DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways
RBBP6 is a 250 kDa splicing-associated protein that has been identified as an E3 ligase due to the presence of a RING finger domain. In humans and mice it interacts with both p53 and Rb, and plays a role in the induction of apoptosis and regulation of the cell cycle. RBBP6 has recently been shown to...
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description | RBBP6 is a 250 kDa splicing-associated protein that has been identified as an E3 ligase due to the presence of a RING finger domain. In humans and mice it interacts with both p53 and Rb, and plays a role in the induction of apoptosis and regulation of the cell cycle. RBBP6 has recently been shown to be highly up-regulated in oesophageal cancer, and to be a promising target for immunotherapy against the disease.
We show here using heteronuclear NMR that the N-terminal 81 amino acids of RBBP6 constitute a novel ubiquitin-like domain, which we have called the DWNN domain. The domain lacks conserved equivalents of K48 and K63, although the equivalents of K6 and K29 are highly, although not absolutely, conserved. The di-glycine motif that is characteristic of proteins involved in ubiquitination is found in the human and mouse form of the domain, although it is not present in all organisms. It forms part of a three-domain form of RBBP6 containing the DWNN domain, a zinc knuckle and a RING finger domain, which is found in all eukaryotic genomes so far examined, in the majority of cases at single copy number. The domain is also independently expressed in vertebrates as a single domain protein.
DWNN is a novel ubiquitin-like domain found only at the N-terminus of the RBBP6 family of splicing-associated proteins. The ubiquitin-like structure of the domain greatly increases the likelihood that RBBP6 functions through some form of ubiquitin-like modification. Furthermore, the fact that the DWNN domain is independently expressed in higher vertebrates leads us to propose that the domain may itself function as a novel ubiquitin-like modifier of other proteins. |
doi_str_mv | 10.1186/1472-6807-6-1 |
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We show here using heteronuclear NMR that the N-terminal 81 amino acids of RBBP6 constitute a novel ubiquitin-like domain, which we have called the DWNN domain. The domain lacks conserved equivalents of K48 and K63, although the equivalents of K6 and K29 are highly, although not absolutely, conserved. The di-glycine motif that is characteristic of proteins involved in ubiquitination is found in the human and mouse form of the domain, although it is not present in all organisms. It forms part of a three-domain form of RBBP6 containing the DWNN domain, a zinc knuckle and a RING finger domain, which is found in all eukaryotic genomes so far examined, in the majority of cases at single copy number. The domain is also independently expressed in vertebrates as a single domain protein.
DWNN is a novel ubiquitin-like domain found only at the N-terminus of the RBBP6 family of splicing-associated proteins. The ubiquitin-like structure of the domain greatly increases the likelihood that RBBP6 functions through some form of ubiquitin-like modification. Furthermore, the fact that the DWNN domain is independently expressed in higher vertebrates leads us to propose that the domain may itself function as a novel ubiquitin-like modifier of other proteins.</description><identifier>ISSN: 1472-6807</identifier><identifier>EISSN: 1472-6807</identifier><identifier>DOI: 10.1186/1472-6807-6-1</identifier><identifier>PMID: 16396680</identifier><language>eng</language><publisher>England: BioMed Central Ltd</publisher><subject>Alternative Splicing ; Amino Acid Sequence ; Carrier Proteins - chemistry ; Carrier Proteins - physiology ; Computational Biology ; DNA - chemistry ; DNA, Complementary - metabolism ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - physiology ; Esophageal Neoplasms - metabolism ; Humans ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Models, Statistical ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Protein Isoforms ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Messenger - metabolism ; Sequence Homology, Amino Acid ; Ubiquitin - chemistry ; Up-Regulation ; Zinc Fingers</subject><ispartof>BMC structural biology, 2006-01, Vol.6 (1), p.1-1, Article 1</ispartof><rights>Copyright © 2006 Pugh et al; licensee BioMed Central Ltd. 2006 Pugh et al; licensee BioMed Central Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b572t-5794246fdc8cd53423b8095dadec1ffaba7be4c79f5f18abdbdc69d3976b15a3</citedby><cites>FETCH-LOGICAL-b572t-5794246fdc8cd53423b8095dadec1ffaba7be4c79f5f18abdbdc69d3976b15a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1360078/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1360078/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,886,24806,27929,27930,53796,53798,75743,75744</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16396680$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pugh, David J R</creatorcontrib><creatorcontrib>Ab, Eiso</creatorcontrib><creatorcontrib>Faro, Andrew</creatorcontrib><creatorcontrib>Lutya, Portia T</creatorcontrib><creatorcontrib>Hoffmann, Eberhard</creatorcontrib><creatorcontrib>Rees, D Jasper G</creatorcontrib><title>DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways</title><title>BMC structural biology</title><addtitle>BMC Struct Biol</addtitle><description>RBBP6 is a 250 kDa splicing-associated protein that has been identified as an E3 ligase due to the presence of a RING finger domain. In humans and mice it interacts with both p53 and Rb, and plays a role in the induction of apoptosis and regulation of the cell cycle. RBBP6 has recently been shown to be highly up-regulated in oesophageal cancer, and to be a promising target for immunotherapy against the disease.
