DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216624X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216631X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216627X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216637X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216625X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216626X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216640X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216644X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216639X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216636X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216638X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216635X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216634X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216630X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216628X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. 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 Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216632X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216642X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216629X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216633X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216643X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS biology 2010 imex curation Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Rellos P., Pike AC., Niesen FH., Salah E., Lee WH., von Delft F., Knapp S. DIP original experiment: DIP-216641X PLoS biology 2010 IMEx Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. kcc2b_human Calcium/calmodulin-dependent protein kinase type II subunit beta CAMK2B CAM2 CAMKB CAMK2 protein protein human Homo sapiens Human MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTKNSAAATSPKGTLPPAALEPQTTVIHNPVDGIKESSDSANTTIEDEDAKAPRVPDILSSVRRGSGAPEAEGPLPCPSPAPFSPLPAPSPRISDILNSVRRGSGTPEAEGPLSAGPPPCLSPALLGPLSSPSPRISDILNSVRRGSGTPEAEGPSPVGPPPCPSPTIPGPLPTPSRKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAPVAPLQ DIP protein Q13554 original sequence version: 110 8CACFC3E392C3857 kcc2g_human Calcium/calmodulin-dependent protein kinase type II subunit gamma CAMK CAMK-II CAMK2G CAMKG protein protein human Homo sapiens Human MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKKRKSSSSVHLMPQSNNKNSLVSPAQEPAPLQTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKGRVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWLNVHYHCSGAPAAPLQ DIP protein Q13555 original sequence version: 104 DIP protein Q13555 original sequence version: 109 7D61AB799B8F8CEB kcc2d_human Calcium/calmodulin-dependent protein kinase type II subunit delta CAMK2D CAMKD protein protein human Homo sapiens Human MASTTTCTRFTDEYQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRITASEALKHPWICQRSTVASMMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSAAKSLLKKPDGVKESTESSNTTIEDEDVKARKQEIIKVTEQLIEAINNGDFEAYTKICDPGLTAFEPEALGNLVEGMDFHRFYFENALSKSNKPIHTIILNPHVHLVGDDAACIAYIRLTQYMDGSGMPKTMQSEETRVWHRRDGKWQNVHFHRSGSPTVPIKPPCIPNGKENFSGGTSLWQNI DIP protein Q13557 original sequence version: 123 DIP protein Q13557 original sequence version: 113 62999FBAB98120CE kcc1a_human Calcium/calmodulin-dependent protein kinase type 1 CAMK1 CaM kinase I CaM kinase I alpha protein protein human Homo sapiens Human MLGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKEALEGKEGSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAKSKWKQAFNATAVVRHMRKLQLGTSQEGQGQTASHGELLTPVAGGPAAGCCCRDCCVEPGTELSPTLPHQL DIP protein Q14012 original sequence version: 107 DIP protein Q14012 original sequence version: 157 57FA20ECE00FA76C kcc4_human Calcium/calmodulin-dependent protein kinase type IV CAMK CAMK-GR CAMKIV CaM kinase-GR CAMK4 protein protein human Homo sapiens Human MLKVTVPSCSASSCSSVTASAAPGTASLVPDYWIDGSNRDALSDFFEVESELGRGATSIVYRCKQKGTQKPYALKVLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVEHQVLMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGIITYILLCGFEPFYDERGDQFMFRRILNCEYYFISPWWDEVSLNAKDLVRKLIVLDPKKRLTTFQALQHPWVTGKAANFVHMDTAQKKLQEFNARRKLKAAVKAVVASSRLGSASSSHGSIQESHKASRDPSPIQDGNEDMKAIPEGEKIQGDGAQAAVKGAQAELMKVQALEKVKGADINAEEAPKMVPKAVEDGIKVADLELEEGLAEEKLKTVEEAAAPREGQGSSAVGFEVPQQDVILPEY DIP protein Q16566 original sequence version: 102 EFEE51E5612326DC calm_human Calmodulin CALM1 CALM CAM CAM1 CALM2 CAMB CALM3 CAM3 CAMC CAMIII CAM2 CALML2 protein protein human Homo sapiens Human MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK DIP protein P62158 original sequence version: 97 DIP protein P62158 original sequence version: 144 DIP protein P62158 original sequence version: 146 DIP protein P62158 original sequence version: 73 DIP protein P62158 original sequence version: 102 DIP protein P62158 original sequence version: 98 DIP protein P62158 original sequence version: 96 DIP protein P62158 original sequence version: 111 DIP protein P62158 original sequence version: 131 DIP protein P62158 original sequence version: 136 DIP protein P62158 original sequence version: 