| UniProt ID | ELP4_YEAST | |
|---|---|---|
| UniProt AC | Q02884 | |
| Protein Name | Elongator complex protein 4 | |
| Gene Name | ELP4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 456 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | Acts as component of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (RNAPII) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling. It acetylates histones H3, preferentially at 'Lys-14', and H4, preferentially at 'Lys-8'. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitiviy to Pichia inositovora toxin. May be involved in tRNA modification. ELP4 is required for the complex integrity and the complex HAT activity but is not required for the association of the complex with nascent RNA transcript. Is required for an early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) groups present on uridines at the wobble position in tRNA.. | |
| Protein Sequence | MSFRKRGEILNDRGSGLRGPLLRGPPRTSSTPLRTGNRRAPGNVPLSDTTARLKKLNIADESKTKMGLDSSHVGVRPSPATSQPTTSTGSADLDSILGHMGLPLGNSVLVEEQSTTEFHSILGKLFAAQGIVHNRISDSSADKTRNGDTHVIVLSLNQMFAKELPGIYKGSRKQMKKNLISEEESKVTVQNLNETQRSTPSRYKDLKIAWKYKLADEKRLGSPDRDDIQQNSEYKDYNHQFDITTRLMPAPIASELTFIAPTQPVSTILSQIEQTIKRNDKKLIRIVIPSLLHPAMYPPKMFESSEIIGLMHGVRSLVKKYYERVVLFASISIDIITPPLLVLLRNMFDSVINLEPFNQEMTEFLERVYKSQPGKIQHGLVHILKLPVFTDRGEMRVLKSEWAFKNGRKKFEIEQWGIPVDDAEGSAASEQSHSHSHSDEISHNIPAKKTKISLDY | |
| 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 |
|---|---|---|---|---|---|
| 47 | Phosphorylation | APGNVPLSDTTARLK CCCCCCCCHHHHHHH | 27.17 | 28889911 | |
| 222 | Phosphorylation | ADEKRLGSPDRDDIQ CCCCCCCCCCHHHHH | 28.37 | 17330950 | |
| 232 | Phosphorylation | RDDIQQNSEYKDYNH HHHHHHCHHCCCCCC | 37.66 | 19823750 | |
| 234 | Phosphorylation | DIQQNSEYKDYNHQF HHHHCHHCCCCCCCC | 14.69 | 19823750 |
| 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 ELP4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ELP4_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 ELP4_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-222, 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-222, AND MASSSPECTROMETRY. | |
