123

- YPT1_YEAST

UniProt

P01123 - YPT1_YEAST

Protein

GTP-binding protein YPT1

Gene

YPT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Involved in the trafficking of secretory vesicles from the endoplasmic reticulum (ER) to the Golgi. Regulates correct targeting and tethering of vesicles to target membranes by catalyzing the selective recruitment of proteins required for tethering and fusion onto membranes. Vesicular transport depends on shuttling of YPT1 between membrane and cytosol by GDI1, probably by recycling it to its membrane of origin after a vesicle fusion event. Required for sorting and transport of proteins from the ER through the Golgi compartment. Also involved in the recycling of membrane proteins.5 Publications

    Enzyme regulationi

    Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the guanine nucleotide-exchange factors (GEFs) DSS4 and TRAPP complex, and inactivated by GTPase-activating proteins (GAPs) GYP1, GYP5 and GYP8.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 228GTPBy similarity
    Nucleotide bindingi63 – 675GTPBy similarity
    Nucleotide bindingi121 – 1244GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: SGD
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. SNARE binding Source: SGD

    GO - Biological processi

    1. COPII-coated vesicle budding Source: SGD
    2. CVT pathway Source: SGD
    3. early endosome to Golgi transport Source: SGD
    4. endocytic recycling Source: SGD
    5. ER to Golgi vesicle-mediated transport Source: SGD
    6. Golgi vesicle budding Source: SGD
    7. Golgi vesicle docking Source: SGD
    8. GTP catabolic process Source: GOC
    9. macroautophagy Source: SGD
    10. pre-mRNA catabolic process Source: SGD
    11. protein complex assembly Source: SGD
    12. regulation of endoplasmic reticulum unfolded protein response Source: SGD
    13. retrograde vesicle-mediated transport, Golgi to ER Source: SGD
    14. small GTPase mediated signal transduction Source: InterPro
    15. SNARE complex disassembly Source: SGD

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30424-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP-binding protein YPT1
    Alternative name(s):
    Protein YP2
    Rab GTPase YPT1
    Transport GTPase YPT1
    Gene namesi
    Name:YPT1
    Synonyms:YP2
    Ordered Locus Names:YFL038C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VI

    Organism-specific databases

    CYGDiYFL038c.
    SGDiS000001856. YPT1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication. Golgi apparatus membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasm 1 Publication
    Note: ER and Golgi when GTP-bound. Cytoplasmic when bound to GDI1.

    GO - Cellular componenti

    1. cytoplasmic vesicle Source: SGD
    2. endoplasmic reticulum membrane Source: SGD
    3. Golgi membrane Source: SGD
    4. Golgi stack Source: SGD
    5. pre-autophagosomal structure Source: SGD
    6. trans-Golgi network Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171S → G: Decreases GTP binding and increases GTP hydrolysis. 2 Publications
    Mutagenesisi21 – 211K → M: Abolishes GTP binding. 2 Publications
    Mutagenesisi37 – 371Y → F: No change. 2 Publications
    Mutagenesisi39 – 391S → A: No change. 2 Publications
    Mutagenesisi40 – 401T → S: No change. 2 Publications
    Mutagenesisi41 – 411I → M: Lethal. 2 Publications
    Mutagenesisi43 – 431V → E: No change. 2 Publications
    Mutagenesisi44 – 441D → N: Temperature-sensitive phenotype. 2 Publications
    Mutagenesisi65 – 651A → T: Decreases GTP binding and GTP hydrolysis. 2 Publications
    Mutagenesisi67 – 671Q → L: Locks YPT1 in the GTP-bound form by reducing GTP hydrolysis rate 40-fold. 3 Publications
    Mutagenesisi121 – 1211N → I: Abolishes GTP binding. 2 Publications
    Mutagenesisi136 – 1361A → D: Loss of function at 37 degrees Celsius. 2 Publications
    Mutagenesisi205 – 2051C → S: Abolishes membrane association. Lethal; when associated with S-206. 3 Publications
    Mutagenesisi206 – 2061C → S: Abolishes membrane association. Lethal; when associated with S-205. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 206206GTP-binding protein YPT1PRO_0000121318Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Lipidationi23 – 231S-palmitoyl cysteineSequence Analysis
    Lipidationi123 – 1231S-palmitoyl cysteineSequence Analysis
    Modified residuei172 – 1721Phosphoserine1 Publication
    Modified residuei174 – 1741Phosphoserine1 Publication
    Lipidationi205 – 2051S-geranylgeranyl cysteine1 Publication
    Lipidationi206 – 2061S-geranylgeranyl cysteine1 Publication

    Post-translational modificationi

    Prenylation is required for interaction with GDI1 and YIP1.1 Publication

    Keywords - PTMi

    Acetylation, Lipoprotein, Palmitate, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP01123.
    PaxDbiP01123.
    PeptideAtlasiP01123.
    PRIDEiP01123.

    Expressioni

    Gene expression databases

    GenevestigatoriP01123.

