| UniProt ID | SEC4_YEAST | |
|---|---|---|
| UniProt AC | P07560 | |
| Protein Name | Ras-related protein SEC4 | |
| Gene Name | SEC4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 215 | |
| Subcellular Localization |
Cytoplasmic vesicle, secretory vesicle membrane Lipid-anchor Cytoplasmic side. Cell membrane Lipid-anchor Cytoplasmic side. Cytoplasm. A small fraction is soluble. |
|
| Protein Description | Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle.. | |
| Protein Sequence | MSGLRTVSASSGNGKSYDSIMKILLIGDSGVGKSCLLVRFVEDKFNPSFITTIGIDFKIKTVDINGKKVKLQLWDTAGQERFRTITTAYYRGAMGIILVYDVTDERTFTNIKQWFKTVNEHANDEAQLLLVGNKSDMETRVVTADQGEALAKELGIPFIESSAKNDDNVNEIFFTLAKLIQEKIDSNKLVGVGNGKEGNISINSGSGNSSKSNCC | |
| 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 | Phosphorylation | ------MSGLRTVSA ------CCCCCEEEC | 46.68 | 19795423 | |
| 6 | Phosphorylation | --MSGLRTVSASSGN --CCCCCEEECCCCC | 24.69 | 21440633 | |
| 8 | Phosphorylation | MSGLRTVSASSGNGK CCCCCEEECCCCCCC | 23.09 | 19823750 | |
| 10 | Phosphorylation | GLRTVSASSGNGKSY CCCEEECCCCCCCCH | 31.13 | 19684113 | |
| 11 | Phosphorylation | LRTVSASSGNGKSYD CCEEECCCCCCCCHH | 35.67 | 19823750 | |
| 15 | Succinylation | SASSGNGKSYDSIMK ECCCCCCCCHHHCEE | 50.25 | 23954790 | |
| 15 | Acetylation | SASSGNGKSYDSIMK ECCCCCCCCHHHCEE | 50.25 | 24489116 | |
| 16 | Phosphorylation | ASSGNGKSYDSIMKI CCCCCCCCHHHCEEE | 35.25 | 28889911 | |
| 22 | Acetylation | KSYDSIMKILLIGDS CCHHHCEEEEEECCC | 28.65 | 24489116 | |
| 70 | Acetylation | DINGKKVKLQLWDTA EECCEEEEEEEECCC | 39.12 | 24489116 | |
| 86 | Phosphorylation | QERFRTITTAYYRGA HHHHHHHHHHHHCCC | 12.54 | 27017623 | |
| 87 | Phosphorylation | ERFRTITTAYYRGAM HHHHHHHHHHHCCCC | 14.60 | 27017623 | |
| 89 | Phosphorylation | FRTITTAYYRGAMGI HHHHHHHHHCCCCEE | 7.51 | 27017623 | |
| 90 | Phosphorylation | RTITTAYYRGAMGII HHHHHHHHCCCCEEE | 10.50 | 27017623 | |
| 103 | Phosphorylation | IILVYDVTDERTFTN EEEEEECCCCCCCCC | 29.28 | 27017623 | |
| 112 | Acetylation | ERTFTNIKQWFKTVN CCCCCCHHHHHHHHH | 43.47 | 24489116 | |
| 116 | Acetylation | TNIKQWFKTVNEHAN CCHHHHHHHHHHHCC | 48.91 | 24489116 | |
| 152 | Ubiquitination | DQGEALAKELGIPFI HHHHHHHHHHCCCEE | 55.08 | 23749301 | |
| 152 | Acetylation | DQGEALAKELGIPFI HHHHHHHHHHCCCEE | 55.08 | 24489116 | |
| 183 | Ubiquitination | LAKLIQEKIDSNKLV HHHHHHHHHCCCCEE | 35.12 | 23749301 | |
| 183 | Acetylation | LAKLIQEKIDSNKLV HHHHHHHHHCCCCEE | 35.12 | 24489116 | |
| 186 | Phosphorylation | LIQEKIDSNKLVGVG HHHHHHCCCCEEEEC | 39.06 | 21551504 | |
| 196 | Ubiquitination | LVGVGNGKEGNISIN EEEECCCCCCCEEEE | 67.46 | 23749301 | |
| 201 | Phosphorylation | NGKEGNISINSGSGN CCCCCCEEEECCCCC | 21.51 | 22369663 | |
| 204 | Phosphorylation | EGNISINSGSGNSSK CCCEEEECCCCCCCC | 32.44 | 22369663 | |
| 206 | Phosphorylation | NISINSGSGNSSKSN CEEEECCCCCCCCCC | 34.32 | 25521595 | |
| 209 | Phosphorylation | INSGSGNSSKSNCC- EECCCCCCCCCCCC- | 42.54 | 22890988 | |
| 210 | Phosphorylation | NSGSGNSSKSNCC-- ECCCCCCCCCCCC-- | 44.07 | 22890988 | |
| 214 | Geranylgeranylation | GNSSKSNCC------ CCCCCCCCC------ | 3.63 | - | |
| 215 | Geranylgeranylation | NSSKSNCC------- CCCCCCCC------- | 7.96 | - |
| 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 SEC4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC4_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 SEC4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-201 AND SER-204, ANDMASS 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-201 AND SER-204, ANDMASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-11; SER-201 ANDSER-204, AND MASS SPECTROMETRY. | |
