IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ ERK2-Dependent Phosphorylation of CSN6 Is Critical in Colorectal Cancer Development. ERK2-Dependent Phosphorylation of CSN6 Is Critical in Colorectal Cancer Development. Cancer cell 2015 imex curation Fang L., Lu W., Choi HH., Yeung SC., Tung JY., Hsiao CD., Fuentes-Mattei E., Menter D., Chen C., Wang L., Wang J., Lee MH. Results obtained using the an ERK or ERK 1/2 antibody have not been included due to lack of specificity. Myc-ERK2 and myc-ERK2-D318/321N + myc-ERK2-T159/160E constructs were determined to be of Human origin by mutation mapping. wangjpgz@163.com,mhlee@mdanderson.org 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro protein kinase assay protein kinase assay western blot western blot Immuno blot Immuno blot Fang L., Lu W., Choi HH., Yeung SC., Tung JY., Hsiao CD., Fuentes-Mattei E., Menter D., Chen C., Wang L., Wang J., Lee MH. Results obtained using the an ERK or ERK 1/2 antibody have not been included due to lack of specificity. Myc-ERK2 and myc-ERK2-D318/321N + myc-ERK2-T159/160E constructs were determined to be of Human origin by mutation mapping. wangjpgz@163.com,mhlee@mdanderson.org Accepted 2016-JAN-20 AT 09:32 GMT AT 09:32 GMT by ORCHARD Cancer cell 2015 Only protein-protein interactions imex curation imex curation ERK2-Dependent Phosphorylation of CSN6 Is Critical in Colorectal Cancer Development. ERK2-Dependent Phosphorylation of CSN6 Is Critical in Colorectal Cancer Development. Cancer cell 2015 imex curation Fang L., Lu W., Choi HH., Yeung SC., Tung JY., Hsiao CD., Fuentes-Mattei E., Menter D., Chen C., Wang L., Wang J., Lee MH. Results obtained using the an ERK or ERK 1/2 antibody have not been included due to lack of specificity. Myc-ERK2 and myc-ERK2-D318/321N + myc-ERK2-T159/160E constructs were determined to be of Human origin by mutation mapping. wangjpgz@163.com,mhlee@mdanderson.org 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-dld1 Human colorectal adenocarcinoma dld1 Human colon adenocarcinoma anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Fang L., Lu W., Choi HH., Yeung SC., Tung JY., Hsiao CD., Fuentes-Mattei E., Menter D., Chen C., Wang L., Wang J., Lee MH. Results obtained using the an ERK or ERK 1/2 antibody have not been included due to lack of specificity. Myc-ERK2 and myc-ERK2-D318/321N + myc-ERK2-T159/160E constructs were determined to be of Human origin by mutation mapping. wangjpgz@163.com,mhlee@mdanderson.org Accepted 2016-JAN-20 AT 09:32 GMT AT 09:32 GMT by ORCHARD Cancer cell 2015 Only protein-protein interactions imex curation imex curation ERK2-Dependent Phosphorylation of CSN6 Is Critical in Colorectal Cancer Development. ERK2-Dependent Phosphorylation of CSN6 Is Critical in Colorectal Cancer Development. Cancer cell 2015 imex curation Fang L., Lu W., Choi HH., Yeung SC., Tung JY., Hsiao CD., Fuentes-Mattei E., Menter D., Chen C., Wang L., Wang J., Lee MH. Results obtained using the an ERK or ERK 1/2 antibody have not been included due to lack of specificity. Myc-ERK2 and myc-ERK2-D318/321N + myc-ERK2-T159/160E constructs were determined to be of Human origin by mutation mapping. wangjpgz@163.com,mhlee@mdanderson.org 22-Feb-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-dld1 Human colorectal adenocarcinoma dld1 Human colon adenocarcinoma anti bait coip anti bait coimmunoprecipitation anti bait coip anti tag western anti tag western blot anti tag western Fang L., Lu W., Choi HH., Yeung SC., Tung JY., Hsiao CD., Fuentes-Mattei E., Menter D., Chen C., Wang L., Wang J., Lee MH. Results obtained using the an ERK or ERK 1/2 antibody have not been included due to lack of specificity. Myc-ERK2 and myc-ERK2-D318/321N + myc-ERK2-T159/160E constructs were determined to be of Human origin by mutation mapping. wangjpgz@163.com,mhlee@mdanderson.org Accepted 2016-JAN-20 AT 09:32 GMT AT 09:32 GMT by ORCHARD Cancer cell 2015 Only protein-protein interactions imex curation imex curation csn6_human COP9 signalosome complex subunit 6 COPS6 CSN6 HVIP JAB1-containing signalosome subunit 6 Vpr-interacting protein MOV34 homolog protein protein human Homo sapiens Human