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/ Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Mol. Cell (1097-2765) 2005 imex curation Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P. nikola@xray2.mskcc.org 26-Jun-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P. nikola@xray2.mskcc.org Accepted 2013-JUN-18 by ORCHARD 26-Jun-2013: Contacted by IntAct-Help. Mol. Cell (1097-2765) 2005 Only protein-protein interactions imex curation Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Mol. Cell (1097-2765) 2005 imex curation Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P. nikola@xray2.mskcc.org 26-Jun-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P. nikola@xray2.mskcc.org Accepted 2013-JUN-18 by ORCHARD 26-Jun-2013: Contacted by IntAct-Help. Mol. Cell (1097-2765) 2005 Only protein-protein interactions imex curation Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Mol. Cell (1097-2765) 2005 imex curation Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P. nikola@xray2.mskcc.org 26-Jun-2013: Contacted by IntAct-Help. 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 Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P. nikola@xray2.mskcc.org Accepted 2013-JUN-18 by ORCHARD 26-Jun-2013: Contacted by IntAct-Help. Mol. Cell (1097-2765) 2005 Only protein-protein interactions imex curation 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 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 cdk2_human Cyclin-dependent kinase 2 CDK2 p33 protein kinase Cell division protein kinase 2 CDKN2 protein protein human Homo sapiens Human MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL DIP protein P24941 original sequence version: 142 DIP protein P24941 original sequence version: 118 DIP protein P24941 original sequence version: 143 DIP protein P24941 original sequence version: 144 DIP protein P24941 original sequence version: 152 DIP protein P24941 original sequence version: 182 DIP protein P24941-1 original sequence version: 204 DIP protein P24941 original sequence version: 90 DIP protein P24941 original sequence version: 190 DIP protein P24941 original sequence version: 168 F90A0F4E70910B51 cks1_human Cyclin-dependent kinases regulatory subunit 1 PNAS-16 PNAS-143 CKS1B CKS1 protein protein human Homo sapiens Human MSHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKPKK E64207B140FA38D5 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 cdn1b_human Cyclin-dependent kinase inhibitor 1B Cyclin-dependent kinase inhibitor p27 p27Kip1 CDKN1B KIP1 protein protein human Homo sapiens Human MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT DIP protein P46527 original sequence version: 120 DIP protein P46527 original sequence version: 115 DIP protein P46527 original sequence version: 154 DIP protein P46527 original sequence version: 168 DIP protein P46527 original sequence version: 164 DIP protein P46527 original sequence version: 118 1118D58901CDF3FC ccna2_human Cyclin-A2 Cyclin A CCNA2 CCN1 CCNA protein protein human Homo sapiens Human MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRGLAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKIEREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIILEDEKPVSVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSKYHGVSLLNPPETLNL DIP protein P20248 original sequence version: 183 DIP protein P20248 original sequence version: 146 DIP protein P20248 original sequence version: 168 DIP protein P20248 original sequence version: 149 DIP protein P20248 original sequence version: 111 97763A2897DD35F4 cks1b-skp1 3 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P63208:p.Pro2Ala mutation mutation certain certain sequence position certain certain certain sequence position certain P A Wed May 02 19:14:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro2ala' Tue Jun 30 18:35:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro2Ala' ecolx Escherichia coli physical association physical association Suppl. Fig. 7, Table 2 working 21.4%, free 24.2% 3.00A Presence of benzamidine in the crystal. For Skp2 only residues 95 to 419 are visible in the structure. cdkn1b-cks1b 3 9 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P63208:p.Pro2Ala mutation mutation certain certain sequence position certain certain certain sequence position certain P A Wed May 02 15:03:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro2ala' Tue Jun 30 16:27:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro2Ala' ecolx Escherichia coli 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli p27Kip1 10 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain thr187 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association Fig. 2, Fig. 3, Suppl. Fig. 1, Table 2 working 20.2%, free 22.1% 2.30A Presence of Benzamidine in the crystal. For Skp2 only residues 95 to 419 are visible in the structure. For Cdn1b/p27Kip1 only residues 181 to 190 are visible in the structure. cks1b-skp1-1 1 9 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association Table 1 Binding of Cks1 to the Skp1-Skp2 complex was measured. Kd for binding of Cks1 to Skp1-Skp2 complex = 0.006 +/- 0.001 micromolar. Kd for binding of Cks1 (5-73) to Skp1-Skp2 complex = 0.006 +/- 0.002 micromolar. Temp = 25C cdkn1b-cks1b-1 1 7 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli p27Kip1 10 unspecified role unspecified role neutral component neutral component thr187 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association Table 1 Binding of phosphorylated Cdn1b/p27Kip1 to Skp1-Skp2-Cks1 complex was measured. Kd for binding of phospho-Cdn1b/p27Kip1 to Skp1-Skp2-Cks1 complex = 7 +/- 2 micromolar. Kd for binding of phospho-Cdn1b/p27Kip1 (175-198) to Skp1-Skp2-Cks1 complex = 7 +/- 1 micromolar. Kd for binding of phospho-Cdn1b/p27Kip1 (175-198) to Skp1-Skp2-Cks1 (5-73) complex = 9 +/- 2 micromolar. Temp = 25C ccna2-cdk2-12 2 p27Kip1 10 unspecified role unspecified role neutral component neutral component thr187 opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain unknown Unknown 5 unspecified role unspecified role neutral component neutral component unknown Unknown 6 unspecified role unspecified role neutral component neutral component unknown Unknown 11 unspecified role unspecified role neutral component neutral component unknown Unknown 7 unspecified role unspecified role neutral component neutral component unknown Unknown 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain unknown Unknown 9 unspecified role unspecified role neutral component neutral component unknown Unknown 4 unspecified role unspecified role neutral component neutral component unknown Unknown association association Fig. 6c