|
|
(One intermediate revision not shown.) |
Line 1: |
Line 1: |
| | | |
| ==Solution structure of RNA binding domain in RNA binding motif protein 21== | | ==Solution structure of RNA binding domain in RNA binding motif protein 21== |
- | <StructureSection load='2e5g' size='340' side='right' caption='[[2e5g]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2e5g' size='340' side='right'caption='[[2e5g]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2e5g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E5G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2e5g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5G FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TUT1, RBM21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_uridylyltransferase RNA uridylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.52 2.7.7.52] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5g OCA], [https://pdbe.org/2e5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5g RCSB], [https://www.ebi.ac.uk/pdbsum/2e5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5g ProSAT], [https://www.topsan.org/Proteins/RSGI/2e5g TOPSAN]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5g OCA], [http://pdbe.org/2e5g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2e5g RCSB], [http://www.ebi.ac.uk/pdbsum/2e5g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5g ProSAT], [http://www.topsan.org/Proteins/RSGI/2e5g TOPSAN]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/STPAP_HUMAN STPAP_HUMAN]] Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.<ref>PMID:16790842</ref> <ref>PMID:18288197</ref> <ref>PMID:21102410</ref> | + | [https://www.uniprot.org/uniprot/STPAP_HUMAN STPAP_HUMAN] Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.<ref>PMID:16790842</ref> <ref>PMID:18288197</ref> <ref>PMID:21102410</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
Line 27: |
Line 26: |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Human]] | + | [[Category: Homo sapiens]] |
- | [[Category: RNA uridylyltransferase]] | + | [[Category: Large Structures]] |
- | [[Category: Inoue, M]] | + | [[Category: Inoue M]] |
- | [[Category: Kigawa, T]] | + | [[Category: Kigawa T]] |
- | [[Category: Muto, Y]] | + | [[Category: Muto Y]] |
- | [[Category: Structural genomic]]
| + | [[Category: Shirouzu M]] |
- | [[Category: Shirouzu, M]] | + | [[Category: Terada T]] |
- | [[Category: Terada, T]] | + | [[Category: Tsuda K]] |
- | [[Category: Tsuda, K]] | + | [[Category: Yokoyama S]] |
- | [[Category: Yokoyama, S]] | + | |
- | [[Category: National project on protein structural and functional analyse]]
| + | |
- | [[Category: Nppsfa]]
| + | |
- | [[Category: Rbd]]
| + | |
- | [[Category: Rrm domain]]
| + | |
- | [[Category: Rsgi]]
| + | |
- | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
STPAP_HUMAN Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Trippe R, Guschina E, Hossbach M, Urlaub H, Luhrmann R, Benecke BJ. Identification, cloning, and functional analysis of the human U6 snRNA-specific terminal uridylyl transferase. RNA. 2006 Aug;12(8):1494-504. Epub 2006 Jun 21. PMID:16790842 doi:http://dx.doi.org/rna.87706
- ↑ Mellman DL, Gonzales ML, Song C, Barlow CA, Wang P, Kendziorski C, Anderson RA. A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs. Nature. 2008 Feb 21;451(7181):1013-7. doi: 10.1038/nature06666. PMID:18288197 doi:http://dx.doi.org/10.1038/nature06666
- ↑ Laishram RS, Anderson RA. The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA. EMBO J. 2010 Dec 15;29(24):4132-45. doi: 10.1038/emboj.2010.287. Epub 2010 Nov, 19. PMID:21102410 doi:http://dx.doi.org/10.1038/emboj.2010.287
|