UniProt ID | ARA1_YEAST | |
---|---|---|
UniProt AC | P38115 | |
Protein Name | D-arabinose dehydrogenase [NAD(P)+] heavy chain | |
Gene Name | ARA1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 344 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Catalyzes the oxidation of D-arabinose, L-xylose, L-fucose and L-galactose in the presence of NADP(+).. | |
Protein Sequence | MSSSVASTENIVENMLHPKTTEIYFSLNNGVRIPALGLGTANPHEKLAETKQAVKAAIKAGYRHIDTAWAYETEPFVGEAIKELLEDGSIKREDLFITTKVWPVLWDEVDRSLNESLKALGLEYVDLLLQHWPLCFEKIKDPKGISGLVKTPVDDSGKTMYAADGDYLETYKQLEKIYLDPNDHRVRAIGVSNFSIEYLERLIKECRVKPTVNQVETHPHLPQMELRKFCFMHDILLTAYSPLGSHGAPNLKIPLVKKLAEKYNVTGNDLLISYHIRQGTIVIPRSLNPVRISSSIEFASLTKDELQELNDFGEKYPVRFIDEPFAAILPEFTGNGPNLDNLKY | |
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 | ------MSSSVASTE ------CCCCCCCCH | 31.18 | 22369663 | |
3 | Phosphorylation | -----MSSSVASTEN -----CCCCCCCCHH | 27.77 | 22369663 | |
4 | Phosphorylation | ----MSSSVASTENI ----CCCCCCCCHHH | 17.88 | 22369663 | |
7 | Phosphorylation | -MSSSVASTENIVEN -CCCCCCCCHHHHHH | 33.81 | 22369663 | |
8 | Phosphorylation | MSSSVASTENIVENM CCCCCCCCHHHHHHH | 24.26 | 22369663 | |
21 | Phosphorylation | NMLHPKTTEIYFSLN HHCCCCCCEEEEECC | 26.89 | 27017623 | |
24 | Phosphorylation | HPKTTEIYFSLNNGV CCCCCEEEEECCCCC | 4.85 | 27017623 | |
26 | Phosphorylation | KTTEIYFSLNNGVRI CCCEEEEECCCCCEE | 17.14 | 27017623 | |
46 | Acetylation | GTANPHEKLAETKQA CCCCHHHHHHHHHHH | 50.38 | 24489116 | |
91 | 2-Hydroxyisobutyrylation | LLEDGSIKREDLFIT HHHCCCCCHHHCEEE | 51.97 | - | |
143 | Acetylation | FEKIKDPKGISGLVK HHHCCCCCCCCCCEE | 78.12 | 24489116 | |
150 | Ubiquitination | KGISGLVKTPVDDSG CCCCCCEECEECCCC | 52.75 | 23749301 | |
150 | Acetylation | KGISGLVKTPVDDSG CCCCCCEECEECCCC | 52.75 | 24489116 | |
151 | Phosphorylation | GISGLVKTPVDDSGK CCCCCEECEECCCCC | 22.51 | 22369663 | |
156 | Phosphorylation | VKTPVDDSGKTMYAA EECEECCCCCEEEEE | 37.41 | 30377154 | |
158 | Ubiquitination | TPVDDSGKTMYAADG CEECCCCCEEEEECC | 33.79 | 23749301 | |
158 | Acetylation | TPVDDSGKTMYAADG CEECCCCCEEEEECC | 33.79 | 24489116 | |
159 | Phosphorylation | PVDDSGKTMYAADGD EECCCCCEEEEECCC | 20.95 | 28889911 | |
161 | Phosphorylation | DDSGKTMYAADGDYL CCCCCEEEEECCCHH | 12.13 | 28889911 | |
167 | Phosphorylation | MYAADGDYLETYKQL EEEECCCHHHHHHHH | 16.39 | 28889911 | |
170 | Phosphorylation | ADGDYLETYKQLEKI ECCCHHHHHHHHHHH | 33.16 | 28889911 | |
172 | Acetylation | GDYLETYKQLEKIYL CCHHHHHHHHHHHCC | 56.69 | 24489116 | |
280 | Phosphorylation | SYHIRQGTIVIPRSL EEEEECCEEEEECCC | 12.06 | 28889911 | |
293 | Phosphorylation | SLNPVRISSSIEFAS CCCCEECCCEEEECC | 13.89 | 22369663 | |
294 | Phosphorylation | LNPVRISSSIEFASL CCCEECCCEEEECCC | 32.72 | 22369663 | |
295 | Phosphorylation | NPVRISSSIEFASLT CCEECCCEEEECCCC | 21.24 | 22369663 | |
300 | Phosphorylation | SSSIEFASLTKDELQ CCEEEECCCCHHHHH | 41.72 | 22369663 | |
302 | Phosphorylation | SIEFASLTKDELQEL EEEECCCCHHHHHHH | 33.67 | 22369663 | |
315 | Acetylation | ELNDFGEKYPVRFID HHHHHCHHCCEEECC | 56.06 | 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 ARA1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARA1_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 ARA1_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 THR-151 AND SER-294, ANDMASS 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 THR-151, AND MASSSPECTROMETRY. |