DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Su Q., Wang S., Baltzis D., Qu LK., Wong AH., Koromilas AE. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Su Q., Wang S., Baltzis D., Qu LK., Wong AH., Koromilas AE. DIP original experiment: DIP-262456X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Su Q., Wang S., Baltzis D., Qu LK., Wong AH., Koromilas AE. Only protein-protein interactions in vitro In vitro far western blotting far western blotting Affinity blotting Affinity blotting autoradiography autoradiography Su Q., Wang S., Baltzis D., Qu LK., Wong AH., Koromilas AE. DIP original experiment: DIP-262457X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Su Q., Wang S., Baltzis D., Qu LK., Wong AH., Koromilas AE. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Su Q., Wang S., Baltzis D., Qu LK., Wong AH., Koromilas AE. DIP original experiment: DIP-262458X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. e2ak2_human Interferon-induced, double-stranded RNA-activated protein kinase Interferon-inducible RNA-dependent protein kinase Eukaryotic translation initiation factor 2-alpha kinase 2 Protein kinase RNA-activated p68 kinase P1/eIF-2A protein kinase EIF2AK2 PKR PRKR Tyrosine-protein kinase EIF2AK2 protein protein human Homo sapiens Human MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC DIP protein P19525 original sequence version: 164 DIP protein P19525-1 original sequence version: 177 DIP protein P19525-1 original sequence version: 178 DIP protein P19525-1 original sequence version: 170 DIP protein P19525 original sequence version: 153 815AD83ACAB45DA3 eif2a_yeast Eukaryotic translation initiation factor 2A YGR054W protein protein yeast Saccharomyces cerevisiae Baker's yeast MSSQFFLKTSQDIELFQSYPTFEQSNTNSKDFPVISSVLSPCGRFLALSTKENVKVFTGPCLDNVLLTMKLSDVYDLHFSPAGNYLSTWERASIQDPNHKNVKVWYLNKPFKKDCVSEDIVPAYEYQAKSQSGWFLQFSKLDNYGLRLFKHDLKIVKLSSANADNFDFQSPFAVLSDDETSQHFTTYLISPAEHPTICTFTPEKGGKPAQLIIWALSEGKITKKIASKTFFKADSCQLKWNPLGNAILCLAITDFDSSNKSYYGENTLYLLSFQGVNGTLGGNSVRVSLTTGPVHDFTWSPTSRQFGVIAGYMPATISFFDLRGNVVHSLPQQAKNTMLFSPSGHYILIAGFGNLQGSVEILDRLDKFKCVSKFDATNTSVCKWSPGGEFIMTATTSPRLRVDNGVKIWHVSGSLVFVKEFKELLKVDWRSPCNYKTLENKDEAFFENHIINNWEPLPDSTTSSLDPKISNKSELQIHSSVQEYISQHPSREASSNGNGSKAKAGGAYKPPHARRTGGGRIVPGVPPGAAKKTIPGLVPGMSANKDANTKNRRRRANKKSSETSPDSTPAPSAPASTNAPTNNKETSPEEKKIRSLLKKLRAIETLKERQAVGDKLEDTQVLKIQTEEKVLKDLEKLGWKDE F3C2E78504D83418 F3C2E78504D83418 eif2ak2-eif_2a-1 1 5 enzyme target enzyme target substrate substrate unspecified role unspecified role ecolx Escherichia coli 4 enzyme enzyme unspecified role unspecified role P19525:p.Lys296Arg K296R mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K R This feature has been corrected as a result of our quality control procedures. The original label was 'K296R'. Wed May 02 19:12:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys296arg' Tue Jun 30 19:37:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys296Arg' P19525:p.Tyr293Phe Y293F mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Y F This feature has been corrected as a result of our quality control procedures. The original label was 'Y293F'. Wed May 02 15:20:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr293phe' Tue Jun 30 17:04:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr293Phe' ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation eif2ak2-1 3 4 putative self putative self unspecified role unspecified role P19525:p.Lys296Arg K296R mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K R This feature has been corrected as a result of our quality control procedures. The original label was 'K296R'. Wed May 02 16:07:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys296arg' Tue Jun 30 19:02:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys296Arg' P19525:p.Tyr293Phe Y293F mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Y F This feature has been corrected as a result of our quality control procedures. The original label was 'Y293F'. Wed May 02 15:10:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr293phe' Tue Jun 30 19:29:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr293Phe' ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation true eif2ak2-eif2ak2-1 2 4 unspecified role unspecified role prey prey 32P-label 32P-label 32p radiolabel 32p radiolabel P32 32P 32P P32 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli 4 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P19525:p.Tyr101Phe Y101F mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Y F This feature has been corrected as a result of our quality control procedures. The original label was 'Y101F'. Wed May 02 19:47:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr101phe' Tue Jun 30 15:39:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr101Phe' P19525:p.Tyr162Phe Y162F mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Y F This feature has been corrected as a result of our quality control procedures. The original label was 'Y162F'. Wed May 02 16:38:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr162phe' Tue Jun 30 18:04:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr162Phe' P19525:p.Tyr293Phe Y293F mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Y F This feature has been corrected as a result of our quality control procedures. The original label was 'Y293F'. Wed May 02 17:34:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr293phe' Tue Jun 30 16:00:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr293Phe' ecolx Escherichia coli direct interaction direct interaction