The tripartite motif family identifies cell compartments
A functional genomic approach, based on systematic data gathering, was used to characterize a family of proteins containing a tri partite m otif (TRIM). A total of 37 TRIM genes/proteins were studied, 21 of which were novel. The results demonstrate that TRIM proteins share a common function: by mean...
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| Veröffentlicht in: | The EMBO journal 2001-05, Vol.20 (9), p.2140-2151 |
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| container_title | The EMBO journal |
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| creator | Reymond, Alexandre Meroni, Germana Fantozzi, Anna Merla, Giuseppe Cairo, Stefano Luzi, Lucilla Riganelli, Daniela Zanaria, Elena Messali, Silvia Cainarca, Silvia Guffanti, Alessandro Minucci, Saverio Pelicci, Pier Giuseppe Ballabio, Andrea |
| description | A functional genomic approach, based on systematic data gathering, was used to characterize a family of proteins containing a
tri
partite
m
otif (TRIM). A total of 37 TRIM genes/proteins were studied, 21 of which were novel. The results demonstrate that TRIM proteins share a common function: by means of homo‐multimerization they identify specific cell compartments. |
| doi_str_mv | 10.1093/emboj/20.9.2140 |
| format | Article |
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tri
partite
m
otif (TRIM). A total of 37 TRIM genes/proteins were studied, 21 of which were novel. The results demonstrate that TRIM proteins share a common function: by means of homo‐multimerization they identify specific cell compartments.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/20.9.2140</identifier><identifier>PMID: 11331580</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Motifs - physiology ; Animals ; Blotting, Northern ; Carrier Proteins ; cell compartmentalization ; Cell Compartmentation - physiology ; Cell Line ; Chromosome Mapping ; Cloning, Molecular ; Databases, Factual ; Embryo, Mammalian ; functional genomics ; Humans ; In Situ Hybridization ; Mice ; Molecular Sequence Data ; Multigene Family - genetics ; Mutagenesis, Site-Directed ; Nerve Tissue Proteins ; nuclear bodies ; Organ Specificity ; Protein Binding - physiology ; Protein Structure, Tertiary - physiology ; Proteins - physiology ; RBCC ; Sequence Homology, Amino Acid ; Subcellular Fractions - metabolism ; tripartite motif ; Two-Hybrid System Techniques ; Ubiquitin-Protein Ligases</subject><ispartof>The EMBO journal, 2001-05, Vol.20 (9), p.2140-2151</ispartof><rights>European Molecular Biology Organization 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) May 01, 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6114-c30c7a08e8e855a8230788ae3bbfcfe0931c26480623f8831bcda2759c1637553</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125245/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125245/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11331580$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reymond, Alexandre</creatorcontrib><creatorcontrib>Meroni, Germana</creatorcontrib><creatorcontrib>Fantozzi, Anna</creatorcontrib><creatorcontrib>Merla, Giuseppe</creatorcontrib><creatorcontrib>Cairo, Stefano</creatorcontrib><creatorcontrib>Luzi, Lucilla</creatorcontrib><creatorcontrib>Riganelli, Daniela</creatorcontrib><creatorcontrib>Zanaria, Elena</creatorcontrib><creatorcontrib>Messali, Silvia</creatorcontrib><creatorcontrib>Cainarca, Silvia</creatorcontrib><creatorcontrib>Guffanti, Alessandro</creatorcontrib><creatorcontrib>Minucci, Saverio</creatorcontrib><creatorcontrib>Pelicci, Pier Giuseppe</creatorcontrib><creatorcontrib>Ballabio, Andrea</creatorcontrib><title>The tripartite motif family identifies cell compartments</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>A functional genomic approach, based on systematic data gathering, was used to characterize a family of proteins containing a
tri
partite
m
otif (TRIM). A total of 37 TRIM genes/proteins were studied, 21 of which were novel. The results demonstrate that TRIM proteins share a common function: by means of homo‐multimerization they identify specific cell compartments.</description><subject>Amino Acid Motifs - physiology</subject><subject>Animals</subject><subject>Blotting, Northern</subject><subject>Carrier Proteins</subject><subject>cell compartmentalization</subject><subject>Cell Compartmentation - physiology</subject><subject>Cell Line</subject><subject>Chromosome Mapping</subject><subject>Cloning, Molecular</subject><subject>Databases, Factual</subject><subject>Embryo, Mammalian</subject><subject>functional genomics</subject><subject>Humans</subject><subject>In Situ Hybridization</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family - genetics</subject><subject>Mutagenesis, Site-Directed</subject><subject>Nerve Tissue Proteins</subject><subject>nuclear bodies</subject><subject>Organ Specificity</subject><subject>Protein Binding - physiology</subject><subject>Protein Structure, Tertiary - physiology</subject><subject>Proteins - physiology</subject><subject>RBCC</subject><subject>Sequence Homology, Amino Acid</subject><subject>Subcellular Fractions - metabolism</subject><subject>tripartite motif</subject><subject>Two-Hybrid System Techniques</subject><subject>Ubiquitin-Protein 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Anna</creator><creator>Merla, Giuseppe</creator><creator>Cairo, Stefano</creator><creator>Luzi, Lucilla</creator><creator>Riganelli, Daniela</creator><creator>Zanaria, Elena</creator><creator>Messali, Silvia</creator><creator>Cainarca, Silvia</creator><creator>Guffanti, Alessandro</creator><creator>Minucci, Saverio</creator><creator>Pelicci, Pier Giuseppe</creator><creator>Ballabio, Andrea</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><general>Oxford University 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tri
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m
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Motifs - physiology Animals Blotting, Northern Carrier Proteins cell compartmentalization Cell Compartmentation - physiology Cell Line Chromosome Mapping Cloning, Molecular Databases, Factual Embryo, Mammalian functional genomics Humans In Situ Hybridization Mice Molecular Sequence Data Multigene Family - genetics Mutagenesis, Site-Directed Nerve Tissue Proteins nuclear bodies Organ Specificity Protein Binding - physiology Protein Structure, Tertiary - physiology Proteins - physiology RBCC Sequence Homology, Amino Acid Subcellular Fractions - metabolism tripartite motif Two-Hybrid System Techniques Ubiquitin-Protein Ligases |
| title | The tripartite motif family identifies cell compartments |
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