| http://purl.uniprot.org/citations/21912646 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21912646 | http://www.w3.org/2000/01/rdf-schema#comment | "Using a complete set of RING domains from Drosophila melanogaster, all the solved RING domains and cocrystal structures of RING-containing ubiquitin-ligases (RING-E3) and ubiquitin-conjugating enzyme (E2) pairs, we analyzed RING domains structures from their primary to quarternary structures. The results showed that: i) putative orthologs of RING domains between Drosophila melanogaster and the human largely occur (118/139, 84.9%); ii) of the 118 orthologous pairs from Drosophila melanogaster and the human, 117 pairs (117/118, 99.2%) were found to retain entirely uniform domain architectures, only Iap2/Diap2 experienced evolutionary expansion of domain architecture; iii) 4 evolutionary structurally conserved regions (SCRs) are responsible for homologous folding of RING domains at the superfamily level; iv) besides the conserved Cys/His chelating zinc ions, 6 equivalent residues (4 hydrophobic and 2 polar residues) in the SCRs possess good-consensus and conservation-these 4 SCRs function in the structural positioning of 6 equivalent residues as determinants for RING-E3 catalysis; v) members of these RING proteins located nucleus, multiple subcellular compartments, membrane protein and mitochondrion are respectively 42 (42/139, 30.2%), 71 (71/139, 51.1%), 22 (22/139, 15.8%) and 4 (4/139, 2.9%); vi) CG15104 (Topors) and CG1134 (Mul1) in C3HC4, and CG3929 (Deltex) in C3H2C3 seem to display broader E2s binding profiles than other RING-E3s; vii) analyzing intermolecular interfaces of E2/RING-E3 complexes indicate that residues directly interacting with E2s are all from the SCRs in RING domains. Of the 6 residues, 2 hydrophobic ones contribute to constructing the conserved hydrophobic core, while the 2 hydrophobic and 2 polar residues directly participate in E2/RING-E3 interactions. Based on sequence and structural data, SCRs, conserved equivalent residues and features of intermolecular interfaces were extracted, highlighting the presence of a nucleus for RING domain fold and formation of catalytic core in which related residues and regions exhibit preferential evolutionary conservation."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0023863"xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/author | "Huang X."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/author | "Huang C."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/author | "Wu Y."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/author | "Zhao H."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/author | "Wan F."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/author | "Ying M."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/author | "Jie K."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/pages | "e23863"xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/title | "Comprehensively surveying structure and function of RING domains from Drosophila melanogaster."xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://purl.uniprot.org/core/volume | "6"xsd:string |
| http://purl.uniprot.org/citations/21912646 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21912646 |
| http://purl.uniprot.org/citations/21912646 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21912646 |
| http://purl.uniprot.org/uniprot/O76924#attribution-941DAD2E7E42A57496767B599801BC1B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21912646 |
| http://purl.uniprot.org/uniprot/Q94981#attribution-941DAD2E7E42A57496767B599801BC1B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21912646 |
| http://purl.uniprot.org/uniprot/Q9VRP9#attribution-941DAD2E7E42A57496767B599801BC1B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21912646 |
| http://purl.uniprot.org/uniprot/O97159#attribution-941DAD2E7E42A57496767B599801BC1B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21912646 |
| http://purl.uniprot.org/uniprot/Q24307#attribution-941DAD2E7E42A57496767B599801BC1B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21912646 |
| http://purl.uniprot.org/uniprot/Q24306#attribution-941DAD2E7E42A57496767B599801BC1B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21912646 |
| http://purl.uniprot.org/uniprot/Q23985#attribution-941DAD2E7E42A57496767B599801BC1B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21912646 |
| http://purl.uniprot.org/uniprot/M9PBE2#attribution-941DAD2E7E42A57496767B599801BC1B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21912646 |