UniProt ID | SAR1_YEAST | |
---|---|---|
UniProt AC | P20606 | |
Protein Name | Small COPII coat GTPase SAR1 | |
Gene Name | SAR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 190 | |
Subcellular Localization |
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 Cytoplasmic side . N |
|
Protein Description | Small GTPase 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. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP by SEC12 binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits.. | |
Protein Sequence | MAGWDIFGWFRDVLASLGLWNKHGKLLFLGLDNAGKTTLLHMLKNDRLATLQPTWHPTSEELAIGNIKFTTFDLGGHIQARRLWKDYFPEVNGIVFLVDAADPERFDEARVELDALFNIAELKDVPFVILGNKIDAPNAVSEAELRSALGLLNTTGSQRIEGQRPVEVFMCSVVMRNGYLEAFQWLSQYI | |
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 |
---|---|---|---|---|---|
22 | Ubiquitination | ASLGLWNKHGKLLFL HHCCCCCCCCCEEEE | 42.00 | 22817900 | |
22 | Acetylation | ASLGLWNKHGKLLFL HHCCCCCCCCCEEEE | 42.00 | 24489116 | |
25 | Ubiquitination | GLWNKHGKLLFLGLD CCCCCCCCEEEEECC | 41.56 | 22817900 | |
36 | Ubiquitination | LGLDNAGKTTLLHML EECCCCCCHHHHHHH | 35.61 | 17644757 | |
36 | Acetylation | LGLDNAGKTTLLHML EECCCCCCHHHHHHH | 35.61 | 24489116 | |
44 | Acetylation | TTLLHMLKNDRLATL HHHHHHHHCCCCCCC | 49.59 | 24489116 | |
68 | Ubiquitination | ELAIGNIKFTTFDLG CEEECEEEEEEEECC | 40.43 | 23749301 | |
133 | Ubiquitination | PFVILGNKIDAPNAV CEEEECCCCCCCCCC | 39.92 | 23749301 | |
147 | Phosphorylation | VSEAELRSALGLLNT CCHHHHHHHHHCCCC | 40.23 | 22369663 | |
154 | Phosphorylation | SALGLLNTTGSQRIE HHHHCCCCCCCCCCC | 32.29 | 22369663 | |
155 | Phosphorylation | ALGLLNTTGSQRIEG HHHCCCCCCCCCCCC | 33.49 | 22369663 | |
157 | Phosphorylation | GLLNTTGSQRIEGQR HCCCCCCCCCCCCCC | 17.75 | 22369663 |
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 SAR1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SAR1_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 SAR1_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TMEDA_YEAST | ERV25 | physical | 12426381 | |
ERV41_YEAST | ERV41 | physical | 12426381 | |
ERV46_YEAST | ERV46 | physical | 12426381 | |
BET1_YEAST | BET1 | physical | 9428766 | |
EMP24_YEAST | EMP24 | physical | 9428766 | |
GAP1_YEAST | GAP1 | physical | 9428766 | |
HIP1_YEAST | HIP1 | physical | 9428766 | |
SEC22_YEAST | SEC22 | physical | 9428766 | |
SEC23_YEAST | SEC23 | physical | 8004676 | |
SEC23_YEAST | SEC23 | physical | 12426382 | |
SEC22_YEAST | SEC22 | physical | 12426382 | |
ERV29_YEAST | ERV29 | physical | 12426382 | |
SED5_YEAST | SED5 | physical | 12426382 | |
BET1_YEAST | BET1 | physical | 12426382 | |
SEC23_YEAST | SEC23 | physical | 11907269 | |
SEC24_YEAST | SEC24 | physical | 11907269 | |
ERV14_YEAST | ERV14 | physical | 11907269 | |
SEC23_YEAST | SEC23 | physical | 9428766 | |
SEC24_YEAST | SEC24 | physical | 9428766 | |
HRD3_YEAST | HRD3 | genetic | 9880808 | |
SEC12_YEAST | SEC12 | genetic | 9880808 | |
SEC16_YEAST | SEC16 | genetic | 9880808 | |
SED4_YEAST | SED4 | genetic | 9880808 | |
SED4_YEAST | SED4 | genetic | 11168590 | |
IRE1_YEAST | IRE1 | genetic | 12176017 | |
HRR25_YEAST | HRR25 | genetic | 9920934 | |
TVP15_YEAST | TVP15 | physical | 18719252 | |
SEC31_YEAST | SEC31 | physical | 22300850 |
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 THR-155 AND SER-157, ANDMASS SPECTROMETRY. |