UniProt ID | MST27_YEAST | |
---|---|---|
UniProt AC | P53176 | |
Protein Name | Multicopy suppressor of SEC21 protein 27 | |
Gene Name | MST27 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 234 | |
Subcellular Localization |
Endoplasmic reticulum . Golgi apparatus . Cytoplasmic vesicle, COPI-coated vesicle membrane Multi-pass membrane protein . Cytoplasmic vesicle, COPII-coated vesicle membrane Multi-pass membrane protein . |
|
Protein Description | Involved in protein trafficking vesicle formation, probably by stabilizing of coatomer at the Golgi membrane and thus allowing the efficient formation of COPI coated vesicles.. | |
Protein Sequence | MQTPLESTDVKLDTLNEPSAHLIEKNVALPKDIFRSYLSYWIYEIARYTPVMILSLVIGVLVLLIIFFNDNEACVFNSAYYAYLSLVVLLIILGDGNPKLVSRRNFRTELLVDVITRKPAVEGKEWRIITYNMNQYLFNHGQWHTPYYFYSDEDCYRYFLRLVEGVTPKKQTATSIGNSPVTAKPEDAIESASPSSRLNYRNFLLKAAEIERQAQENYWRRRHPNIDALLKKTE | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MQTPLESTDV -----CCCCCCCCCC | 28.66 | - | |
7 | Phosphorylation | -MQTPLESTDVKLDT -CCCCCCCCCCCCCC | 37.28 | 27214570 | |
167 | Phosphorylation | LRLVEGVTPKKQTAT HHHHCCCCCCCCCCC | 40.00 | 27214570 | |
172 | Phosphorylation | GVTPKKQTATSIGNS CCCCCCCCCCCCCCC | 40.56 | 28889911 | |
174 | Phosphorylation | TPKKQTATSIGNSPV CCCCCCCCCCCCCCC | 25.02 | 29688323 | |
175 | Phosphorylation | PKKQTATSIGNSPVT CCCCCCCCCCCCCCC | 26.49 | 27017623 | |
179 | Phosphorylation | TATSIGNSPVTAKPE CCCCCCCCCCCCCHH | 18.61 | 21440633 | |
182 | Phosphorylation | SIGNSPVTAKPEDAI CCCCCCCCCCHHHHH | 32.14 | 23749301 | |
191 | Phosphorylation | KPEDAIESASPSSRL CHHHHHHHCCCCHHH | 28.12 | 29688323 | |
193 | Phosphorylation | EDAIESASPSSRLNY HHHHHHCCCCHHHHH | 34.30 | 23749301 | |
195 | Phosphorylation | AIESASPSSRLNYRN HHHHCCCCHHHHHHH | 26.12 | 23749301 | |
196 | Phosphorylation | IESASPSSRLNYRNF HHHCCCCHHHHHHHH | 44.14 | 29688323 |
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 MST27_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MST27_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 MST27_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MST28_YEAST | MST28 | physical | 10688190 | |
SEC24_YEAST | SEC24 | physical | 12925749 | |
COPB_YEAST | SEC26 | physical | 17954604 | |
COPB2_YEAST | SEC27 | physical | 17954604 | |
COPG_YEAST | SEC21 | physical | 17954604 | |
COPD_YEAST | RET2 | physical | 17954604 | |
COPA_YEAST | COP1 | physical | 17954604 | |
MST27_YEAST | MST27 | physical | 18719252 | |
MST28_YEAST | MST28 | physical | 18719252 | |
GNTK_YEAST | YDR248C | genetic | 20093466 | |
EAF1_YEAST | EAF1 | genetic | 20093466 | |
6P21_YEAST | PFK26 | genetic | 20093466 | |
BRE2_YEAST | BRE2 | genetic | 20093466 | |
GTR1_YEAST | GTR1 | genetic | 20093466 | |
ERG2_YEAST | ERG2 | genetic | 20093466 | |
ATP23_YEAST | ATP23 | genetic | 20093466 | |
MST28_YEAST | MST28 | physical | 16093310 | |
PHO88_YEAST | PHO88 | physical | 16093310 | |
RT23_YEAST | RSM23 | physical | 16093310 | |
THI73_YEAST | THI73 | physical | 16093310 | |
HXT2_YEAST | HXT2 | physical | 16093310 | |
GPI2_YEAST | GPI2 | physical | 16093310 | |
MST27_YEAST | MST27 | physical | 16093310 | |
UBC9_HUMAN | UBE2I | physical | 27107014 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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