UniProt ID | RPAB2_YEAST | |
---|---|---|
UniProt AC | P20435 | |
Protein Name | DNA-directed RNA polymerases I, II, and III subunit RPABC2 | |
Gene Name | RPO26 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 155 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds.. | |
Protein Sequence | MSDYEEAFNDGNENFEDFDVEHFSDEETYEEKPQFKDGETTDANGKTIVTGGNGPEDFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEELIVDL | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSDYEEAFN ------CCHHHHHHC | 49.23 | 22369663 | |
4 | Phosphorylation | ----MSDYEEAFNDG ----CCHHHHHHCCC | 14.36 | 19795423 | |
24 | Phosphorylation | DFDVEHFSDEETYEE CCCCCCCCCCCCCCC | 46.12 | 22369663 | |
28 | Phosphorylation | EHFSDEETYEEKPQF CCCCCCCCCCCCCCC | 33.90 | 22369663 | |
29 | Phosphorylation | HFSDEETYEEKPQFK CCCCCCCCCCCCCCC | 25.93 | 22369663 | |
46 | Ubiquitination | ETTDANGKTIVTGGN CEECCCCCEEEECCC | 34.58 | 23749301 | |
46 | Acetylation | ETTDANGKTIVTGGN CEECCCCCEEEECCC | 34.58 | 24489116 | |
82 | Phosphorylation | PKDQRATTPYMTKYE CCCHHCCCCCCCHHH | 16.07 | 28889911 | |
102 | Phosphorylation | GTRALQISMNAPVFV CCEEEEEECCCCEEE | 7.94 | 28889911 | |
123 | Ubiquitination | DPLRIAMKELAEKKI CHHHHHHHHHHHCCC | 40.32 | 23749301 |
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 RPAB2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPAB2_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 RPAB2_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-24 AND THR-82, AND MASSSPECTROMETRY. |