    Interactioni

    Subunit structurei

    Forms a complex with the Rab escort protein (REP) MRS6, which is recognized by Rab geranylgeranyltransferase BET2-BET4. Interacts with the Rab GDP dissociation inhibitor GDI1, which can retrieve from and deliver to membranes the GDP-bound and prenylated form of YPT1. Interacts with YIP1, which is required for proper membrane targeting of prenylated YPT1. Interacts with YIF1, YIP3, YIP4 and YIP5.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GDI1P399585EBI-29496,EBI-7517
    YIF1P538453EBI-29496,EBI-28230
    YIP3P536332EBI-29496,EBI-25301
    YIP4P530932EBI-29496,EBI-24124

    Protein-protein interaction databases

    BioGridi31108. 132 interactions.
    DIPiDIP-2019N.
    IntActiP01123. 23 interactions.
    MINTiMINT-389361.
    STRINGi4932.YFL038C.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 1611
    Helixi21 – 3010
    Beta strandi45 – 528
    Beta strandi55 – 628
    Turni65 – 717
    Helixi75 – 784
    Beta strandi82 – 898
    Helixi93 – 10917
    Beta strandi115 – 1217
    Turni126 – 1283
    Helixi133 – 14210
    Beta strandi147 – 1493
    Turni152 – 1543
    Helixi158 – 17215
    Helixi175 – 1795
    Helixi183 – 1853

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UKVX-ray1.50Y1-206[»]
    1YZNX-ray2.06A3-172[»]
    2BCGX-ray1.48Y1-206[»]
    3CUEX-ray3.70F/L/R/X1-206[»]
    ProteinModelPortaliP01123.
    SMRiP01123. Positions 3-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01123.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni63 – 8018Interaction with GDI1Add
    BLAST
    Regioni189 – 1957Interaction with GDI1

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 459Effector regionCurated

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rab family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00720000108592.
    HOGENOMiHOG000233968.
    KOiK07874.
    OMAiTMHASEY.
    OrthoDBiEOG7BGHXR.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view]
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00175. RAB. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51419. RAB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P01123-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSEYDYLFK LLLIGNSGVG KSCLLLRFSD DTYTNDYIST IGVDFKIKTV    50
    ELDGKTVKLQ IWDTAGQERF RTITSSYYRG SHGIIIVYDV TDQESFNGVK 100
    MWLQEIDRYA TSTVLKLLVG NKCDLKDKRV VEYDVAKEFA DANKMPFLET 150
    SALDSTNVED AFLTMARQIK ESMSQQNLNE TTQKKEDKGN VNLKGQSLTN 200
    TGGGCC 206
    Length:206
    Mass (Da):23,214
    Last modified:November 1, 1995 - v2
    Checksum:iF8C704F6BF2D227B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711E → Q in CAA25036. (PubMed:6318115)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00209 Genomic DNA. Translation: CAA25036.1.
    D50617 Genomic DNA. Translation: BAA09201.1.
    AY558467 Genomic DNA. Translation: AAS56793.1.
    BK006940 Genomic DNA. Translation: DAA12402.1.
    PIRiS56216. TVBYQ2.
    RefSeqiNP_116615.1. NM_001179928.1.

    Genome annotation databases

    EnsemblFungiiYFL038C; YFL038C; YFL038C.
    GeneIDi850505.
    KEGGisce:YFL038C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00209 Genomic DNA. Translation: CAA25036.1 .
    D50617 Genomic DNA. Translation: BAA09201.1 .
    AY558467 Genomic DNA. Translation: AAS56793.1 .
    BK006940 Genomic DNA. Translation: DAA12402.1 .
    PIRi S56216. TVBYQ2.
    RefSeqi NP_116615.1. NM_001179928.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UKV X-ray 1.50 Y 1-206 [» ]
    1YZN X-ray 2.06 A 3-172 [» ]
    2BCG X-ray 1.48 Y 1-206 [» ]
    3CUE X-ray 3.70 F/L/R/X 1-206 [» ]
    ProteinModelPortali P01123.
    SMRi P01123. Positions 3-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31108. 132 interactions.
    DIPi DIP-2019N.
    IntActi P01123. 23 interactions.
    MINTi MINT-389361.
    STRINGi 4932.YFL038C.

    Proteomic databases

    MaxQBi P01123.
    PaxDbi P01123.
    PeptideAtlasi P01123.
    PRIDEi P01123.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YFL038C ; YFL038C ; YFL038C .
    GeneIDi 850505.
    KEGGi sce:YFL038C.

    Organism-specific databases

    CYGDi YFL038c.
    SGDi S000001856. YPT1.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00720000108592.
    HOGENOMi HOG000233968.
    KOi K07874.
    OMAi TMHASEY.
    OrthoDBi EOG7BGHXR.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30424-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P01123.
    NextBioi 966209.
    PROi P01123.

