DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220153X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220155X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220154X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220160X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro field flow fractionation field flow fractionation predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220158X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro field flow fractionation field flow fractionation predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220159X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220147X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220156X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220150X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220151X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220161X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220148X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220157X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220152X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure (London, England : 1993) 2011 imex curation Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Elegheert J., Desfosses A., Shkumatov AV., Wu X., Bracke N., Verstraete K., Van Craenenbroeck K., Brooks BR., Svergun DI., Vergauwen B., Gutsche I., Savvides SN. DIP original experiment: DIP-220149X Structure (London, England : 1993) 2011 IMEx Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. csf1r_human Macrophage colony-stimulating factor 1 receptor CSF1R FMS Proto-oncogene c-Fms CSF-1 receptor protein protein human Homo sapiens Human MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGAHTHPPDEFLFTPVVVACMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRRERDYTNLPSSSRSGGSGSSSSELEEESSSEHLTCCEQGDIAQPLLQPNNYQFC DIP protein P07333 original sequence version: 159 DIP protein P07333-1 original sequence version: 185 DIP protein P07333 original sequence version: 145 DIP protein P07333 original sequence version: 148 DIP protein P07333 original sequence version: 153 A8D99BE237573FE8 csf1r_mouse Macrophage colony-stimulating factor 1 receptor Csf1r Csfmr Fms CSF-1 receptor Proto-oncogene c-Fms protein protein mouse Mus musculus Mouse MELGPPLVLLLATVWHGQGAPVIEPSGPELVVEPGETVTLRCVSNGSVEWDGPISPYWTLDPESPGSTLTTRNATFKNTGTYRCTELEDPMAGSTTIHLYVKDPAHSWNLLAQEVTVVEGQEAVLPCLITDPALKDSVSLMREGGRQVLRKTVYFFSPWRGFIIRKAKVLDSNTYVCKTMVNGRESTSTGIWLKVNRVHPEPPQIKLEPSKLVRIRGEAAQIVCSATNAEVGFNVILKRGDTKLEIPLNSDFQDNYYKKVRALSLNAVDFQDAGIYSCVASNDVGTRTATMNFQVVESAYLNLTSEQSLLQEVSVGDSLILTVHADAYPSIQHYNWTYLGPFFEDQRKLEFITQRAIYRYTFKLFLNRVKASEAGQYFLMAQNKAGWNNLTFELTLRYPPEVSVTWMPVNGSDVLFCDVSGYPQPSVTWMECRGHTDRCDEAQALQVWNDTHPEVLSQKPFDKVIIQSQLPIGTLKHNMTYFCKTHNSVGNSSQYFRAVSLGQSKQLPDESLFTPVVVACMSVMSLLVLLLLLLLYKYKQKPKYQVRWKIIERYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDSEGDSSYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSSDSFFKQDLDKEASRPLELWDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTSGHVAKIGDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNNKFYKLVKDGYQMAQPVFAPKNIYSIMQSCWDLEPTRRPTFQQICFLLQEQARLERRDQDYANLPSSGGSSGSDSGGGSSGGSSSEPEEESSSEHLACCEPGDIAQPLLQPNNYQFC DIP protein P09581 original sequence version: 115 DIP protein P09581 original sequence version: 149 DIP protein P09581 original sequence version: 160 DIP protein P09581 original sequence version: 156 7EDF8310CCF98906 csf1_human Macrophage colony-stimulating factor 1 CSF1 Lanimostim protein protein human Homo sapiens Human MTAPGAAGRCPPTTWLGSLLLLVCLLASRSITEEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQDVVTKPDCNCLYPKAIPSSDPASVSPHQPLAPSMAPVAGLTWEDSEGTEGSSLLPGEQPLHTVDPGSAKQRPPRSTCQSFEPPETPVVKDSTIGGSPQPRPSVGAFNPGMEDILDSAMGTNWVPEEASGEASEIPVPQGTELSPSRPGGGSMQTEPARPSNFLSASSPLPASAKGQQPADVTGTALPRVGPVRPTGQDWNHTPQKTDHPSALLRDPPEPGSPRISSLRPQGLSNPSTLSAQPQLSRSHSSGSVLPLGELEGRRSTRDRRSPAEPEGGPASEGAARPLPRFNSVPLTDTGHERQSEGSFSPQLQESVFHLLVPSVILVLLAVGGLLFYRWRRRSHQEPQRADSPLEQPEGSPLTQDDRQVELPV DIP protein P09603 original sequence version: 166 DIP protein P09603-1 original sequence version: 127 DIP protein P09603 original sequence version: 130 DIP protein P09603 original sequence version: 139 DIP protein P09603 original sequence version: 135 656B0894F9255AED csf1_mouse Macrophage colony-stimulating factor 1 Csf1 Csfm protein protein mouse Mus musculus Mouse MTARGAAGRCPSSTWLGSRLLLVCLLMSRSIAKEVSEHCSHMIGNGHLKVLQQLIDSQMETSCQIAFEFVDQEQLDDPVCYLKKAFFLVQDIIDETMRFKDNTPNANATERLQELSNNLNSCFTKDYEEQNKACVRTFHETPLQLLEKIKNFFNETKNLLEKDWNIFTKNCNNSFAKCSSRDVVTKPDCNCLYPKATPSSDPASASPHQPPAPSMAPLAGLAWDDSQRTEGSSLLPSELPLRIEDPGSAKQRPPRSTCQTLESTEQPNHGDRLTEDSQPHPSAGGPVPGVEDILESSLGTNWVLEEASGEASEGFLTQEAKFSPSTPVGGSIQAETDRPRALSASPFPKSTEDQKPVDITDRPLTEVNPMRPIGQTQNNTPEKTDGTSTLREDHQEPGSPHIATPNPQRVSNSATPVAQLLLPKSHSWGIVLPLGELEGKRSTRDRRSPAELEGGSASEGAARPVARFNSIPLTDTGHVEQHEGSSDPQIPESVFHLLVPGIILVLLTVGGLLFYKWKWRSHRDPQTLDSSVGRPEDSSLTQDEDRQVELPV DIP protein P07141 original sequence version: 88 DIP protein P07141-1 original sequence version: 117 DIP protein P07141 original sequence version: 122 3886D72D70E770AF csf1-1 7 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-csf1r-1 14 17 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-298 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 19 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1r-1 11 16 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-517 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human direct interaction direct interaction csf1-csf1r-2 8 16 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-517 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-8 12 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-9 1 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-csf1r-3 15 16 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-290 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-csf1r-11 13 16 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-290 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-csf1r-12 9 16 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-290 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-csf1r-13 3 19 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-517 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human direct interaction direct interaction csf1-csf1r-14 5 16 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-290 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-csf1r-15 4 17 unspecified role unspecified role unspecified role unspecified role Region 20-298 Region 20-298 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 19 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-csf1r-16 10 16 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-290 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction csf1-csf1r-17 2 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Ectodomain Region 20-515 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human direct interaction direct interaction csf1-10 6 18 unspecified role unspecified role unspecified role unspecified role Region 33-181 Region 33-181 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction