DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structure (London, England : 1993) 2005 imex curation Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. 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 Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. DIP original experiment: DIP-132733X Structure (London, England : 1993) 2005 IMEx Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structure (London, England : 1993) 2005 imex curation Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. DIP original experiment: DIP-132736X Structure (London, England : 1993) 2005 IMEx Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structure (London, England : 1993) 2005 imex curation Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. DIP original experiment: DIP-132735X Structure (London, England : 1993) 2005 IMEx Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structure (London, England : 1993) 2005 imex curation Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. 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 Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. DIP original experiment: DIP-132737X Structure (London, England : 1993) 2005 IMEx Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. Structure (London, England : 1993) 2005 imex curation Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. 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 Siwanowicz I., Popowicz GM., Wisniewska M., Huber R., Kuenkele KP., Lang K., Engh RA., Holak TA. DIP original experiment: DIP-132734X Structure (London, England : 1993) 2005 IMEx Structural basis for the regulation of insulin-like growth factors by IGF binding proteins. ibp5_human Insulin-like growth factor-binding protein 5 IGFBP5 IBP5 protein protein human Homo sapiens Human MVLLTAVLLLLAAYAGPAQSLGSFVHCEPCDEKALSMCPPSPLGCELVKEPGCGCCMTCALAEGQSCGVYTERCAQGLRCLPRQDEEKPLHALLHGRGVCLNEKSYREQVKIERDSREHEEPTTSEMAEETYSPKIFRPKHTRISELKAEAVKKDRRKKLTQSKFVGGAENTAHPRIISAPEMRQESEQGPCRRHMEASLQELKASPRMVPRAVYLPNCDRKGFYKRKQCKPSRGRKRGICWCVDKYGMKLPGMEYVDGDFQCHTFDSSNVE DIP protein P24593 original sequence version: 117 0A7AD37C6EEA3A81 igf1_human Insulin-like growth factor I IGF1 IBP1 Somatomedin-C Mechano growth factor protein protein human Homo sapiens Human MGKISSLPTQLFKCCFCDFLKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKYQPPSTNKNTKSQRRKGWPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK DIP protein P05019 original sequence version: 130 DIP protein P05019 original sequence version: 178 DIP protein P05019 original sequence version: 140 DIP protein P05019 original sequence version: 186 DIP protein P05019 original sequence version: 151 The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity Defects in IGF1 are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) [MIM:608747]. IGF1 deficiency is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation mint E88A8CFBD1CD1873 ibp4_human Insulin-like growth factor-binding protein 4 IGFBP4 IBP4 protein protein human Homo sapiens Human MLPLCLVAALLLAAGPGPSLGDEAIHCPPCSEEKLARCRPPVGCEELVREPGCGCCATCALGLGMPCGVYTPRCGSGLRCYPPRGVEKPLHTLMHGQGVCMELAEIEAIQESLQPSDKDEGDHPNNSFSPCSAHDRRCLQKHFAKIRDRSTSGGKMKVNGAPREDARPVPQGSCQSELHRALERLAASQSRTHEDLYIIPIPNCDRNGNFHPKQCHPALDGQRGKCWCVDRKTGVKLPGGLEPKGELDCHQLADSFRE DIP protein P22692 original sequence version: 113 DIP protein P22692-1 original sequence version: 153 DIP protein P22692 original sequence version: 145 5E8F4638D99F0A94 igf1-igfbp4-1 3 7 unspecified role unspecified role unspecified role unspecified role Mature protein Region 49-118 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role N-terminal Domain Region 24-103 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain The range was changed because the region in the paper corresponded to the N-terminal of the mature protein, ecolx Escherichia coli direct interaction direct interaction igf1-igfbp4-2 4 7 unspecified role unspecified role unspecified role unspecified role Mature protein Region 49-118 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role N-terminal Domain Region 24-103 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain The range was changed because the region in the paper corresponded to the N-terminal of the mature protein, C-terminal domain Region 172-253 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain The range was changed because the region in the paper corresponded to the C-terminal of the mature protein, ecolx Escherichia coli direct interaction direct interaction igf1-igfbp4-3 1 7 unspecified role unspecified role unspecified role unspecified role Mature protein Region 49-118 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role N-terminal Domain Region 24-103 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain The range was changed because the region in the paper corresponded to the N-terminal of the mature protein, ecolx Escherichia coli direct interaction direct interaction igf1-igfbp5-1 2 7 unspecified role unspecified role unspecified role unspecified role Mature protein Region 49-118 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role N-terminal Domain Region 60-103 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain The range was changed because the region in the paper corresponded to the N-terminal of the mature protein, P24593:p.Leu94Met L94M mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L M This feature has been corrected as a result of our quality control procedures. The original label was 'L94M'. Wed May 02 15:33:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu94met' Tue Jun 30 15:39:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu94Met' ecolx Escherichia coli direct interaction direct interaction igf1-igfbp4-4 5 7 unspecified role unspecified role unspecified role unspecified role Mature protein Region 49-118 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role N-terminal Domain Region 24-103 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain The range was changed because the region in the paper corresponded to the N-terminal of the mature protein, ecolx Escherichia coli direct interaction direct interaction