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/ CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol. Cell (1097-2765) 2002 Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 pull down pull down western blot western blot Immuno blot Immuno blot Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu Mol. Cell (1097-2765) 2002 CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol. Cell (1097-2765) 2002 Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 anti bait coip anti bait coimmunoprecipitation anti bait coip protein sequence protein sequence identification protein sequence Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu Mol. Cell (1097-2765) 2002 CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol. Cell (1097-2765) 2002 Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. A modified form of Human 293T cells were used in this study. The lines were created by placing into 293T cells constructs capable of producing gag-pol, and envelope protein for ecotropic and amphotropic viruses. The unique feature of this cell line is that it is highly transfectable with either calcium phosphate mediated transfection or lipid-based transfection protocols. The CAND1 protein was overexpressed in this cell line. hui.zhang@yale.edu Mol. Cell (1097-2765) 2002 CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol. Cell (1097-2765) 2002 Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. Hela cells were transfected with siRNA against the endogenous CAND1 transcript to lower CAND1 protein levels. hui.zhang@yale.edu Mol. Cell (1097-2765) 2002 CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol. Cell (1097-2765) 2002 Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 anti bait coip anti bait coimmunoprecipitation anti bait coip predetermined predetermined participant predetermined Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu Mol. Cell (1097-2765) 2002 CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol. Cell (1097-2765) 2002 Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Zheng J., Yang X., Harrell JM., Ryzhikov S., Shim EH., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H. hui.zhang@yale.edu Mol. Cell (1097-2765) 2002 cul1_human Cullin-1 CUL1 protein protein human Homo sapiens Human MSSTRSQNPHGLKQIGLDQIWDDLRAGIQQVYTRQSMAKSRYMELYTHVYNYCTSVHQSNQARGAGVPPSKSKKGQTPGGAQFVGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYTQQWEDYRFSSKVLNGICAYLNRHWVRRECDEGRKGIYEIYSLALVTWRDCLFRPLNKQVTNAVLKLIEKERNGETINTRLISGVVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADTERFYTRESTEFLQQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHLEIFHTEFQNLLDADKNEDLGRMYNLVSRIQDGLGELKKLLETHIHNQGLAAIEKCGEAALNDPKMYVQTVLDVHKKYNALVMSAFNNDAGFVAALDKACGRFINNNAVTKMAQSSSKSPELLARYCDSLLKKSSKNPEEAELEDTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMISKLKQACGFEYTSKLQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVLSSGSWPFQQSCTFALPSELERSYQRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYTLQASTFQMAILLQYNTEDAYTVQQLTDSTQIKMDILAQVLQILLKSKLLVLEDENANVDEVELKPDTLIKLYLGYKNKKLRVNINVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMKMRKVLKHQQLLGEVLTQLSSRFKPRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA DIP protein Q13616 original sequence version: 144 DIP protein Q13616 original sequence version: 133 DIP protein Q13616 original sequence version: null DIP protein Q13616 original sequence version: 135 DIP protein Q13616 original sequence version: 98 DIP protein Q13616 original sequence version: 110 DIP protein Q13616 original sequence version: 146 DIP protein Q13616 original sequence version: 148 DIP protein Q13616 original sequence version: 100 DIP protein Q13616 original sequence version: 85 DIP protein Q13616 original sequence version: 114 DIP protein Q13616 original sequence version: 119 DIP protein Q13616 original sequence version: 136 DIP protein Q13616 original sequence version: 117 DIP protein Q13616 original sequence version: 99 DIP protein Q13616 original sequence version: 108 6625A1FFA7799BBA cul2_human Cullin-2 CUL2 protein protein human Homo sapiens Human MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA DIP protein Q13617 original sequence version: 129 DIP protein Q13617 original sequence version: 127 DIP protein Q13617-1 original sequence version: 139 DIP protein Q13617 original sequence version: 111 DIP protein Q13617 original sequence version: 102 30647248F671AB0E cul4a_human Cullin-4A CUL4A protein protein human Homo sapiens Human MADEAPRKGSFSALVGRTNGLTKPAALAAAPAKPGGAGGSKKLVIKNFRDRPRLPDNYTQDTWRKLHEAVRAVQSSTSIRYNLEELYQAVENLCSHKVSPMLYKQLRQACEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNSTLPSIWDMGLELFRTHIISDKMVQSKTIDGILLLIERERSGEAVDRSLLRSLLGMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQEREVPEYLNHVSKRLEEEGDRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLDHLLDENRVPDLAQMYQLFSRVRGGQQALLQHWSEYIKTFGTAIVINPEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINKRPNKPAELIAKHVDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSDSGPIDLTVNILTMGYWPTYTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQTTLGHAVLKAEFKEGKKEFQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNGEFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLKFPVKPGDLKKRIESLIDRDYMERDKDNPNQYHYVA DIP protein Q13619 original sequence version: 136 DIP protein Q13619 original sequence version: 131 DIP protein Q13619 original sequence version: 129 DIP protein Q13619 original sequence version: 87 DIP protein Q13619 original sequence version: 104 DIP protein Q13619 original sequence version: 151 DIP protein Q13619 original sequence version: 111 DIP protein Q13619 original sequence version: 140 3C4C6A1BBD94D51B q13620-2 Cullin-4B CUL4B KIAA0695 protein protein human Homo sapiens Human MMSQSSGSGDGNDDEATTSKDGGFSSPSPSAAAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSSNSSNEREDFDSTSSSSSTPPLQPRDSASPSTSSFCLGVSVAASSHVPIQKKLRFEDTLEFVGFDAKMAEESSSSSSSSSPTAATSQQQQLKNKSILISSVASVHHANGLAKSSTTVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDICFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA No experimental confirmation available 3E58C5868FDF0700 rbx1_human E3 ubiquitin-protein ligase RBX1 RBX1 RNF75 ROC1 Regulator of cullins 1 RING finger protein 75 Protein ZYP RING-box protein 1 E3 ubiquitin-protein transferase RBX1 protein protein human Homo sapiens Human MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH DIP protein P62877 original sequence version: 120 DIP protein P62877 original sequence version: 115 DIP protein P62877 original sequence version: 78 DIP protein P62877 original sequence version: 113 DIP protein P62877 original sequence version: 75 DIP protein P62877 original sequence version: 86 DIP protein P62877 original sequence version: 136 DIP protein P62877 original sequence version: 126 DIP protein P62877 original sequence version: 90 DIP protein P62877 original sequence version: 114 30FC5ADF66096C0E cand1_human Cullin-associated NEDD8-dissociated protein 1 KIAA0829 TIP120 TIP120A Cullin-associated and neddylation-dissociated protein 1 p120 CAND1 TBP-interacting protein of 120 kDa A CAND1 protein protein human Homo sapiens Human MASASYHISNLLEKMTSSDKDFRFMATNDLMTELQKDSIKLDDDSERKVVKMILKLLEDKNGEVQNLAVKCLGPLVSKVKEYQVETIVDTLCTNMLSDKEQLRDISSIGLKTVIGELPPASSGSALAANVCKKITGRLTSAIAKQEDVSVQLEALDIMADMLSRQGGLLVNFHPSILTCLLPQLTSPRLAVRKRTIIALGHLVMSCGNIVFVDLIEHLLSELSKNDSMSTTRTYIQCIAAISRQAGHRIGEYLEKIIPLVVKFCNVDDDELREYCIQAFESFVRRCPKEVYPHVSTIINICLKYLTYDPNYNYDDEDEDENAMDADGGDDDDQGSDDEYSDDDDMSWKVRRAAAKCLDAVVSTRHEMLPEFYKTVSPALISRFKEREENVKADVFHAYLSLLKQTRPVQSWLCDPDAMEQGETPLTMLQSQVPNIVKALHKQMKEKSVKTRQCCFNMLTELVNVLPGALTQHIPVLVPGIIFSLNDKSSSSNLKIDALSCLYVILCNHSPQVFHPHVQALVPPVVACVGDPFYKITSEALLVTQQLVKVIRPLDQPSSFDATPYIKDLFTCTIKRLKAADIDQEVKERAISCMGQIICNLGDNLGSDLPNTLQIFLERLKNEITRLTTVKALTLIAGSPLKIDLRPVLGEGVPILASFLRKNQRALKLGTLSALDILIKNYSDSLTAAMIDAVLDELPPLISESDMHVSQMAISFLTTLAKVYPSSLSKISGSILNELIGLVRSPLLQGGALSAMLDFFQALVVTGTNNLGYMDLLRMLTGPVYSQSTALTHKQSYYSIAKCVAALTRACPKEGPAVVGQFIQDVKNSRSTDSIRLLALLSLGEVGHHIDLSGQLELKSVILEAFSSPSEEVKSAASYALGSISVGNLPEYLPFVLQEITSQPKRQYLLLHSLKEIISSASVVGLKPYVENIWALLLKHCECAEEGTRNVVAECLGKLTLIDPETLLPRLKGYLISGSSYARSSVVTAVKFTISDHPQPIDPLLKNCIGDFLKTLEDPDLNVRRVALVTFNSAAHNKPSLIRDLLDTVLPHLYNETKVRKELIREVEMGPFKHTVDDGLDIRKAAFECMYTLLDSCLDRLDIFEFLNHVEDGLKDHYDIKMLTFLMLVRLSTLCPSAVLQRLDRLVEPLRATCTTKVKANSVKQEFEKQDELKRSAMRAVAALLTIPEAEKSPLMSEFQSQISSNPELAAIFESIQKDSSSTNLESMDTS DIP protein Q86VP6 original sequence version: 120 DIP protein Q86VP6 original sequence version: 77 DIP protein Q86VP6 original sequence version: 122 FE344558F72D79D8 skp2_human S-phase kinase-associated