| UniProt ID | NGG1_YEAST | |
|---|---|---|
| UniProt AC | P32494 | |
| Protein Name | Chromatin-remodeling complexes subunit NGG1 | |
| Gene Name | NGG1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 702 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Transcription regulator. Could inhibit GAL4 DNA-binding or its ability to activate transcription. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, SLIK and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B.. | |
| Protein Sequence | MPRHGRRGKLPKGEKLPKKEGGDNTPSKLLSSMLKTLDLTFERDIGMLNGKSVRSIPNKKTLLELQSQLDSLNEILGTIARGDQETIEALRKIRDSKNEKQANDEKQETSNADGQHESSTATEETNIIDKGVQSPPKPPPSNEISGTIENDVESIKQAADNMAKEEINEDKDLQVHRDQPREKRPFDSETENRATENENTQRPDNKKQKIDVDKMENDPTVKNPKSEFVVSQTLPRAAAALGLFNEEGLESTGEDFLKKKYNVASYPTNDLKDLLPGELPDMDFSHPKPTNQIQFNTFLAFVENFFKDLSDDNLKFLKMKYIIPDSLQFDKTYDPEVNPFIIPKLGPLYTDVWFKDENDKNSAYKKPSPYSNDASTILPKKSANELDDNALESGSISCGPLLSRLLSAVLKDDNDKSELQSSKIIRDGGLPRTGGEDDIQSFRNNNNDTVDMTLSQENGPSVQTPDNDIDEEASFQAKLAENKGSNGGTTSTLPQQIGWITNGINLDYPTFEERLKRELKYVGIYMNLPKDENNPNSDDPDWVTGREDDEISAELRELQGTLKQVTKKNQKRKAQLIPLVERQLAWQEYSSILEDLDKQIDQAYVKRIRVPKKRKKHHTAASNNVNTGTTSQIAQQKAANSSLKSLLDKRQRWINKIGPLFDKPEIMKRIPNESVFKDMDQEEDEDEADVFAQNTNKDVELN | |
| 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 |
|---|---|---|---|---|---|
| 15 | Acetylation | GKLPKGEKLPKKEGG CCCCCCCCCCCCCCC | 77.94 | 22865919 | |
| 25 | Phosphorylation | KKEGGDNTPSKLLSS CCCCCCCCHHHHHHH | 33.41 | 27214570 | |
| 27 | Phosphorylation | EGGDNTPSKLLSSML CCCCCCHHHHHHHHH | 33.62 | 27214570 | |
| 51 | Acetylation | DIGMLNGKSVRSIPN HHHCCCCCCCCCCCC | 44.71 | 24489116 | |
| 134 | Phosphorylation | IIDKGVQSPPKPPPS CCCCCCCCCCCCCCC | 40.54 | 22369663 | |
| 141 | Phosphorylation | SPPKPPPSNEISGTI CCCCCCCCCCCCCCC | 53.52 | 25521595 | |
| 145 | Phosphorylation | PPPSNEISGTIENDV CCCCCCCCCCCHHHH | 24.57 | 22369663 | |
| 147 | Phosphorylation | PSNEISGTIENDVES CCCCCCCCCHHHHHH | 20.51 | 22369663 | |
| 154 | Phosphorylation | TIENDVESIKQAADN CCHHHHHHHHHHHHH | 34.63 | 22369663 | |
| 156 | Acetylation | ENDVESIKQAADNMA HHHHHHHHHHHHHHH | 43.07 | 25381059 | |
| 183 | Acetylation | HRDQPREKRPFDSET CCCCCCCCCCCCHHH | 67.65 | 24489116 | |
| 188 | Phosphorylation | REKRPFDSETENRAT CCCCCCCHHHCCCCC | 46.96 | 28889911 | |
| 190 | Phosphorylation | KRPFDSETENRATEN CCCCCHHHCCCCCCC | 42.38 | 28889911 | |
| 206 | Acetylation | NTQRPDNKKQKIDVD CCCCCCCCCCCCCHH | 65.05 | 25381059 | |
| 231 | Phosphorylation | PKSEFVVSQTLPRAA CCHHHEEECHHHHHH | 16.49 | 25752575 | |
| 259 | Acetylation | TGEDFLKKKYNVASY CCHHHHHHHHCCCCC | 63.74 | 24489116 | |
| 260 | Acetylation | GEDFLKKKYNVASYP CHHHHHHHHCCCCCC | 40.23 | 25381059 | |
| 362 | Phosphorylation | KDENDKNSAYKKPSP CCCCCCCCCCCCCCC | 38.42 | 26447709 | |
| 364 | Phosphorylation | ENDKNSAYKKPSPYS CCCCCCCCCCCCCCC | 21.26 | 26447709 | |
| 365 | Acetylation | NDKNSAYKKPSPYSN CCCCCCCCCCCCCCC | 58.90 | 24489116 | |
| 368 | Phosphorylation | NSAYKKPSPYSNDAS CCCCCCCCCCCCCCC | 45.40 | 26447709 | |
| 407 | Phosphorylation | PLLSRLLSAVLKDDN HHHHHHHHHHHCCCC | 22.41 | 28889911 | |
| 416 | Acetylation | VLKDDNDKSELQSSK HHCCCCCCHHHHHCC | 52.68 | 24489116 | |
| 423 | Acetylation | KSELQSSKIIRDGGL CHHHHHCCEEECCCC | 47.61 | 25381059 | |
| 441 | Phosphorylation | GGEDDIQSFRNNNND CCCCHHHHHHHCCCC | 26.89 | 27214570 | |
| 464 | Phosphorylation | ENGPSVQTPDNDIDE CCCCCCCCCCCCCCH | 30.38 | 28889911 | |
| 537 | Phosphorylation | KDENNPNSDDPDWVT CCCCCCCCCCCCCCC | 44.65 | 28889911 | |
| 668 | Acetylation | FDKPEIMKRIPNESV CCCHHHHHHCCCCHH | 53.49 | 22865919 |
| 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 NGG1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NGG1_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 NGG1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-134; SER-231; SER-407;SER-441 AND THR-464, AND MASS SPECTROMETRY. | |
| "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-134, AND MASSSPECTROMETRY. | |
| "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 SER-134, AND MASSSPECTROMETRY. | |
