UniProt ID | GCN2_SCHPO | |
---|---|---|
UniProt AC | Q9HGN1 | |
Protein Name | eIF-2-alpha kinase GCN2 {ECO:0000312|PomBase:SPBC36B7.09} | |
Gene Name | gcn2 {ECO:0000312|PomBase:SPBC36B7.09} | |
Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
Sequence Length | 1576 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/tif211) on 'Ser-52' in response to low amino acid availability. [PubMed: 15611163 Plays a role as an activator of the general amino acid control (GAAC) pathway required for adapatation to amino acid starvation. Converts phosphorylated eIF-2-alpha/tif211 either to a competitive inhibitor of translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of specific mRNAs, such as the transcriptional activator gcn4, and hence allowing GCN4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion. Binds uncharged tRNAs (By similarity] | |
Protein Sequence | MDAAKRLELCKEIQENEIEALKAIFMDDFEELKVRNAWNVTNGHVYCIHLCSRSANSKSIAKLDLCIELGRSYPYVKPVIKLQNGENVLNSQIRFLLDKLDTKAKDLLGEEMIFELASIVQDYLNDWQSDLSSQFASLEEERAVQLKHDRERAEVDLQLRLKREKDALFEEEQTLQNKIQDELQRRSYETPQSSSKKKTNSKETTSLETLPTSIYFDCSISVRDCHDSLVTFNRVLPLYTISHSNLSTLTLVKPESKEISLQDCVFLLRTVRISTPYWSTEDGKREIQELEYELESLKVIRHDLLASIYEYQLERETRGYGWRLYVLQEYSPKFTLFSLLQTVLTLDVETVRAFSNNILEGLAELHRLGISHKSLHLDNVVLFHSGHRTFAKLMDFGFTRTLRDMNASHPFNINSQSITNILPEGLYPPEVSESSFAAASRKTDIWCFGLLVLQMLCGAHVLNKFSSLKLIMTHVIPLLPGSYQDLVRRCLMRDSRKRPSAIDLLSSHVIRLGTAVLPPVEQGTFSKSARPSYGGQQDGIIDLLYRKSVSRYETDFEELEFLGRGGFGEVVKVKNRIDGRFYAVKKLVLLSDDKENSRILREVMTLSRLHHEHVVRYYTAWVETEANDTVTEIISSDSESLSQSLNMAVDFRQSSSLPADKLSSLDIHFEDDYNSSADEEDPEASDISFQYSNTSDKEGSSDKDSSIEEASSVKTQENGLNATLYIQMEYCEKLSLQDIIRDKIPVDEMWRLFRQILEALAYIHSRGMMHRDLKPGNIFLDENRNVKLGDFGLATENENYQDNNDKWKNRQSADEDLTTGVGTALYVAPELLSRRNGVRYDAKVDMYSLGIILFEMCMTFSTSMERIRIIDTIRSPSISFPSTFPFSRASHEFKVIHCLLQHDPTKRPSSQELLESEAIPPKVGEEFIQEGLRLLSNPNTPYYLKLLKVLFGQVPDRHKDFTYDFNLSEESGVLSKVSDRGWDSLLACLVRDHVVKVFRRHGAKERESHILFPKSSQYDKDQASVSLLDKNGTLLQLPYDTVLPYARNVARNAVEEEKTYLISDVFREAKGGGRPKAIKEISFDITTNSDNLDWYDAETIKALDEVLTEIPSLTESCILINHADILSSILDYLQVSKDKRRMATHILGQINQRLTLSQVRNQLRIESLVPSTTLDDLSLFDFRENYEEGASKLRKIFGKEMPQKMRTALNYMERVVKLLRALKISHQLYFMPLCVYNFEFYDGGLMFQAINLAEKSELICAGGRYDKLVRFFDPPLMRTARKKHVVGICFALEKLVFSMLRYIRFHNSKQSSKHSPSPTLKSVGPWAPRRVDVLVTSIGKDSILEKCSLLQELWALNIQADIVLRGASSLEEIVTHYRSEGINWVLVVRQKNTQMEHSVKARNILKNEDDEIRFDEVGMWLLGEINERKRNESMLQSKRILDSAQQDVAKFVDTSQSNLDVQLISLKDVNDRKYKWKHKQNAMNKVYDLVQSAIRESSEDAIALAVDCDSEAMEKLRSTTTLDEESWKRLIESCPASQREYMQRLQKKLVTLAEQDKKRVWICSFRTNEIYLYGLK | |
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 |
---|---|---|---|---|---|
1315 | Phosphorylation | SKQSSKHSPSPTLKS CCCCCCCCCCCCCCC | 30.70 | 24763107 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of GCN2_SCHPO !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GCN2_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 GCN2_SCHPO !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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