UniProt ID | GBP2_YEAST | |
---|---|---|
UniProt AC | P25555 | |
Protein Name | Single-strand telomeric DNA-binding protein GBP2 | |
Gene Name | GBP2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 427 | |
Subcellular Localization | Nucleus . Chromosome, telomere. | |
Protein Description | Binds single-stranded telomeric sequences of the type (TG[1-3])n in vitro. Also binds to RNA. Influences the localization of RAP1 in the nuclei. Involved in modulating telomere length.. | |
Protein Sequence | MERELGMYGNDRSRSRSPVRRRLSDDRDRYDDYNDSSSNNGNGSRRQRRDRGSRFNDRYDQSYGGSRYHDDRNWPPRRGGRGRGGSRSFRGGRGGGRGRTLGPIVERDLERQFDATKRNFENSIFVRNLTFDCTPEDLKELFGTVGEVVEADIITSKGHHRGMGTVEFTKNESVQDAISKFDGALFMDRKLMVRQDNPPPEAAKEFSKKATREEIDNGFEVFIINLPYSMNWQSLKDMFKECGHVLRADVELDFNGFSRGFGSVIYPTEDEMIRAIDTFNGMEVEGRVLEVREGRFNKRKNNDRYNQRREDLEDTRGTEPGLAQDAAVHIDETAAKFTEGVNPGGDRNCFIYCSNLPFSTARSDLFDLFGPIGKINNAELKPQENGQPTGVAVVEYENLVDADFCIQKLNNYNYGGCSLQISYARRD | |
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 |
---|---|---|---|---|---|
8 | Phosphorylation | MERELGMYGNDRSRS CCCCCCCCCCCCCCC | 15.81 | 28132839 | |
13 | Phosphorylation | GMYGNDRSRSRSPVR CCCCCCCCCCCCCCH | 37.15 | 19684113 | |
15 | Phosphorylation | YGNDRSRSRSPVRRR CCCCCCCCCCCCHHH | 38.05 | 19684113 | |
17 | Phosphorylation | NDRSRSRSPVRRRLS CCCCCCCCCCHHHCC | 29.06 | 19684113 | |
24 | Phosphorylation | SPVRRRLSDDRDRYD CCCHHHCCCCCCCCC | 35.34 | 17563356 | |
30 | Phosphorylation | LSDDRDRYDDYNDSS CCCCCCCCCCCCCCC | 19.91 | 28889911 | |
33 | Phosphorylation | DRDRYDDYNDSSSNN CCCCCCCCCCCCCCC | 20.26 | 28889911 | |
36 | Phosphorylation | RYDDYNDSSSNNGNG CCCCCCCCCCCCCCC | 31.84 | 28889911 | |
37 | Phosphorylation | YDDYNDSSSNNGNGS CCCCCCCCCCCCCCC | 39.69 | 28889911 | |
38 | Phosphorylation | DDYNDSSSNNGNGSR CCCCCCCCCCCCCCC | 37.96 | 28889911 | |
44 | Phosphorylation | SSNNGNGSRRQRRDR CCCCCCCCCHHHHHC | 28.43 | 30377154 | |
130 | Phosphorylation | SIFVRNLTFDCTPED CEEEEEEEECCCHHH | 22.45 | 28889911 | |
169 | Phosphorylation | GMGTVEFTKNESVQD CCCEEEEECCHHHHH | 21.32 | 27017623 | |
170 | Acetylation | MGTVEFTKNESVQDA CCEEEEECCHHHHHH | 65.13 | 24489116 | |
180 | Acetylation | SVQDAISKFDGALFM HHHHHHHHCCCCEEE | 41.16 | 24489116 | |
240 | Acetylation | QSLKDMFKECGHVLR HHHHHHHHHHCCEEE | 45.52 | 24489116 | |
363 | Phosphorylation | LPFSTARSDLFDLFG CCCCCCCHHHHHHHC | 35.88 | 30377154 |
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 GBP2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GBP2_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 GBP2_YEAST !! |
Kegg Drug | ||||||
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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-24, AND MASSSPECTROMETRY. | |
"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-130, AND MASSSPECTROMETRY. |