| UniProt ID | SEC24_YEAST | |
|---|---|---|
| UniProt AC | P40482 | |
| Protein Name | Protein transport protein SEC24 | |
| Gene Name | SEC24 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 926 | |
| Subcellular Localization |
Cytoplasm . Cytoplasmic vesicle, COPII-coated vesicle membrane Peripheral membrane protein Cytoplasmic side . Endoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side. Golgi apparatus membrane Peripheral membrane protein Cyto |
|
| Protein Description | Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalisation of plasma membrane proteins like the maltose transporter.. | |
| Protein Sequence | MSHHKKRVYPQAQLQYGQNATPLQQPAQFMPPQDPAAAGMSYGQMGMPPQGAVPSMGQQQFLTPAQEQLHQQIDQATTSMNDMHLHNVPLVDPNAYMQPQVPVQMGTPLQQQQQPMAAPAYGQPSAAMGQNMRPMNQLYPIDLLTELPPPITDLTLPPPPLVIPPERMLVPSELSNASPDYIRSTLNAVPKNSSLLKKSKLPFGLVIRPYQHLYDDIDPPPLNEDGLIVRCRRCRSYMNPFVTFIEQGRRWRCNFCRLANDVPMQMDQSDPNDPKSRYDRNEIKCAVMEYMAPKEYTLRQPPPATYCFLIDVSQSSIKSGLLATTINTLLQNLDSIPNHDERTRISILCVDNAIHYFKIPLDSENNEESADQINMMDIADLEEPFLPRPNSMVVSLKACRQNIETLLTKIPQIFQSNLITNFALGPALKSAYHLIGGVGGKIIVVSGTLPNLGIGKLQRRNESGVVNTSKETAQLLSCQDSFYKNFTIDCSKVQITVDLFLASEDYMDVASLSNLSRFTAGQTHFYPGFSGKNPNDIVKFSTEFAKHISMDFCMETVMRARGSTGLRMSRFYGHFFNRSSDLCAFSTMPRDQSYLFEVNVDESIMADYCYVQVAVLLSLNNSQRRIRIITLAMPTTESLAEVYASADQLAIASFYNSKAVEKALNSSLDDARVLINKSVQDILATYKKEIVVSNTAGGAPLRLCANLRMFPLLMHSLTKHMAFRSGIVPSDHRASALNNLESLPLKYLIKNIYPDVYSLHDMADEAGLPVQTEDGEATGTIVLPQPINATSSLFERYGLYLIDNGNELFLWMGGDAVPALVFDVFGTQDIFDIPIGKQEIPVVENSEFNQRVRNIINQLRNHDDVITYQSLYIVRGASLSEPVNHASAREVATLRLWASSTLVEDKILNNESYREFLQIMKARISK | |
| 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 |
|---|---|---|---|---|---|
| 172 | Phosphorylation | PERMLVPSELSNASP HHHHCCCHHHHCCCH | 43.63 | 21126336 | |
| 175 | Phosphorylation | MLVPSELSNASPDYI HCCCHHHHCCCHHHH | 26.71 | 28889911 | |
| 178 | Phosphorylation | PSELSNASPDYIRST CHHHHCCCHHHHHHH | 23.66 | 22369663 | |
| 181 | Phosphorylation | LSNASPDYIRSTLNA HHCCCHHHHHHHHHC | 11.13 | 22369663 | |
| 191 | Acetylation | STLNAVPKNSSLLKK HHHHCCCCCCHHHHH | 63.96 | 24489116 | |
| 275 | Acetylation | QSDPNDPKSRYDRNE CCCCCCCCHHCCHHH | 50.89 | 24489116 | |
| 275 | Ubiquitination | QSDPNDPKSRYDRNE CCCCCCCCHHCCHHH | 50.89 | 23749301 | |
| 358 | Ubiquitination | DNAIHYFKIPLDSEN CCCHHEEECCCCCCC | 35.93 | 17644757 | |
| 429 | Ubiquitination | FALGPALKSAYHLIG HCHHHHHHHHHHHHC | 34.84 | 17644757 | |
| 441 | Ubiquitination | LIGGVGGKIIVVSGT HHCCCCCEEEEEECC | 24.27 | 17644757 | |
| 456 | Ubiquitination | LPNLGIGKLQRRNES CCCCCCCCCCCCCCC | 39.25 | 17644757 | |
| 463 | Phosphorylation | KLQRRNESGVVNTSK CCCCCCCCCCCCCCH | 40.20 | 23749301 | |
| 470 | Acetylation | SGVVNTSKETAQLLS CCCCCCCHHHHHHHH | 57.98 | 24489116 | |
| 532 | Acetylation | FYPGFSGKNPNDIVK ECCCCCCCCHHHHHH | 68.95 | 24489116 | |
| 532 | Ubiquitination | FYPGFSGKNPNDIVK ECCCCCCCCHHHHHH | 68.95 | 17644757 | |
| 539 | Ubiquitination | KNPNDIVKFSTEFAK CCHHHHHHHHHHHHH | 33.65 | 17644757 | |
| 539 | Acetylation | KNPNDIVKFSTEFAK CCHHHHHHHHHHHHH | 33.65 | 24489116 | |
| 563 | Phosphorylation | TVMRARGSTGLRMSR HHHHHHCCCCCCHHH | 17.47 | 19779198 | |
| 564 | Phosphorylation | VMRARGSTGLRMSRF HHHHHCCCCCCHHHH | 42.96 | 19779198 | |
| 662 | Ubiquitination | YNSKAVEKALNSSLD HCHHHHHHHHHCCHH | 52.13 | 23749301 | |
| 687 | Succinylation | QDILATYKKEIVVSN HHHHHHHCCEEEEEC | 39.31 | 23954790 | |
| 687 | Acetylation | QDILATYKKEIVVSN HHHHHHHCCEEEEEC | 39.31 | 24489116 | |
| 693 | Phosphorylation | YKKEIVVSNTAGGAP HCCEEEEECCCCCCC | 19.98 | 27214570 | |
| 716 | Phosphorylation | MFPLLMHSLTKHMAF HHHHHHHHHHHHHHH | 24.62 | 22369663 | |
| 718 | Phosphorylation | PLLMHSLTKHMAFRS HHHHHHHHHHHHHHC | 23.17 | 22369663 | |
| 725 | Phosphorylation | TKHMAFRSGIVPSDH HHHHHHHCCCCCCCH | 26.81 | 19684113 | |
| 746 | Ubiquitination | NLESLPLKYLIKNIY CHHHCCHHHHHHHHC | 35.75 | 23749301 | |
| 906 | Acetylation | SSTLVEDKILNNESY CCCHHHHHHCCCHHH | 35.27 | 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 SEC24_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC24_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 SEC24_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-178, AND MASSSPECTROMETRY. | |
| "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-175 AND SER-178, ANDMASS SPECTROMETRY. | |
