UniProt ID | CIP2_SCHPO | |
---|---|---|
UniProt AC | Q09868 | |
Protein Name | RNA-binding post-transcriptional regulator cip2 | |
Gene Name | cip2 | |
Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
Sequence Length | 576 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Regulates global gene expression after oxidative stress. Interacts and stabilizes mRNAs and may regulate their transition between different cytoplasmic components after oxidative stress.. | |
Protein Sequence | MAEGTSQRPLTPLSQAFLSTNTLSPASSPLTFHSEAASLRRKRSNFFPKLDELNGAQDEEMRGLNIPGGSGYLENRYGRDKFTFSDAAVNSAGMGGSGIFSHNNADDGLGDGSSTVLPSSLKQMLDPEISTANNPSAKPRRTRLQTAWKEATNSAGLSLRSASALDVLKNSGPATTSLLSSTTYPFDSLNAFNEPSHSHVPNSASSTALSRGMSNSVTLTAPPEPDEETIPTAIVIKNIPFSLKKEVLFKVFTALDIPRPYAFNYHFDNGVFRGLAFANFHSPEEAKTVVQVLNGYEITGRRLRVEWKRQLPPAERERVERGKQEKRAVEERKNQLKSPFSVANIGAGIDFDLNDPAILNVYSHILLFYYRSDNTNDLVFDSSTTQEERRVAALLASRLNLNHSVTGDGEAKQVVITMPSTHFTPANNSSANHSPLMAPNASTLNPSSLGASNLSQPSLANHLSSSGLFDNGLFSSGGLSSNFSSLRRPAPSMHLADSIRSLRGLNDSKAFSDIRSMPATPLELATPFANLNVSSPLDRNATNSSNTLNGSAMNDYFASLTPSNTGAIGSRTFTKN | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MAEGTSQRPLTP ---CCCCCCCCCCCH | 17.12 | 29996109 | |
6 | Phosphorylation | --MAEGTSQRPLTPL --CCCCCCCCCCCHH | 34.74 | 29996109 | |
11 | Phosphorylation | GTSQRPLTPLSQAFL CCCCCCCCHHHHHHH | 25.51 | 24763107 | |
14 | Phosphorylation | QRPLTPLSQAFLSTN CCCCCHHHHHHHHCC | 22.21 | 29996109 | |
19 | Phosphorylation | PLSQAFLSTNTLSPA HHHHHHHHCCCCCCC | 17.10 | 24763107 | |
20 | Phosphorylation | LSQAFLSTNTLSPAS HHHHHHHCCCCCCCC | 34.08 | 21712547 | |
22 | Phosphorylation | QAFLSTNTLSPASSP HHHHHCCCCCCCCCC | 28.80 | 21712547 | |
24 | Phosphorylation | FLSTNTLSPASSPLT HHHCCCCCCCCCCCC | 19.17 | 21712547 | |
27 | Phosphorylation | TNTLSPASSPLTFHS CCCCCCCCCCCCCCH | 35.55 | 24763107 | |
28 | Phosphorylation | NTLSPASSPLTFHSE CCCCCCCCCCCCCHH | 26.49 | 21712547 | |
31 | Phosphorylation | SPASSPLTFHSEAAS CCCCCCCCCCHHHHH | 23.76 | 29996109 | |
34 | Phosphorylation | SSPLTFHSEAASLRR CCCCCCCHHHHHHHH | 25.41 | 24763107 | |
38 | Phosphorylation | TFHSEAASLRRKRSN CCCHHHHHHHHHHHH | 29.47 | 29996109 | |
44 | Phosphorylation | ASLRRKRSNFFPKLD HHHHHHHHHCCHHHH | 40.81 | 24763107 | |
70 | Phosphorylation | GLNIPGGSGYLENRY CCCCCCCCCCCCCCC | 30.13 | 25720772 | |
72 | Phosphorylation | NIPGGSGYLENRYGR CCCCCCCCCCCCCCC | 16.73 | 25720772 | |
91 | Phosphorylation | FSDAAVNSAGMGGSG CCHHHHCCCCCCCCC | 21.43 | 21712547 | |
97 | Phosphorylation | NSAGMGGSGIFSHNN CCCCCCCCCCCCCCC | 24.00 | 27738172 | |
120 | Phosphorylation | SSTVLPSSLKQMLDP CCCCCCHHHHHHHCC | 37.33 | 29996109 | |
152 | Phosphorylation | QTAWKEATNSAGLSL HHHHHHHHHHHCCCC | 30.69 | 21712547 | |
