UniProt ID | 6PGD1_YEAST | |
---|---|---|
UniProt AC | P38720 | |
Protein Name | 6-phosphogluconate dehydrogenase, decarboxylating 1 | |
Gene Name | GND1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 489 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.. | |
Protein Sequence | MSADFGLIGLAVMGQNLILNAADHGFTVCAYNRTQSKVDHFLANEAKGKSIIGATSIEDFISKLKRPRKVMLLVKAGAPVDALINQIVPLLEKGDIIIDGGNSHFPDSNRRYEELKKKGILFVGSGVSGGEEGARYGPSLMPGGSEEAWPHIKNIFQSISAKSDGEPCCEWVGPAGAGHYVKMVHNGIEYGDMQLICEAYDIMKRLGGFTDKEISDVFAKWNNGVLDSFLVEITRDILKFDDVDGKPLVEKIMDTAGQKGTGKWTAINALDLGMPVTLIGEAVFARCLSALKNERIRASKVLPGPEVPKDAVKDREQFVDDLEQALYASKIISYAQGFMLIREAAATYGWKLNNPAIALMWRGGCIIRSVFLGQITKAYREEPDLENLLFNKFFADAVTKAQSGWRKSIALATTYGIPTPAFSTALSFYDGYRSERLPANLLQAQRDYFGAHTFRVLPECASDNLPVDKDIHINWTGHGGNVSSSTYQA | |
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 |
---|---|---|---|---|---|
36 | Phosphorylation | CAYNRTQSKVDHFLA EEEECCHHHHHHHHH | 33.75 | 30377154 | |
37 | Acetylation | AYNRTQSKVDHFLAN EEECCHHHHHHHHHC | 41.69 | 24489116 | |
37 | Ubiquitination | AYNRTQSKVDHFLAN EEECCHHHHHHHHHC | 41.69 | 23749301 | |
37 | Succinylation | AYNRTQSKVDHFLAN EEECCHHHHHHHHHC | 41.69 | 23954790 | |
47 | 2-Hydroxyisobutyrylation | HFLANEAKGKSIIGA HHHHCHHCCCCEECC | 61.77 | - | |
47 | Ubiquitination | HFLANEAKGKSIIGA HHHHCHHCCCCEECC | 61.77 | 17644757 | |
47 | Acetylation | HFLANEAKGKSIIGA HHHHCHHCCCCEECC | 61.77 | 22865919 | |
49 | Ubiquitination | LANEAKGKSIIGATS HHCHHCCCCEECCCC | 37.46 | 17644757 | |
50 | Phosphorylation | ANEAKGKSIIGATSI HCHHCCCCEECCCCH | 28.27 | 21440633 | |
55 | Phosphorylation | GKSIIGATSIEDFIS CCCEECCCCHHHHHH | 25.64 | 24961812 | |
56 | Phosphorylation | KSIIGATSIEDFISK CCEECCCCHHHHHHH | 24.36 | 24961812 | |
62 | Phosphorylation | TSIEDFISKLKRPRK CCHHHHHHHCCCCCE | 31.74 | 30377154 | |
63 | Ubiquitination | SIEDFISKLKRPRKV CHHHHHHHCCCCCEE | 53.89 | 17644757 | |
63 | Acetylation | SIEDFISKLKRPRKV CHHHHHHHCCCCCEE | 53.89 | 24489116 | |
65 | Ubiquitination | EDFISKLKRPRKVML HHHHHHCCCCCEEEE | 65.18 | 17644757 | |
75 | Ubiquitination | RKVMLLVKAGAPVDA CEEEEEEECCCCHHH | 40.86 | 19722269 | |
116 | Acetylation | NRRYEELKKKGILFV CHHHHHHHHCCEEEE | 56.57 | 25381059 | |
117 | Ubiquitination | RRYEELKKKGILFVG HHHHHHHHCCEEEEC | 69.71 | 17644757 | |
118 | Ubiquitination | RYEELKKKGILFVGS HHHHHHHCCEEEECC | 49.98 | 17644757 | |
128 | Phosphorylation | LFVGSGVSGGEEGAR EEECCCCCCCCCCCC | 44.60 | 28889911 | |
