| UniProt ID | GCN2_YEAST | |
|---|---|---|
| UniProt AC | P15442 | |
| Protein Name | eIF-2-alpha kinase GCN2 {ECO:0000250|UniProtKB:Q9HGN1} | |
| Gene Name | GCN2 {ECO:0000312|SGD:S000002691} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1659 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52' in response to low amino acid availability. [PubMed: 1739968] | |
| Protein Sequence | MSLSHLTLDQYYEIQCNELEAIRSIYMDDFTDLTKRKSSWDKQPQIIFEITLRSVDKEPVESSITLHFAMTPMYPYTAPEIEFKNVQNVMDSQLQMLKSEFKKIHNTSRGQEIIFEITSFTQEKLDEFQNVVNTQSLEDDRLQRIKETKEQLEKEEREKQQETIKKRSDEQRRIDEIVQRELEKRQDDDDDLLFNRTTQLDLQPPSEWVASGEAIVFSKTIKAKLPNNSMFKFKAVVNPKPIKLTSDIFSFSKQFLVKPYIPPESPLADFLMSSEMMENFYYLLSEIELDNSYFNTSNGKKEIANLEKELETVLKAKHDNVNRLFGYTVERMGRNNATFVWKIRLLTEYCNYYPLGDLIQSVGFVNLATARIWMIRLLEGLEAIHKLGIVHKCINLETVILVKDADFGSTIPKLVHSTYGYTVLNMLSRYPNKNGSSVELSPSTWIAPELLKFNNAKPQRLTDIWQLGVLFIQIISGSDIVMNFETPQEFLDSTSMDETLYDLLSKMLNNDPKKRLGTLELLPMKFLRTNIDSTINRFNLVSESVNSNSLELTPGDTITVRGNGGRTLSQSSIRRRSFNVGSRFSSINPATRSRYASDFEEIAVLGQGAFGQVVKARNALDSRYYAIKKIRHTEEKLSTILSEVMLLASLNHQYVVRYYAAWLEEDSMDENVFESTDEESDLSESSSDFEENDLLDQSSIFKNRTNHDLDNSNWDFISGSGYPDIVFENSSRDDENEDLDHDTSSTSSSESQDDTDKESKSIQNVPRRRNFVKPMTAVKKKSTLFIQMEYCENRTLYDLIHSENLNQQRDEYWRLFRQILEALSYIHSQGIIHRDLKPMNIFIDESRNVKIGDFGLAKNVHRSLDILKLDSQNLPGSSDNLTSAIGTAMYVATEVLDGTGHYNEKIDMYSLGIIFFEMIYPFSTGMERVNILKKLRSVSIEFPPDFDDNKMKVEKKIIRLLIDHDPNKRPGARTLLNSGWLPVKHQDEVIKEALKSLSNPSSPWQQQVRESLFNQSYSLTNDILFDNSVPTSTPFANILRSQMTEEVVKIFRKHGGIENNAPPRIFPKAPIYGTQNVYEVLDKGGTVLQLQYDLTYPMARYLSKNPSLISKQYRMQHVYRPPDHSRSSLEPRKFGEIDFDIISKSSSESGFYDAESLKIIDEILTVFPVFEKTNTFFILNHADILESVFNFTNIDKAQRPLVSRMLSQVGFARSFKEVKNELKAQLNISSTALNDLELFDFRLDFEAAKKRLYKLMIDSPHLKKIEDSLSHISKVLSYLKPLEVARNVVISPLSNYNSAFYKGGIMFHAVYDDGSSRNMIAAGGRYDTLISFFARPSGKKSSNTRKAVGFNLAWETIFGIAQNYFKLASGNRIKKRNRFLKDTAVDWKPSRCDVLISSFSNSLLDTIGVTILNTLWKQNIKADMLRDCSSVDDVVTGAQQDGIDWILLIKQQAYPLTNHKRKYKPLKIKKLSTNVDIDLDLDEFLTLYQQETGNKSLINDSLTLGDKADEFKRWDENSSAGSSQEGDIDDVVAGSTNNQKVIYVPNMATRSKKANKREKWVYEDAARNSSNMILHNLSNAPIITVDALRDETLEIISITSLAQKEEWLRKVFGSGNNSTPRSFATSIYNNLSKEAHKGNRWAILYCHKTGKSSVIDLQR | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSLSHLTLD ------CCCCCCCHH | 50.30 | 30377154 | |
| 4 | Phosphorylation | ----MSLSHLTLDQY ----CCCCCCCHHHE | 26.24 | 30377154 | |
| 7 | Phosphorylation | -MSLSHLTLDQYYEI -CCCCCCCHHHEEEE | 23.90 | 30377154 | |
| 11 | Phosphorylation | SHLTLDQYYEIQCNE CCCCHHHEEEEECHH | 11.61 | 30377154 | |
| 12 | Phosphorylation | HLTLDQYYEIQCNEL CCCHHHEEEEECHHH | 10.83 | 30377154 | |
| 24 | Phosphorylation | NELEAIRSIYMDDFT HHHHHHHHHHCCCCC | 16.38 | 30377154 | |
| 26 | Phosphorylation | LEAIRSIYMDDFTDL HHHHHHHHCCCCCHH | 8.85 | 30377154 | |
| 34 | Phosphorylation | MDDFTDLTKRKSSWD CCCCCHHHHCCCCCC | 31.45 | 30377154 | |
