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 plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions human Homo sapiens Human pull down pull down predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-131996X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-131998X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-132001X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-132000X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions human Homo sapiens Human x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-131992X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions human Homo sapiens Human molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-131994X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-131999X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions human Homo sapiens Human x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-131995X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions human Homo sapiens Human molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-131997X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-132002X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure (London, England : 1993) 2009 imex curation Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. Only protein-protein interactions human Homo sapiens Human pull down pull down predetermined predetermined participant predetermined Bowden TA., Aricescu AR., Nettleship JE., Siebold C., Rahman-Huq N., Owens RJ., Stuart DI., Jones EY. DIP original experiment: DIP-131993X Structure (London, England : 1993) 2009 IMEx Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. epha4_human Ephrin type-A receptor 4 EPHA4 EPH-like kinase 8 HEK8 SEK TYRO1 Tyrosine-protein kinase TYRO1 Tyrosine-protein kinase receptor SEK protein protein human Homo sapiens Human MAGIFYFALFSCLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERSGECQACKIGYYKALSTDATCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEWSSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTKVSITDLLAHTNYTFEIWAVNGVSKYNPNPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPLEVTTNTVPSRIIGDGANSTVLLVSVSGSVVLVVILIAAFVISRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGTESSRPNTALLDPSSPEFSAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHVNQEDLARIGITAITHQNKILSSVQAMRTQMQQMHGRMVPV DIP protein P54764 original sequence version: 106 DIP protein P54764 original sequence version: 143 0C39C1152EDDD46F efna1_human Ephrin-A1 EPH-related receptor tyrosine kinase ligand 1 Immediate early response protein B61 Tumor necrosis factor alpha-induced protein 4 EFNA1 EPLG1 LERK1 TNFAIP4 protein protein human Homo sapiens Human MEFLWAPLLGLCCSLAAADRHTVFWNSSNPKFRNEDYTIHVQLNDYVDIICPHYEDHSVADAAMEQYILYLVEHEEYQLCQPQSKDQVRWQCNRPSAKHGPEKLSEKFQRFTPFTLGKEFKEGHSYYYISKPIHQHEDRCLRLKVTVSGKITHSPQAHDNPQEKRLAADDPEVRVLHSIGHSAAPRLFPLAWTVLLLPLLLLQTP DIP protein P20827 original sequence version: 161 DIP protein P20827 original sequence version: 96 DIP protein P20827 original sequence version: 111 DIP protein P20827 original sequence version: 116 EFF026BF4C12461F efna5_human Ephrin-A5 EFNA5 EPLG7 LERK7 EPH-related receptor tyrosine kinase ligand 7 AL-1 protein protein human Homo sapiens Human MLHVEMLTLVFLVLWMCVFSQDPGSKAVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGENAAQTPRIPSRLLAILLFLLAMLLTL DIP protein P52803 original sequence version: 83 DIP protein P52803 original sequence version: 81 DIP protein P52803 original sequence version: 82 DIP protein P52803 original sequence version: 90 DIP protein P52803 original sequence version: 109 6893B1CCACFF3F57 efna4_human Ephrin-A4 EFNA4 EPLG4 LERK4 EPH-related receptor tyrosine kinase ligand 4 protein protein human Homo sapiens Human MRLLPLLRTVLWAAFLGSPLRGGSSLRHVVYWNSSNPRLLRGDAVVELGLNDYLDIVCPHYEGPGPPEGPETFALYMVDWPGYESCQAEGPRAYKRWVCSLPFGHVQFSEKIQRFTPFSLGFEFLPGETYYYISVPTPESSGQCLRLQVSVCCKERKSESAHPVGSPGESGTSGWRGGDTPSPLCLLLLLLLLILRLLRIL DIP protein P52798 original sequence version: 88 ABE8D5443A9AF28D efna2_human Ephrin-A2 EFNA2 EPLG6 LERK6 EPH-related receptor tyrosine kinase ligand 6 HEK7 ligand protein protein human Homo sapiens Human MAPAQRPLLPLLLLLLPLPPPPFARAEDAARANSDRYAVYWNRSNPRFHAGAGDDGGGYTVEVSINDYLDIYCPHYGAPLPPAERMEHYVLYMVNGEGHASCDHRQRGFKRWECNRPAAPGGPLKFSEKFQLFTPFSLGFEFRPGHEYYYISATPPNAVDRPCLRLKVYVRPTNETLYEAPEPIFTSNNSCSSPGGCRLFLSTIPVLWTLLGS