GCN2_SCHPO - dbPTM
GCN2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1315PhosphorylationSKQSSKHSPSPTLKS
CCCCCCCCCCCCCCC
30.7024763107

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 GCN2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCN2_SCHPO !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MLH1_SCHPOmlh1genetic
22681890
VHT1_SCHPOvht1genetic
22681890
FLP1_SCHPOclp1genetic
22681890
YAKA_SCHPOSPAC1F7.10genetic
22681890
YAJ1_SCHPOgto2genetic
22681890
ILVB_SCHPOilv1genetic
22681890
YE38_SCHPOpdc1genetic
22681890
ALY1_SCHPOSPBC839.02genetic
22681890
ELP6_SCHPOelp6genetic
22681890
PROB_SCHPOSPAC17H9.13cgenetic
22681890
PDX1_SCHPOsnz1genetic
22681890
PTH_SCHPOpth1genetic
22681890
OXR1_SCHPOmug63genetic
22681890
YDA5_SCHPOSPAC1F12.05genetic
22681890
AATC_SCHPOSPAC10F6.13cgenetic
22681890
YDA4_SCHPOSPAC1F12.04cgenetic
22681890
ZIP1_SCHPOzip1genetic
22681890
CISY_SCHPOcit1genetic
22681890
YEE2_SCHPOSPAC19A8.02genetic
22681890
HHP2_SCHPOhhp2genetic
22681890
BCA1_SCHPOeca39genetic
22681890
YEEB_SCHPOSPAC19A8.11cgenetic
22681890
YF65_SCHPOSPAC23C4.05cgenetic
22681890
YFM8_SCHPOSPAC222.08cgenetic
22681890
CORO_SCHPOcrn1genetic
22681890
AROG_SCHPOSPAP8A3.07cgenetic
22681890
TYW1_SCHPOSPCC1020.08genetic
22681890
YAG9_SCHPOSPAC12G12.09genetic
22681890
ELP1_SCHPOelp1genetic
22681890
YII1_SCHPOSPAC139.01cgenetic
22681890
YJ53_SCHPOSPCC4F11.03cgenetic
22681890
MED1_SCHPOpmc2genetic
22681890
TSR4_SCHPOSPBC25H2.15genetic
22681890
ALM1_SCHPOalm1genetic
22681890
RLP1_SCHPOrlp1genetic
22681890
SAT1_SCHPOsat1genetic
22681890
MYH1_SCHPOmyh1genetic
22681890
MID1_SCHPOmid1genetic
22681890
MUG51_SCHPOmug51genetic
22681890
TSC1_SCHPOtsc1genetic
22681890
YIW2_SCHPOSPAC694.02genetic
22681890
RS4A_SCHPOrps401genetic
22681890
GCN2_SCHPOgcn2physical
23671279
RS3_SCHPOrps3physical
23671279

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GCN2_SCHPO

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Related Literatures of Post-Translational Modification

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