| 118 | Phosphorylation | QEIIFEITSFTQEKL CEEEEEEECCCHHHH | 15.58 | 27017623 | |
| 119 | Phosphorylation | EIIFEITSFTQEKLD EEEEEEECCCHHHHH | 31.77 | 27017623 | |
| 121 | Phosphorylation | IFEITSFTQEKLDEF EEEEECCCHHHHHHH | 35.27 | 27017623 | |
| 542 | Phosphorylation | INRFNLVSESVNSNS HHHHHHCCCCCCCCC | 27.59 | 19779198 | |
| 547 | Phosphorylation | LVSESVNSNSLELTP HCCCCCCCCCCEECC | 26.16 | 19779198 | |
| 549 | Phosphorylation | SESVNSNSLELTPGD CCCCCCCCCEECCCC | 24.04 | 19779198 | |
| 553 | Phosphorylation | NSNSLELTPGDTITV CCCCCEECCCCEEEE | 18.82 | 27214570 | |
| 567 | Phosphorylation | VRGNGGRTLSQSSIR ECCCCCCEECHHHHH | 33.75 | 22369663 | |
| 569 | Phosphorylation | GNGGRTLSQSSIRRR CCCCCEECHHHHHCC | 27.66 | 22369663 | |
| 571 | Phosphorylation | GGRTLSQSSIRRRSF CCCEECHHHHHCCCC | 25.10 | 22369663 | |
| 572 | Phosphorylation | GRTLSQSSIRRRSFN CCEECHHHHHCCCCC | 16.69 | 22369663 | |
| 577 | Phosphorylation | QSSIRRRSFNVGSRF HHHHHCCCCCCCCCC | 21.25 | 21082442 | |
| 585 | Phosphorylation | FNVGSRFSSINPATR CCCCCCCCCCCHHCC | 29.24 | 23749301 | |
| 730 | Phosphorylation | PDIVFENSSRDDENE CCEEEECCCCCCCCC | 21.39 | 28889911 | |
| 759 | Phosphorylation | QDDTDKESKSIQNVP CCCCCHHHHHHHCCC | 37.13 | 28889911 | |
| 761 | Phosphorylation | DTDKESKSIQNVPRR CCCHHHHHHHCCCCC | 38.39 | 22369663 | |
| 846 | Phosphorylation | MNIFIDESRNVKIGD CEEEEECCCCCCCCC | 25.96 | 27017623 | |
| 877 | Phosphorylation | DSQNLPGSSDNLTSA CCCCCCCCCCCHHHH | 32.36 | 28889911 | |
| 878 | Phosphorylation | SQNLPGSSDNLTSAI CCCCCCCCCCHHHHH | 36.11 | 28889911 | |
| 882 | Phosphorylation | PGSSDNLTSAIGTAM CCCCCCHHHHHHHHH | 23.51 | 20404097 | |
| 887 | Phosphorylation | NLTSAIGTAMYVATE CHHHHHHHHHHHHHH | 11.35 | 8798780 | |
| 974 | Phosphorylation | NKRPGARTLLNSGWL CCCCCHHHHHHCCCC | 34.75 | 28889911 | |
| 1002 | Phosphorylation | KSLSNPSSPWQQQVR HHCCCCCCHHHHHHH | 31.26 | 25752575 | |
| 1127 | Phosphorylation | RPPDHSRSSLEPRKF CCCCCCCCCCCCCCC | 42.14 | 30377154 | |
| 1268 | Phosphorylation | HLKKIEDSLSHISKV HHHHHHHHHHHHHHH | 20.98 | 19779198 | |
| 1518 | Phosphorylation | FKRWDENSSAGSSQE HHCCCCCCCCCCCCC | 21.37 | 21440633 | |
| 1519 | Phosphorylation | KRWDENSSAGSSQEG HCCCCCCCCCCCCCC | 48.51 | 21440633 | |
| 1522 | Phosphorylation | DENSSAGSSQEGDID CCCCCCCCCCCCCHH | 28.68 | 21440633 | |
| 1523 | Phosphorylation | ENSSAGSSQEGDIDD CCCCCCCCCCCCHHC | 31.19 | 20377248 | |
| 1648 | Acetylation | WAILYCHKTGKSSVI EEEEEEECCCCCCEE | 56.25 | 25381059 |
* 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_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 THR-553; SER-569; SER-577AND SER-1002, AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-761, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND SER-577, ANDMASS SPECTROMETRY. | |
