DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ anantharajan-2013-1 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. DIP original experiment: DIP-255883X Structure (London, England : 1993) 2013 IMEx The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase. Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. Only protein-protein interactions imex curation anantharajan-2013-2 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. DIP original experiment: DIP-255886X Structure (London, England : 1993) 2013 IMEx The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase. Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. Only protein-protein interactions imex curation anantharajan-2013-3 ecolx Escherichia coli sls static light scattering sls predetermined predetermined participant predetermined Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. DIP original experiment: DIP-255887X Structure (London, England : 1993) 2013 IMEx The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase. Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. Only protein-protein interactions imex curation anantharajan-2013-4 ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. DIP original experiment: DIP-255884X Structure (London, England : 1993) 2013 IMEx The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase. Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. Only protein-protein interactions imex curation anantharajan-2013-5 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. DIP original experiment: DIP-255885X Structure (London, England : 1993) 2013 IMEx The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase. Anantharajan J., Koski MK., Kursula P., Hieta R., Bergmann U., Myllyharju J., Wierenga RK. Only protein-protein interactions imex curation p4ha1_human Prolyl 4-hydroxylase subunit alpha-1 P4HA1 P4HA Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1 protein protein human Homo sapiens Human MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE p4ha1-1 3259939 N/A 3259944 unspecified role unspecified role unspecified role unspecified role Region 1-238 Region 1-238 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false p4ha1-2 3259940 N/A 3259944 unspecified role unspecified role unspecified role unspecified role Region 1-244 Region 1-244 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false p4ha1-3 3259941 N/A 3259944 unspecified role unspecified role unspecified role unspecified role Region 1-238 Region 1-238 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false p4ha1-4 3259942 N/A 3259944 unspecified role unspecified role unspecified role unspecified role Region 1-238 Region 1-238 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false p4ha1-5 3259943 N/A 3259944 unspecified role unspecified role unspecified role unspecified role Region 1-238 Region 1-238 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false