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TRIADs: A new class of proteins with a novel cysteine‐rich signature
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| Zeitschriftentitel: | Protein Science |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Protein Science, 8, 1999, 7, S. 1557-1561 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Van Der Reijden, Bert A. Erpelinck‐Verschueren, Claudia A.J. BOB LÖWENBERG Jansen, Joop H. Van Der Reijden, Bert A. Erpelinck‐Verschueren, Claudia A.J. BOB LÖWENBERG Jansen, Joop H. |
|---|---|
| author |
Van Der Reijden, Bert A. Erpelinck‐Verschueren, Claudia A.J. BOB LÖWENBERG Jansen, Joop H. |
| spellingShingle |
Van Der Reijden, Bert A. Erpelinck‐Verschueren, Claudia A.J. BOB LÖWENBERG Jansen, Joop H. Protein Science TRIADs: A new class of proteins with a novel cysteine‐rich signature Molecular Biology Biochemistry |
| author_sort |
van der reijden, bert a. |
| spelling |
Van Der Reijden, Bert A. Erpelinck‐Verschueren, Claudia A.J. BOB LÖWENBERG Jansen, Joop H. 0961-8368 1469-896X Wiley Molecular Biology Biochemistry http://dx.doi.org/10.1110/ps.8.7.1557 <jats:title>Abstract</jats:title><jats:p>Triad1 was recently identified as a nuclear RING finger protein, which is up‐regulated during retinoic acid induced granulocytic differentiation of acute leukemia cells. Here we show that a cysteine‐rich domain (C6HC), present in Triad1, is conserved in at least 24 proteins encoded by various eukaryotes. The C6HC consensus pattern C‐x(4)‐C‐x(14–30)‐C‐x(1–4)‐C‐x(4)‐C‐x(2)‐C‐x(4)‐H‐x(4)‐C defines this structure as the fourth family member of the zinc‐binding RING, LIM, and LAP/PHD fingers. Strikingly, in 22 of 24 proteins the C6HC domain is flanked by two RING finger structures. We have termed the novel C6HC motif DRIL (double RING finger linked). The strong conservation of the larger tripartite TRIAD (two RING fingers and DRIL) structure indicates that the three subdomains are functionally linked and identifies a novel class of proteins.</jats:p> TRIADs: A new class of proteins with a novel cysteine‐rich signature Protein Science |
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Biologie Chemie und Pharmazie |
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Wiley, 1999 |
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Wiley, 1999 |
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Wiley |
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Protein Science |
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49 |
| title |
TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_unstemmed |
TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_full |
TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_fullStr |
TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_full_unstemmed |
TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_short |
TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_sort |
triads: a new class of proteins with a novel cysteine‐rich signature |
| topic |
Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1110/ps.8.7.1557 |
| publishDate |
1999 |
| physical |
1557-1561 |
| description |
<jats:title>Abstract</jats:title><jats:p>Triad1 was recently identified as a nuclear RING finger protein, which is up‐regulated during retinoic acid induced granulocytic differentiation of acute leukemia cells. Here we show that a cysteine‐rich domain (C6HC), present in Triad1, is conserved in at least 24 proteins encoded by various eukaryotes. The C6HC consensus pattern C‐x(4)‐C‐x(14–30)‐C‐x(1–4)‐C‐x(4)‐C‐x(2)‐C‐x(4)‐H‐x(4)‐C defines this structure as the fourth family member of the zinc‐binding RING, LIM, and LAP/PHD fingers. Strikingly, in 22 of 24 proteins the C6HC domain is flanked by two RING finger structures. We have termed the novel C6HC motif DRIL (double RING finger linked). The strong conservation of the larger tripartite TRIAD (two RING fingers and DRIL) structure indicates that the three subdomains are functionally linked and identifies a novel class of proteins.</jats:p> |
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| author | Van Der Reijden, Bert A., Erpelinck‐Verschueren, Claudia A.J., BOB LÖWENBERG, Jansen, Joop H. |
| author_facet | Van Der Reijden, Bert A., Erpelinck‐Verschueren, Claudia A.J., BOB LÖWENBERG, Jansen, Joop H., Van Der Reijden, Bert A., Erpelinck‐Verschueren, Claudia A.J., BOB LÖWENBERG, Jansen, Joop H. |
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| description | <jats:title>Abstract</jats:title><jats:p>Triad1 was recently identified as a nuclear RING finger protein, which is up‐regulated during retinoic acid induced granulocytic differentiation of acute leukemia cells. Here we show that a cysteine‐rich domain (C6HC), present in Triad1, is conserved in at least 24 proteins encoded by various eukaryotes. The C6HC consensus pattern C‐x(4)‐C‐x(14–30)‐C‐x(1–4)‐C‐x(4)‐C‐x(2)‐C‐x(4)‐H‐x(4)‐C defines this structure as the fourth family member of the zinc‐binding RING, LIM, and LAP/PHD fingers. Strikingly, in 22 of 24 proteins the C6HC domain is flanked by two RING finger structures. We have termed the novel C6HC motif DRIL (double RING finger linked). The strong conservation of the larger tripartite TRIAD (two RING fingers and DRIL) structure indicates that the three subdomains are functionally linked and identifies a novel class of proteins.</jats:p> |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMC9wcy44LjcuMTU1Nw |
| imprint | Wiley, 1999 |
| imprint_str_mv | Wiley, 1999 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| series | Protein Science |
| source_id | 49 |
| spelling | Van Der Reijden, Bert A. Erpelinck‐Verschueren, Claudia A.J. BOB LÖWENBERG Jansen, Joop H. 0961-8368 1469-896X Wiley Molecular Biology Biochemistry http://dx.doi.org/10.1110/ps.8.7.1557 <jats:title>Abstract</jats:title><jats:p>Triad1 was recently identified as a nuclear RING finger protein, which is up‐regulated during retinoic acid induced granulocytic differentiation of acute leukemia cells. Here we show that a cysteine‐rich domain (C6HC), present in Triad1, is conserved in at least 24 proteins encoded by various eukaryotes. The C6HC consensus pattern C‐x(4)‐C‐x(14–30)‐C‐x(1–4)‐C‐x(4)‐C‐x(2)‐C‐x(4)‐H‐x(4)‐C defines this structure as the fourth family member of the zinc‐binding RING, LIM, and LAP/PHD fingers. Strikingly, in 22 of 24 proteins the C6HC domain is flanked by two RING finger structures. We have termed the novel C6HC motif DRIL (double RING finger linked). The strong conservation of the larger tripartite TRIAD (two RING fingers and DRIL) structure indicates that the three subdomains are functionally linked and identifies a novel class of proteins.</jats:p> TRIADs: A new class of proteins with a novel cysteine‐rich signature Protein Science |
| spellingShingle | Van Der Reijden, Bert A., Erpelinck‐Verschueren, Claudia A.J., BOB LÖWENBERG, Jansen, Joop H., Protein Science, TRIADs: A new class of proteins with a novel cysteine‐rich signature, Molecular Biology, Biochemistry |
| title | TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_full | TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_fullStr | TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_full_unstemmed | TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_short | TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| title_sort | triads: a new class of proteins with a novel cysteine‐rich signature |
| title_unstemmed | TRIADs: A new class of proteins with a novel cysteine‐rich signature |
| topic | Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1110/ps.8.7.1557 |