DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. 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 Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132049X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions human Homo sapiens Human bifc bimolecular fluorescence complementation bifc predetermined predetermined participant predetermined Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132052X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132050X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132058X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions ecolx Escherichia coli density sedimentation cosedimentation through density gradient density sedimentation anti tag western anti tag western blot anti tag western Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132055X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions ecolx Escherichia coli density sedimentation cosedimentation through density gradient density sedimentation western blot western blot Immuno blot Immuno blot Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132054X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions ecolx Escherichia coli h1-h2 ms mass spectrometry study of hydrogen/deuterium exchange h1-h2 ms predetermined predetermined participant predetermined Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132053X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation anti tag western anti tag western blot anti tag western Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132056X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132057X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. Structure (London, England : 1993) 2009 imex curation Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Pires R., Hartlieb B., Signor L., Schoehn G., Lata S., Roessle M., Moriscot C., Popov S., Hinz A., Jamin M., Boyer V., Sadoul R., Forest E., Svergun DI., Göttlinger HG., Weissenhorn W. DIP original experiment: DIP-132051X Structure (London, England : 1993) 2009 IMEx A crescent-shaped ALIX dimer targets ESCRT-III CHMP4 filaments. chm4b_human Charged multivesicular body protein 4b Chromatin-modifying protein 4b Vacuolar protein sorting-associated protein 32-2 SNF7-2 SNF7 homolog associated with Alix 1 CHMP4B C20orf178 SHAX1 protein protein human Homo sapiens Human MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM DIP protein Q9H444 original sequence version: 48 DIP protein Q9H444 original sequence version: 50 DIP protein Q9H444 original sequence version: 69 DIP protein Q9H444 original sequence version: 85 DIP protein Q9H444 original sequence version: 90 DB1D79DD3803CB2F q9wu78-1 Programmed cell death 6-interacting protein Pdcd6ip Aip1 Alix ALG-2-interacting protein 1 ALG-2-interacting protein X E2F1-inducible protein Eig2 protein protein mouse Mus musculus Mouse MASFIWVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRSALGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKTAAKQYQFASGAFLHIKDTVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKEVFPTLAAKQCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKNVASRYDEYVNVKDFSDKINRALTAAKKDNDFIYHDRVPDLKDLDPIGKATLVKPTPVNVPVSQKFTDLFEKMVPVSVQQSLAVFSQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSTSVVEQGGIQTVDQLIKELPELLQRNREILEESLRLLDEEEATDNDLRAKFKDRWQRTPSNDLYKPLRAEGAKFRAVLDKAVQADGQVKERYQSHRDTIALLCKPEPELNAAIPSANPAKTMQGSEVVSVLKSLLSNLDEIKKERESLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRIYGGLTSKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTERDELLKDLQQSIAREPSAPSIPPPAYQSSPAAGHAAAPPTPAPRTMPPAKPQPPARPPPPVLPANRVPPASAAAAPAGVGTASAAPPQTPGSAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPTYPFPQPPQQSYYPQQ DIP protein Q9WU78-1 original sequence version: 72 DIP protein Q9WU78 original sequence version: 77 DIP protein Q9WU78 original sequence version: 115 chmp4b-1 5 11 unspecified role unspecified role unspecified role unspecified role Region 1-193 Region 1-193 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-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 pdcd6ip-1 1 12 unspecified role unspecified role unspecified role unspecified role Region 355-714 Region 355-714 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9WU78-1:p.[Lys638Glu;Met639Ala;Lys640Ala;Asn643Tyr;Asn644Lys;Glu645Lys] K638E/M639A/K640A/N643Y/N644K/E645K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain N K certain certain sequence position certain certain certain sequence position certain N Y certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain M A certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K638E/M639A/K640A/N643Y/N644K/E645K'. Wed May 02 17:33:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys638glu,met639ala,lys640ala,asn643tyr,asn644lys,glu645lys' Tue Jun 30 18:37:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys638Glu;Met639Ala;Lys640Ala;Asn643Tyr;Asn644Lys;Glu645Lys]' ecolx Escherichia coli direct interaction direct interaction pdcd6ip-4 2 12 unspecified role unspecified role unspecified role unspecified role Region 1-714 Region 1-714 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human direct interaction direct interaction chmp4b-4 9 11 unspecified role unspecified role unspecified role unspecified role Region 1-193 Region 1-193 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction chmp4b-pdcd6ip-4 4 11 unspecified role unspecified role unspecified role unspecified role Region 1-175/204-224 Region 1-175/204-224 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 1-714 Region 1-714 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pdcd6ip-5 3 12 unspecified role unspecified role unspecified role unspecified role Region 355-714 Region 355-714 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9WU78-1:p.[Lys638Glu;Met639Ala;Lys640Ala;Asn643Tyr;Asn644Lys;Glu645Lys] K638E/M639A/K640A/N643Y/N644K/E645K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain N K certain certain sequence position certain certain certain sequence position certain N Y certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain M A certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K638E/M639A/K640A/N643Y/N644K/E645K'. Wed May 02 15:19:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys638glu,met639ala,lys640ala,asn643tyr,asn644lys,glu645lys' Tue Jun 30 18:22:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys638Glu;Met639Ala;Lys640Ala;Asn643Tyr;Asn644Lys;Glu645Lys]' ecolx Escherichia coli direct interaction direct interaction pdcd6ip-6 7 12 unspecified role unspecified role unspecified role unspecified role Region 1-714 Region 1-714 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction chmp4b-pdcd6ip-5 8 11 unspecified role unspecified role unspecified role unspecified role Region 1-175/204-224 Region 1-175/204-224 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 1-714 Region 1-714 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pdcd6ip-7 6 12 unspecified role unspecified role unspecified role unspecified role Region 1-714 Region 1-714 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction pdcd6ip-8 10 12 unspecified role unspecified role unspecified role unspecified role Region 355-714 Region 355-714 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9WU78-1:p.[Lys638Glu;Met639Ala;Lys640Ala;Asn643Tyr;Asn644Lys;Glu645Lys] K638E/M639A/K640A/N643Y/N644K/E645K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain N K certain certain sequence position certain certain certain sequence position certain N Y certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain M A certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K638E/M639A/K640A/N643Y/N644K/E645K'. Wed May 02 19:38:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys638glu,met639ala,lys640ala,asn643tyr,asn644lys,glu645lys' Tue Jun 30 19:33:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys638Glu;Met639Ala;Lys640Ala;Asn643Tyr;Asn644Lys;Glu645Lys]' ecolx Escherichia coli direct interaction direct interaction