| UniProt ID | NGG1_SCHPO | |
|---|---|---|
| UniProt AC | Q9USU8 | |
| Protein Name | Chromatin-remodeling complexes subunit ngg1 | |
| Gene Name | ngg1 | |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
| Sequence Length | 551 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Transcription regulator. 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 a subset of 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 and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. 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. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B.. | |
| Protein Sequence | MSSEQQNEADSKPAVIPQCFKIENQYETFSRLSETSTPGVVPSVSTLWRLLFELQKMIECEPSCVEYFRQRKEELESHVDSEIETSKDESSVNKVEEKVEEFKEDNVEQEIKQKRSLSESPQESMLEKVSKKPKVSEAHNEEISPENVETIENELDLPVKGKDEQTTGLVYKNANDLLTGSLLSFIVDDSFSYEQKKKLLCVDSFPTSDVRSLVAGTPATDDFSHNKPNNQISISTFYSSLDPYFRAFNDDDIAFLKKGFDVSSSYNIPPLGERYYDLTPEDEMTNLCANSIYQNLQTSAQGSLEAFNEADTVSEEVRCGPLTERLMASLIPCYTQNDEEQKPSIAVGEFAETDSGSEKSKIGTSIDGIESGNNEYTEQPDIQESSLSICEDRLRYTLKQLGILYDGDVDWSKRQDDEISATLRSLNARLKVVSDENEKMRNALLQMLPEEMAFQEFQNVMDDLDKQIEQAYVKRNRSLKVKKKRIVTDKIGSSATSGSFPVIKSLMDKRSMWLEKLQPLFQDKLTQHLGSPTSIFNDLSDHTTSNYSTSV | |
| 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 |
|---|---|---|---|---|---|
| 77 | Phosphorylation | QRKEELESHVDSEIE HHHHHHHHHHCHHCC | 41.24 | 24763107 | |
| 81 | Phosphorylation | ELESHVDSEIETSKD HHHHHHCHHCCCCCC | 39.11 | 21712547 | |
| 116 | Phosphorylation | QEIKQKRSLSESPQE HHHHHHHCCCCCCCH | 43.19 | 21712547 | |
| 118 | Phosphorylation | IKQKRSLSESPQESM HHHHHCCCCCCCHHH | 36.96 | 24763107 | |
| 120 | Phosphorylation | QKRSLSESPQESMLE HHHCCCCCCCHHHHH | 28.62 | 28889911 | |
| 136 | Phosphorylation | VSKKPKVSEAHNEEI HHCCCCHHHHCCCCC | 34.88 | 21712547 | |
| 144 | Phosphorylation | EAHNEEISPENVETI HHCCCCCCHHHHHHH | 29.46 | 28889911 |
| 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_SCHPO !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NGG1_SCHPO !! | ||||||
* 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_SCHPO !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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