145 DIP protein P62158 original sequence version: 154 DIP protein P62158 original sequence version: 148 DIP protein P62158 original sequence version: 116 DIP protein P62158 original sequence version: 120 DIP protein P62158 original sequence version: 130 6B4BC3FCDE10727B kcc2a_human Calcium/calmodulin-dependent protein kinase type II subunit alpha CAMK2A CAMKA KIAA0968 protein protein human Homo sapiens Human MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGGNKKSDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSVLPH DIP protein Q9UQM7 original sequence version: 96 208143A311BA9262 camk2g-1 8 23 unspecified role unspecified role unspecified role unspecified role Region 387-527 Region 387-527 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction camk2a-1 1 28 unspecified role unspecified role unspecified role unspecified role Region 13-301 Region 13-301 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk2a-1 11 28 unspecified role unspecified role unspecified role unspecified role Region 13-301 Region 13-301 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction camk2b-1 5 22 unspecified role unspecified role unspecified role unspecified role Region 11-302 Region 11-302 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk2a-2 13 28 unspecified role unspecified role unspecified role unspecified role Region 13-301 Region 13-301 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction camk2d-camk2g-3 14 24 unspecified role unspecified role unspecified role unspecified role Region 282-310 Region 282-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 23 unspecified role unspecified role unspecified role unspecified role Region 5-317 Region 5-317 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction camk2g-2 6 23 unspecified role unspecified role unspecified role unspecified role Region 5-317 Region 5-317 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction camk2d-1 20 24 unspecified role unspecified role unspecified role unspecified role Region 334-475 Region 334-475 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk2d-1 12 24 unspecified role unspecified role unspecified role unspecified role Region 282-310 Region 282-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 24 unspecified role unspecified role unspecified role unspecified role Region 1-333 Region 1-333 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association calm1-camk2b-1 9 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 22 unspecified role unspecified role unspecified role unspecified role Region 11-302 Region 11-302 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction camk2d-camk2d-1 2 24 unspecified role unspecified role unspecified role unspecified role Region 282-310 Region 282-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 24 unspecified role unspecified role unspecified role unspecified role Region 11-335 Region 11-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk4-1 21 26 unspecified role unspecified role unspecified role unspecified role Region 15-340 Region 15-340 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction camk2d-2 3 24 unspecified role unspecified role unspecified role unspecified role Region 11-335 Region 11-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk2d-2 10 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 24 unspecified role unspecified role unspecified role unspecified role Region 11-335 Region 11-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction camk2a-camk2d-2 15 24 unspecified role unspecified role unspecified role unspecified role Region 282-310 Region 282-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 28 unspecified role unspecified role unspecified role unspecified role Region 13-301 Region 13-301 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk2d-3 16 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 24 unspecified role unspecified role unspecified role unspecified role Region 1-333 Region 1-333 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk2g-1 7 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 5-317 Region 5-317 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk1-1 17 25 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction camk2b-camk2d-1 18 24 unspecified role unspecified role unspecified role unspecified role Region 282-310 Region 282-310 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 22 unspecified role unspecified role unspecified role unspecified role Region 11-302 Region 11-302 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-camk2d-4 4 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 24 unspecified role unspecified role unspecified role unspecified role Region 296-315 Region 296-315 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction calm1-camk2d-5 19 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 24 unspecified role unspecified role unspecified role unspecified role Region 1-333 Region 1-333 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction