| UniProt ID | RUD3_YEAST | |
|---|---|---|
| UniProt AC | Q12234 | |
| Protein Name | GRIP domain-containing protein RUD3 | |
| Gene Name | RUD3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 484 | |
| Subcellular Localization | Golgi apparatus lumen . The Golgi localization needs the presence of ARF1 and ERV14. | |
| Protein Description | Involved in the structural organization of the cis-Golgi and in vesicle targeting/fusion stages of ER to Golgi transport.. | |
| Protein Sequence | MGKNKKKTGKKAKSHPHVEDVDETVNKPEEIINSVNVTVPPKMSTDPEADGIVASPDDEGKDLSEGVDKQKVNDGLTVDTINPLEDKKAGDEMKELREEIERLKLELSHKKDQETPNEDFKNELANVIKERDEFKTQYDTLLSKISSMKSIFNKMKEAQKQLEEVQEQLTEYESQNLKLKKKLEATKTENSELQSTIVTLNTELENLEKEQESTEEVFLEYESRIEALEDEKHDIIEKHSKELNTYRKEKDQLNLQVQELMIILENNKQDISDLRTERDELRQALESHEKEKAVLKNSLNDLELKIEEVDNKREEEARERDQEVKSLRSQLDTEIETHNNDTEALESMKKQLEAMKEDASMKEKYEEESKQHILQIGKLRHEAIILNEHLTKALAMLKKSSDSESVDKELISNLLISFVSIPRADPRKFEVLELLSNFLNWDEDKKQQAGLISNNESKNSSAVSRTESFVSLWTNYLEKESEKD | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | VTVPPKMSTDPEADG EECCCCCCCCCCCCC | 35.47 | 28889911 | |
| 45 | Phosphorylation | TVPPKMSTDPEADGI ECCCCCCCCCCCCCC | 52.66 | 26447709 | |
| 55 | Phosphorylation | EADGIVASPDDEGKD CCCCCCCCCCCCCCC | 20.26 | 22369663 | |
| 64 | Phosphorylation | DDEGKDLSEGVDKQK CCCCCCCCCCCCHHH | 42.30 | 22369663 | |
| 115 | Phosphorylation | SHKKDQETPNEDFKN HCCCCCCCCCHHHHH | 26.27 | 22369663 | |
| 144 | Acetylation | QYDTLLSKISSMKSI HHHHHHHHHHHHHHH | 46.72 | 24489116 | |
| 149 | Acetylation | LSKISSMKSIFNKMK HHHHHHHHHHHHHHH | 42.20 | 24489116 | |
| 232 | Acetylation | IEALEDEKHDIIEKH HHHHHHHCCHHHHHH | 59.92 | 24489116 | |
| 238 | Acetylation | EKHDIIEKHSKELNT HCCHHHHHHHHHHHH | 42.65 | 24489116 | |
| 326 | Phosphorylation | ERDQEVKSLRSQLDT HHHHHHHHHHHHHHH | 33.90 | 23749301 | |
| 369 | Phosphorylation | KEKYEEESKQHILQI HHHHHHHHHHHHHHH | 40.68 | 27017623 | |
| 403 | Phosphorylation | MLKKSSDSESVDKEL HHHCCCCCHHHCHHH | 33.45 | 28889911 | |
| 453 | Phosphorylation | KQQAGLISNNESKNS HHHHCCCCCCCCCCC | 38.35 | 22369663 | |
| 457 | Phosphorylation | GLISNNESKNSSAVS CCCCCCCCCCCCCCC | 38.98 | 22369663 | |
| 458 | Ubiquitination | LISNNESKNSSAVSR CCCCCCCCCCCCCCH | 55.45 | 23749301 | |
| 460 | Phosphorylation | SNNESKNSSAVSRTE CCCCCCCCCCCCHHH | 24.34 | 19795423 | |
| 461 | Phosphorylation | NNESKNSSAVSRTES CCCCCCCCCCCHHHH | 41.92 | 24961812 | |
| 464 | Phosphorylation | SKNSSAVSRTESFVS CCCCCCCCHHHHHHH | 32.95 | 21440633 | |
| 466 | Phosphorylation | NSSAVSRTESFVSLW CCCCCCHHHHHHHHH | 28.60 | 22369663 | |
| 468 | Phosphorylation | SAVSRTESFVSLWTN CCCCHHHHHHHHHHH | 30.27 | 22369663 | |
| 471 | Phosphorylation | SRTESFVSLWTNYLE CHHHHHHHHHHHHHH | 19.04 | 22369663 | |
| 474 | Phosphorylation | ESFVSLWTNYLEKES HHHHHHHHHHHHHHH | 21.19 | 22369663 |
| 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 RUD3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RUD3_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 RUD3_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-55 AND SER-64, AND MASSSPECTROMETRY. | |
| "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-55 AND THR-115, AND MASSSPECTROMETRY. | |
| "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-55, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468, AND MASSSPECTROMETRY. | |
