Ubiquitin-interacting motif (original) (raw)

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In molecular biology, the Ubiquitin-Interacting Motif (UIM), or 'LALAL-motif', is a sequence motif of about 20 amino acid residues, which was first described in the 26S proteasome subunit PSD4/RPN-10 that is known to recognise ubiquitin. In addition, the UIM is found, often in tandem or triplet arrays, in a variety of proteins either involved in ubiquitination and ubiquitin metabolism, or known to interact with ubiquitin-like modifiers. Among the UIM proteins are two different subgroups of the UBP (ubiquitin carboxy-terminal hydrolase) family of deubiquitinating enzymes, one F-box protein, one family of HECT-containing ubiquitin-ligases (E3s) from plants, and several proteins containing ubiquitin-associated UBA and/or UBX domains. In most of these proteins, the UIM occurs in multiple copie

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dbo:abstract In molecular biology, the Ubiquitin-Interacting Motif (UIM), or 'LALAL-motif', is a sequence motif of about 20 amino acid residues, which was first described in the 26S proteasome subunit PSD4/RPN-10 that is known to recognise ubiquitin. In addition, the UIM is found, often in tandem or triplet arrays, in a variety of proteins either involved in ubiquitination and ubiquitin metabolism, or known to interact with ubiquitin-like modifiers. Among the UIM proteins are two different subgroups of the UBP (ubiquitin carboxy-terminal hydrolase) family of deubiquitinating enzymes, one F-box protein, one family of HECT-containing ubiquitin-ligases (E3s) from plants, and several proteins containing ubiquitin-associated UBA and/or UBX domains. In most of these proteins, the UIM occurs in multiple copies and in association with other domains such as UBA (INTERPRO), UBX (INTERPRO), ENTH domain, EH (INTERPRO), VHS (INTERPRO), SH3 domain, HECT, VWFA (INTERPRO), EF-hand calcium-binding, WD-40, F-box (INTERPRO), LIM, protein kinase, ankyrin, PX, phosphatidylinositol 3- and 4-kinase (INTERPRO), C2 domain, OTU (INTERPRO), DnaJ domain (INTERPRO), RING-finger (INTERPRO) or FYVE-finger (INTERPRO). UIMs have been shown to bind ubiquitin and to serve as a specific targeting signal important for monoubiquitination. Thus, UIMs may have several functions in ubiquitin metabolism each of which may require different numbers of UIMs. The UIM is unlikely to form an independent protein domain. Instead, based on the spacing of the conserved residues, the motif probably forms a short alpha-helix that can be embedded into different protein folds. Some proteins known to contain an UIM are listed below: * Eukaryotic PSD4/RPN-10/S5, a multi-ubiquitin binding subunit of the 26S proteasome. * Vertebrate Machado-Joseph disease protein 1 (Ataxin-3), which acts as a histone-binding protein that regulates transcription; defects in Ataxin-3 cause the neurodegenerative disorder Machado-Joseph disease (MJD). * Vertebrate epsin and epsin2. * Vertebrate hepatocyte growth factor-regulated tyrosine kinase substrate (HRS). * Mammalian epidermal growth factor receptor substrate 15 (EPS15), which is involved in cell growth regulation. * Mammalian epidermal growth factor receptor substrate EPS15R. * Drosophila melanogaster (Fruit fly) liquid facets (lqf), an epsin. * Yeast VPS27 vacuolar sorting protein, which is required for membrane traffic to the vacuole. (en)
dbo:symbol UIM
dbo:thumbnail wiki-commons:Special:FilePath/PDB_1yx5_EBI.jpg?width=300
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dbo:wikiPageWikiLink dbr:Proteasome dbr:Protein-protein_interaction dbr:Proteins dbr:Epidermal_growth_factor dbr:Epidermal_growth_factor_receptor dbr:Ankyrin dbr:Ubiquitin-like_protein dbr:Vertebrate dbr:ENTH_domain dbr:Saccharomyces_cerevisiae dbr:Conserved_sequence dbr:Protein_domains dbr:Mammalia dbr:Mammalian dbr:Substrate_(biochemistry) dbr:Protein_kinase dbr:C2_domain dbr:Transcriptional_regulation dbr:WD40_repeat dbr:HECT_domain dbr:Amino_acid dbc:Protein_structural_motifs dbr:Drosophila dbr:Eukaryotic dbr:Cell_growth dbr:Cell_membrane dbr:Binding_(molecular) dbr:Disease dbr:Protein_domain dbr:Protein dbr:Receptor_(biochemistry) dbr:Regulation dbr:LIM_domain dbr:Hepatocyte dbr:Tertiary_structure dbr:Phosphatidylinositol dbr:Metabolism dbr:Sequence_motif dbr:Molecular_binding dbr:Tyrosine_kinase dbr:PX_domain dbr:SH3_domain dbr:Enzyme_substrate dbr:Ubiquitination dbr:Alpha-helix
dbp:caption solution structure of s5a uim-1/ubiquitin complex (en)
dbp:interpro IPR003903 (en)
dbp:name UIM (en)
dbp:pfam PF02809 (en)
dbp:scop 777600.0 (dbd:second)
dbp:symbol UIM (en)
dbp:wikiPageUsesTemplate dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist
dct:subject dbc:Protein_structural_motifs
gold:hypernym dbr:Motif
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rdfs:comment In molecular biology, the Ubiquitin-Interacting Motif (UIM), or 'LALAL-motif', is a sequence motif of about 20 amino acid residues, which was first described in the 26S proteasome subunit PSD4/RPN-10 that is known to recognise ubiquitin. In addition, the UIM is found, often in tandem or triplet arrays, in a variety of proteins either involved in ubiquitination and ubiquitin metabolism, or known to interact with ubiquitin-like modifiers. Among the UIM proteins are two different subgroups of the UBP (ubiquitin carboxy-terminal hydrolase) family of deubiquitinating enzymes, one F-box protein, one family of HECT-containing ubiquitin-ligases (E3s) from plants, and several proteins containing ubiquitin-associated UBA and/or UBX domains. In most of these proteins, the UIM occurs in multiple copie (en)
rdfs:label Ubiquitin-interacting motif (en)
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