154 | Phosphorylation | AWKEATNSAGLSLRS HHHHHHHHHCCCCCC | 21.25 | 29996109 | |
158 | Phosphorylation | ATNSAGLSLRSASAL HHHHHCCCCCCHHHH | 22.33 | 29996109 | |
163 | Phosphorylation | GLSLRSASALDVLKN CCCCCCHHHHHHHHH | 30.52 | 28889911 | |
171 | Phosphorylation | ALDVLKNSGPATTSL HHHHHHHCCCCCHHH | 44.56 | 29996109 | |
175 | Phosphorylation | LKNSGPATTSLLSST HHHCCCCCHHHHCCC | 21.76 | 29996109 | |
203 | Phosphorylation | SHSHVPNSASSTALS CCCCCCCCHHHHCHH | 24.37 | 27738172 | |
214 | Phosphorylation | TALSRGMSNSVTLTA HCHHCCCCCCEEEEC | 28.86 | 29996109 | |
216 | Phosphorylation | LSRGMSNSVTLTAPP HHCCCCCCEEEECCC | 14.79 | 25720772 | |
220 | Phosphorylation | MSNSVTLTAPPEPDE CCCCEEEECCCCCCC | 27.96 | 29996109 | |
512 | Phosphorylation | LNDSKAFSDIRSMPA CCCCCCHHHHHCCCC | 36.67 | 25720772 | |
516 | Phosphorylation | KAFSDIRSMPATPLE CCHHHHHCCCCCCHH | 29.47 | 25720772 | |
520 | Phosphorylation | DIRSMPATPLELATP HHHCCCCCCHHHCCC | 23.64 | 29996109 | |
526 | Phosphorylation | ATPLELATPFANLNV CCCHHHCCCCCCCCC | 31.40 | 29996109 | |
534 | Phosphorylation | PFANLNVSSPLDRNA CCCCCCCCCCCCCCC | 25.76 | 29996109 | |
535 | Phosphorylation | FANLNVSSPLDRNAT CCCCCCCCCCCCCCC | 25.79 | 25720772 | |
542 | Phosphorylation | SPLDRNATNSSNTLN CCCCCCCCCCCCCCC | 38.90 | 25720772 | |
544 | Phosphorylation | LDRNATNSSNTLNGS CCCCCCCCCCCCCHH | 22.17 | 25720772 | |
545 | Phosphorylation | DRNATNSSNTLNGSA CCCCCCCCCCCCHHH | 35.58 | 25720772 | |
561 | Phosphorylation | NDYFASLTPSNTGAI HHHHHHCCCCCCCCC | 23.36 | 27738172 | |
563 | Phosphorylation | YFASLTPSNTGAIGS HHHHCCCCCCCCCCC | 41.61 | 27738172 |
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 CIP2_SCHPO !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CIP2_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 CIP2_SCHPO !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MPH1L_SCHPO | mph1 | genetic | 22681890 | |
LUB1_SCHPO | lub1 | genetic | 22681890 | |
CIP1_SCHPO | cip1 | genetic | 22681890 | |
SEY1_SCHPO | SPAC222.14c | genetic | 22681890 | |
SPP1_SCHPO | spf1 | genetic | 22681890 | |
SET1_SCHPO | set1 | genetic | 22681890 | |
RL16B_SCHPO | rpl1601 | genetic | 22681890 | |
ASK1_SCHPO | ask1 | genetic | 22681890 | |
FFT3_SCHPO | fft3 | genetic | 22681890 | |
DAD2_SCHPO | dad2 | genetic | 22681890 | |
TBA2_SCHPO | atb2 | genetic | 22681890 | |
MU154_SCHPO | mug154 | genetic | 22681890 | |
ASE1_SCHPO | ase1 | genetic | 22681890 | |
HOG1_SCHPO | sty1 | physical | 24755092 | |
CIP2_SCHPO | cip2 | physical | 26771498 | |
SPK1_SCHPO | spk1 | physical | 26771498 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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