| UniProt ID | GAS1_YEAST | |
|---|---|---|
| UniProt AC | P22146 | |
| Protein Name | 1,3-beta-glucanosyltransferase GAS1 | |
| Gene Name | GAS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 559 | |
| Subcellular Localization |
Cell membrane Lipid-anchor, GPI-anchor . Secreted, cell wall . Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. |
|
| Protein Description | Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis.. | |
| Protein Sequence | MLFKSLSKLATAAAFFAGVATADDVPAIEVVGNKFFYSNNGSQFYIRGVAYQADTANETSGSTVNDPLANYESCSRDIPYLKKLNTNVIRVYAINTTLDHSECMKALNDADIYVIADLAAPATSINRDDPTWTVDLFNSYKTVVDTFANYTNVLGFFAGNEVTNNYTNTDASAFVKAAIRDVRQYISDKNYRKIPVGYSSNDDEDTRVKMTDYFACGDDDVKADFYGINMYEWCGKSDFKTSGYADRTAEFKNLSIPVFFSEYGCNEVTPRLFTEVEALYGSNMTDVWSGGIVYMYFEETNKYGLVSIDGNDVKTLDDFNNYSSEINKISPTSANTKSYSATTSDVACPATGKYWSAATELPPTPNGGLCSCMNAANSCVVSDDVDSDDYETLFNWICNEVDCSGISANGTAGKYGAYSFCTPKEQLSFVMNLYYEKSGGSKSDCSFSGSATLQTATTQASCSSALKEIGSMGTNSASGSVDLGSGTESSTASSNASGSSSKSNSGSSGSSSSSSSSSASSSSSSKKNAATNVKANLAQVVFTSIISLSIAAGVGFALV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 34 | Ubiquitination | AIEVVGNKFFYSNNG EEEEECCEEEECCCC | 30.81 | 15699485 | |
| 40 | N-linked_Glycosylation | NKFFYSNNGSQFYIR CEEEECCCCCEEEEE | 45.62 | - | |
| 57 | N-linked_Glycosylation | AYQADTANETSGSTV EEECCCCCCCCCCCC | 55.99 | - | |
| 92 | Phosphorylation | NTNVIRVYAINTTLD CCCEEEEEEEECCCC | 7.60 | 27017623 | |
| 95 | N-linked_Glycosylation | VIRVYAINTTLDHSE EEEEEEEECCCCHHH | 20.88 | - | |
| 149 | N-linked_Glycosylation | TVVDTFANYTNVLGF HHHHHHCCCCCEEEE | 39.71 | - | |
| 165 | N-linked_Glycosylation | AGNEVTNNYTNTDAS CCCCCCCCCCCCCHH | 35.32 | - | |
| 189 | Acetylation | VRQYISDKNYRKIPV HHHHHHCCCCCCCCC | 49.43 | 24489116 | |
| 189 | Ubiquitination | VRQYISDKNYRKIPV HHHHHHCCCCCCCCC | 49.43 | 22817900 | |
| 193 | Ubiquitination | ISDKNYRKIPVGYSS HHCCCCCCCCCCCCC | 40.79 | 23749301 | |
| 198 | Phosphorylation | YRKIPVGYSSNDDED CCCCCCCCCCCCCCC | 14.79 | 21440633 | |
| 200 | Phosphorylation | KIPVGYSSNDDEDTR CCCCCCCCCCCCCCC | 35.48 | 28889911 | |
| 206 | Phosphorylation | SSNDDEDTRVKMTDY CCCCCCCCCEEEEEE | 35.00 | 21440633 | |
| 211 | Phosphorylation | EDTRVKMTDYFACGD CCCCEEEEEEEECCC | 23.10 | 23749301 | |
| 216 | Glutathionylation | KMTDYFACGDDDVKA EEEEEEECCCCCCCC | 4.38 | 22833525 | |
| 226 | Phosphorylation | DDVKADFYGINMYEW CCCCCCCCEEECCEE | 20.04 | 23749301 | |
| 234 | Glutathionylation | GINMYEWCGKSDFKT EEECCEECCCCCCCC | 3.08 | 22833525 | |
| 240 | Ubiquitination | WCGKSDFKTSGYADR ECCCCCCCCCCCCCC | 46.93 | 23749301 | |
| 240 | Succinylation | WCGKSDFKTSGYADR ECCCCCCCCCCCCCC | 46.93 | 23954790 | |
| 240 | Acetylation | WCGKSDFKTSGYADR ECCCCCCCCCCCCCC | 46.93 | 22865919 | |
| 242 | Phosphorylation | GKSDFKTSGYADRTA CCCCCCCCCCCCCCH | 30.32 | 28889911 | |
| 253 | N-linked_Glycosylation | DRTAEFKNLSIPVFF CCCHHHCCCCCCEEE | 44.32 | - | |
