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 bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. Structure (London, England : 1993) 2015 imex curation Zhang H., Amick J., Chakravarti R., Santarriaga S., Schlanger S., McGlone C., Dare M., Nix JC., Scaglione KM., Stuehr DJ., Misra S., Page RC. 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 Zhang H., Amick J., Chakravarti R., Santarriaga S., Schlanger S., McGlone C., Dare M., Nix JC., Scaglione KM., Stuehr DJ., Misra S., Page RC. DIP original experiment: DIP-264824X Structure (London, England : 1993) 2015 IMEx A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. Structure (London, England : 1993) 2015 imex curation Zhang H., Amick J., Chakravarti R., Santarriaga S., Schlanger S., McGlone C., Dare M., Nix JC., Scaglione KM., Stuehr DJ., Misra S., Page RC. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Zhang H., Amick J., Chakravarti R., Santarriaga S., Schlanger S., McGlone C., Dare M., Nix JC., Scaglione KM., Stuehr DJ., Misra S., Page RC. DIP original experiment: DIP-264825X Structure (London, England : 1993) 2015 IMEx A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. Structure (London, England : 1993) 2015 imex curation Zhang H., Amick J., Chakravarti R., Santarriaga S., Schlanger S., McGlone C., Dare M., Nix JC., Scaglione KM., Stuehr DJ., Misra S., Page RC. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Zhang H., Amick J., Chakravarti R., Santarriaga S., Schlanger S., McGlone C., Dare M., Nix JC., Scaglione KM., Stuehr DJ., Misra S., Page RC. DIP original experiment: DIP-264822X Structure (London, England : 1993) 2015 IMEx A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. Structure (London, England : 1993) 2015 imex curation Zhang H., Amick J., Chakravarti R., Santarriaga S., Schlanger S., McGlone C., Dare M., Nix JC., Scaglione KM., Stuehr DJ., Misra S., Page RC. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Zhang H., Amick J., Chakravarti R., Santarriaga S., Schlanger S., McGlone C., Dare M., Nix JC., Scaglione KM., Stuehr DJ., Misra S., Page RC. DIP original experiment: DIP-264823X Structure (London, England : 1993) 2015 IMEx A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. q9une7-1 E3 ubiquitin-protein ligase CHIP STUB1 CHIP Antigen NY-CO-7 CLL-associated antigen KW-8 Carboxy terminus of Hsp70-interacting protein RING-type E3 ubiquitin transferase CHIP STIP1 homology and U box-containing protein 1 PP1131 protein protein human Homo sapiens Human MKGKEEKEGGARLGAGGGSPEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLSRLIAAERERELEECQRNHEGDEDDSHVRAQQACIEAKHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY DIP protein Q9UNE7-1 original sequence version: 134 DIP protein Q9UNE7-1 original sequence version: 56 DIP protein Q9UNE7 original sequence version: 87 p11142-1 Heat shock cognate 71 kDa protein HSPA8 HSC70 HSP73 HSPA10 Heat shock 70 kDa protein 8 Lipopolysaccharide-associated protein 1 protein protein human Homo sapiens Human MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD DIP protein P11142-1 original sequence version: 185 9AA27B210730670C hspa8-stub1-1 3 5 unspecified role unspecified role unspecified role unspecified role Region 21-154 Region 21-154 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9UNE7-1:p.[Val59Asp;Leu129Asp] V59D/L129D mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain V D certain certain sequence position certain certain certain sequence position certain L D This feature has been corrected as a result of our quality control procedures. The original label was 'V59D/L129D'. Wed May 02 15:30:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val59asp,leu129asp' Tue Jun 30 18:49:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Val59Asp;Leu129Asp]' ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role Region 541-638 Region 541-638 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction hspa8-stub1-2 1 5 unspecified role unspecified role unspecified role unspecified role Region 21-154 Region 21-154 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role Region 541-625/639-646 Region 541-625/639-646 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction hspa8-stub1-3 4 5 unspecified role unspecified role unspecified role unspecified role Region 21-154 Region 21-154 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role Region 639-646 Region 639-646 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction stub1-hspa8-2 2 5 unspecified role unspecified role bait bait 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 6 unspecified role unspecified role prey prey Region 395-646 Region 395-646 sufficient to bind sufficient binding region sufficient to bind 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 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli direct interaction direct interaction