UniProt ID | RAD26_YEAST | |
---|---|---|
UniProt AC | P40352 | |
Protein Name | DNA repair and recombination protein RAD26 | |
Gene Name | RAD26 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1085 | |
Subcellular Localization | Nucleus . | |
Protein Description | May be involved in the preferential repair of active genes.. | |
Protein Sequence | MEDKEQQDNAKLENNESLKDLGVNVLSQSSLEEKIANDVTNFSNLQSLQQEETRLERSKTALQRYVNKKNHLTRKLNNTTRISVKQNLRDQIKNLQSDDIERVLKDIDDIQSRIKELKEQVDQGAENKGSKEGLQRPGETEKEFLIRTGKITAFGHKAGFSLDTANREYAKNDEQKDEDFEMATEQMVENLTDEDDNLSDQDYQMSGKESEDDEEEENDDKILKELEDLRFRGQPGEAKDDGDELYYQERLKKWVKQRSCGSQRSSDLPEWRRPHPNIPDAKLNSQFKIPGEIYSLLFNYQKTCVQWLYELYQQNCGGIIGDEMGLGKTIQVIAFIAALHHSGLLTGPVLIVCPATVMKQWCNEFQHWWPPLRTVILHSMGSGMASDQKFKMDENDLENLIMNSKPSDFSYEDWKNSTRTKKALESSYHLDKLIDKVVTDGHILITTYVGLRIHSDKLLKVKWQYAVLDEGHKIRNPDSEISLTCKKLKTHNRIILSGTPIQNNLTELWSLFDFIFPGKLGTLPVFQQQFVIPINIGGYANATNIQVQTGYKCAVALRDLISPYLLRRVKADVAKDLPQKKEMVLFCKLTKYQRSKYLEFLHSSDLNQIQNGKRNVLFGIDILRKICNHPDLLDRDTKRHNPDYGDPKRSGKMQVVKQLLLLWHKQGYKALLFTQSRQMLDILEEFISTKDPDLSHLNYLRMDGTTNIKGRQSLVDRFNNESFDVFLLTTRVGGLGVNLTGANRIIIFDPDWNPSTDMQARERAWRIGQKREVSIYRLMVGGSIEEKIYHRQIFKQFLTNRILTDPKQKRFFKIHELHDLFSLGGENGYSTEELNEEVQKHTENLKNSKSEESDDFEQLVNLSGVSKLESFYNGKEKKENSKTEDDRLIEGLLGGESNLETVMSHDSVVNSHAGSSSSNIITKEASRVAIEAVNALRKSRKKITKQYEIGTPTWTGRFGKAGKIRKRDPLKNKLTGSAAILGNITKSQKEASKEARQENYDDGITFARSKEINSNTKTLENIRAYLQKQNNFFSSSVSILNSIGVSLSDKEDVIKVRALLKTIAQFDKERKGWVLDEEFRNNNAS | |
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 |
---|---|---|---|---|---|
17 | Phosphorylation | AKLENNESLKDLGVN HHHCCCHHHHHHCCC | 42.73 | 19795423 | |
19 | Ubiquitination | LENNESLKDLGVNVL HCCCHHHHHHCCCCC | 61.25 | 19722269 | |
27 | Phosphorylation | DLGVNVLSQSSLEEK HHCCCCCCCHHHHHH | 24.59 | 28152593 | |
29 | Phosphorylation | GVNVLSQSSLEEKIA CCCCCCCHHHHHHHH | 33.25 | 28889911 | |
30 | Phosphorylation | VNVLSQSSLEEKIAN CCCCCCHHHHHHHHH | 31.96 | 28152593 | |
97 | Phosphorylation | DQIKNLQSDDIERVL HHHHHCCHHHHHHHH | 40.18 | 28889911 | |
184 | Phosphorylation | DEDFEMATEQMVENL HHHHHHHHHHHHHHC | 25.99 | 19779198 | |
192 | Phosphorylation | EQMVENLTDEDDNLS HHHHHHCCCCCCCCC | 49.26 | 19779198 | |
206 | Phosphorylation | SDQDYQMSGKESEDD CHHHHHHCCCCCCCC | 31.05 | 28889911 | |
210 | Phosphorylation | YQMSGKESEDDEEEE HHHCCCCCCCCCHHH | 50.22 | 28889911 | |
853 | Phosphorylation | KNSKSEESDDFEQLV HCCCCCCCCCHHHHH | 38.13 | 27214570 | |
863 | Phosphorylation | FEQLVNLSGVSKLES HHHHHCHHHHHHHHH | 31.76 | 27017623 | |
866 | Phosphorylation | LVNLSGVSKLESFYN HHCHHHHHHHHHHHC | 34.74 | 30377154 | |
870 | Phosphorylation | SGVSKLESFYNGKEK HHHHHHHHHHCCCCC | 43.39 | 30377154 | |
872 | Phosphorylation | VSKLESFYNGKEKKE HHHHHHHHCCCCCCC | 32.08 | 30377154 | |
975 | Phosphorylation | DPLKNKLTGSAAILG CCCCCCCCCCHHHHH | 30.60 | 19823750 | |
977 | Phosphorylation | LKNKLTGSAAILGNI CCCCCCCCHHHHHCC | 14.86 | 19823750 | |
985 | Phosphorylation | AAILGNITKSQKEAS HHHHHCCCHHHHHHH | 28.74 | 19823750 | |
1042 | Phosphorylation | SSVSILNSIGVSLSD HHHHHHHHCCCCCCC | 19.78 | 28889911 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
27 | S | Phosphorylation | Kinase | MEC1 | P38111 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD26_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 RAD26_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-27 AND SER-29, AND MASSSPECTROMETRY. |