UniProt ID | RPAB4_YEAST | |
---|---|---|
UniProt AC | P40422 | |
Protein Name | DNA-directed RNA polymerases I, II, and III subunit RPABC4 | |
Gene Name | RPC10 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 70 | |
Subcellular Localization | Nucleus, nucleolus . | |
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 a small RNAs, such as 5S rRNA and tRNAs, respectively. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, the core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center.. | |
Protein Sequence | MSREGFQIPTNLDAAAAGTSQARTATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLVQFEAR | |
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 | ------MSREGFQIP ------CCCCCCCCC | 38.75 | 22369663 | |
10 | Phosphorylation | REGFQIPTNLDAAAA CCCCCCCCCHHHHHC | 50.47 | 22369663 | |
19 | Phosphorylation | LDAAAAGTSQARTAT HHHHHCCCHHHHHHH | 16.97 | 22369663 | |
20 | Phosphorylation | DAAAAGTSQARTATL HHHHCCCHHHHHHHH | 22.41 | 22369663 | |
26 | Phosphorylation | TSQARTATLKYICAE CHHHHHHHHHHHHHH | 24.14 | 21440633 | |
28 | Ubiquitination | QARTATLKYICAECS HHHHHHHHHHHHHCC | 28.37 | 23749301 | |
28 | Acetylation | QARTATLKYICAECS HHHHHHHHHHHHHCC | 28.37 | 24489116 | |
35 | Phosphorylation | KYICAECSSKLSLSR HHHHHHCCCCCCCCC | 23.24 | 28889911 | |
36 | Phosphorylation | YICAECSSKLSLSRT HHHHHCCCCCCCCCC | 49.64 | 21440633 | |
39 | Phosphorylation | AECSSKLSLSRTDAV HHCCCCCCCCCCCCE | 28.21 | 30377154 | |
41 | Phosphorylation | CSSKLSLSRTDAVRC CCCCCCCCCCCCEEC | 29.74 | 30377154 | |
43 | Phosphorylation | SKLSLSRTDAVRCKD CCCCCCCCCCEECCC | 25.57 | 21440633 |
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 RPAB4_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPAB4_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 RPAB4_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RPA2_YEAST | RPA135 | physical | 10531351 | |
PAN3_YEAST | PAN3 | physical | 10531351 | |
TFC4_YEAST | TFC4 | physical | 10559229 | |
RPC2_YEAST | RET1 | genetic | 10531351 | |
RPB2_YEAST | RPB2 | genetic | 10531351 | |
RPA2_YEAST | RPA135 | genetic | 10531351 | |
DED1_YEAST | DED1 | genetic | 10531351 | |
PABP_YEAST | PAB1 | genetic | 10531351 | |
PBP2_YEAST | PBP2 | genetic | 10531351 | |
TFC4_YEAST | TFC4 | genetic | 10559229 | |
INA22_YEAST | INA22 | physical | 16554755 | |
MSH2_YEAST | MSH2 | physical | 16554755 | |
RPA43_YEAST | RPA43 | physical | 16554755 | |
RPA1_YEAST | RPA190 | physical | 16554755 | |
RPA2_YEAST | RPA135 | physical | 16554755 | |
RPAC1_YEAST | RPC40 | physical | 16554755 | |
SEC23_YEAST | SEC23 | genetic | 20101242 | |
TCPB_YEAST | CCT2 | genetic | 20101242 | |
RS5_YEAST | RPS5 | genetic | 20101242 |
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-20, AND MASSSPECTROMETRY. |