| UniProt ID | PMT2_YEAST | |
|---|---|---|
| UniProt AC | P31382 | |
| Protein Name | Dolichyl-phosphate-mannose--protein mannosyltransferase 2 {ECO:0000305} | |
| Gene Name | PMT2 {ECO:0000303|PubMed:8543034} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 759 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.. | |
| Protein Sequence | MSSSSSTGYSKNNAAHIKQENTLRQRESSSISVSEELSSADERDAEDFSKEKPAAQSSLLRLESVVMPVIFTALALFTRMYKIGINNHVVWDEAHFGKFGSYYLRHEFYHDVHPPLGKMLVGLSGYLAGYNGSWDFPSGEIYPDYLDYVKMRLFNASFSALCVPLAYFTAKAIGFSLPTVWLMTVLVLFENSYSTLGRFILLDSMLLFFTVASFFSFVMFHNQRSKPFSRKWWKWLLITGISLGCTISVKMVGLFIITMVGIYTVIDLWTFLADKSMSWKTYINHWLARIFGLIIVPFCIFLLCFKIHFDLLSHSGTGDANMPSLFQARLVGSDVGQGPRDIALGSSVVSIKNQALGGSLLHSHIQTYPDGSNQQQVTCYGYKDANNEWFFNRERGLPSWSENETDIEYLKPGTSYRLVHKSTGRNLHTHPVAAPVSKTQWEVSGYGDNVVGDNKDNWVIEIMDQRGDEDPEKLHTLTTSFRIKNLEMGCYLAQTGNSLPEWGFRQQEVVCMKNPFKRDKRTWWNIETHENERLPPRPEDFQYPKTNFLKDFIHLNLAMMATNNALVPDPDKFDYLASSAWQWPTLNVGLRLCGWGDDNPKYFLLGTPASTWASSVAVLAFMATVVILLIRWQRQYVDLRNPSNWNVFLMGGFYPLLAWGLHYMPFVIMSRVTYVHHYLPALYFALIILAYCFDAGLQKWSRSKCGRIMRFVLYAGFMALVIGCFWYFSPISFGMEGPSSNFRYLNWFSTWDIADKQEA | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSSSSSTGY ------CCCCCCCCC | 38.64 | 22814378 | |
| 2 | Phosphorylation | ------MSSSSSTGY ------CCCCCCCCC | 38.64 | 30377154 | |
| 3 | Phosphorylation | -----MSSSSSTGYS -----CCCCCCCCCC | 32.70 | 30377154 | |
| 4 | Phosphorylation | ----MSSSSSTGYSK ----CCCCCCCCCCC | 22.47 | 30377154 | |
| 5 | Phosphorylation | ---MSSSSSTGYSKN ---CCCCCCCCCCCC | 33.59 | 30377154 | |
| 6 | Phosphorylation | --MSSSSSTGYSKNN --CCCCCCCCCCCCC | 28.00 | 30377154 | |
| 7 | Phosphorylation | -MSSSSSTGYSKNNA -CCCCCCCCCCCCCH | 41.93 | 28889911 | |
| 9 | Phosphorylation | SSSSSTGYSKNNAAH CCCCCCCCCCCCHHH | 19.29 | 28889911 | |
| 10 | Phosphorylation | SSSSTGYSKNNAAHI CCCCCCCCCCCHHHH | 30.19 | 30377154 | |
| 11 | Acetylation | SSSTGYSKNNAAHIK CCCCCCCCCCHHHHH | 45.82 | 22865919 | |
| 11 | Ubiquitination | SSSTGYSKNNAAHIK CCCCCCCCCCHHHHH | 45.82 | 17644757 | |
| 18 | Acetylation | KNNAAHIKQENTLRQ CCCHHHHHHHHHHHH | 41.51 | 24489116 | |
| 18 | Ubiquitination | KNNAAHIKQENTLRQ CCCHHHHHHHHHHHH | 41.51 | 17644757 | |
| 22 | Phosphorylation | AHIKQENTLRQRESS HHHHHHHHHHHHHHH | 23.67 | 24961812 | |
| 28 | Phosphorylation | NTLRQRESSSISVSE HHHHHHHHHCCCHHH | 31.41 | 22369663 | |
| 29 | Phosphorylation | TLRQRESSSISVSEE HHHHHHHHCCCHHHH | 27.26 | 22369663 | |