145 | Phosphorylation | PSLMPGGSEEAWPHI CCCCCCCCHHHHHHH | 37.87 | 21082442 | |
153 | Ubiquitination | EEAWPHIKNIFQSIS HHHHHHHHHHHHHHH | 40.74 | 17644757 | |
153 | Acetylation | EEAWPHIKNIFQSIS HHHHHHHHHHHHHHH | 40.74 | 24489116 | |
158 | Phosphorylation | HIKNIFQSISAKSDG HHHHHHHHHHCCCCC | 14.04 | 22369663 | |
160 | Phosphorylation | KNIFQSISAKSDGEP HHHHHHHHCCCCCCC | 34.59 | 22369663 | |
162 | Ubiquitination | IFQSISAKSDGEPCC HHHHHHCCCCCCCCC | 42.14 | 17644757 | |
163 | Phosphorylation | FQSISAKSDGEPCCE HHHHHCCCCCCCCCC | 51.03 | 21440633 | |
182 | Ubiquitination | AGAGHYVKMVHNGIE CCCCCCEEEEECCCC | 28.21 | 17644757 | |
212 | Acetylation | RLGGFTDKEISDVFA HHCCCCCHHHHHHHH | 54.62 | 24489116 | |
239 | Acetylation | EITRDILKFDDVDGK HHHHHHHCCCCCCCC | 47.26 | 24489116 | |
239 | 2-Hydroxyisobutyrylation | EITRDILKFDDVDGK HHHHHHHCCCCCCCC | 47.26 | - | |
239 | Ubiquitination | EITRDILKFDDVDGK HHHHHHHCCCCCCCC | 47.26 | 17644757 | |
246 | 2-Hydroxyisobutyrylation | KFDDVDGKPLVEKIM CCCCCCCCCHHHHHH | 30.62 | - | |
246 | Acetylation | KFDDVDGKPLVEKIM CCCCCCCCCHHHHHH | 30.62 | 24489116 | |
246 | Ubiquitination | KFDDVDGKPLVEKIM CCCCCCCCCHHHHHH | 30.62 | 23749301 | |
251 | Acetylation | DGKPLVEKIMDTAGQ CCCCHHHHHHHCCCC | 35.53 | 24489116 | |
251 | Ubiquitination | DGKPLVEKIMDTAGQ CCCCHHHHHHHCCCC | 35.53 | 17644757 | |
259 | Ubiquitination | IMDTAGQKGTGKWTA HHHCCCCCCCCCCCH | 58.48 | 23749301 | |
259 | 2-Hydroxyisobutyrylation | IMDTAGQKGTGKWTA HHHCCCCCCCCCCCH | 58.48 | - | |
259 | Succinylation | IMDTAGQKGTGKWTA HHHCCCCCCCCCCCH | 58.48 | 23954790 | |
263 | Ubiquitination | AGQKGTGKWTAINAL CCCCCCCCCCHHHHH | 41.01 | 23749301 | |
289 | Phosphorylation | AVFARCLSALKNERI HHHHHHHHHHHCCCC | 34.87 | 23749301 | |
292 | Ubiquitination | ARCLSALKNERIRAS HHHHHHHHCCCCCHH | 57.38 | 23749301 | |
292 | Acetylation | ARCLSALKNERIRAS HHHHHHHHCCCCCHH | 57.38 | 25381059 | |
292 | Succinylation | ARCLSALKNERIRAS HHHHHHHHCCCCCHH | 57.38 | 23954790 | |
300 | Succinylation | NERIRASKVLPGPEV CCCCCHHCCCCCCCC | 46.97 | 23954790 | |
309 | Acetylation | LPGPEVPKDAVKDRE CCCCCCCHHHHCCHH | 64.59 | 24489116 | |
309 | Succinylation | LPGPEVPKDAVKDRE CCCCCCCHHHHCCHH | 64.59 | 23954790 | |
309 | 2-Hydroxyisobutyrylation | LPGPEVPKDAVKDRE CCCCCCCHHHHCCHH | 64.59 | - | |
313 | Acetylation | EVPKDAVKDREQFVD CCCHHHHCCHHHHHH | 53.43 | 24489116 | |
313 | Succinylation | EVPKDAVKDREQFVD CCCHHHHCCHHHHHH | 53.43 | 23954790 | |
330 | Ubiquitination | EQALYASKIISYAQG HHHHHHHHHHHHHHH | 35.57 | 17644757 | |