protein 2 F-box protein Skp2 Cyclin-A/CDK2-associated protein p45 p45skp2 F-box/LRR-repeat protein 1 SKP2 FBXL1 protein protein human Homo sapiens Human MHRKHLQEIPDLSSNVATSFTWGWDSSKTSELLSGMGVSALEKEEPDSENIPQELLSNLGHPESPPRKRLKSKGSDKDFVIVRRPKLNRENFPGVSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDLTGKNLHPDVTGRLLSQGVIAFRCPRSFMDQPLAEHFSPFRVQHMDLSNSVIEVSTLHGILSQCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEKHVQVAVAHVSETITQLNLSGYRKNLQKSDLSTLVRRCPNLVHLDLSDSVMLKNDCFQEFFQLNYLQHLSLSRCYDIIPETLLELGEIPTLKTLQVFGIVPDGTLQLLKEALPHLQINCSHFTTIARPTIGNKKNQEIWGIKCRLTLQKPSCL F29B7C338A7A37E9 skp1_human S-phase kinase-associated protein 1 SKP1 EMC19 OCP2 SKP1A TCEB1L Cyclin-A/CDK2-associated protein p19 p19skp1 RNA polymerase II elongation factor-like protein Organ of Corti protein 2 Organ of Corti protein II SIII Transcription elongation factor B polypeptide 1-like protein protein human Homo sapiens Human MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQWCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTCKTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK C794D62AFB75528A cul1-cand1 2 7 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey physical association physical association cul2-cand1 6 12 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait physical association physical association cul4a-cand1 6 12 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait physical association physical association cul4b-cand1 6 12 unspecified role unspecified role prey prey 10 unspecified role unspecified role bait bait physical association physical association cul1-skp2 6 7 unspecified role unspecified role bait bait Q13616:p.Lys720Arg Alters kinetics of interaction mutation mutation certain certain sequence position certain certain certain sequence position certain K R Thu Jul 07 12:16:45 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was lys720arg Wed May 02 19:13:15 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys720arg' Tue Jun 30 17:04:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys720Arg' 13 unspecified role unspecified role prey prey physical association physical association Binding of Cul1 to SKP2 was inhibited by the CAND1 protein Neddylation of CUL1 enhanced SKP2 binding ATP reduced interaction between CAND1 and CUL1 cul1-cand1-1 6 14 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey association association cand1-cul1 6 7 unspecified role unspecified role prey prey 12 unspecified role unspecified role bait bait physical association physical association CAND1 preferentially associates with unneddylated form of CUL1 cand1-cul1-1 6 11 unspecified role unspecified role prey prey 7 unspecified role unspecified role prey prey 12 unspecified role unspecified role bait bait association association CAND1 preferentially associates with unneddylated form of CUL1 cul1-cand1-2 6 12 unspecified role unspecified role prey prey 11 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait association association cul1-skp1 6 13 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait Q13616:p.Lys720Arg Alters kinetics of interaction mutation mutation certain certain sequence position certain certain certain sequence position certain K R Thu Jul 07 12:16:35 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was lys720arg Wed May 02 15:26:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys720arg' Tue Jun 30 18:14:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys720Arg' physical association physical association Binding of Cul1 to SKP1 was inhibited by the CAND1 protein Neddylation of Cul1 enhanced SKP1 binding ATP reduced interaction between CAND1 and CUL1 cand1-cul1-2 1 7 unspecified role unspecified role prey prey 12 unspecified role unspecified role bait bait 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 physical association physical association This study demonstrated that the CAND1 protein preferentially interacted with the unneddylated form of CUL1. cul1-cand1-4 5 7 unspecified role unspecified role prey prey region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-597778]Certain and ragged-n-terminus positions must always be strictly superior to 0 and inferior or equal to the protein sequence length. Actual positions : 777-777, sequence