| UniProt ID | SEC23_YEAST | |
|---|---|---|
| UniProt AC | P15303 | |
| Protein Name | Protein transport protein SEC23 | |
| Gene Name | SEC23 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 768 | |
| Subcellular Localization |
Cytoplasmic vesicle, COPII-coated vesicle membrane Peripheral membrane protein Cytoplasmic side . Cytoplasm . 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. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.. | |
| Protein Sequence | MDFETNEDINGVRFTWNVFPSTRSDANSNVVPVGCLYTPLKEYDELNVAPYNPVVCSGPHCKSILNPYCVIDPRNSSWSCPICNSRNHLPPQYTNLSQENMPLELQSTTIEYITNKPVTVPPIFFFVVDLTSETENLDSLKESIITSLSLLPPNALIGLITYGNVVQLHDLSSETIDRCNVFRGDREYQLEALTEMLTGQKPTGPGGAASHLPNAMNKVTPFSLNRFFLPLEQVEFKLNQLLENLSPDQWSVPAGHRPLRATGSALNIASLLLQGCYKNIPARIILFASGPGTVAPGLIVNSELKDPLRSHHDIDSDHAQHYKKACKFYNQIAQRVAANGHTVDIFAGCYDQIGMSEMKQLTDSTGGVLLLTDAFSTAIFKQSYLRLFAKDEEGYLKMAFNGNMAVKTSKDLKVQGLIGHASAVKKTDANNISESEIGIGATSTWKMASLSPYHSYAIFFEIANTAANSNPMMSAPGSADRPHLAYTQFITTYQHSSGTNRIRVTTVANQLLPFGTPAIAASFDQEAAAVLMARIAVHKAETDDGADVIRWLDRTLIKLCQKYADYNKDDPQSFRLAPNFSLYPQFTYYLRRSQFLSVFNNSPDETAFYRHIFTREDTTNSLIMIQPTLTSFSMEDDPQPVLLDSISVKPNTILLLDTFFFILIYHGEQIAQWRKAGYQDDPQYADFKALLEEPKLEAAELLVDRFPLPRFIDTEAGGSQARFLLSKLNPSDNYQDMARGGSTIVLTDDVSLQNFMTHLQQVAVSGQA | |
| 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 | -------MDFETNED -------CCCCCCCC | 13.87 | 22814378 | |
| 24 | Phosphorylation | NVFPSTRSDANSNVV EECCCCCCCCCCCEE | 40.96 | 28889911 | |
| 28 | Phosphorylation | STRSDANSNVVPVGC CCCCCCCCCEEEEEC | 32.49 | 28152593 | |
| 38 | Phosphorylation | VPVGCLYTPLKEYDE EEEECEECCHHHCCC | 14.81 | 21440633 | |
| 41 | Ubiquitination | GCLYTPLKEYDELNV ECEECCHHHCCCCCC | 56.27 | 22817900 | |
| 77 | Phosphorylation | VIDPRNSSWSCPICN EECCCCCCCCCCCCC | 26.93 | 19779198 | |
| 85 | Phosphorylation | WSCPICNSRNHLPPQ CCCCCCCCCCCCCCC | 30.01 | 19779198 | |
| 262 | Phosphorylation | GHRPLRATGSALNIA CCCCCCCCCHHHHHH | 25.82 | 22369663 | |
| 264 | Phosphorylation | RPLRATGSALNIASL CCCCCCCHHHHHHHH | 25.81 | 22369663 | |
| 270 | Phosphorylation | GSALNIASLLLQGCY CHHHHHHHHHHHHHH | 18.76 | 22369663 | |
| 277 | Phosphorylation | SLLLQGCYKNIPARI HHHHHHHHHCCCEEE | 17.56 | 22369663 | |
| 278 | Acetylation | LLLQGCYKNIPARII HHHHHHHHCCCEEEE | 53.10 | 24489116 | |
| 327 | Acetylation | QHYKKACKFYNQIAQ HHHHHHHHHHHHHHH | 56.60 | 24489116 | |
| 362 | Phosphorylation | MSEMKQLTDSTGGVL HHHHHHHHCCCCCEE | 25.96 | 22369663 | |
| 364 | Phosphorylation | EMKQLTDSTGGVLLL HHHHHHCCCCCEEEE | 24.58 | 22369663 | |
| 365 | Phosphorylation | MKQLTDSTGGVLLLT HHHHHCCCCCEEEEC | 40.54 | 22369663 | |
| 372 | Phosphorylation | TGGVLLLTDAFSTAI CCCEEEECCHHHHHH | 25.83 | 22369663 | |
| 376 | Phosphorylation | LLLTDAFSTAIFKQS EEECCHHHHHHHHHH | 20.74 | 22369663 | |
| 377 | Phosphorylation | LLTDAFSTAIFKQSY EECCHHHHHHHHHHH | 19.81 | 22369663 | |
| 413 | Ubiquitination | VKTSKDLKVQGLIGH EEECCCCEEEHHHCC | 42.52 | 17644757 | |
| 425 | Ubiquitination | IGHASAVKKTDANNI HCCHHHCCCCCCCCC | 50.07 | 17644757 | |
| 426 | Ubiquitination | GHASAVKKTDANNIS CCHHHCCCCCCCCCC | 45.07 | 17644757 | |
| 539 | Ubiquitination | MARIAVHKAETDDGA HHHHHHHHHCCCCCH | 41.12 | 23749301 | |
| 539 | Acetylation | MARIAVHKAETDDGA HHHHHHHHHCCCCCH | 41.12 | 24489116 | |
| 555 | Phosphorylation | VIRWLDRTLIKLCQK HHHHHHHHHHHHHHH | 32.28 | 21532587 | |
| 562 | Acetylation | TLIKLCQKYADYNKD HHHHHHHHHHHCCCC | 41.22 | 24489116 | |
| 568 | Succinylation | QKYADYNKDDPQSFR HHHHHCCCCCHHHCC | 58.23 | 23954790 | |
| 568 | Acetylation | QKYADYNKDDPQSFR HHHHHCCCCCHHHCC | 58.23 | 24489116 | |
| 675 | Ubiquitination | EQIAQWRKAGYQDDP HHHHHHHHCCCCCCC | 43.11 | 23749301 | |
| 695 | Acetylation | KALLEEPKLEAAELL HHHHHCCCHHHHHHH | 63.34 | 24489116 | |
| 727 | Ubiquitination | QARFLLSKLNPSDNY HHHHHHHCCCCCCCH | 52.86 | 23749301 | |
| 742 | Phosphorylation | QDMARGGSTIVLTDD HHHHCCCCEEEECCC | 20.13 | 21532587 | |
| 747 | Phosphorylation | GGSTIVLTDDVSLQN CCCEEEECCCCCHHH | 21.18 | 21532587 |
| 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 SEC23_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC23_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 SEC23_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-24, AND MASSSPECTROMETRY. | |
