UniProt ID | SFB2_YEAST | |
---|---|---|
UniProt AC | P53953 | |
Protein Name | SED5-binding protein 2 | |
Gene Name | SFB2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 876 | |
Subcellular Localization | Cytoplasm. Golgi apparatus membrane. Endoplasmic reticulum membrane. | |
Protein Description | Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.. | |
Protein Sequence | MSHHKKRVYPQAQVPYIASMPIVAEQQQSQQQIDQTAYAMGNLQLNNRANSFTQLAQNQQFPGSGKVVNQLYPVDLFTELPPPIRDLSLPPLPITISQDNIVTPSEYSNVPYQYVRSTLKAVPKTNSLLKKTKLPFAIVIRPYLHLQDSDNQVPLNTDGVIVRCRRCRSYMNPFVVFINQGRKWQCNICRFKNDVPFGFDQNLQGAPINRYERNEIKNSVVDYLAPVEYSVREPPPSVYVFLLDVSQNAVKNGLLATSARTILENIEFLPNHDGRTRIAIICVDHSLHYFYVPLDDDYEVSDEDDEESDGEEEDEDEEEEDVDNSETIQMFDIGDLDEPFLPMPSDELVVPLKYCKNNLETLLKKIPEIFQDTHSSKFALGPALKAASNLIKSTGGKVEVISSTLPNTGIGKLKKRSEQGILNTPKESSQLLSCKDSFYKTFTIECNKLQITVDMFLASEDYMDVATLSHLGRFSGGQTHFYPGFNATSLNDVTKFTRELSRHLSMDISMEAVMRVRCSTGLRATSFFGHFFNRSSDLCAFSTMPRDQSYLFGISIEDSLMAEYCYLQVSTLLTLNTGERRIRVMTLALPTSESAREVFASADQLAITDFMTQNAVTKALNSSMYSARDFITKSLEDILNAYKKEISMSNINSVTSLNLCANLRMLPLLMNGLSKHIALRPGVVPSDYRASALNRLETEPLHYLIKSIYPTVYSLHDMPDEVGLPDFEGKTVLPEPINATISLFERYGLYLIDNSAELFLWVGGDAVPELLIDVFNTDTISQIPVGKSELPLLNDSPFNERLRRIIGRIRENNDTITFQSLYIIRGPSINEPANLNSEKDMASLRLWVLSTLVEDKVLNCASYREYLQSMKTSINR | |
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 |
---|---|---|---|---|---|
51 | Phosphorylation | QLNNRANSFTQLAQN HCCCCCCHHHHHHHH | 28.78 | 22369663 | |
53 | Phosphorylation | NNRANSFTQLAQNQQ CCCCCHHHHHHHHCC | 23.61 | 22369663 | |
97 | Phosphorylation | PPLPITISQDNIVTP CCCCCEECCCCCCCH | 23.88 | 28889911 | |
192 | Acetylation | QCNICRFKNDVPFGF ECEEEEEECCCCCCC | 32.65 | 24489116 | |
217 | Ubiquitination | RYERNEIKNSVVDYL HHHHHHHCCCHHHHC | 36.67 | 17644757 | |
251 | Ubiquitination | DVSQNAVKNGLLATS ECCCHHHHCCCCHHH | 42.77 | 17644757 | |
377 | Acetylation | FQDTHSSKFALGPAL HCCCCCCCCCHHHHH | 37.36 | 24489116 | |
412 | Acetylation | LPNTGIGKLKKRSEQ CCCCCCCHHCHHHHC | 56.03 | 24489116 | |
424 | Phosphorylation | SEQGILNTPKESSQL HHCCCCCCCHHHHHH | 32.09 | 28152593 | |
495 | Ubiquitination | TSLNDVTKFTRELSR CCHHHHHHHHHHHHH | 44.58 | 17644757 | |
501 | Phosphorylation | TKFTRELSRHLSMDI HHHHHHHHHHHCCCC | 16.95 | 28889911 | |
509 | Phosphorylation | RHLSMDISMEAVMRV HHHCCCCCHHHHHHH | 13.30 | 28889911 | |
709 | Phosphorylation | HYLIKSIYPTVYSLH HHHHHHHHCCCCCCC | 10.43 | 28132839 | |
713 | Phosphorylation | KSIYPTVYSLHDMPD HHHHCCCCCCCCCCC | 14.16 | 28132839 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of SFB2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SFB2_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 SFB2_YEAST !! |
Kegg Drug | ||||||
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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-51; THR-53 AND SER-97,AND MASS SPECTROMETRY. | |
"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-51, AND MASSSPECTROMETRY. |