| Standard Name | YPT1 1 |
|---|---|
| Systematic Name | YFL038C |
| Feature Type | ORF, Verified |
| Description | Rab family GTPase, involved in the ER-to-Golgi step of the secretory pathway; complex formation with the Rab escort protein Mrs6p is required for prenylation of Ypt1p by protein geranylgeranyltransferase type II (Bet2p-Bet4p) (2, 3 and see Summary Paragraph) Also known as: YP2 |
| Name Description | Yeast Protein Two 1 |
| Chromosomal Location | |
|---|---|
| Note: this feature is encoded on the Crick strand. | |
| Genetic position: -59 cM |
| View Computational GO annotations for YPT1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated |
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| Cellular Component | |
| Manually curated | |
| High-throughput |
| Classical genetics | |
|---|---|
| conditional |
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| null | |
| repressible | |
| Large-scale survey | |
| conditional | |
| null | |
| overexpression | |
| reduction of function | |
| Resources |
| 177 total interaction(s) for 90 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| Note: this feature is encoded on the Crick strand. | |||||||||||||
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| Genetic position: -59 cM | |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
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| Retrieve sequences | |||||||||||||
| S288C only | |
|---|---|
| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000001856 |
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Rab proteins are small Ras-related GTPases that function in multiple stages in membrane traffic. Rabs continuously cycle between the cytosol and membranes. The GDP-bound form of the Rab is complexed with
Ypt1p is a Rab GTPase required for vesicle docking and fidelity of vesicle targeting during ER to Golgi and intra Golgi trafficking (7, reviewed in 5). The docking and tethering step, mediated by Ypt1p, Uso1p, the Sec34/35 complex and the TRAPP complex, occurs before SNARE complex assembly and vesicle fusion (8, 9, 3). Activation of Ypt1p to the GTP-bound form is mediated by the guanine nucleotide exchange factor (GEF) TRAPP1 complex. The GTP-bound Ypt1p regulates the assembly of the SNARE proteins consisting of Sed5p, Bet1p, Bos1p and Sly1p. Gyp1p, the GTPase-activating protein (GAP) stimulates the hydrolysis of GTP to GDP and serves as a negative regulator of Ypt1p(10)
| 1) | Gallwitz D, et al. (1983) A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product. Nature 306(5944):704-7 |
| 2) | Miaczynska M, et al. (1997) The yeast Rab escort protein binds intracellular membranes in vivo and in vitro. J Biol Chem 272(27):16972-7 |
| 3) | Morsomme P and Riezman H (2002) The Rab GTPase Ypt1p and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus. Dev Cell 2(3):307-17 |
| 4) | Cai H, et al. (2007) Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev Cell 12(5):671-82 |
| 5) | Grosshans BL, et al. (2006) Rabs and their effectors: achieving specificity in membrane traffic. Proc Natl Acad Sci U S A 103(32):11821-7 |
| 6) | Bialek-Wyrzykowska U, et al. (2000) Low levels of Ypt protein prenylation cause vesicle polarization defects and thermosensitive growth that can be suppressed by genes involved in cell wall maintenance. Mol Microbiol 35(6):1295-311 |
| 7) | Jedd G, et al. (1995) The Ypt1 GTPase is essential for the first two steps of the yeast secretory pathway. J Cell Biol 131(3):583-90 |
| 8) | Cai Y, et al. (2008) The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. Cell 133(7):1202-13 |
| 9) | Cao X, et al. (1998) Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J 17(8):2156-65 |
| 10) | Du LL, et al. (1998) Identification of a Sec4p GTPase-activating protein (GAP) as a novel member of a Rab GAP family. J Biol Chem 273(6):3253-6 |






