UniProt ID | YNG2_YEAST | |
---|---|---|
UniProt AC | P38806 | |
Protein Name | Chromatin modification-related protein YNG2 | |
Gene Name | YNG2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 282 | |
Subcellular Localization | Nucleus . | |
Protein Description | Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in cell cycle progression and meiosis.. | |
Protein Sequence | MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKKKYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQSLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPVEEDGDMDSAAEASRESSVVSNSSVKKRRAASSSGSVPPTLKKKKTSRTSKLQNEIDVSSREKSVTPVSPSIEKKIARTKEFKNSRNGKGQNGSPENEEEDKTLYCFCQRVSFGEMVACDGPNCKYEWFHYDCVNLKEPPKGTWYCPECKIEMEKNKLKRKRN | |
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 |
---|---|---|---|---|---|
128 | Phosphorylation | EEDGDMDSAAEASRE CCCCCHHHHHHHHHH | 23.81 | 21440633 | |
133 | Phosphorylation | MDSAAEASRESSVVS HHHHHHHHHHHHCCC | 28.25 | 21440633 | |
136 | Phosphorylation | AAEASRESSVVSNSS HHHHHHHHHCCCCCH | 27.59 | 21551504 | |
137 | Phosphorylation | AEASRESSVVSNSSV HHHHHHHHCCCCCHH | 23.06 | 21551504 | |
140 | Phosphorylation | SRESSVVSNSSVKKR HHHHHCCCCCHHHHH | 28.92 | 28889911 | |
143 | Phosphorylation | SSVVSNSSVKKRRAA HHCCCCCHHHHHHHH | 42.05 | 21440633 | |
145 | Acetylation | VVSNSSVKKRRAASS CCCCCHHHHHHHHHC | 42.37 | 23572591 | |
146 | Acetylation | VSNSSVKKRRAASSS CCCCHHHHHHHHHCC | 44.98 | 23572591 | |
151 | Phosphorylation | VKKRRAASSSGSVPP HHHHHHHHCCCCCCC | 24.85 | 21440633 | |
155 | Phosphorylation | RAASSSGSVPPTLKK HHHHCCCCCCCCCCC | 33.14 | 29734811 | |
170 | Acetylation | KKTSRTSKLQNEIDV CCCCCCHHHHHHCCC | 54.18 | 24489116 | |
178 | Phosphorylation | LQNEIDVSSREKSVT HHHHCCCCCCCCCCC | 21.67 | 24961812 | |
179 | Phosphorylation | QNEIDVSSREKSVTP HHHCCCCCCCCCCCC | 44.28 | 24961812 | |
183 | Phosphorylation | DVSSREKSVTPVSPS CCCCCCCCCCCCCHH | 26.86 | 22369663 | |
185 | Phosphorylation | SSREKSVTPVSPSIE CCCCCCCCCCCHHHH | 25.68 | 22369663 | |
188 | Phosphorylation | EKSVTPVSPSIEKKI CCCCCCCCHHHHHHH | 17.71 | 22369663 | |
190 | Phosphorylation | SVTPVSPSIEKKIAR CCCCCCHHHHHHHHH | 35.55 | 22369663 | |
199 | Acetylation | EKKIARTKEFKNSRN HHHHHHCHHHHCCCC | 56.45 | 25381059 | |
202 | Acetylation | IARTKEFKNSRNGKG HHHCHHHHCCCCCCC | 55.92 | 25381059 | |
208 | Acetylation | FKNSRNGKGQNGSPE HHCCCCCCCCCCCCC | 61.95 | 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 YNG2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YNG2_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 YNG2_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-188, AND MASSSPECTROMETRY. | |
"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-188, AND MASSSPECTROMETRY. |