| UniProt ID | YAJ8_YEAST | |
|---|---|---|
| UniProt AC | P39548 | |
| Protein Name | DUP240 protein YAR028W | |
| Gene Name | YAR028W | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 234 | |
| Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
| Protein Description | ||
| Protein Sequence | MQTPSENTDVKMDTLDEPSAHLIEENVALPEDTFSSHLSYVLYEIAHCKPIMFMIIIIVSLISLIVLFHDNDGCTVILVMSLIVASMALMVVAAFTFGKAITEQEFMIKLLVEVIARKPAGKEWGTVAYNMNQYLFMKRLWYTPYYFYSGKKCHEFFTTLIKEVNSGSHSDSSSNSAEDTQSPVSAGKTSNGLNNFYSIRSDPILMAYVLKATQIEKEAQSEYWRKQYPDADLP | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MQTPSENTDV -----CCCCCCCCCC | 27.73 | 21126336 | |
| 5 | Phosphorylation | ---MQTPSENTDVKM ---CCCCCCCCCCCC | 47.03 | 27717283 | |
| 8 | Phosphorylation | MQTPSENTDVKMDTL CCCCCCCCCCCCCCC | 37.81 | 27717283 | |
| 118 | Ubiquitination | LVEVIARKPAGKEWG HHHHHHCCCCCCCCC | 30.14 | 22817900 | |
| 122 | Ubiquitination | IARKPAGKEWGTVAY HHCCCCCCCCCCEEE | 53.02 | 22817900 | |
| 142 | Phosphorylation | LFMKRLWYTPYYFYS HHHHHHHCCCEEEEC | 11.48 | 30377154 | |
| 143 | Phosphorylation | FMKRLWYTPYYFYSG HHHHHHCCCEEEECC | 8.01 | 28889911 | |
| 145 | Phosphorylation | KRLWYTPYYFYSGKK HHHHCCCEEEECCCH | 9.82 | 30377154 | |
| 146 | Phosphorylation | RLWYTPYYFYSGKKC HHHCCCEEEECCCHH | 9.39 | 30377154 | |
| 148 | Phosphorylation | WYTPYYFYSGKKCHE HCCCEEEECCCHHHH | 10.61 | 28889911 | |
| 149 | Phosphorylation | YTPYYFYSGKKCHEF CCCEEEECCCHHHHH | 33.95 | 28889911 | |
| 166 | Phosphorylation | TLIKEVNSGSHSDSS HHHHHHHCCCCCCCC | 47.01 | 22369663 | |
| 168 | Phosphorylation | IKEVNSGSHSDSSSN HHHHHCCCCCCCCCC | 21.46 | 22369663 | |
| 170 | Phosphorylation | EVNSGSHSDSSSNSA HHHCCCCCCCCCCCC | 40.67 | 20377248 | |
| 172 | Phosphorylation | NSGSHSDSSSNSAED HCCCCCCCCCCCCCC | 38.39 | 23749301 | |
| 173 | Phosphorylation | SGSHSDSSSNSAEDT CCCCCCCCCCCCCCC | 38.23 | 22369663 | |
| 174 | Phosphorylation | GSHSDSSSNSAEDTQ CCCCCCCCCCCCCCC | 38.46 | 22369663 | |
| 176 | Phosphorylation | HSDSSSNSAEDTQSP CCCCCCCCCCCCCCC | 34.68 | 22369663 | |
| 180 | Phosphorylation | SSNSAEDTQSPVSAG CCCCCCCCCCCCCCC | 23.58 | 22369663 | |
| 182 | Phosphorylation | NSAEDTQSPVSAGKT CCCCCCCCCCCCCCC | 29.39 | 22369663 | |
| 185 | Phosphorylation | EDTQSPVSAGKTSNG CCCCCCCCCCCCCCC | 34.39 | 22369663 | |
| 188 | Ubiquitination | QSPVSAGKTSNGLNN CCCCCCCCCCCCCCC | 48.79 | 23749301 | |
| 217 | Ubiquitination | LKATQIEKEAQSEYW HHHHHHHHHHHHHHH | 61.04 | 23749301 | |
| 226 | Ubiquitination | AQSEYWRKQYPDADL HHHHHHHHHCCCCCC | 39.78 | 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 YAJ8_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YAJ8_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 YAJ8_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-182, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery."; Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.; Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-217, AND MASSSPECTROMETRY. | |