DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. Structure (London, England : 1993) 2012 imex curation Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. Only protein-protein interactions ecolx Escherichia coli sls static light scattering sls predetermined predetermined participant predetermined Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. DIP original experiment: DIP-251182X Structure (London, England : 1993) 2012 IMEx The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. Structure (London, England : 1993) 2012 imex curation Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. Only protein-protein interactions drome Drosophila melanogaster (Fruit fly) Fruit fly anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. DIP original experiment: DIP-251187X Structure (London, England : 1993) 2012 IMEx The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. Structure (London, England : 1993) 2012 imex curation Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. Only protein-protein interactions drome Drosophila melanogaster (Fruit fly) Fruit fly anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. DIP original experiment: DIP-251186X Structure (London, England : 1993) 2012 IMEx The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. Structure (London, England : 1993) 2012 imex curation Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. DIP original experiment: DIP-251184X Structure (London, England : 1993) 2012 IMEx The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. Structure (London, England : 1993) 2012 imex curation Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. DIP original experiment: DIP-251185X Structure (London, England : 1993) 2012 IMEx The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. Structure (London, England : 1993) 2012 imex curation Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. Only protein-protein interactions drome Drosophila melanogaster (Fruit fly) Fruit fly anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. DIP original experiment: DIP-251188X Structure (London, England : 1993) 2012 IMEx The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. Structure (London, England : 1993) 2012 imex curation Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. 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 Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. DIP original experiment: DIP-251181X Structure (London, England : 1993) 2012 IMEx The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. Structure (London, England : 1993) 2012 imex curation Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. Only protein-protein interactions ecolx Escherichia coli dls dynamic light scattering dls predetermined predetermined participant predetermined Slevin LK., Nye J., Pinkerton DC., Buster DW., Rogers GC., Slep KC. DIP original experiment: DIP-251183X Structure (London, England : 1993) 2012 IMEx The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication. q9vne4_drome DmAsl asl CG2919 ASL Asl Dmel\CG2919 mecD sdu Dmel_CG2919 Cep152 MecD protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MNTPGISLFQGADALNINSTLDRQEEEEALQDQKRREEELGRIMVNAFDDLLDEENTIDSTTNYQSELEQPPVLPNYPSHPHHKPLQDDAQRANEIEMHRLQILLESKNNELQNVNQVANAAHKKLDDLQKHLSIMQAELDRAIREKQNTHELLVETKETCSNKDSDLDKLRSEKKQLEEDNTRLVGQLEAAKTLLTDVQSKYDMVQASKQKWEERNADLRLKQMEEAHRAQSDLLQQQLCQMKDQLDRKQNELDQINSRYNALQSGHETMLVDKAAKINELSQALDEAQMRCNQLSARPDLQAENRRQQQCIVDLKARIAYLEQTVASLHERLNETTTELDLIDSVIQQHQADESPTSRLSQMGGSRLVGSTPLNPLDRVGHIKQELYRALGNLKNKREEVRRLEKLLEERNQELRVLRDQENQSLVQLETLNEGKMRLENKVKAMQQELEEQKHRSQQESDVHSQLNSIVAERDALREKRQQIEEDLEQLKQQNESLQRNYDQLSQENRQLRTRETADNLRLELERHKILLRDSQSEVERLKKLYSDIATDKESLGYELRKLRESDTLKELQDQRQNLATVQRNLQLAEMKSEELKKLLETEKLSHERDLQALRQRSEREKREEAVAVAKESSENCSKCIESIAEITKAEIQLLKLQNVNSMQAKELKELEHALEQSKNLQAEMQEKIELSNKQDELISDLKERAKQFEAYIRQQEEHKQQNKCTPSPKSNSVSPSDPSPKELTQNRIRLIEQRVRDEMAKLFAAELKRFTNRLQKSEERSQCLQREYQTVCAELQQRQTEVDLLKQTILAERENIDEILAGREEKQKEMLQKCRQELQAKNQRIAELLREVEEQHASIDSERQSMKAVMAQWEKQRQSVDQVEHHWRQQLESLRSTHEEAMRSAQQRYQSAKRTAHNYKLYAEDKEAHMKREYERIKHEYELSLAKIEATMNQHLERRSREKHRDKENVPSNSSSDPITNSNRKPKGNGHS DIP protein Q9VNE4 original sequence version: 59 DIP protein Q9VNE4 original sequence version: 88 DIP protein Q9VNE4 original sequence version: 90 DIP protein Q9VNE4 original sequence version: 107 DIP protein Q9VNE4 original sequence version: 73 75A90C8496BA9EC5 plk4_drome Serine/threonine-protein kinase PLK4 SAK CG7186 Polo-like kinase 4 Serine/threonine-protein kinase SAK protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRTSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSAPGALNVFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIREEFKQVHHKLPYEQTGLFGQASTGLAEPNWPGAAKSSAFCMEAGNVPNSKQASLKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFLKFRPTYNEDRINDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYDNLPSKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPSEGLKVYDRNGMLLSDYSCSESRSLIEHGNECFTHCVNISNALEVAQTKDNSCFPVTIGRRPITDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSLSTISSTRNTSDFGTNCSRSNMLAAHQNIPIKRINVPEIGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKGDDLPFPVRDRVGQIPNIQLKLKTAPLLGSGRKTDYNNAMTPKTTTPYYNRMLL DIP protein O97143 original sequence version: 100 DIP protein O97143 original sequence version: 130 DIP protein O97143 original sequence version: 114 F050BF60A5D94AA4 q9vde3_drome slmb beta-TrCP BcDNA:GM02031 Beta-TRCP1 Dmel\CG3412 FBXW1 MENE (3R)-B MENE(3R)-B SLIMB SLMB Slimb Slmb beta-TRCP betaTrCP crd ica l(3)00295 shv slimb wel Dmel_CG3412 CG3412 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MMKMETDKIMDETNSNAQAFTTTMLYDPVRKKDSSPTYQTERELCFQYFTQWSESGQVDFVEHLLSRMCHYQHGQINAYLKPMLQRDFITLLPIKGLDHIAENILSYLDAESLKSSELVCKEWLRVISEGMLWKKLIERKVRTDSLWRGLAERRNWMQYLFKPRPGQTQRPHSFHRELFPKIMNDIDSIENNWRTGRHMLRRINCRSENSKGVYCLQYDDGKIVSGLRDNTIKIWDRTDLQCVKTLMGHTGSVLCLQYDDKVIISGSSDSTVRVWDVNTGEMVNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMTSPSEITLRRVLVGHRAAVNVVDFDEKYIVSASGDRTIKVWSTSSCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNSIRLWDIECGACLRVLEGHEELVRCIRFDTKRIVSGAYDGKIKVWDLVAALDPRAASNTLCLNTLVEHTGRVFRLQFDEFQIVSSSHDDTILIWDFLNFTPNENKTGRTPSPALMEH DIP protein Q9VDE3 original sequence version: 100 DIP protein Q9VDE3 original sequence version: 116 DIP protein Q9VDE3 original sequence version: 118 DIP protein Q9VDE3 original sequence version: 135 F4D5DF126F58A012 sak-9 4 10 unspecified role unspecified role unspecified role unspecified role PB1-2 domain Region 382-602 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 sak-10 7 10 unspecified role unspecified role unspecified role unspecified role PB1-2 domain Region 382-602 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 sak-11 5 10 putative self putative self unspecified role unspecified role Kinase domain Region 1-317 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation true sak-12 1 10 unspecified role unspecified role unspecified role unspecified role PB1-2 domain Region 382-602 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 sak-sak-1 2 10 unspecified role unspecified role prey prey Myc-tag Myc-tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range drome Drosophila melanogaster (Fruit fly) Fruit fly 10 unspecified role unspecified role bait bait GFP-tag GFP-tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range PB1-2 domain Region 382-602 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain drome Drosophila melanogaster (Fruit fly) Fruit fly physical association physical association sak-asl-7 3 9 unspecified role unspecified role prey prey Region 1-300 Region 1-300 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain V5-tag V5-tag v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range drome Drosophila melanogaster (Fruit fly) Fruit fly 10 unspecified role unspecified role bait bait PB1-2 domain Region 382-602 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain O97143:p.[Ser293Ala;Thr297Ala] S293A/T297A mutation increasing strength mutation increasing interaction strength mutation increasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain T A certain certain sequence position certain certain certain sequence position certain S A This feature has been corrected as a result of our quality control procedures. The original label was 'S293A/T297A'. Wed May 02 18:17:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser293ala,thr297ala' Tue Jun 30 19:16:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser293Ala;Thr297Ala]' GFP-tag GFP-tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range drome Drosophila melanogaster (Fruit fly) Fruit fly physical association physical association sak-13 8 10 unspecified role unspecified role unspecified role unspecified role PB1-2 domain Region 382-602 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 sak-slmb-1 6 11 unspecified role unspecified role prey prey drome Drosophila melanogaster (Fruit fly) Fruit fly 10 unspecified role unspecified role bait bait GFP-tag GFP-tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range drome Drosophila melanogaster (Fruit fly) Fruit fly physical association physical association Deletion of region 382-602 decreased the interaction rate/strength.