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==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]]
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__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]]

Latest revision as of 21:47, 29 May 2024

Solution structure of RNA binding domain in RNA binding motif protein 21Solution structure of RNA binding domain in RNA binding motif protein 21

Structural highlights

2e5g is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
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