351 | Ubiquitination | AAATYGWKLNNPAIA HHHHHCCCCCCHHHH | 36.65 | 17644757 | |
377 | Acetylation | VFLGQITKAYREEPD HHHHHHHHHHHHCCC | 45.08 | 24489116 | |
400 | 2-Hydroxyisobutyrylation | FFADAVTKAQSGWRK HHHHHHHHHHHCHHH | 37.52 | - | |
400 | Acetylation | FFADAVTKAQSGWRK HHHHHHHHHHHCHHH | 37.52 | 24489116 | |
408 | Phosphorylation | AQSGWRKSIALATTY HHHCHHHHHHHHHHC | 12.43 | 22369663 | |
413 | Phosphorylation | RKSIALATTYGIPTP HHHHHHHHHCCCCCH | 22.77 | 22369663 | |
414 | Phosphorylation | KSIALATTYGIPTPA HHHHHHHHCCCCCHH | 17.72 | 22369663 | |
415 | Phosphorylation | SIALATTYGIPTPAF HHHHHHHCCCCCHHH | 14.54 | 22369663 | |
419 | Phosphorylation | ATTYGIPTPAFSTAL HHHCCCCCHHHHHHH | 25.90 | 22369663 | |
423 | Phosphorylation | GIPTPAFSTALSFYD CCCCHHHHHHHHHHH | 18.19 | 22369663 | |
424 | Phosphorylation | IPTPAFSTALSFYDG CCCHHHHHHHHHHHC | 25.76 | 22369663 | |
427 | Phosphorylation | PAFSTALSFYDGYRS HHHHHHHHHHHCCCC | 21.21 | 22369663 | |
429 | Phosphorylation | FSTALSFYDGYRSER HHHHHHHHHCCCCCC | 12.70 | 22369663 | |
432 | Phosphorylation | ALSFYDGYRSERLPA HHHHHHCCCCCCCCH | 14.20 | 22369663 | |
462 | Phosphorylation | RVLPECASDNLPVDK EECHHHHCCCCCCCC | 38.40 | 28889911 | |
476 | Phosphorylation | KDIHINWTGHGGNVS CCEEEECCCCCCCCC | 18.14 | 22369663 | |
483 | Phosphorylation | TGHGGNVSSSTYQA- CCCCCCCCCCCCCC- | 23.67 | 21440633 | |
484 | Phosphorylation | GHGGNVSSSTYQA-- CCCCCCCCCCCCC-- | 23.55 | 22369663 | |
485 | Phosphorylation | HGGNVSSSTYQA--- CCCCCCCCCCCC--- | 24.51 | 22369663 | |
486 | Phosphorylation | GGNVSSSTYQA---- CCCCCCCCCCC---- | 22.92 | 22369663 | |
487 | Phosphorylation | GNVSSSTYQA----- CCCCCCCCCC----- | 12.37 | 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 6PGD1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 6PGD1_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 6PGD1_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MDHM_YEAST | MDH1 | physical | 11805837 | |
EF3B_YEAST | HEF3 | physical | 11805837 | |
KIP3_YEAST | KIP3 | physical | 11805837 | |
6PGD2_YEAST | GND2 | physical | 16554755 | |
6PGD1_YEAST | GND1 | physical | 17570834 | |
6PGD2_YEAST | GND2 | genetic | 18408719 | |
6PGD2_YEAST | GND2 | genetic | 16941010 | |
RPE_YEAST | RPE1 | genetic | 16941010 | |
TKT1_YEAST | TKL1 | genetic | 16941010 | |
TKT2_YEAST | TKL2 | genetic | 16941010 |
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-128, AND MASSSPECTROMETRY. |