| UniProt ID | SEC2_YEAST | |
|---|---|---|
| UniProt AC | P17065 | |
| Protein Name | Rab guanine nucleotide exchange factor SEC2 | |
| Gene Name | SEC2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 759 | |
| Subcellular Localization | Bud neck . Bud tip . Cytoplasmic vesicle, secretory vesicle . Localizes to sites of polarized growth, namely to the bud neck and to the bud tip of growing buds, and associates with membranes. Colocalizes with secretory vesicles at exocytic sites. Pro | |
| Protein Description | Guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. Binds the Rab GTPase YPT32, but does not have exchange activity on YPT32.. | |
| Protein Sequence | MDASEEAKRVSIQVTSLSTQLIESVDKQSHLEEQLNKSLKTIASQKAAIENYNQLKEDYNTLKRELSDRDDEVKRLREDIAKENELRTKAEEEADKLNKEVEDLTASLFDEANNMVADARKEKYAIEILNKRLTEQLREKDTLLDTLTLQLKNLKKVMHSLDNESTVTNNSNRYSTILSDSATSSSTSLNKVPTSYSLASQDIYSGIVYSPSISSIRYDISLYNEFLKFVAALPRCENIKATSTESKLIRRLVNDEIQPILKIDNASGIGWLVKKTLLSLIIDGLVVVEPLSGVNATYQIGYNSSSPAKQATSNMPKMFKFPLDSPPVAVHAACSFCGESRDDIIEHARMYILKTLHKTDDGKEQVTNTYPLCHWCLLKLRQTCEIFAFLRSLKVGAWHLEKLTTQNITKEDLEKFSEVTKHTKRDGRVSSQDKKTKRLSFMAGLGINSSTKNKPKMEIFSSETNAKPGQPTTNIQRAWLQLCKLRCILHWTHIGIWAVDDSISSKIGPLVEDDSDEDQNDAISVRLQDKALWKQDAKRPFSSSSAEESQKSDAFDFESGDMENEITGESSSDESSSDGSSTDNSTADSSSEDESSLADSTTSSADSSSPESIDNGEGDDTVTKDDKSSIKSANNNEENSDCGDKKGRSIIKKKAPQRKIQKKKLLQDLDDLEEQFREESAIDQTEFENAESNVKQNISSKRASSGDENSKKDNNEKTLKTNLTIGDKTQEQIGENSPSSGLHASSSNDDNFDDAQEQQ | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDASEEAK -------CCHHHHHH | 9.78 | 22814378 | |
| 134 | Phosphorylation | EILNKRLTEQLREKD HHHHHHHHHHHHHHC | 26.22 | 28889911 | |
| 168 | Phosphorylation | LDNESTVTNNSNRYS CCCCCCCCCCCCCCE | 28.86 | 28889911 | |
| 171 | Phosphorylation | ESTVTNNSNRYSTIL CCCCCCCCCCCEEEE | 25.42 | 23749301 | |
| 174 | Phosphorylation | VTNNSNRYSTILSDS CCCCCCCCEEEECCC | 17.89 | 22369663 | |
| 175 | Phosphorylation | TNNSNRYSTILSDSA CCCCCCCEEEECCCC | 13.01 | 22369663 | |
| 176 | Phosphorylation | NNSNRYSTILSDSAT CCCCCCEEEECCCCC | 19.60 | 22369663 | |
| 179 | Phosphorylation | NRYSTILSDSATSSS CCCEEEECCCCCCCC | 26.18 | 22369663 | |
| 181 | Phosphorylation | YSTILSDSATSSSTS CEEEECCCCCCCCCC | 30.03 | 22369663 | |
| 183 | Phosphorylation | TILSDSATSSSTSLN EEECCCCCCCCCCCC | 32.85 | 22369663 | |
| 184 | Phosphorylation | ILSDSATSSSTSLNK EECCCCCCCCCCCCC | 23.23 | 22369663 | |
| 185 | Phosphorylation | LSDSATSSSTSLNKV ECCCCCCCCCCCCCC | 33.03 | 22369663 | |
| 186 | Phosphorylation | SDSATSSSTSLNKVP CCCCCCCCCCCCCCC | 23.06 | 22369663 | |
| 187 | Phosphorylation | DSATSSSTSLNKVPT CCCCCCCCCCCCCCC | 38.90 | 22369663 | |
| 188 | Phosphorylation | SATSSSTSLNKVPTS CCCCCCCCCCCCCCC | 31.71 | 22369663 | |
| 194 | Phosphorylation | TSLNKVPTSYSLASQ CCCCCCCCCCCCCCC | 43.19 | 22369663 | |
| 195 | Phosphorylation | SLNKVPTSYSLASQD CCCCCCCCCCCCCCC | 13.47 | 22369663 | |
| 196 | Phosphorylation | LNKVPTSYSLASQDI CCCCCCCCCCCCCCC | 15.35 | 22369663 | |
| 197 | Phosphorylation | NKVPTSYSLASQDIY CCCCCCCCCCCCCCC | 19.75 | 22369663 | |
