UniProt ID | IMDH4_YEAST | |
---|---|---|
UniProt AC | P50094 | |
Protein Name | Inosine-5'-monophosphate dehydrogenase 4 {ECO:0000255|HAMAP-Rule:MF_03156} | |
Gene Name | IMD4 {ECO:0000255|HAMAP-Rule:MF_03156} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 524 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.. | |
Protein Sequence | MSAAPLDYKKALEHLKTYSSKDGLSVQELMDSTTRGGLTYNDFLVLPGLVNFPSSAVSLQTKLTKKITLNTPFVSSPMDTVTEADMAIYMALLGGIGFIHHNCTPKEQASMVKKVKMFENGFINSPIVISPTTTVGEVKVMKRKFGFSGFPVTEDGKCPGKLVGLVTSRDIQFLEDDSLVVSEVMTKNPVTGIKGITLKEGNEILKQTKKGKLLIVDDNGNLVSMLSRADLMKNQNYPLASKSATTKQLLCGAAIGTIEADKERLRLLVEAGLDVVILDSSQGNSVFQLNMIKWIKETFPDLEIIAGNVATREQAANLIAAGADGLRIGMGSGSICITQEVMACGRPQGTAVYNVCQFANQFGVPCMADGGVQNIGHITKALALGSSTVMMGGMLAGTTESPGEYFYKDGKRLKAYRGMGSIDAMQKTGNKGNASTSRYFSESDSVLVAQGVSGAVVDKGSIKKFIPYLYNGLQHSCQDIGCESLTSLKENVQNGEVRFEFRTASAQLEGGVHNLHSYEKRLYN | |
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 | ------MSAAPLDYK ------CCCCCCCHH | 32.89 | 22369663 | |
8 | Phosphorylation | MSAAPLDYKKALEHL CCCCCCCHHHHHHHH | 23.28 | 22369663 | |
9 | Succinylation | SAAPLDYKKALEHLK CCCCCCHHHHHHHHH | 31.10 | 23954790 | |
16 | Acetylation | KKALEHLKTYSSKDG HHHHHHHHHCCCCCC | 47.53 | 22865919 | |
16 | Ubiquitination | KKALEHLKTYSSKDG HHHHHHHHHCCCCCC | 47.53 | 22817900 | |
21 | Succinylation | HLKTYSSKDGLSVQE HHHHCCCCCCCCHHH | 50.29 | 23954790 | |
21 | Acetylation | HLKTYSSKDGLSVQE HHHHCCCCCCCCHHH | 50.29 | 24489116 | |
21 | Ubiquitination | HLKTYSSKDGLSVQE HHHHCCCCCCCCHHH | 50.29 | 22817900 | |
71 | Phosphorylation | TKKITLNTPFVSSPM CCEEECCCCCCCCCC | 22.63 | 30377154 | |
76 | Phosphorylation | LNTPFVSSPMDTVTE CCCCCCCCCCCCCCH | 20.95 | 30377154 | |
80 | Phosphorylation | FVSSPMDTVTEADMA CCCCCCCCCCHHHHH | 24.07 | 30377154 | |
89 | Phosphorylation | TEADMAIYMALLGGI CHHHHHHHHHHHCCC | 2.70 | 30377154 | |
104 | Phosphorylation | GFIHHNCTPKEQASM CCCCCCCCHHHHHHH | 42.59 | 30377154 | |
113 | Succinylation | KEQASMVKKVKMFEN HHHHHHHHHHHEECC | 43.11 | 23954790 | |
125 | Phosphorylation | FENGFINSPIVISPT ECCCCCCCCEEECCC | 15.93 | 28889911 | |
144 | Acetylation | EVKVMKRKFGFSGFP EEEEEECCCCCCCCC | 44.30 | 24489116 | |
157 | Acetylation | FPVTEDGKCPGKLVG CCCCCCCCCCCEEEE | 49.96 | 24489116 | |
161 | Acetylation | EDGKCPGKLVGLVTS CCCCCCCEEEEEEEC | 25.74 | 22865919 | |
168 | Phosphorylation | KLVGLVTSRDIQFLE EEEEEEECCCCCCCC | 22.07 | 28889911 | |
194 | Acetylation | KNPVTGIKGITLKEG CCCCCCCCCEEECCC | 45.68 | 22865919 | |
199 | Succinylation | GIKGITLKEGNEILK CCCCEEECCCCHHHH | 55.73 | 23954790 | |
