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/ Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site. Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site. Cell (0092-8674) 2007 imex curation Allingham JS., Sproul LR., Rayment I., Gilbert SP. A unique UniProtKB entry could not be associated with conventional kinesin K401 since organism andexact gene product of interactor cannot be ascertained. ivan_rayment@biochem.wisc.edu,spg1@pitt.edu 26-APR-2007: Contacted by JYOTI. Only protein-protein interactions 3 in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation predetermined predetermined participant predetermined Allingham JS., Sproul LR., Rayment I., Gilbert SP. A unique UniProtKB entry could not be associated with conventional kinesin K401 since organism andexact gene product of interactor cannot be ascertained. ivan_rayment@biochem.wisc.edu,spg1@pitt.edu Accepted 2007-MAY-3 by DAVET. 26-APR-2007: Contacted by JYOTI. Cell (0092-8674) 2007 Only protein-protein interactions 3 imex curation Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site. Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site. Cell (0092-8674) 2007 imex curation Allingham JS., Sproul LR., Rayment I., Gilbert SP. A unique UniProtKB entry could not be associated with conventional kinesin K401 since organism andexact gene product of interactor cannot be ascertained. ivan_rayment@biochem.wisc.edu,spg1@pitt.edu 26-APR-2007: Contacted by JYOTI. Only protein-protein interactions 3 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 Allingham JS., Sproul LR., Rayment I., Gilbert SP. A unique UniProtKB entry could not be associated with conventional kinesin K401 since organism andexact gene product of interactor cannot be ascertained. ivan_rayment@biochem.wisc.edu,spg1@pitt.edu Accepted 2007-MAY-3 by DAVET. 26-APR-2007: Contacted by JYOTI. Cell (0092-8674) 2007 Only protein-protein interactions 3 imex curation kar3_yeast Kinesin-like protein KAR3 KAR3 YPR141C P9659.16 Nuclear fusion protein protein protein yeast Saccharomyces cerevisiae Baker's yeast MESLPRTPTKGRSTQHLSTPSPKNDILAMNGHKRRNTTTPPPKHTLLKPQRTDIHRHSLASQSRISMSPNRELLKNYKGTANLIYGNQKSNSGVTSFYKENVNELNRTQAILFEKKATLDLLKDELTETKEKINAVNLKFETLREEKIKIEQQLNLKNNELISIKEEFLSKKQFMNEGHEIHLKQLAASNKKELKQMENEYKTKIEKLKFMKIKQFENERASLLDKIEEVRNKITMNPSTLQEMLNDVEQKHMLEKEEWLTEYQSQWKKDIELNNKHMQEIESIKKEIENTLKPELAEKKKLLTEKRNAYEAIKVKVKEKEEETTRLRDEVALKQKTNLETLEKIKELEEYIKDTELGMKELNEILIKEETVRRTLHNELQELRGNIRVYCRIRPALKNLENSDTSLINVNEFDDNSGVQSMEVTKIQNTAQVHEFKFDKIFDQQDTNVDVFKEVGQLVQSSLDGYNVCIFAYGQTGSGKTFTMLNPGDGIIPSTISHIFNWINKLKTKGWDYKVNCEFIEIYNENIVDLLRSDNNNKEDTSIGLKHEIRHDQETKTTTITNVTSCKLESEEMVEIILKKANKLRSTASTASNEHSSRSHSIFIIHLSGSNAKTGAHSYGTLNLVDLAGSERINVSQVVGDRLRETQNINKSLSCLGDVIHALGQPDSTKRHIPFRNSKLTYLLQYSLTGDSKTLMFVNISPSSSHINETLNSLRFASKVNSTRLVSRK BAEF98BC783ABDB9 cik1_yeast Spindle pole body-associated protein CIK1 CIK1 YMR198W YM9646.11 Chromosome instability and karyogamy protein 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MNNSKIPKLSFHSDPNNVTRDFPKTKRQKVQKREMDMILTPNNNKLNILHSSGSGIRRCYTDDTSATYTKKLTFGGDPKIIERVKNNERKVRKDIDSLLNAISEIEKESVRIHARELPAITLELDAKVKACRELQNEIDGLSTEMDLKDNQCDLQRKNVELSSKNIVSMHAVKVQEFENDLEEELSNAKREWTYKLMEVENLKPDERLTDEMRQLKTEFEEVNRKLFILQNENENECKNYKKELDKKFEIFKKVKNDARIELDGEQERLSKVLKDLQDTHGELKENIKTCRDEFNDFEKRIGEAEVNFHSMELAVVPLKKKLASTSQALTQVQEEKKQVEGEANNWKKKYVNELEKVQQELYTRQNLATSIEEIKGYTRCFAYANERQMPDEFHINYVDRCICENSGEKRVQVFDRVVLEEIHKDHKRLYNECIPFLEKYISKLINCSIIVVSQQPTAPMKKTLLKQLIEQYGENYKMTLNILHLDGSIKHSDVGLDNPTEIRDLSQDEECMNILTLDTKLGKDEESHSMNIYIGSMSTVQLNRELDDAPSVLSHILTKTKQCFVFKINAGENIEKALALAGKLKRTITLPQLD