UniProt ID | SERA_YEAST | |
---|---|---|
UniProt AC | P40054 | |
Protein Name | D-3-phosphoglycerate dehydrogenase 1 | |
Gene Name | SER3 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 469 | |
Subcellular Localization | ||
Protein Description | Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.. | |
Protein Sequence | MTSIDINNLQNTFQQAMNMSGSPGAVCTSPTQSFMNTVPQRLNAVKHPKILKPFSTGDMKILLLENVNQTAITIFEEQGYQVEFYKSSLPEEELIEKIKDVHAIGIRSKTRLTSNVLQHAKNLVCIGCFCIGTNQVDLDYATSRGIAVFNSPFSNSRSVAELVIAEIISLARQLGDRSIELHTGTWNKVAARCWEVRGKTLGIIGYGHIGSQLSVLAEAMGLHVLYYDIVTIMALGTARQVSTLDELLNKSDFVTLHVPATPETEKMLSAPQFAAMKDGAYVINASRGTVVDIPSLIQAVKANKIAGAALDVYPHEPAKNGEGSFNDELNSWTSELVSLPNIILTPHIGGSTEEAQSSIGIEVATALSKYINEGNSVGSVNFPEVALKSLSYDQENTVRVLYIHQNVPGVLKTVNDILSNHNIEKQFSDSNGEIAYLMADISSVDQSDIKDIYEQLNQTSAKISIRLLY | |
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 | ------MTSIDINNL ------CCCEEHHHH | 34.10 | 30377154 | |
12 | Phosphorylation | DINNLQNTFQQAMNM EHHHHHHHHHHHHHC | 15.17 | 30377154 | |
20 | Phosphorylation | FQQAMNMSGSPGAVC HHHHHHCCCCCCCEE | 30.99 | 28889911 | |
22 | Phosphorylation | QAMNMSGSPGAVCTS HHHHCCCCCCCEECC | 16.92 | 28889911 | |
29 | Phosphorylation | SPGAVCTSPTQSFMN CCCCEECCCCHHHHH | 22.33 | 28889911 | |
33 | Phosphorylation | VCTSPTQSFMNTVPQ EECCCCHHHHHCHHH | 29.01 | 30377154 | |
46 | Acetylation | PQRLNAVKHPKILKP HHHHHCCCCCCCCCC | 52.35 | 25381059 | |
52 | Acetylation | VKHPKILKPFSTGDM CCCCCCCCCCCCCCE | 47.71 | 22865919 | |
55 | Phosphorylation | PKILKPFSTGDMKIL CCCCCCCCCCCEEEE | 39.75 | 19823750 | |
56 | Phosphorylation | KILKPFSTGDMKILL CCCCCCCCCCEEEEE | 37.26 | 19823750 | |
97 | Acetylation | PEEELIEKIKDVHAI CHHHHHHHHHHHHHC | 48.32 | 22865919 | |
99 | Acetylation | EELIEKIKDVHAIGI HHHHHHHHHHHHCCC | 65.84 | 22865919 | |
121 | Ubiquitination | SNVLQHAKNLVCIGC HHHHHHHHCEEEEEE | 49.00 | 17644757 | |
188 | Ubiquitination | LHTGTWNKVAARCWE EECCCHHHHHHHHHE | 25.47 | 17644757 | |
188 | Acetylation | LHTGTWNKVAARCWE EECCCHHHHHHHHHE | 25.47 | 24489116 | |
242 | Phosphorylation | LGTARQVSTLDELLN HCCHHCCCCHHHHHC | 18.21 | 28889911 | |
243 | Phosphorylation | GTARQVSTLDELLNK CCHHCCCCHHHHHCC | 39.10 | 30377154 | |
250 | Acetylation | TLDELLNKSDFVTLH CHHHHHCCCCCEEEE | 51.91 | 24489116 | |
250 | Ubiquitination | TLDELLNKSDFVTLH CHHHHHCCCCCEEEE | 51.91 | 24961812 | |
261 | Phosphorylation | VTLHVPATPETEKML EEEECCCCHHHHHHH | 18.65 | 22369663 | |
264 | Phosphorylation | HVPATPETEKMLSAP ECCCCHHHHHHHCCH | 41.95 | 22369663 | |
369 | Ubiquitination | EVATALSKYINEGNS HHHHHHHHHHHCCCC | 51.50 | 17644757 | |
388 | Ubiquitination | NFPEVALKSLSYDQE CCHHHHHHHCCCCCC | 39.34 | 17644757 | |
412 | Ubiquitination | QNVPGVLKTVNDILS CCCCCHHHHHHHHHH | 48.28 | 17644757 | |
413 | Phosphorylation | NVPGVLKTVNDILSN CCCCHHHHHHHHHHC | 22.00 | 19823750 | |
419 | Phosphorylation | KTVNDILSNHNIEKQ HHHHHHHHCCCHHHH | 36.06 | 19823750 | |
425 | Ubiquitination | LSNHNIEKQFSDSNG HHCCCHHHHCCCCCC | 53.50 | 17644757 | |
428 | Phosphorylation | HNIEKQFSDSNGEIA CCHHHHCCCCCCCEE | 37.32 | 22369663 | |
430 | Phosphorylation | IEKQFSDSNGEIAYL HHHHCCCCCCCEEEE | 45.60 | 22369663 | |
436 | Phosphorylation | DSNGEIAYLMADISS CCCCCEEEEEEECCC | 11.59 | 22369663 | |
442 | Phosphorylation | AYLMADISSVDQSDI EEEEEECCCCCHHHH | 25.51 | 22369663 | |
443 | Phosphorylation | YLMADISSVDQSDIK EEEEECCCCCHHHHH | 30.01 | 22369663 | |
447 | Phosphorylation | DISSVDQSDIKDIYE ECCCCCHHHHHHHHH | 36.52 | 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 SERA_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SERA_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 SERA_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-20; SER-22 AND SER-29,AND MASS SPECTROMETRY. |