| 30 | Phosphorylation | LRQRESSSISVSEEL HHHHHHHCCCHHHHH | 28.32 | 22369663 | |
| 32 | Phosphorylation | QRESSSISVSEELSS HHHHHCCCHHHHHHC | 22.87 | 22369663 | |
| 34 | Phosphorylation | ESSSISVSEELSSAD HHHCCCHHHHHHCCC | 20.68 | 22369663 | |
| 38 | Phosphorylation | ISVSEELSSADERDA CCHHHHHHCCCHHCH | 27.10 | 22369663 | |
| 39 | Phosphorylation | SVSEELSSADERDAE CHHHHHHCCCHHCHH | 52.98 | 22369663 | |
| 49 | Phosphorylation | ERDAEDFSKEKPAAQ HHCHHHHHCCCHHHH | 52.83 | 22369663 | |
| 124 | Phosphorylation | GKMLVGLSGYLAGYN HHHHHHHHHHHCCCC | 21.33 | 30377154 | |
| 126 | Phosphorylation | MLVGLSGYLAGYNGS HHHHHHHHHCCCCCC | 7.04 | 30377154 | |
| 130 | Phosphorylation | LSGYLAGYNGSWDFP HHHHHCCCCCCCCCC | 15.67 | 30377154 | |
| 131 | N-linked_Glycosylation | SGYLAGYNGSWDFPS HHHHCCCCCCCCCCC | 36.78 | - | |
| 133 | Phosphorylation | YLAGYNGSWDFPSGE HHCCCCCCCCCCCCC | 21.60 | 30377154 | |
| 138 | Phosphorylation | NGSWDFPSGEIYPDY CCCCCCCCCCCCCCH | 49.40 | 30377154 | |
| 142 | Phosphorylation | DFPSGEIYPDYLDYV CCCCCCCCCCHHHHH | 5.92 | 30377154 | |
| 145 | Phosphorylation | SGEIYPDYLDYVKMR CCCCCCCHHHHHHHH | 9.29 | 30377154 | |
| 148 | Phosphorylation | IYPDYLDYVKMRLFN CCCCHHHHHHHHHHC | 10.20 | 30377154 | |
| 155 | N-linked_Glycosylation | YVKMRLFNASFSALC HHHHHHHCCCHHHHH | 38.99 | - | |
| 352 | Ubiquitination | GSSVVSIKNQALGGS CCCEEEEECCCCCCH | 35.19 | 17644757 | |
| 383 | Ubiquitination | QVTCYGYKDANNEWF EEEEEEEECCCCEEE | 46.10 | 17644757 | |
| 403 | N-linked_Glycosylation | GLPSWSENETDIEYL CCCCCCCCCCCHHHC | 52.53 | - | |
| 422 | Phosphorylation | SYRLVHKSTGRNLHT EEEEEECCCCCCCCC | 22.63 | 22890988 | |
| 423 | Phosphorylation | YRLVHKSTGRNLHTH EEEEECCCCCCCCCC | 44.99 | 22890988 | |
| 429 | Phosphorylation | STGRNLHTHPVAAPV CCCCCCCCCCEECCC | 30.92 | 22890988 | |
| 437 | Phosphorylation | HPVAAPVSKTQWEVS CCEECCCCCCEEEEE | 29.00 | 22890988 | |
| 438 | Ubiquitination | PVAAPVSKTQWEVSG CEECCCCCCEEEEEE | 44.99 | 17644757 | |
| 473 | Acetylation | RGDEDPEKLHTLTTS CCCCCHHHHHHEEEE | 51.46 | 24489116 | |
| 545 | Ubiquitination | PEDFQYPKTNFLKDF CHHCCCCCCCHHHHH | 51.68 | 17644757 |
| 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 PMT2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PMT2_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 PMT2_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-32 AND SER-39, AND MASSSPECTROMETRY. | |
