UniProt ID | GPT1_YEAST | |
---|---|---|
UniProt AC | P32784 | |
Protein Name | Glycerol-3-phosphate O-acyltransferase 1 | |
Gene Name | SCT1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 759 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
Protein Description | G-3-P/dihydroxyacetone phosphate dual substrate-specific sn-1 acyltransferase.. | |
Protein Sequence | MPAPKLTEKFASSKSTQKTTNYSSIEAKSVKTSADQAYIYQEPSATKKILYSIATWLLYNIFHCFFREIRGRGSFKVPQQGPVIFVAAPHANQFVDPVILMGEVKKSVNRRVSFLIAESSLKQPPIGFLASFFMAIGVVRPQDNLKPAEGTIRVDPTDYKRVIGHDTHFLTDCMPKGLIGLPKSMGFGEIQSIESDTSLTLRKEFKMAKPEIKTALLTGTTYKYAAKVDQSCVYHRVFEHLAHNNCIGIFPEGGSHDRTNLLPLKAGVAIMALGCMDKHPDVNVKIVPCGMNYFHPHKFRSRAVVEFGDPIEIPKELVAKYHNPETNRDAVKELLDTISKGLQSVTVTCSDYETLMVVQTIRRLYMTQFSTKLPLPLIVEMNRRMVKGYEFYRNDPKIADLTKDIMAYNAALRHYNLPDHLVEEAKVNFAKNLGLVFFRSIGLCILFSLAMPGIIMFSPVFILAKRISQEKARTALSKSTVKIKANDVIATWKILIGMGFAPLLYIFWSVLITYYLRHKPWNKIYVFSGSYISCVIVTYSALIVGDIGMDGFKSLRPLVLSLTSPKGLQKLQKDRRNLAERIIEVVNNFGSELFPDFDSAALREEFDVIDEEEEDRKTSELNRRKMLRKQKIKRQEKDSSSPIISQRDNHDAYEHHNQDSDGVSLVNSDNSLSNIPLFSSTFHRKSESSLASTSVAPSSSSEFEVENEILEEKNGLASKIAQAVLNKRIGENTAREEEEEEEEEEEEEEEEEEGKEGDA | |
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 |
---|---|---|---|---|---|
7 | Phosphorylation | -MPAPKLTEKFASSK -CCCCHHHHHHHCCC | 43.16 | 28889911 | |
13 | Phosphorylation | LTEKFASSKSTQKTT HHHHHHCCCCCCCCC | 27.48 | 28889911 | |
223 | Acetylation | LLTGTTYKYAAKVDQ HHHCCHHHHEEECCH | 26.73 | 24489116 | |
509 | Phosphorylation | PLLYIFWSVLITYYL HHHHHHHHHHHHHHH | 9.04 | 30377154 | |
513 | Phosphorylation | IFWSVLITYYLRHKP HHHHHHHHHHHHCCC | 11.27 | 30377154 | |
514 | Phosphorylation | FWSVLITYYLRHKPW HHHHHHHHHHHCCCC | 8.10 | 30377154 | |
515 | Phosphorylation | WSVLITYYLRHKPWN HHHHHHHHHHCCCCC | 6.65 | 30377154 | |
639 | Phosphorylation | IKRQEKDSSSPIISQ HHHHCCCCCCCCCCC | 43.73 | 28889911 | |
640 | Phosphorylation | KRQEKDSSSPIISQR HHHCCCCCCCCCCCC | 50.71 | 22369663 | |
641 | Phosphorylation | RQEKDSSSPIISQRD HHCCCCCCCCCCCCC | 24.87 | 22369663 | |
645 | Phosphorylation | DSSSPIISQRDNHDA CCCCCCCCCCCCCCC | 21.63 | 29688323 | |
686 | Phosphorylation | SSTFHRKSESSLAST EEECCCCCCCCCCCC | 42.54 | 19779198 | |
688 | Phosphorylation | TFHRKSESSLASTSV ECCCCCCCCCCCCCC | 37.43 | 27017623 | |
689 | Phosphorylation | FHRKSESSLASTSVA CCCCCCCCCCCCCCC | 24.73 | 19779198 | |
692 | Phosphorylation | KSESSLASTSVAPSS CCCCCCCCCCCCCCC | 26.89 | 19779198 | |
693 | Phosphorylation | SESSLASTSVAPSSS CCCCCCCCCCCCCCC | 22.93 | 19779198 | |
694 | Phosphorylation | ESSLASTSVAPSSSS CCCCCCCCCCCCCCC | 17.49 | 19779198 | |
698 | Phosphorylation | ASTSVAPSSSSEFEV CCCCCCCCCCCCCHH | 32.87 | 21440633 | |
699 | Phosphorylation | STSVAPSSSSEFEVE CCCCCCCCCCCCHHH | 36.50 | 20377248 | |
700 | Phosphorylation | TSVAPSSSSEFEVEN CCCCCCCCCCCHHHH | 37.92 | 20377248 | |
701 | Phosphorylation | SVAPSSSSEFEVENE CCCCCCCCCCHHHHH | 48.53 | 21440633 | |
733 | Phosphorylation | NKRIGENTAREEEEE HHHHCCCCCCHHHHH | 23.84 | 23749301 |
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 GPT1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GPT1_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 GPT1_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-641, AND MASSSPECTROMETRY. |