DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68455X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68457X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68459X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68456X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68460X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro sls static light scattering sls predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68454X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions ecolx Escherichia coli sls static light scattering sls predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68452X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68449X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68450X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68451X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68453X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure (London, England : 1993) 2008 imex curation Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Rushe M., Silvian L., Bixler S., Chen LL., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. DIP original experiment: DIP-68458X Structure (London, England : 1993) 2008 IMEx Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. ikkalpha/beta IKKalpha/beta hybrid peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) PAKKSEELVAEAHNLCTLLENAIQDTVREQGNSMMNLDWSWLTE ikkb_human Inhibitor of nuclear factor kappa-B kinase subunit beta IKBKB IKKB I-kappa-B kinase 2 Nuclear factor NF-kappa-B inhibitor kinase beta Serine/threonine protein kinase IKBKB protein protein human Homo sapiens Human MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMRRLTHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGTVKFSSSLPYPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPTYGPNGCFKALDDILNLKLVHILNMVTGTIHTYPVTEDESLQSLKARIQQDTGIPEEDQELLQEAGLALIPDKPATQCISDGKLNEGHTLDMDLVFLFDNSKITYETQISPRPQPESVSCILQEPKRNLAFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMNLLRNNSCLSKMKNSMASMSQQLKAKLDFFKTSIQIDLEKYSEQTEFGITSDKLLLAWREMEQAVELCGRENEVKLLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRRLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDEKTVVRLQEKRQKELWNLLKIACSKVRGPVSGSPDSMNASRLSQPGQLMSQPSTASNSLPEPAKKSEELVAEAHNLCTLLENAIQDTVREQDQSFTALDWSWLQTEEEEHSCLEQAS DIP protein O14920 original sequence version: 89 DIP protein O14920 original sequence version: 100 DIP protein O14920 original sequence version: 121 DIP protein O14920 original sequence version: 126 DIP protein O14920 original sequence version: 136 DIP protein O14920 original sequence version: 128 DIP protein O14920-1 original sequence version: 151 DIP protein O14920 original sequence version: 142 DIP protein O14920 original sequence version: 159 DIP protein O14920 original sequence version: 93 DIP protein O14920 original sequence version: 124 DIP protein O14920-1 original sequence version: 178 DIP protein O14920 original sequence version: 85 F9CADF671AE9E14E nemo_human NF-kappa-B essential modulator IKBKG FIP3 NEMO NF-kappa-B essential modifier Inhibitor of nuclear factor kappa-B kinase subunit gamma IkB kinase-associated protein 1 FIP-3 protein protein human Homo sapiens Human MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE DIP protein Q9Y6K9 original sequence version: 85 DIP protein Q9Y6K9 original sequence version: 118 DIP protein Q9Y6K9 original sequence version: 123 DIP protein Q9Y6K9 original sequence version: 141 DIP protein Q9Y6K9 original sequence version: 125 DIP protein Q9Y6K9 original sequence version: 156 DIP protein Q9Y6K9 original sequence version: 83 DIP protein Q9Y6K9 original sequence version: 132 DIP protein Q9Y6K9 original sequence version: 124 DIP protein Q9Y6K9 original sequence version: 90 322D1037881447FF ikkalpha IKK-alpha peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) MMNLDWSWLTE ikkbeta IKK-beta peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) FTALDWSWLQT ikbkg-ikkalpha-1 3 16 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept Biotin-tag Biotin-tag biotin tag biotin tag n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 15 unspecified role unspecified role fluorescence donor fluorescence donor Region 1-196 Region 1-196 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 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 ecolx Escherichia coli direct interaction direct interaction ikbkg-ikkalpha/beta-1 8 13 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept Biotin-tag Biotin-tag biotin tag biotin tag n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 15 unspecified role unspecified role fluorescence donor fluorescence donor Region 44-111 Region 44-111 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain 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 ecolx Escherichia coli direct interaction direct interaction ikbkg-ikkalpha/beta-2 6 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Region 44-111 Region 44-111 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ikbkg-1 7 15 unspecified role unspecified role unspecified role unspecified role Region 1-196 Region 1-196 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ikbkg-ikkalpha/beta-3 1 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Region 44-111 Region 44-111 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ikbkb-ikbkg-11 2 14 unspecified role unspecified role unspecified role unspecified role Region 701-746 Region 701-746 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Region 44-111 Region 44-111 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ikbkg-ikkalpha/beta-4 11 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Region 44-111 Region 44-111 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ikbkg-ikkbeta-1 5 17 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept Biotin-tag Biotin-tag biotin tag biotin tag n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal n-terminal n-terminal position amino-terminus n-terminus n-term n-term amino-terminus n-terminus n-terminal in vitro In vitro 15 unspecified role unspecified role fluorescence donor fluorescence donor Region 1-196 Region 1-196 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 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 ecolx Escherichia coli direct interaction direct interaction ikbkg-2 9 15 unspecified role unspecified role unspecified role unspecified role Region 1-196 Region 1-196 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ikbkg-ikkalpha/beta-5 4 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Region 44-111 Region 44-111 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ikbkg-ikkalpha/beta-6 12 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role Region 44-111 Region 44-111 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ikbkg-3 10 15 unspecified role unspecified role unspecified role unspecified role Region 1-196 Region 1-196 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction