UniProt ID | MPI_YEAST | |
---|---|---|
UniProt AC | P29952 | |
Protein Name | Mannose-6-phosphate isomerase | |
Gene Name | PMI40 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 429 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.. | |
Protein Sequence | MSNKLFRLDAGYQQYDWGKIGSSSAVAQFAAHSDPSVQIEQDKPYAELWMGTHSKMPSYNHESKESLRDIISKNPSAMLGKDIIDKFHATNELPFLFKVLSIEKVLSIQAHPDKALGKILHAQDPKNYPDDNHKPEMAIAVTDFEGFCGFKPLQEIADELKRIPELRNIVGEETSRNFIENIQPSAQKGSPEDEQNKKLLQAVFSRVMNASDDKIKIQARSLVERSKNSPSDFNKPDLPELIQRLNKQFPDDVGLFCGCLLLNHCRLNAGEAIFLRAKDPHAYISGDIMECMAASDNVVRAGFTPKFKDVKNLVSMLTYTYDPVEKQKMQPLKFDRSSGNGKSVLYNPPIEEFAVLETTFDEKLGQRHFEGVDGPSILITTKGNGYIKADGQKLKAEPGFVFFIAPHLPVDLEAEDEAFTTYRAFVEPN | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MSNKLFRLD ------CCCCCEEEC | 42.55 | 1377774 | |
22 | Phosphorylation | YDWGKIGSSSAVAQF ECCCCCCCHHHHHHH | 25.29 | 21440633 | |
64 | Acetylation | PSYNHESKESLRDII CCCCCCCHHHHHHHH | 48.62 | 24489116 | |
73 | Acetylation | SLRDIISKNPSAMLG HHHHHHHHCHHHHCC | 63.57 | 24489116 | |
81 | Acetylation | NPSAMLGKDIIDKFH CHHHHCCHHHHHHHH | 41.62 | 24489116 | |
86 | Acetylation | LGKDIIDKFHATNEL CCHHHHHHHHHCCCC | 28.74 | 24489116 | |
104 | Ubiquitination | FKVLSIEKVLSIQAH HHHHCHHHHHHCCCC | 46.97 | 24961812 | |
107 | Phosphorylation | LSIEKVLSIQAHPDK HCHHHHHHCCCCCCH | 18.68 | 21440633 | |
114 | Acetylation | SIQAHPDKALGKILH HCCCCCCHHHHHHHH | 50.38 | 24489116 | |
161 | Acetylation | QEIADELKRIPELRN HHHHHHHCCCHHHHH | 46.35 | 24489116 | |
185 | Phosphorylation | FIENIQPSAQKGSPE HHHHCCHHHHCCCCH | 27.27 | 24909858 | |
197 | Succinylation | SPEDEQNKKLLQAVF CCHHHHHHHHHHHHH | 44.48 | 23954790 | |
198 | Acetylation | PEDEQNKKLLQAVFS CHHHHHHHHHHHHHH | 63.08 | 24489116 | |
214 | Ubiquitination | VMNASDDKIKIQARS HHCCCCCHHHHHHHH | 51.38 | 23749301 | |
214 | Acetylation | VMNASDDKIKIQARS HHCCCCCHHHHHHHH | 51.38 | 24489116 | |
229 | Phosphorylation | LVERSKNSPSDFNKP HHHHHCCCCCCCCCC | 29.53 | 28889911 | |
231 | Phosphorylation | ERSKNSPSDFNKPDL HHHCCCCCCCCCCCH | 55.44 | 28889911 | |
235 | Acetylation | NSPSDFNKPDLPELI CCCCCCCCCCHHHHH | 39.64 | 24489116 | |
306 | Acetylation | VRAGFTPKFKDVKNL EECCCCCCHHCHHHH | 63.09 | 24489116 | |
326 | Acetylation | YTYDPVEKQKMQPLK HCCCHHHHCCCCCCC | 56.29 | 24489116 | |
333 | Acetylation | KQKMQPLKFDRSSGN HCCCCCCCCCCCCCC | 52.48 | 24489116 | |
393 | Acetylation | YIKADGQKLKAEPGF EEEECCCEEEECCCE | 58.44 | 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 MPI_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MPI_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 MPI_YEAST !! |
Kegg Drug | ||||||
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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-107, AND MASSSPECTROMETRY. |