The PWWP domain: a potential protein–protein interaction domain in nuclear proteins influencing differentiation?
Upon characterization of WHSC1, a gene mapping to the Wolf–Hirschhorn syndrome critical region and at its C-terminus similar to the Drosophila ASH1/trithorax group proteins, we identified a novel protein domain designated PWWP domain. To gain insight into its structure, evolutionary conservation and...
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| Veröffentlicht in: | FEBS Letters 2000-05, Vol.473 (1), p.1-5 |
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| creator | Stec, Ingrid Nagl, Sylvia B. van Ommen, Gert-Jan B. den Dunnen, Johan T. |
| description | Upon characterization of
WHSC1, a gene mapping to the Wolf–Hirschhorn syndrome critical region and at its C-terminus similar to the
Drosophila ASH1/trithorax group proteins, we identified a novel protein domain designated PWWP domain. To gain insight into its structure, evolutionary conservation and its potential functional role, we performed database searches to identify other PWWP domain-containing proteins. We retrieved 39 proteins, and a multiple alignment shows that the domain spans some 70 amino acids. It is present in proteins of nuclear origin and plays a role in cell growth and differentiation. Due to its position, the composition of amino acids close to the PWWP motif and the pattern of other domains present, we hypothesize that the domain is involved in protein–protein interactions. |
| doi_str_mv | 10.1016/S0014-5793(00)01449-6 |
| format | Article |
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WHSC1, a gene mapping to the Wolf–Hirschhorn syndrome critical region and at its C-terminus similar to the
Drosophila ASH1/trithorax group proteins, we identified a novel protein domain designated PWWP domain. To gain insight into its structure, evolutionary conservation and its potential functional role, we performed database searches to identify other PWWP domain-containing proteins. We retrieved 39 proteins, and a multiple alignment shows that the domain spans some 70 amino acids. It is present in proteins of nuclear origin and plays a role in cell growth and differentiation. Due to its position, the composition of amino acids close to the PWWP motif and the pattern of other domains present, we hypothesize that the domain is involved in protein–protein interactions.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(00)01449-6</identifier><identifier>PMID: 10802047</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Differentiation ; Computational Biology ; Databases, Factual ; Evolution, Molecular ; Humans ; Molecular Sequence Data ; Multiple alignment ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Protein Binding ; Protein domain ; Protein Structure, Tertiary ; Protein–protein interaction</subject><ispartof>FEBS Letters, 2000-05, Vol.473 (1), p.1-5</ispartof><rights>2000 Federation of European Biochemical Societies</rights><rights>FEBS Letters 473 (2000) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4926-a4aaf2eeab51d6c22f4f678aaac2c9abc4a4ce1a343a72b3363c2f0fa937065d3</citedby><cites>FETCH-LOGICAL-c4926-a4aaf2eeab51d6c22f4f678aaac2c9abc4a4ce1a343a72b3363c2f0fa937065d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2800%2901449-6$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(00)01449-6$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>313,314,780,784,792,1417,1433,3549,27921,27923,27924,45573,45574,45994,46408,46832</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10802047$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stec, Ingrid</creatorcontrib><creatorcontrib>Nagl, Sylvia B.</creatorcontrib><creatorcontrib>van Ommen, Gert-Jan B.</creatorcontrib><creatorcontrib>den Dunnen, Johan T.</creatorcontrib><title>The PWWP domain: a potential protein–protein interaction domain in nuclear proteins influencing differentiation?</title><title>FEBS Letters</title><addtitle>FEBS Lett</addtitle><description>Upon characterization of
WHSC1, a gene mapping to the Wolf–Hirschhorn syndrome critical region and at its C-terminus similar to the
Drosophila ASH1/trithorax group proteins, we identified a novel protein domain designated PWWP domain. To gain insight into its structure, evolutionary conservation and its potential functional role, we performed database searches to identify other PWWP domain-containing proteins. We retrieved 39 proteins, and a multiple alignment shows that the domain spans some 70 amino acids. It is present in proteins of nuclear origin and plays a role in cell growth and differentiation. 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WHSC1, a gene mapping to the Wolf–Hirschhorn syndrome critical region and at its C-terminus similar to the
Drosophila ASH1/trithorax group proteins, we identified a novel protein domain designated PWWP domain. To gain insight into its structure, evolutionary conservation and its potential functional role, we performed database searches to identify other PWWP domain-containing proteins. We retrieved 39 proteins, and a multiple alignment shows that the domain spans some 70 amino acids. It is present in proteins of nuclear origin and plays a role in cell growth and differentiation. Due to its position, the composition of amino acids close to the PWWP motif and the pattern of other domains present, we hypothesize that the domain is involved in protein–protein interactions.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10802047</pmid><doi>10.1016/S0014-5793(00)01449-6</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Motifs Amino Acid Sequence Animals Cell Differentiation Computational Biology Databases, Factual Evolution, Molecular Humans Molecular Sequence Data Multiple alignment Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Protein Binding Protein domain Protein Structure, Tertiary Protein–protein interaction |
| title | The PWWP domain: a potential protein–protein interaction domain in nuclear proteins influencing differentiation? |
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