| UniProt ID | FCP1_YEAST | |
|---|---|---|
| UniProt AC | Q03254 | |
| Protein Name | RNA polymerase II subunit A C-terminal domain phosphatase | |
| Gene Name | FCP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 732 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). This promotes the activity of RNA polymerase II.. | |
| Protein Sequence | MTTQIRSPQGLPYPIQIDKLIPSVGSYLHEGDRLLVYKFWYLVERASDTGDDDNEHDVSPGGSAGSNGVSPPTKQLRESIEFFESPYEGDLISWNVDVGDEVATANQVICEIKRPCNHDIVYGGLCTQCGKEVSADAFDGVPLDVVGDVDLQISETEAIRTGKALKEHLRRDKKLILVVDLDQTIIHCGVDPTIAEWKNDPNNPNFETLRDVKSFTLDEELVLPLMYMNDDGSMLRPPPVRKCWYYVKVRPGLKEFFAKVAPLFEMHIYTMATRAYALQIAKIVDPTGELFGDRILSRDENGSLTTKSLAKLFPTDQSMVVVIDDRGDVWNWCPNLIKVVPYNFFVGVGDINSNFLPKQSTGMLQLGRKTRQKSQESQELLTDIMDNEKKLQEKIDKEVKRQEEKLNHQLATAEEPPANESKEELTKKLEYSASLEVQQQNRPLAKLQKHLHDQKLLVDDDDELYYLMGTLSNIHKTYYDMLSQQNEPEPNLMEIIPSLKQKVFQNCYFVFSGLIPLGTDIQRSDIVIWTSTFGATSTPDIDYLTTHLITKNPSTYKARLAKKFNPQIKIVHPDWIFECLVNWKKVDEKPYTLIVDSPISDEELQNFQTQLQKRQEYLEETQEQQHMLTSQENLNLFAAGTSWLNNDDDEDIPDTASDDDEDDDHDDESDDENNSEGIDRKRSIEDNHDDTSQKKTKAEPSQDGPVQHKGEGDDNEDSDSQLEEELMDMLDD | |
| 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 | WYLVERASDTGDDDN HHHHHHHHCCCCCCC | 41.76 | 22369663 | |
| 49 | Phosphorylation | LVERASDTGDDDNEH HHHHHHCCCCCCCCC | 39.76 | 22369663 | |
| 59 | Phosphorylation | DDNEHDVSPGGSAGS CCCCCCCCCCCCCCC | 24.72 | 22369663 | |
| 63 | Phosphorylation | HDVSPGGSAGSNGVS CCCCCCCCCCCCCCC | 35.06 | 22369663 | |
| 66 | Phosphorylation | SPGGSAGSNGVSPPT CCCCCCCCCCCCCCH | 30.08 | 22369663 | |
| 70 | Phosphorylation | SAGSNGVSPPTKQLR CCCCCCCCCCHHHHH | 26.93 | 23749301 | |
| 74 | Ubiquitination | NGVSPPTKQLRESIE CCCCCCHHHHHHHHH | 53.78 | 23749301 | |
| 214 | Phosphorylation | ETLRDVKSFTLDEEL HHHHCCCCCCCCHHH | 24.26 | 19779198 | |
| 216 | Phosphorylation | LRDVKSFTLDEELVL HHCCCCCCCCHHHEE | 40.15 | 19779198 | |
| 227 | Phosphorylation | ELVLPLMYMNDDGSM HHEEEEEEECCCCCC | 10.64 | 19779198 | |
| 233 | Phosphorylation | MYMNDDGSMLRPPPV EEECCCCCCCCCCCC | 22.95 | 30377154 | |
| 303 | Phosphorylation | LSRDENGSLTTKSLA CCCCCCCCCCHHHHH | 33.84 | 25752575 | |
| 370 | Phosphorylation | MLQLGRKTRQKSQES CHHHCHHHHHHHHHH | 36.65 | 28889911 | |
| 374 | Phosphorylation | GRKTRQKSQESQELL CHHHHHHHHHHHHHH | 30.73 | 28889911 | |
| 377 | Phosphorylation | TRQKSQESQELLTDI HHHHHHHHHHHHHHH | 22.71 | 28889911 | |
| 382 | Phosphorylation | QESQELLTDIMDNEK HHHHHHHHHHHHHHH | 35.78 | 28889911 | |
| 422 | Acetylation | EPPANESKEELTKKL CCCCCCCHHHHHHHH | 49.37 | 24489116 | |
| 683 | Phosphorylation | EGIDRKRSIEDNHDD CCCCHHHCCCCCCCC | 33.11 | 28889911 | |
| 691 | Phosphorylation | IEDNHDDTSQKKTKA CCCCCCCCCCCCCCC | 38.83 | 30377154 | |
| 692 | Phosphorylation | EDNHDDTSQKKTKAE CCCCCCCCCCCCCCC | 47.17 | 30377154 | |
| 694 | Acetylation | NHDDTSQKKTKAEPS CCCCCCCCCCCCCCC | 63.28 | 25381059 | |
| 701 | Phosphorylation | KKTKAEPSQDGPVQH CCCCCCCCCCCCCCC | 32.20 | 28889911 | |
| 718 | Phosphorylation | EGDDNEDSDSQLEEE CCCCCCCCHHHHHHH | 32.74 | 21440633 | |
| 720 | Phosphorylation | DDNEDSDSQLEEELM CCCCCCHHHHHHHHH | 40.39 | 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 FCP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FCP1_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 FCP1_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-701, AND MASSSPECTROMETRY. | |