199 | Acetylation | GIKGITLKEGNEILK CCCCEEECCCCHHHH | 55.73 | 24489116 | |
212 | Acetylation | LKQTKKGKLLIVDDN HHCCCCCCEEEECCC | 49.34 | 24489116 | |
233 | Acetylation | LSRADLMKNQNYPLA HHHHHHHHCCCCCCC | 63.78 | 24489116 | |
386 | Phosphorylation | TKALALGSSTVMMGG HHHHHHCCCEEEECC | 24.56 | 19823750 | |
387 | Phosphorylation | KALALGSSTVMMGGM HHHHHCCCEEEECCC | 24.19 | 19823750 | |
388 | Phosphorylation | ALALGSSTVMMGGML HHHHCCCEEEECCCC | 17.70 | 19823750 | |
398 | Phosphorylation | MGGMLAGTTESPGEY ECCCCCCCCCCCCCC | 23.06 | 19823750 | |
399 | Phosphorylation | GGMLAGTTESPGEYF CCCCCCCCCCCCCCC | 33.28 | 19823750 | |
401 | Phosphorylation | MLAGTTESPGEYFYK CCCCCCCCCCCCCCC | 35.79 | 19823750 | |
405 | Phosphorylation | TTESPGEYFYKDGKR CCCCCCCCCCCCCCE | 20.37 | 19823750 | |
407 | Phosphorylation | ESPGEYFYKDGKRLK CCCCCCCCCCCCEEE | 13.78 | 19823750 | |
408 | Acetylation | SPGEYFYKDGKRLKA CCCCCCCCCCCEEEE | 50.54 | 22865919 | |
416 | Phosphorylation | DGKRLKAYRGMGSID CCCEEEECCCCCHHH | 13.20 | 27717283 | |
421 | Phosphorylation | KAYRGMGSIDAMQKT EECCCCCHHHHHHHH | 14.38 | 22369663 | |
428 | Phosphorylation | SIDAMQKTGNKGNAS HHHHHHHHCCCCCCC | 29.15 | 23749301 | |
439 | Phosphorylation | GNASTSRYFSESDSV CCCCCCCCCCCCCEE | 15.95 | 27017623 | |
441 | Phosphorylation | ASTSRYFSESDSVLV CCCCCCCCCCCEEEE | 27.53 | 28889911 | |
443 | Phosphorylation | TSRYFSESDSVLVAQ CCCCCCCCCEEEEEC | 33.71 | 30377154 | |
445 | Phosphorylation | RYFSESDSVLVAQGV CCCCCCCEEEEECCC | 26.99 | 30377154 | |
459 | Ubiquitination | VSGAVVDKGSIKKFI CCCEEECHHHHHHHH | 42.84 | 22817900 | |
463 | Ubiquitination | VVDKGSIKKFIPYLY EECHHHHHHHHHHHH | 43.24 | 22817900 | |
464 | Ubiquitination | VDKGSIKKFIPYLYN ECHHHHHHHHHHHHH | 47.02 | 22817900 | |
503 | Phosphorylation | EVRFEFRTASAQLEG EEEEEEECCEEEECC | 30.22 | 24961812 | |
505 | Phosphorylation | RFEFRTASAQLEGGV EEEEECCEEEECCCC | 18.88 | 28889911 | |
517 | Phosphorylation | GGVHNLHSYEKRLYN CCCCCHHHHHHHHCC | 37.85 | 24961812 | |
518 | Phosphorylation | GVHNLHSYEKRLYN- CCCCHHHHHHHHCC- | 18.09 | 30377154 | |
520 | Acetylation | HNLHSYEKRLYN--- CCHHHHHHHHCC--- | 39.20 | 25381059 | |
520 | Ubiquitination | HNLHSYEKRLYN--- CCHHHHHHHHCC--- | 39.20 | 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 IMDH4_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IMDH4_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 IMDH4_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-125 AND SER-168, ANDMASS SPECTROMETRY. |