MAAAAAAAAATNGTGGSSGMEVDAAVVPSVMACGVTGSVSVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRNIEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELEFLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVFESVIDIINGEATMLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILEYVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCNTMNQFVNKFNVLYDRQGIGRRMRGLFF DIP protein Q7L5N1 original sequence version: 63 DIP protein Q7L5N1 original sequence version: 102 DIP protein Q7L5N1 original sequence version: 119 E33CAC6ADF799A8D fbw1a_human F-box/WD repeat-containing protein 1A BTRC BTRCP FBW1A FBXW1A F-box and WD repeats protein beta-TrCP E3RSIkappaB pIkappaBalpha-E3 receptor subunit Epididymis tissue protein Li 2a protein protein human Homo sapiens Human MDPAEAVLQEKALKFMCSMPRSLWLGCSSLADSMPSLRCLYNPGTGALTAFQNSSEREDCNNGEPPRKIIPEKNSLRQTYNSCARLCLNQETVCLASTAMKTENCVAKTKLANGTSSMIVPKQRKLSASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVRTDSLWRGLAERRGWGQYLFKNKPPDGNAPPNSFYRALYPKIIQDIETIESNWRCGRHSLQRIHCRSETSKGVYCLQYDDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQYDERVIITGSSDSTVRVWDVNTGEMLNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMASPTDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLVAALDPRAPAGTLCLRTLVEHSGRVFRLQFDEFQIVSSSHDDTILIWDFLNDPAAQAEPPRSPSRTYTYISR DIP protein Q9Y297 original sequence version: 142 DIP protein Q9Y297 original sequence version: 153 DIP protein Q9Y297 original sequence version: 144 DIP protein Q9Y297 original sequence version: 145 DIP protein Q9Y297 original sequence version: 106 DIP protein Q9Y297 original sequence version: 82 DIP protein Q9Y297 original sequence version: 111 DIP protein Q9Y297 original sequence version: 125 4C67F3B7E400FD37 mk01_human Mitogen-activated protein kinase 1 MAPK1 ERK2 PRKM1 Extracellular signal-regulated kinase 2 Mitogen-activated protein kinase 2 MAP kinase isoform p42 ERT1 PRKM2 protein protein human Homo sapiens Human MAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS DIP protein P28482 original sequence version: 173 DIP protein P28482 original sequence version: 103 DIP protein P28482 original sequence version: 101 DIP protein P28482 original sequence version: 131 DIP protein P28482 original sequence version: 156 DIP protein P28482 original sequence version: 166 DIP protein P28482 original sequence version: 144 E85D0B2A5D2D724E cops6-mapk1-1 3 6 unspecified role unspecified role prey prey P28482:p.[Asp318Asn;Asp321Asn] mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain D N certain certain sequence position certain certain certain sequence position certain D N Wed May 02 14:52:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp318asn,asp321asn' Tue Jun 30 16:45:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp318Asn;Asp321Asn]' P28482:p.Thr159_Thr160delinsGluGlu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain TT EE Wed May 02 15:33:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr_thr159-160glu_glu' Tue Jun 30 19:23:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr159_Thr160delinsGluGlu' region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 4 unspecified role unspecified role bait bait physical association physical association 2G cops6-mapk1-2 1 6 enzyme enzyme neutral component neutral component n_terminus 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 region phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined observed-ptm observed-ptm observed ptm observed-ptm ecoli Escherichia coli (strain K12) 4 enzyme target enzyme target substrate substrate neutral component neutral component n_terminus 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 region opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined resulting-ptm resulting-ptm resulting ptm resulting-ptm Q7L5N1:p.Ser148Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain S A Wed May 02 19:20:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser148ala' Tue Jun 30 18:49:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser148Ala' ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation 3E cops6-mapk1-3 2 4 unspecified role unspecified role bait bait 5 unspecified role unspecified role prey prey physical association physical association 4F