| 283 | N-linked_Glycosylation | VEALYGSNMTDVWSG HHHHHCCCCCCCCCC | 32.77 | - | |
| 321 | N-linked_Glycosylation | KTLDDFNNYSSEINK CCHHHCCCCCHHHHC | 37.75 | - | |
| 337 | Ubiquitination | SPTSANTKSYSATTS CCCCCCCCCCEEECC | 47.40 | 23749301 | |
| 409 | N-linked_Glycosylation | DCSGISANGTAGKYG CCCCCCCCCCCCCCC | 41.37 | - | |
| 421 | Glutathionylation | KYGAYSFCTPKEQLS CCCCEECCCCHHHHH | 5.39 | 22833525 | |
| 441 | Phosphorylation | YYEKSGGSKSDCSFS EEECCCCCCCCCCCC | 32.29 | 25704821 | |
| 478 | Phosphorylation | SMGTNSASGSVDLGS CCCCCCCCCCEECCC | 31.27 | 25521595 | |
| 495 | N-linked_Glycosylation | ESSTASSNASGSSSK CCCCCCCCCCCCCCC | 35.31 | - | |
| 503 | Phosphorylation | ASGSSSKSNSGSSGS CCCCCCCCCCCCCCC | 37.87 | 28889911 | |
| 505 | Phosphorylation | GSSSKSNSGSSGSSS CCCCCCCCCCCCCCC | 47.33 | 28889911 | |
| 507 | Phosphorylation | SSKSNSGSSGSSSSS CCCCCCCCCCCCCCC | 31.20 | 25521595 | |
| 508 | Phosphorylation | SKSNSGSSGSSSSSS CCCCCCCCCCCCCCC | 46.34 | 28889911 | |
| 514 | Phosphorylation | SSGSSSSSSSSSASS CCCCCCCCCCCCCCC | 35.87 | 28889911 | |
| 516 | Phosphorylation | GSSSSSSSSSASSSS CCCCCCCCCCCCCCC | 30.20 | 25521595 | |
| 517 | Phosphorylation | SSSSSSSSSASSSSS CCCCCCCCCCCCCCC | 31.69 | 28889911 | |
| 528 | GPI-anchor | SSSSSKKNAATNVKA CCCCCHHHHHHHHHH | 38.25 | 1824714 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of GAS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GAS1_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of GAS1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| GPI-anchor | |
| Reference | PubMed |
| "Comprehensive proteomic analysis of Saccharomyces cerevisiae cellwalls: identification of proteins covalently attached viaglycosylphosphatidylinositol remnants or mild alkali-sensitivelinkages."; Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,de Koster C.G.; J. Biol. Chem. 280:20894-20901(2005). Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ANDPROBABLE GPI-ANCHOR. | |
| "The cell cycle modulated glycoprotein GP115 is one of the major yeastproteins containing glycosylphosphatidylinositol."; Vai M., Popolo L., Grandori R., Lacana E., Alberghina L.; Biochim. Biophys. Acta 1038:277-285(1990). Cited for: GPI-ANCHOR. | |
| "A major 125-kd membrane glycoprotein of Saccharomyces cerevisiae isattached to the lipid bilayer through an inositol-containingphospholipid."; Conzelmann A., Riezman H., Desponds C., Bron C.; EMBO J. 7:2233-2240(1988). Cited for: SUBCELLULAR LOCATION, AND GPI-ANCHOR. | |
| "Determinants for glycophospholipid anchoring of the Saccharomycescerevisiae GAS1 protein to the plasma membrane."; Nuoffer C., Jenoe P., Conzelmann A., Riezman H.; Mol. Cell. Biol. 11:27-37(1991). Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-39; 237-240;435-437 AND 527-528, SUBCELLULAR LOCATION, AND GPI-ANCHOR AT ASN-528. | |
