| UniProt ID | RGP1_YEAST | |
|---|---|---|
| UniProt AC | P16664 | |
| Protein Name | Guanine nucleotide exchange factor subunit RGP1 {ECO:0000305} | |
| Gene Name | RGP1 {ECO:0000303|PubMed:2179863, ECO:0000312|SGD:S000002544} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 663 | |
| Subcellular Localization | Golgi apparatus . | |
| Protein Description | The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates YPT6 by exchanging bound GDP for free GTP. It is thereby required for efficient fusion of endosome-derived vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of SNC1, presumably by mediating fusion of endosomal vesicles with the Golgi compartment.; Required for proper mitotic growth.. | |
| Protein Sequence | MRAHRIDTFLIRENIKLEIIHESNSYFGGEHISIAFRFKHLGSQHELFNYKEKLLTVDKAVEEKLEQQAKVQDDGEGTMENQTWSLKSLLGAFKRTGEPEESVDVDNMKMLNESKMLREKIQKQMYFHQPVTLISGYVQISGVFQYDSEVISESKFKQDEVKMVGLDIVPGHTTNSVLALEDGEHFKGKRNLTNYLNSDYTNVTNGLLFSESGSRGRTGTYNERTLMISNDTSIKTLPLLLIPQTLLFSEISLEPGEVRTFYFKSTKLPKDICPSYSSSKVASINYTLEVGADVLSDDNIEKFSNRVPITIAPYISSNAEQYTSRLDKPAIILKTGNIKELKPRLFTRKVSTASAVSFGRRKSSIIDIDSPLEDNEFVKRVKKNFIELVESNQNVSRDIDELIDLQMGVQFGKDEDSSDPEPNDSHFSNEMVTSAESSLRSDAVTKRRKSYSVRDNISNLEQKMWNDCSLVKSDENSNLLPQLINLQNAYQINRNNETMAKVSLSAPFYKTTDDINLVIELDPITTPLLKVTSLTVSLESFEIINPKYKTEGKGIGSKPKGNSVYEKHFICFDECKSVSVKLLPPRSPTNQITGQFKTDVFQHKWMIGLKFVIIAKTESITLDQFYEDKKGILFHSKENLEGEEFTCYVPIPILCTSEDFMGW | |
| 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 |
|---|---|---|---|---|---|
| 59 | Ubiquitination | EKLLTVDKAVEEKLE HHHHHHHHHHHHHHH | 50.42 | 23749301 | |
| 64 | Ubiquitination | VDKAVEEKLEQQAKV HHHHHHHHHHHHHCC | 43.76 | 23749301 | |
| 96 | Phosphorylation | LLGAFKRTGEPEESV HHHHHHHCCCCCCCC | 46.62 | 27017623 | |
| 102 | Phosphorylation | RTGEPEESVDVDNMK HCCCCCCCCCCCHHH | 23.19 | 27017623 | |
| 229 | Phosphorylation | NERTLMISNDTSIKT CCCEEEECCCCCCCH | 18.06 | 28889911 | |
| 232 | Phosphorylation | TLMISNDTSIKTLPL EEEECCCCCCCHHHE | 36.28 | 28889911 | |
| 351 | Phosphorylation | RLFTRKVSTASAVSF CEEECCCCCCHHHHC | 22.69 | 22369663 | |
| 352 | Phosphorylation | LFTRKVSTASAVSFG EEECCCCCCHHHHCC | 27.85 | 22369663 | |
| 354 | Phosphorylation | TRKVSTASAVSFGRR ECCCCCCHHHHCCCC | 29.32 | 22369663 | |
| 357 | Phosphorylation | VSTASAVSFGRRKSS CCCCHHHHCCCCCCC | 23.00 | 22369663 | |
| 363 | Phosphorylation | VSFGRRKSSIIDIDS HHCCCCCCCEEECCC | 25.59 | 22369663 | |
| 364 | Phosphorylation | SFGRRKSSIIDIDSP HCCCCCCCEEECCCC | 26.97 | 22369663 | |
| 370 | Phosphorylation | SSIIDIDSPLEDNEF CCEEECCCCCCCCHH | 31.55 | 22369663 | |
| 417 | Phosphorylation | QFGKDEDSSDPEPND HCCCCCCCCCCCCCC | 34.29 | 28889911 | |
| 418 | Phosphorylation | FGKDEDSSDPEPNDS CCCCCCCCCCCCCCC | 70.30 | 28889911 | |
| 450 | Phosphorylation | AVTKRRKSYSVRDNI HHHHHHHHCCHHHHH | 22.34 | 22369663 | |
| 451 | Phosphorylation | VTKRRKSYSVRDNIS HHHHHHHCCHHHHHH | 17.77 | 20377248 | |
| 452 | Phosphorylation | TKRRKSYSVRDNISN HHHHHHCCHHHHHHH | 20.12 | 20377248 | |
| 458 | Phosphorylation | YSVRDNISNLEQKMW CCHHHHHHHHHHHHH | 41.43 | 21440633 | |
| 498 | Phosphorylation | QINRNNETMAKVSLS EECCCCCCCEEEEEE | 25.26 | 28889911 | |
| 587 | Phosphorylation | VKLLPPRSPTNQITG EEECCCCCCCCCCCE | 41.68 | 30377154 | |
| 593 | Phosphorylation | RSPTNQITGQFKTDV CCCCCCCCEEECCCC | 18.37 | 30377154 | |
| 629 | Acetylation | LDQFYEDKKGILFHS HHHHHHCCCEEEEEE | 40.74 | 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 RGP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RGP1_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 RGP1_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-351; SER-354; SER-357;SER-363 AND SER-364, AND MASS 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-351; SER-354; SER-357;SER-363 AND SER-364, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND SER-364, ANDMASS SPECTROMETRY. | |
