IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Interactions between FATP4 and ichthyin in epidermal lipid processing may provide clues to the pathogenesis of autosomal recessive congenital ichthyosis. Interactions between FATP4 and ichthyin in epidermal lipid processing may provide clues to the pathogenesis of autosomal recessive congenital ichthyosis. J. Dermatol. Sci. (0923-1811) 2013 imex curation Li H., Vahlquist A., Törmä H. Affinomics - Interactions curated for the Affinomics consortium. Rare diseases - Interactions investigated in the context of Rare genetic disease hans.torma@medsci.uu.se 21-Jul-2014: Contacted by IntAct-Help. Only protein-protein interactions human-skin Homo sapiens skin skin pla proximity ligation assay pELISA pELISA PLA antibody detection identification by antibody antibody detection Li H., Vahlquist A., Törmä H. Affinomics - Interactions curated for the Affinomics consortium. Rare diseases - Interactions investigated in the context of Rare genetic disease Healthy skin hans.torma@medsci.uu.se Accepted 2014-JUN-25 by ORCHARD J. Dermatol. Sci. (0923-1811) 2013 Only protein-protein interactions imex curation s27a4_human Long-chain fatty acid transport protein 4 Solute carrier family 27 member 4 SLC27A4 ACSVL4 FATP4 Arachidonate--CoA ligase Long-chain-fatty-acid--CoA ligase Very long-chain acyl-CoA synthetase 4 protein protein human Homo sapiens Human MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLLKVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQARGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL 95E677DB3CEB9A14 nipa4_human Magnesium transporter NIPA4 NIPAL4 ICHN Ichthyin NIPA-like protein 4 NIPA4 Non-imprinted in Prader-Willi/Angelman syndrome region protein 4 protein protein human Homo sapiens Human MPGDSSPGTLPLWDASLSPPLGPDPGGFSRASHAGDKSRPPAPELGSPGAVRPRVGSCAPGPMELRVSNTSCENGSLLHLYCSSQEVLCQIVNDLSPEVPSNATFHSWQERIRQNYGFYIGLGLAFLSSFLIGSSVILKKKGLLRLVATGATRAVDGGFGYLKDAMWWAGFLTMAAGEVANFGAYAFAPATVVTPLGALSVLISAILSSYFLRESLNLLGKLGCVICVAGSTVMVIHAPEEEKVTTIMEMASKMKDTGFIVFAVLLLVSCLILIFVIAPRYGQRNILIYIIICSVIGAFSVAAVKGLGITIKNFFQGLPVVRHPLPYILSLILALSLSTQVNFLNRALDIFNTSLVFPIYYVFFTTVVVTSSIILFKEWYSMSAVDIAGTLSGFVTIILGVFMLHAFKDLDISCASLPHMHKNPPPSPAPEPTVIRLEDKNVLVDNIELASTSSPEEKPKVFIIHS C84D024A68609C9E ichthyin-slc27a4 1 3 unspecified role unspecified role neutral component neutral component Q0D2K0:p.Ala176Asp mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain A D Wed May 02 17:43:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala176asp' Tue Jun 30 18:42:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala176Asp' 2 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain proximity proximity close-contact colocalization neighbourhood interaction 3/4, Supp Fig 3 FATP4 and ichthyin colocalize in the stratum granulosum in healthy skin. Colocalisation was decreased in patients with NIPAL4, SLC27A4, and TGM1 mutations but unchanged in patients with ALOX12B and ALOXE3 mutations.