UniProt ID | ECM33_YEAST | |
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UniProt AC | P38248 | |
Protein Name | Cell wall protein ECM33 | |
Gene Name | ECM33 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 429 | |
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. |
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Protein Description | Required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall. Important for apical bud growth.. | |
Protein Sequence | MQFKNALTATAILSASALAANSTTSIPSSCSIGTSATATAQADLDKISGCSTIVGNLTITGDLGSAALASIQEIDGSLTIFNSSSLSSFSADSIKKITGDLNMQELIILTSASFGSLQEVDSINMVTLPAISTFSTDLQNANNIIVSDTTLESVEGFSTLKKVNVFNINNNRYLNSFQSSLESVSDSLQFSSNGDNTTLAFDNLVWANNITLRDVNSISFGSLQTVNASLGFINNTLPSLNLTQLSKVGQSLSIVSNDELSKAAFSNLTTVGGGFIIANNTQLKVIDGFNKVQTVGGAIEVTGNFSTLDLSSLKSVRGGANFDSSSSNFSCNALKKLQSNGAIQGDSFVCKNGATSTSVKLSSTSTESSKSSATSSASSSGDASNAQANVSASASSSSSSSKKSKGAAPELVPATSFMGVVAAVGVALL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
21 | N-linked_Glycosylation | SASALAANSTTSIPS HHHHHHCCCCCCCCC | 33.99 | - | |
56 | N-linked_Glycosylation | GCSTIVGNLTITGDL CCCEEEEEEEEECCC | 24.10 | - | |
82 | N-linked_Glycosylation | DGSLTIFNSSSLSSF CCCEEEECCCCCCCC | 36.81 | - | |
162 | 2-Hydroxyisobutyrylation | EGFSTLKKVNVFNIN CCCCCCEEEEEEECC | 42.00 | - | |
196 | N-linked_Glycosylation | QFSSNGDNTTLAFDN CCCCCCCCCEEEECC | 36.04 | - | |
209 | N-linked_Glycosylation | DNLVWANNITLRDVN CCEEEECCEEECCCC | 22.37 | - | |
227 | N-linked_Glycosylation | FGSLQTVNASLGFIN CCCCEEEEHHHCCHH | 27.48 | - | |
234 | N-linked_Glycosylation | NASLGFINNTLPSLN EHHHCCHHCCCCCCC | 32.92 | - | |
241 | N-linked_Glycosylation | NNTLPSLNLTQLSKV HCCCCCCCHHHHHHH | 45.43 | - | |
251 | Phosphorylation | QLSKVGQSLSIVSND HHHHHCCCEEEECCH | 20.39 | 28152593 | |
267 | N-linked_Glycosylation | LSKAAFSNLTTVGGG HHHHHHCCCEEECCC | 34.65 | - | |
279 | N-linked_Glycosylation | GGGFIIANNTQLKVI CCCEEECCCCEEEEE | 41.49 | - | |
304 | N-linked_Glycosylation | GAIEVTGNFSTLDLS EEEEEECCCEEEEHH | 20.52 | - | |
328 | N-linked_Glycosylation | NFDSSSSNFSCNALK CCCCCCCCCCHHHHH | 34.50 | - | |
339 | Phosphorylation | NALKKLQSNGAIQGD HHHHHHHHCCCCCCC | 47.90 | 21440633 | |
362 | Phosphorylation | TSTSVKLSSTSTESS EEEEEEEECCCCCCC | 26.33 | 19779198 | |
363 | Phosphorylation | STSVKLSSTSTESSK EEEEEEECCCCCCCC | 36.49 | 19779198 | |
389 | N-linked_Glycosylation | DASNAQANVSASASS CCCCCEEEEEECCCC | 19.05 | - | |
406 | GPI-anchor | SSSKKSKGAAPELVP CCCCCCCCCCCCCCC | 33.78 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ECM33_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ECM33_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 ECM33_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND MASSSPECTROMETRY. |