| UniProt ID | VAN1_YEAST | |
|---|---|---|
| UniProt AC | P23642 | |
| Protein Name | Mannan polymerase I complex VAN1 subunit | |
| Gene Name | VAN1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 535 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type II membrane protein . Golgi apparatus membrane Single-pass type II membrane protein . Cis-Golgi (PubMed:9430634). Recycles between endoplasmic reticulum and Golgi (PubMed:11095735). |
|
| Protein Description | Involved in regulation of the phosphorylation of a number of proteins, some of which appear to be important in cell growth control.; The M-Pol I complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins.. | |
| Protein Sequence | MGMFFNLRSNIKKKAMDNGLSLPISRNGSSNNIKDKRSEHNSNSLKGKYRYQPRSTPSKFQLTVSITSLIIIAVLSLYLFISFLSGMGIGVSTQNGRSLLGSSKSSENYKTIDLEDEEYYDYDFEDIDPEVISKFDDGVQHYLISQFGSEVLTPKDDEKYQRELNMLFDSTVEEYDLSNFEGAPNGLETRDHILLCIPLRNAADVLPLMFKHLMNLTYPHELIDLAFLVSDCSEGDTTLDALIAYSRHLQNGTLSQIFQEIDAVIDSQTKGTDKLYLKYMDEGYINRVHQAFSPPFHENYDKPFRSVQIFQKDFGQVIGQGFSDRHAVKVQGIRRKLMGRARNWLTANALKPYHSWVYWRDADVELCPGSVIQDLMSKNYDVIVPNVWRPLPTFLGTEQPYDLNSWMESQEALALAKTLDEDDVIVEGYAEYPTWRVHLAYIRDAEGDPNEAVDLDGVGGVSILAKAKIFRNGVQFPAFTFENHAETEAFGKMAKKMGYRVGGLPHYTIWHIYEPSDDDLKEIASREREKRRQSE | |
| 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 |
|---|---|---|---|---|---|
| 12 | Acetylation | FNLRSNIKKKAMDNG CCCCHHHHHHHHHCC | 53.09 | 25381059 | |
| 14 | Ubiquitination | LRSNIKKKAMDNGLS CCHHHHHHHHHCCCC | 43.89 | 23749301 | |
| 21 | Phosphorylation | KAMDNGLSLPISRNG HHHHCCCCCCCCCCC | 33.23 | 22890988 | |
| 25 | Phosphorylation | NGLSLPISRNGSSNN CCCCCCCCCCCCCCC | 20.11 | 22369663 | |
| 29 | Phosphorylation | LPISRNGSSNNIKDK CCCCCCCCCCCCCCC | 33.18 | 22369663 | |
| 30 | Phosphorylation | PISRNGSSNNIKDKR CCCCCCCCCCCCCCC | 34.98 | 22369663 | |
| 104 | Ubiquitination | RSLLGSSKSSENYKT CCCCCCCCCCCCCEE | 60.75 | 23749301 | |
| 215 | N-linked_Glycosylation | LMFKHLMNLTYPHEL HHHHHHHCCCCCHHH | 35.27 | - | |
| 251 | N-linked_Glycosylation | AYSRHLQNGTLSQIF HHHHHCCCCCHHHHH | 52.34 | - | |
| 312 | Ubiquitination | RSVQIFQKDFGQVIG CEEEEEECCHHHHHC | 44.25 | 17644757 | |
| 378 | Ubiquitination | VIQDLMSKNYDVIVP HHHHHHHCCCCEEEC | 45.63 | 17644757 | |
| 466 | Ubiquitination | GGVSILAKAKIFRNG CHHHHHHHHHHHCCC | 46.93 | 17644757 | |
| 521 | Ubiquitination | EPSDDDLKEIASRER CCCHHHHHHHHHHHH | 54.81 | 17644757 | |
| 521 | Acetylation | EPSDDDLKEIASRER CCCHHHHHHHHHHHH | 54.81 | 24489116 |
| 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 VAN1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VAN1_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 VAN1_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-25, AND MASSSPECTROMETRY. | |