| 200 | Phosphorylation | PTSYSLASQDIYSGI CCCCCCCCCCCCCCC | 33.41 | 22369663 | |
| 204 | Phosphorylation | SLASQDIYSGIVYSP CCCCCCCCCCCCCCC | 14.77 | 22369663 | |
| 205 | Phosphorylation | LASQDIYSGIVYSPS CCCCCCCCCCCCCCC | 23.52 | 22369663 | |
| 313 | Phosphorylation | SPAKQATSNMPKMFK CHHHHHCCCCCCCCC | 33.86 | 27017623 | |
| 409 | Phosphorylation | KLTTQNITKEDLEKF HHHCCCCCHHHHHHH | 35.61 | 22369663 | |
| 410 | Acetylation | LTTQNITKEDLEKFS HHCCCCCHHHHHHHH | 45.49 | 24489116 | |
| 417 | Phosphorylation | KEDLEKFSEVTKHTK HHHHHHHHHHHHHHC | 42.07 | 28889911 | |
| 484 | Acetylation | RAWLQLCKLRCILHW HHHHHHHHHHHHHCC | 47.78 | 25381059 | |
| 515 | Phosphorylation | GPLVEDDSDEDQNDA CCCCCCCCCCCCCCC | 56.04 | 22369663 | |
| 524 | Phosphorylation | EDQNDAISVRLQDKA CCCCCCHHHHHHHHH | 11.69 | 22369663 | |
| 542 | Phosphorylation | QDAKRPFSSSSAEES CCCCCCCCCCCHHHH | 31.80 | 22369663 | |
| 543 | Phosphorylation | DAKRPFSSSSAEESQ CCCCCCCCCCHHHHH | 28.79 | 22369663 | |
| 544 | Phosphorylation | AKRPFSSSSAEESQK CCCCCCCCCHHHHHC | 32.16 | 22369663 | |
| 545 | Phosphorylation | KRPFSSSSAEESQKS CCCCCCCCHHHHHCC | 41.47 | 22369663 | |
| 549 | Phosphorylation | SSSSAEESQKSDAFD CCCCHHHHHCCCCCC | 34.12 | 22369663 | |
| 628 | Phosphorylation | TVTKDDKSSIKSANN CCCCCCHHHHHCCCC | 44.27 | 29136822 | |
| 629 | Phosphorylation | VTKDDKSSIKSANNN CCCCCHHHHHCCCCC | 39.51 | 29136822 | |
| 632 | Phosphorylation | DDKSSIKSANNNEEN CCHHHHHCCCCCCCC | 34.26 | 29136822 | |
| 640 | Phosphorylation | ANNNEENSDCGDKKG CCCCCCCCCCCCHHC | 37.24 | 29136822 | |
| 699 | Phosphorylation | SNVKQNISSKRASSG HHHHHHHHHCCCCCC | 37.04 | 19823750 | |
| 700 | Phosphorylation | NVKQNISSKRASSGD HHHHHHHHCCCCCCC | 23.51 | 19823750 | |
| 704 | Phosphorylation | NISSKRASSGDENSK HHHHCCCCCCCCCCC | 38.60 | 19823750 | |
| 705 | Phosphorylation | ISSKRASSGDENSKK HHHCCCCCCCCCCCC | 49.64 | 19823750 | |
| 710 | Phosphorylation | ASSGDENSKKDNNEK CCCCCCCCCCCCCCC | 38.75 | 19795423 | |
| 724 | Phosphorylation | KTLKTNLTIGDKTQE CHHHHCEECCCHHHH | 25.61 | 30377154 | |
| 729 | Phosphorylation | NLTIGDKTQEQIGEN CEECCCHHHHHHCCC | 41.92 | 19779198 | |
| 737 | Phosphorylation | QEQIGENSPSSGLHA HHHHCCCCCCCCCCC | 23.12 | 20377248 | |
| 739 | Phosphorylation | QIGENSPSSGLHASS HHCCCCCCCCCCCCC | 36.54 | 20377248 | |
| 740 | Phosphorylation | IGENSPSSGLHASSS HCCCCCCCCCCCCCC | 49.08 | 20377248 | |
| 745 | Phosphorylation | PSSGLHASSSNDDNF CCCCCCCCCCCCCCC | 24.45 | 20377248 | |
| 746 | Phosphorylation | SSGLHASSSNDDNFD CCCCCCCCCCCCCCC | 33.66 | 20377248 | |
| 747 | Phosphorylation | SGLHASSSNDDNFDD CCCCCCCCCCCCCCH | 41.61 | 20377248 |
| 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 SEC2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC2_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 SEC2_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-197; SER-200; TYR-204;THR-409 AND SER-515, 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-544 AND SER-545, 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-515 AND SER-524, ANDMASS SPECTROMETRY. | |
