UniProt ID | GPT2_YEAST | |
---|---|---|
UniProt AC | P36148 | |
Protein Name | Glycerol-3-phosphate O-acyltransferase 2 | |
Gene Name | GPT2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 743 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | G-3-P/dihydroxyacetone phosphate dual substrate-specific sn-1 acyltransferase.. | |
Protein Sequence | MSAPAADHNAAKPIPHVPQASRRYKNSYNGFVYNIHTWLYDVSVFLFNILFTIFFREIKVRGAYNVPEVGVPTILVCAPHANQFIDPALVMSQTRLLKTSAGKSRSRMPCFVTAESSFKKRFISFFGHAMGGIPVPRIQDNLKPVDENLEIYAPDLKNHPEIIKGRSKNPQTTPVNFTKRFSAKSLLGLPDYLSNAQIKEIPDDETIILSSPFRTSKSKVVELLTNGTNFKYAEKIDNTETFQSVFDHLHTKGCVGIFPEGGSHDRPSLLPIKAGVAIMALGAVAADPTMKVAVVPCGLHYFHRNKFRSRAVLEYGEPIVVDGKYGEMYKDSPRETVSKLLKKITNSLFSVTENAPDYDTLMVIQAARRLYQPVKVRLPLPAIVEINRRLLFGYSKFKDDPRIIHLKKLVYDYNRKLDSVGLKDHQVMQLKTTKLEALRCFVTLIVRLIKFSVFAILSLPGSILFTPIFIICRVYSEKKAKEGLKKSLVKIKGTDLLATWKLIVALILAPILYVTYSILLIILARKQHYCRIWVPSNNAFIQFVYFYALLVFTTYSSLKTGEIGVDLFKSLRPLFVSIVYPGKKIEEIQTTRKNLSLELTAVCNDLGPLVFPDYDKLATEIFSKRDGYDVSSDAESSISRMSVQSRSRSSSIHSIGSLASNALSRVNSRGSLTDIPIFSDAKQGQWKSEGETSEDEDEFDEKNPAIVQTARSSDLNKENSRNTNISSKIASLVRQKREHEKKE | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSAPAADHN ------CCCCCCCCC | 42.85 | 24961812 | |
12 | Acetylation | AADHNAAKPIPHVPQ CCCCCCCCCCCCCCH | 40.86 | 25381059 | |
113 | Phosphorylation | SRMPCFVTAESSFKK CCCCEEEEECHHHHH | 12.40 | 19779198 | |
143 | Acetylation | PRIQDNLKPVDENLE CCCCCCCCCCCCCCE | 49.61 | 24489116 | |
211 | Phosphorylation | DETIILSSPFRTSKS CCCEEECCCCCCCCH | 25.31 | 28889911 | |
225 | Phosphorylation | SKVVELLTNGTNFKY HHHHHHHHCCCCCEE | 44.20 | 28889911 | |
231 | Acetylation | LTNGTNFKYAEKIDN HHCCCCCEEEEECCC | 45.69 | 24489116 | |
596 | Phosphorylation | QTTRKNLSLELTAVC HHCCCCCCHHHHHHC | 29.23 | 19779198 | |
600 | Phosphorylation | KNLSLELTAVCNDLG CCCCHHHHHHCCCCC | 13.99 | 19779198 | |
614 | Phosphorylation | GPLVFPDYDKLATEI CCCCCCCHHHHHHHH | 18.40 | 19779198 | |
628 | Phosphorylation | IFSKRDGYDVSSDAE HHHCCCCCCCCCCCC | 19.91 | 22369663 | |
631 | Phosphorylation | KRDGYDVSSDAESSI CCCCCCCCCCCCHHH | 21.43 | 22369663 | |
632 | Phosphorylation | RDGYDVSSDAESSIS CCCCCCCCCCCHHHH | 40.46 | 22369663 | |
636 | Phosphorylation | DVSSDAESSISRMSV CCCCCCCHHHHHHCH | 34.39 | 22369663 | |
637 | Phosphorylation | VSSDAESSISRMSVQ CCCCCCHHHHHHCHH | 18.98 | 22369663 | |
639 | Phosphorylation | SDAESSISRMSVQSR CCCCHHHHHHCHHCC | 24.71 | 22369663 | |
647 | Phosphorylation | RMSVQSRSRSSSIHS HHCHHCCCCCCCCHH | 41.58 | 19795423 | |
649 | Phosphorylation | SVQSRSRSSSIHSIG CHHCCCCCCCCHHHH | 29.68 | 22369663 | |
650 | Phosphorylation | VQSRSRSSSIHSIGS HHCCCCCCCCHHHHH | 32.00 | 22369663 | |
651 | Phosphorylation | QSRSRSSSIHSIGSL HCCCCCCCCHHHHHH | 26.10 | 22369663 | |
654 | Phosphorylation | SRSSSIHSIGSLASN CCCCCCHHHHHHHHH | 27.29 | 22369663 | |
657 | Phosphorylation | SSIHSIGSLASNALS CCCHHHHHHHHHHHH | 21.06 | 22369663 | |
660 | Phosphorylation | HSIGSLASNALSRVN HHHHHHHHHHHHHCC | 28.12 | 22369663 | |
664 | Phosphorylation | SLASNALSRVNSRGS HHHHHHHHHCCCCCC | 31.60 | 22369663 | |
668 | Phosphorylation | NALSRVNSRGSLTDI HHHHHCCCCCCCCCC | 34.85 | 22369663 | |
671 | Phosphorylation | SRVNSRGSLTDIPIF HHCCCCCCCCCCCCC | 27.30 | 22369663 | |
673 | Phosphorylation | VNSRGSLTDIPIFSD CCCCCCCCCCCCCCC | 33.31 | 22369663 | |
679 | Phosphorylation | LTDIPIFSDAKQGQW CCCCCCCCCCCCCCC | 37.06 | 22890988 | |
688 | Phosphorylation | AKQGQWKSEGETSED CCCCCCCCCCCCCCC | 48.12 | 22369663 | |
692 | Phosphorylation | QWKSEGETSEDEDEF CCCCCCCCCCCHHHC | 48.55 | 22369663 | |
693 | Phosphorylation | WKSEGETSEDEDEFD CCCCCCCCCCHHHCH | 38.45 | 22369663 | |
728 | Acetylation | RNTNISSKIASLVRQ CCCCHHHHHHHHHHH | 35.19 | 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 GPT2_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 GPT2_YEAST !! |
Kegg Drug | ||||||
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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-211; SER-631; SER-632;SER-668; SER-671; THR-673; SER-688; THR-692 AND SER-693, AND MASSSPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-637; SER-688AND SER-693, AND MASS SPECTROMETRY. | |
"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-654; SER-668 ANDSER-671, AND MASS SPECTROMETRY. | |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND SER-671, ANDMASS SPECTROMETRY. |