DIP protein O43921 original sequence version: 73 mint 33C9FB1A8168B2D0 efnb2_human Ephrin-B2 EFNB2 EPLG5 HTKL LERK5 EPH-related receptor tyrosine kinase ligand 5 HTK ligand protein protein human Homo sapiens Human MAVRRDSVWKYCWGVLMVLCRTAISKSIVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQADRCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDNQEGGVCQTRAMKILMKVGQDASSAGSTRNKDPTRRPELEAGTNGRSSTTSPFVKPNPGSSTDGNSAGHSGNNILGSEVALFAGIASGCIIFIVIIITLVVLLLKYRRRHRKHSPQHTTTLSLSTLATPKRSGNNNGSEPSDIIIPLRTADSVFCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV DIP protein P52799 original sequence version: 78 DIP protein P52799 original sequence version: 92 mint Binds to the receptor tyrosine kinases EPHB4 and EPHA3. May play a role in constraining the orientation of longitudinally projecting axons 6D9932A632626AEA epha4-efnb2-2 1 17 unspecified role unspecified role prey prey Region 27-167 Region 27-167 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 12 unspecified role unspecified role bait bait Region 30-202 Region 30-202 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range human Homo sapiens Human physical association physical association efna2-epha4-1 2 16 unspecified role unspecified role bait bait Region 33-174 Region 33-174 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 12 unspecified role unspecified role prey prey Region 30-202 Region 30-202 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 efna2-epha4-2 5 16 unspecified role unspecified role unspecified role unspecified role Region 33-177 Region 33-177 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 12 unspecified role unspecified role unspecified role unspecified role Region 30-202 Region 30-202 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 efna2-epha4-3 6 16 unspecified role unspecified role unspecified role unspecified role Region 33-177 Region 33-177 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 12 unspecified role unspecified role unspecified role unspecified role Region 30-202 Region 30-202 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 efna5-epha4-1 10 12 unspecified role unspecified role prey prey Region 30-202 Region 30-202 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 14 unspecified role unspecified role bait bait Region 27-166 Region 27-166 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 efna1-epha4-1 4 12 unspecified role unspecified role prey prey Region 30-202 Region 30-202 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 13 unspecified role unspecified role bait bait Region 16-158 Region 16-158 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 efnb2-epha4-1 7 17 unspecified role unspecified role bait bait Region 25-168 Region 25-168 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 12 unspecified role unspecified role prey prey Region 30-202 Region 30-202 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 epha4-efna2-1 11 16 unspecified role unspecified role prey prey Region 33-177 Region 33-177 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 12 unspecified role unspecified role bait bait Region 30-202 Region 30-202 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range human Homo sapiens Human physical association physical association efnb2-epha4-2 9 17 unspecified role unspecified role unspecified role unspecified role Region 27-167 Region 27-167 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 12 unspecified role unspecified role unspecified role unspecified role Region 30-202 Region 30-202 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 efnb2-epha4-3 8 17 unspecified role unspecified role unspecified role unspecified role Region 27-167 Region 27-167 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 12 unspecified role unspecified role unspecified role unspecified role Region 30-202 Region 30-202 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 efna4-epha4-1 3 12 unspecified role unspecified role prey prey Region 30-202 Region 30-202 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 15 unspecified role unspecified role bait bait Region 23-162 Region 23-162 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