UniProt ID | CRH1_YEAST | |
---|---|---|
UniProt AC | P53301 | |
Protein Name | Probable glycosidase CRH1 | |
Gene Name | CRH1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 507 | |
Subcellular Localization |
Secreted, cell wall. Membrane Lipid-anchor, GPI-anchor. Covalently-linked GPI-modified cell wall protein (GPI-CWP), localized particularly in chitin-rich areas. Found at the incipient bud site, around the septum area in later stages of budding, and |
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Protein Description | Probable glycosidase that plays a role in cell wall architecture. Required for the transfer of chitin to 1,6-beta-glucan in the cell wall.. | |
Protein Sequence | MKVLDLLTVLSASSLLSTFAAAESTATADSTTAASSTASCNPLKTTGCTPDTALATSFSEDFSSSSKWFTDLKHAGEIKYGSDGLSMTLAKRYDNPSLKSNFYIMYGKLEVILKAANGTGIVSSFYLQSDDLDEIDIEWVGGDNTQFQSNFFSKGDTTTYDRGEFHGVDTPTDKFHNYTLDWAMDKTTWYLDGESVRVLSNTSSEGYPQSPMYLMMGIWAGGDPDNAAGTIEWAGGETNYNDAPFTMYIEKVIVTDYSTGKKYTYGDQSGSWESIEADGGSIYGRYDQAQEDFAVLANGGSISSSSTSSSTVSSSASSTVSSSVSSTVSSSASSTVSSSVSSTVSSSSSVSSSSSTSPSSSTATSSKTLASSSVTTSSSISSFEKQSSSSSKKTVASSSTSESIISSTKTPATVSSTTRSTVAPTTQQSSVSSDSPVQDKGGVATSSNDVTSSTTQISSKYTSTIQSSSSEASSTNSVQISNGADLAQSLPREGKLFSVLVALLALL | |
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 |
---|---|---|---|---|---|
73 | Acetylation | SKWFTDLKHAGEIKY CCCCCCCCCCCCCEE | 33.93 | 24489116 | |
80 | Phosphorylation | KHAGEIKYGSDGLSM CCCCCCEECCCCCCE | 27.76 | 22369663 | |
82 | Phosphorylation | AGEIKYGSDGLSMTL CCCCEECCCCCCEEE | 25.97 | 22369663 | |
86 | Phosphorylation | KYGSDGLSMTLAKRY EECCCCCCEEEHHHC | 18.43 | 22369663 | |
88 | Phosphorylation | GSDGLSMTLAKRYDN CCCCCCEEEHHHCCC | 21.86 | 22369663 | |
117 | N-linked_Glycosylation | EVILKAANGTGIVSS EEEEHHHCCCCEEEE | 54.11 | - | |
177 | N-linked_Glycosylation | TPTDKFHNYTLDWAM CCCCCCCCCEEEECC | 34.32 | - | |
201 | N-linked_Glycosylation | ESVRVLSNTSSEGYP CEEEEEECCCCCCCC | 39.56 | - | |
261 | Ubiquitination | VTDYSTGKKYTYGDQ EECCCCCCEEECCCC | 42.57 | 23749301 | |
394 | Phosphorylation | SSSSSKKTVASSSTS CCCCCCCEECCCCCC | 25.66 | 28889911 | |
397 | Phosphorylation | SSKKTVASSSTSESI CCCCEECCCCCCHHH | 22.08 | 28889911 | |
398 | Phosphorylation | SKKTVASSSTSESII CCCEECCCCCCHHHH | 28.09 | 28889911 | |
399 | Phosphorylation | KKTVASSSTSESIIS CCEECCCCCCHHHHH | 33.19 | 28889911 | |
400 | Phosphorylation | KTVASSSTSESIISS CEECCCCCCHHHHHC | 38.16 | 28889911 | |
401 | Phosphorylation | TVASSSTSESIISST EECCCCCCHHHHHCC | 31.15 | 28889911 | |
403 | Phosphorylation | ASSSTSESIISSTKT CCCCCCHHHHHCCCC | 25.62 | 28889911 | |
406 | Phosphorylation | STSESIISSTKTPAT CCCHHHHHCCCCCCE | 30.22 | 28889911 | |
408 | Phosphorylation | SESIISSTKTPATVS CHHHHHCCCCCCEEC | 31.95 | 28889911 | |
410 | Phosphorylation | SIISSTKTPATVSST HHHHCCCCCCEECCC | 20.46 | 28889911 | |
415 | Phosphorylation | TKTPATVSSTTRSTV CCCCCEECCCCCCCC | 20.01 | 28889911 | |
416 | Phosphorylation | KTPATVSSTTRSTVA CCCCEECCCCCCCCC | 29.48 | 28889911 | |
417 | Phosphorylation | TPATVSSTTRSTVAP CCCEECCCCCCCCCC | 20.79 | 27017623 | |
418 | Phosphorylation | PATVSSTTRSTVAPT CCEECCCCCCCCCCC | 25.27 | 28889911 | |
482 | GPI-anchor | TNSVQISNGADLAQS CCEEEECCCHHHHHH | 51.83 | - |
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 CRH1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CRH1_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 CRH1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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