A2A09DEB8C2EC838 A2A09DEB8C2EC838 vik1_yeast Spindle pole body-associated protein VIK1 YPL253C VIK1 Vegetative interaction with KAR3 protein 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MASQQNKHAFLSKNRIFHNPDNVSSSKSRNLMDITNTTNTMNGSRPSSMKSSLALPPVKDSFPSVSRSASLNINMSKIKDLKDRQDKIRFQRHTLRTQLIECEREIKTIKFRDLNKSRFELYKKKSKQAKYLKQVRDLTQNLNSKDGERADLIKKNKSALATLQAELDQNLILKRQESQELYNNKLIFWENELQIMENVEPDHEITEEISQLKKTLQELNINWANLQKQNLERQVNHESQLRKDFIAFKEAKLKSMENLTNKHRELLDQIATLQSESEKLHKEIMDIDRQAEYSEQNISEINENIKQLELANNPLISKSLQNSQDLEHLQNQMENLKEMASKQEKFYNDTYNTVEKELLRSRRLENSIIEQKGTMRCYAYVMEQNLPENLLFDYENGVITQGLSEHVYKFNRVIPHLKVSEDKFFTQEYSVYHDMCLNQKKNFNLISLSTTPHGSLRESLIKFLAEKDTIYQKQYVITLQFVFLSDDEFSQDMLLDYSHNDKDSIKLKFEKHSISLDSKLVIIENGLEDLPLNFSCDEHPNLPHSGMGIIKVQFFPRDSKSDGNNDPVPVDFYFIELNNLKSIEQFDKSIFKKESCETPIALVLKKLISDTKSFFLLNLNDSKNVNKLLTISEEVQTQLCKRKKKLT A6E61C51CC10B8EB kar3-vik1 2 5 unspecified role unspecified role neutral component neutral component c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 3 unspecified role unspecified role neutral component neutral component c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) physical association physical association S1 This truncated version of Kar3/Vik1 contains much of the coiled-coil dimerization region and the C-terminal globular domains of Kar3 and Vik1 (Figure 1 and Figure S1). This construct was designed based on sequence analyses and proteolysis experiments of Kar3, Vik1, and Cik1 to identify the minimal length of coiled-coil that allows the C-terminal globular domains of Vik1 and Cik1 to heterodimerize with the motor domain of Kar3. The dimeric state of this complex was confirmed by analytical gel filtration and equilibrium centrifugation cik1-kar3 2 4 unspecified role unspecified role neutral component neutral component c-terminal sufficient to bind sufficient binding region sufficient to bind undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-1224134]Certain and ragged-n-terminus positions must always be strictly superior to 0 and inferior or equal to the protein sequence length. Actual positions : 647-647, sequence length 594 [EBI-1224134]253-647 ecobb Escherichia coli (strain B / BL21) 3 unspecified role unspecified role neutral component neutral component c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) physical association physical association S1 Analytical gel filtration of Kar3/Vik1, Kar3/Cik1, dimeric conventional kinesin K401, and Kar3MD with the Mr predicted based on amino acid sequence. Stokes radius of Kar3/Vik1 = 4.1 nm, Kar3/Cik1 = 3.9 nm, K401 = 3.8 nm, Kar3MD = 3.4 nm. kar3-vik1-1 1 5 unspecified role unspecified role neutral component neutral component c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 3 unspecified role unspecified role neutral component neutral component c-terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) physical association physical association S5 The scans were corrected for baseline and were best fit to a single species model (-) with a molecular weight of 105,700 (252), which is close to the calculated molecular weight of 101,247.15 for the combined sequence of each protein for a 1:1 complex.