length 776 [EBI-597778]746-777 s35 radiolabelled radiolabelled radiolabel radiolabeled radiolabelled undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 12 unspecified role unspecified role bait bait physical association physical association cul1-skp1-4 6 7 unspecified role unspecified role prey prey Q13616:p.Lys720Arg Alters kinetics of interaction mutation mutation certain certain sequence position certain certain certain sequence position certain K R Thu Jul 07 12:16:30 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was lys720arg Wed May 02 17:03:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys720arg' Tue Jun 30 18:11:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys720Arg' 13 unspecified role unspecified role bait bait physical association physical association Binding of Cul1 to SKP1 was inhibited by the CAND1 protein Neddylation of Cul1 enhanced SKP1 binding ATP reduced interaction between CAND1 and CUL1 cul1-skp2-1 6 7 unspecified role unspecified role prey prey Q13616:p.Lys720Arg Alters kinetics of interaction mutation mutation certain certain sequence position certain certain certain sequence position certain K R Thu Jul 07 12:16:43 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was lys720arg Wed May 02 20:33:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys720arg' Tue Jun 30 19:16:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys720Arg' 13 unspecified role unspecified role bait bait physical association physical association Binding of Cul1 to SKP2 was inhibited by the CAND1 protein Neddylation of CUL1 enhanced SKP2 binding ATP reduced interaction between CAND1 and CUL1 cand1-cul1-4 6 11 unspecified role unspecified role prey prey 7 unspecified role unspecified role prey prey 12 unspecified role unspecified role bait bait association association cul1-cand1-8 6 11 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey association association Apyrase treatment of cellular extract was shown to enhance binding of RBX1 and CAND1 to Cul1. cul1-cand1-5 3 12 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association cul1-cand1-6 3 12 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait 11 unspecified role unspecified role prey prey association association The participant EBI-398523(P62877) was duplicated. It is posssible that originally this interaction did contain more participants pointing to different Trembl proteins which have been merged to a single swissprot protein later. The authors state that the 'overexpression of the CAND1 protein induced significant dissociation of the endogenous SKP1 and SKP2 from CUL1' and 'the interaction between ROC1 and CUL1 was slightly stimulated'. Note: ROC1 is indentified here as RBX1. cul1-skp1-5 4 13 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association The authors state that the reduced level of CAND1 protein enhanced interaction between Cul1 and SKP1. cul1-skp2-2 4 13 unspecified role unspecified role bait bait 7 unspecified role unspecified role prey prey Q13616:p.Lys720Arg Alters kinetics of interaction mutation mutation certain certain sequence position certain certain certain sequence position certain K R Thu Jul 07 12:07:13 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was lys720arg Wed May 02 18:47:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys720arg' Tue Jun 30 15:36:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys720Arg' physical association physical association The authors state that the reduced level of CAND1 protein enhanced interaction between CUL1 and SKP2 protein and also that levels of SKP2 protein were slightly reduced in these cells perhaps indicating that enhanced proteolysis of SKP2 occured. cand1-cul1-3 4 12 unspecified role unspecified role bait bait 11 unspecified role unspecified role prey prey 7 unspecified role unspecified role prey prey association association cul1-cand1-7 4 12 unspecified role unspecified role prey prey 11 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait association association cul1-rbx1-5 4 7 unspecified role unspecified role bait bait 11 unspecified role unspecified role prey prey physical association physical association The authors note that CAND1 silencing caused a 'slight' decrease in RBX1 and CUL1 interaction.