We show here using heteronuclear NMR that the N-terminal 81 amino acids of RBBP6 constitute a novel ubiquitin-like domain, which we have called the DWNN domain. The domain lacks conserved equivalents of K48 and K63, although the equivalents of K6 and K29 are highly, although not absolutely, conserved. The di-glycine motif that is characteristic of proteins involved in ubiquitination is found in the human and mouse form of the domain, although it is not present in all organisms. It forms part of a three-domain form of RBBP6 containing the DWNN domain, a zinc knuckle and a RING finger domain, which is found in all eukaryotic genomes so far examined, in the majority of cases at single copy number. The domain is also independently expressed in vertebrates as a single domain protein.
DWNN is a novel ubiquitin-like domain found only at the N-terminus of the RBBP6 family of splicing-associated proteins. The ubiquitin-like structure of the domain greatly increases the likelihood that RBBP6 functions through some form of ubiquitin-like modification. Furthermore, the fact that the DWNN domain is independently expressed in higher vertebrates leads us to propose that the domain may itself function as a novel ubiquitin-like modifier of other proteins.</description><subject>Alternative Splicing</subject><subject>Amino Acid Sequence</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - physiology</subject><subject>Computational Biology</subject><subject>DNA - chemistry</subject><subject>DNA, Complementary - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - physiology</subject><subject>Esophageal Neoplasms - metabolism</subject><subject>Humans</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Models, Statistical</subject><subject>Molecular Sequence Data</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Isoforms</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Ubiquitin - chemistry</subject><subject>Up-Regulation</subject><subject>Zinc Fingers</subject><issn>1472-6807</issn><issn>1472-6807</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkttLwzAYxYMoXqaPvkqefLLatM2lL-K8CzJFBj6G3DqjbVKbVtl_78bG3BTxKQnnfD8O5wsA-yg-RoiRE5TRJCIsphGJ0BrYXrzXl-5bYCeE1zhGlOFsE2whkuZkImwDffk8GBxBAZ3_MCXspH3vbGtdVNo3A7WvhHVH0FZ1aZVoTYBP5-ePBFoHq6dBH9aNVyYE60ZQOP1zvBbty6cYh12wUYgymL352QPD66vhxW10_3Bzd9G_jySmSRthmmdJRgqtmNI4zZJUsjjHWmijUFEIKag0maJ5gQvEhNRSK5LrNKdEIizSHjidYetOVkYr49pGlLxubCWaMffC8lXF2Rc-8h8cpSSOKZsAzmYAaf0fgFVF-YpPS-bTkjmZgHrgcJ6h8e-dCS2vbFCmLIUzvgucUJKQjOF_jQlCKcNoSoxmRtX4EBpTLPKgmE-_wK8EB8stfLvnO0-_AMcVrsI</recordid><startdate>20060105</startdate><enddate>20060105</enddate><creator>Pugh, David J R</creator><creator>Ab, Eiso</creator><creator>Faro, Andrew</creator><creator>Lutya, Portia T</creator><creator>Hoffmann, Eberhard</creator><creator>Rees, D Jasper G</creator><general>BioMed Central Ltd</general><general>BioMed Central</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20060105</creationdate><title>DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways</title><author>Pugh, David J R ; Ab, Eiso ; Faro, Andrew ; Lutya, Portia T ; Hoffmann, Eberhard ; Rees, D Jasper G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b572t-5794246fdc8cd53423b8095dadec1ffaba7be4c79f5f18abdbdc69d3976b15a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Alternative Splicing</topic><topic>Amino Acid Sequence</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - physiology</topic><topic>Computational Biology</topic><topic>DNA - chemistry</topic><topic>DNA, Complementary - metabolism</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - physiology</topic><topic>Esophageal Neoplasms - metabolism</topic><topic>Humans</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Models, Statistical</topic><topic>Molecular Sequence Data</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Isoforms</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Ubiquitin - chemistry</topic><topic>Up-Regulation</topic><topic>Zinc Fingers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pugh, David J R</creatorcontrib><creatorcontrib>Ab, Eiso</creatorcontrib><creatorcontrib>Faro, Andrew</creatorcontrib><creatorcontrib>Lutya, Portia T</creatorcontrib><creatorcontrib>Hoffmann, Eberhard</creatorcontrib><creatorcontrib>Rees, D Jasper G</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>BMC structural biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pugh, David J R</au><au>Ab, Eiso</au><au>Faro, Andrew</au><au>Lutya, Portia T</au><au>Hoffmann, Eberhard</au><au>Rees, D Jasper G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways</atitle><jtitle>BMC structural biology</jtitle><addtitle>BMC Struct Biol</addtitle><date>2006-01-05</date><risdate>2006</risdate><volume>6</volume><issue>1</issue><spage>1</spage><epage>1</epage><pages>1-1</pages><artnum>1</artnum><issn>1472-6807</issn><eissn>1472-6807</eissn><abstract>RBBP6 is a 250 kDa splicing-associated protein that has been identified as an E3 ligase due to the presence of a RING finger domain. In humans and mice it interacts with both p53 and Rb, and plays a role in the induction of apoptosis and regulation of the cell cycle. RBBP6 has recently been shown to be highly up-regulated in oesophageal cancer, and to be a promising target for immunotherapy against the disease.
We show here using heteronuclear NMR that the N-terminal 81 amino acids of RBBP6 constitute a novel ubiquitin-like domain, which we have called the DWNN domain. The domain lacks conserved equivalents of K48 and K63, although the equivalents of K6 and K29 are highly, although not absolutely, conserved. The di-glycine motif that is characteristic of proteins involved in ubiquitination is found in the human and mouse form of the domain, although it is not present in all organisms. It forms part of a three-domain form of RBBP6 containing the DWNN domain, a zinc knuckle and a RING finger domain, which is found in all eukaryotic genomes so far examined, in the majority of cases at single copy number. The domain is also independently expressed in vertebrates as a single domain protein.
DWNN is a novel ubiquitin-like domain found only at the N-terminus of the RBBP6 family of splicing-associated proteins. The ubiquitin-like structure of the domain greatly increases the likelihood that RBBP6 functions through some form of ubiquitin-like modification. Furthermore, the fact that the DWNN domain is independently expressed in higher vertebrates leads us to propose that the domain may itself function as a novel ubiquitin-like modifier of other proteins.</abstract><cop>England</cop><pub>BioMed Central Ltd</pub><pmid>16396680</pmid><doi>10.1186/1472-6807-6-1</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Alternative Splicing Amino Acid Sequence Carrier Proteins - chemistry Carrier Proteins - physiology Computational Biology DNA - chemistry DNA, Complementary - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - physiology Esophageal Neoplasms - metabolism Humans Magnetic Resonance Spectroscopy Models, Molecular Models, Statistical Molecular Sequence Data Protein Binding Protein Conformation Protein Isoforms Protein Structure, Secondary Protein Structure, Tertiary RNA, Messenger - metabolism Sequence Homology, Amino Acid Ubiquitin - chemistry Up-Regulation Zinc Fingers |
title | DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways |
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