    Gene expression databases

    Genevestigatori P01123.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003579. Small_GTPase_Rab_type.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00175. RAB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51419. RAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product."
      Gallwitz D., Donath C., Sander C.
      Nature 306:704-707(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Bienvenut W.V., Peters C.
      Submitted (MAY-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-46; 49-55; 59-69; 72-79; 101-116 AND 130-167, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Biochemical properties of the ras-related YPT protein in yeast: a mutational analysis."
      Wagner P., Molenaar C.M.T., Rauh A.J.G., Broekel R., Schmitt H.D., Gallwitz D.
      EMBO J. 6:2373-2379(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-17; LYS-21; ALA-65 AND ASN-121.
    7. "A carboxyl-terminal cysteine residue is required for palmitic acid binding and biological activity of the ras-related yeast YPT1 protein."
      Molenaar C.M.T., Prange R., Gallwitz D.
      EMBO J. 7:971-976(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-23 AND CYS-123, MUTAGENESIS OF CYS-205 AND CYS-206.
    8. "Study of a temperature-sensitive mutant of the ras-related YPT1 gene product in yeast suggests a role in the regulation of intracellular calcium."
      Schmitt H.D., Puzicha M., Gallwitz D.
      Cell 53:635-647(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS, POSSIBLE FUNCTION.
    9. "Mutational analysis of the putative effector domain of the GTP-binding Ypt1 protein in yeast suggests specific regulation by a novel GAP activity."
      Becker J., Tan T.J., Trepte H.-H., Gallwitz D.
      EMBO J. 10:785-792(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-37; SER-39; THR-40; ILE-41; VAL-43 AND ASP-44.
    10. "The Ypt1 GTPase is essential for the first two steps of the yeast secretory pathway."
      Jedd G., Richardson C.J., Litt R.J., Segev N.
      J. Cell Biol. 131:583-590(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ALA-136.
    11. "Amino- and carboxy-terminal domains of the yeast Rab escort protein are both required for binding of Ypt small G proteins."
      Bauer B.E., Lorenzetti S., Miaczynska M., Bui D.M., Schweyen R.J., Ragnini A.
      Mol. Biol. Cell 7:1521-1533(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MRS6.
    12. "GTP hydrolysis is not important for Ypt1 GTPase function in vesicular transport."
      Richardson C.J., Jones S., Litt R.J., Segev N.
      Mol. Cell. Biol. 18:827-838(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLN-67.
    13. "Distinct subclasses of small GTPases interact with guanine nucleotide exchange factors in a similar manner."
      Day G.-J., Mosteller R.D., Broek D.
      Mol. Cell. Biol. 18:7444-7454(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    14. "Functional implications of genetic interactions between genes encoding small GTPases involved in vesicular transport in yeast."
      Yoo J.S., Grabowski R., Xing L., Trepte H.H., Schmitt H.D., Gallwitz D.
      Mol. Gen. Genet. 261:80-91(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-205 AND CYS-206, MUTAGENESIS OF CYS-205 AND CYS-206, FUNCTION.
    15. "The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32."
      Jones S., Newman C., Liu F., Segev N.
      Mol. Biol. Cell 11:4403-4411(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    16. "Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus and is a negative regulator of Ypt1p."
      Du L.-L., Novick P.
      Mol. Biol. Cell 12:1215-1226(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    17. "Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab proteins."
      Calero M., Collins R.N.
      Biochem. Biophys. Res. Commun. 290:676-681(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YIP3.
    18. "The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus."
      Morsomme P., Riezman H.
      Dev. Cell 2:307-317(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Identification of the novel proteins Yip4p and Yip5p as Rab GTPase interacting factors."
      Calero M., Winand N.J., Collins R.N.
      FEBS Lett. 515:89-98(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YIF1; YIP4 AND YIP5.
    20. "Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs."
      De Antoni A., Schmitzova J., Trepte H.-H., Gallwitz D., Albert S.
      J. Biol. Chem. 277:41023-41031(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    21. "Dual prenylation is required for Rab protein localization and function."
      Calero M., Chen C.Z., Zhu W., Winand N.J., Havas K.A., Gilbert P.M., Burd C.G., Collins R.N.
      Mol. Biol. Cell 14:1852-1867(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YIP1, SUBCELLULAR LOCATION.
    22. "The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p."
      Lafourcade C., Galan J.-M., Gloor Y., Haguenauer-Tsapis R., Peter M.
      Mol. Cell. Biol. 24:3815-3826(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLN-67.
    23. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase."
      Rak A., Pylypenko O., Durek T., Watzke A., Kushnir S., Brunsveld L., Waldmann H., Goody R.S., Alexandrov K.
      Science 302:646-650(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH GDI1.

    Entry informationi

    Entry nameiYPT1_YEAST
    AccessioniPrimary (citable) accession number: P01123
    Secondary accession number(s): D6VTJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 164 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    In PubMed:3042385 the location of any palmitoylation was not determined. Mutagenesis of either Cys-205 or Cys-206 would disrupt normal geranylgeranylation, and there would be no primary membrane association for secondary S-palmitoylation to occur at some other position, for example Cys-23. Mutagenesis of both Cys-205 and Cys-206 is lethal, so protein production could not have been observed.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VI
      Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

    External Data

    Dasty 3