| UniProt ID | BCH2_YEAST | |
|---|---|---|
| UniProt AC | P36122 | |
| Protein Name | Protein BCH2 | |
| Gene Name | BCH2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 765 | |
| Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Peripheral membrane protein . Trans-Golgi network location requires interaction with CHS5 and with myristoylated GTP-bound ARF1 for the recruitment to the membranes. |
|
| Protein Description | Member of the CHS5-ARF1P-binding proteins (CHAPS) which mediates export of specific cargo proteins, including chitin synthase CHS3.. | |
| Protein Sequence | MSFLWGSTKSKKGKNKKAAGSLPSGVVPQQRVKPTRKNVPIDYPRTLEKVHGESLIFRTSLLSELVSTGKSGIGPPDLIHCTELDKFHDEKIGEFFYITGIDASSVSMPIAFLKLIKWNDGKKLKSASLKNDDITTYCTFNIFQKLDIRLRYESEDVYQVNIVDCLNGNNEIPLSDLIWEETFVSCCIRSVIINSDFERKIPGLVELPFVFENRCASDYKRVIDSLCKFLPRFLECGWDSTKSVYATILNNYLTESLLVFLSITPEFITDYAIQVLDNLMTNDPSNSRYYAIVIISIMERSNDRDVEMIKRIHEILDLLLPVLYGLPSDEPYISDLINCITDVLSIQARFLLNNNDYELSLSISTLATNLSSDNFESWYLLSKGYIFSQQYDKALLSINSMPCLAEYDIVKQAQINAFKFYMNYYKAPLCHSREHCTMTSHELNHLMNIMHYENELELKTIIFGRTVMPNESKYGCIEEIWNKSCLELGPICGPQSDNLINFVSQQEVNTVGDMLLLKRSKETRQESWFIKQVRLLLMELVARIGWNALLQLRSDVFVMESKFKMIESSDKLSTELRQKRLCQRWFDAMFLDVYEDLSISTSSQENKATAKYSGLEWELLGLTLLRVSDLPDAVACLRTSILARFDPISCHHLLNFYLTMDFNDEFMRRFDVDIILDLLVKLISFRIRFYDRFQIFSLQVLRKLEGQLGSEIIKNKIINSPYGQAGITSVIDYMLECLSKNRNEACLAYERPLPDLPSTIKPLAD | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MSFLWGSTKSKKGKN CCCCCCCCCCCCCCC | 35.08 | 30377154 | |
| 46 | Phosphorylation | VPIDYPRTLEKVHGE CCCCCCCCHHHHCCC | 34.46 | 27017623 | |
| 114 | Ubiquitination | SMPIAFLKLIKWNDG CCCHHHHHHHHCCCC | 41.53 | 22817900 | |
| 117 | Ubiquitination | IAFLKLIKWNDGKKL HHHHHHHHCCCCCCC | 50.83 | 22817900 | |
| 504 | Phosphorylation | DNLINFVSQQEVNTV CCHHHHCCHHHCCCH | 23.24 | 28889911 | |
| 568 | Phosphorylation | SKFKMIESSDKLSTE HHHHEHHCCCCCCHH | 32.67 | 24961812 | |
| 569 | Phosphorylation | KFKMIESSDKLSTEL HHHEHHCCCCCCHHH | 26.44 | 25752575 | |
| 573 | Phosphorylation | IESSDKLSTELRQKR HHCCCCCCHHHHHHH | 26.10 | 30377154 | |
| 649 | Phosphorylation | LARFDPISCHHLLNF HHHCCCCCHHHHHHE | 16.88 | 27017623 |
| 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 BCH2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BCH2_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 BCH2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND SER-569, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568, AND MASSSPECTROMETRY. | |