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1x2p

From Proteopedia

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Current revision

Solution structure of the SH3 domain of the Protein arginine N-methyltransferase 2

Structural highlights

1x2p 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

ANM2_HUMAN Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). May be involved in growth regulation.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Qi C, Chang J, Zhu Y, Yeldandi AV, Rao SM, Zhu YJ. Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. J Biol Chem. 2002 Aug 9;277(32):28624-30. Epub 2002 May 30. PMID:12039952 doi:http://dx.doi.org/10.1074/jbc.M201053200
↑ Ganesh L, Yoshimoto T, Moorthy NC, Akahata W, Boehm M, Nabel EG, Nabel GJ. Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis. Mol Cell Biol. 2006 May;26(10):3864-74. PMID:16648481 doi:http://dx.doi.org/10.1128/MCB.26.10.3864-3874.2006
↑ Meyer R, Wolf SS, Obendorf M. PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor. J Steroid Biochem Mol Biol. 2007 Oct;107(1-2):1-14. Epub 2007 May 24. PMID:17587566 doi:http://dx.doi.org/10.1016/j.jsbmb.2007.05.006
↑ Lakowski TM, Frankel A. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochem J. 2009 Jun 26;421(2):253-61. doi: 10.1042/BJ20090268. PMID:19405910 doi:10.1042/BJ20090268

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x2p"

@@ Line 1: / Line 1: @@
 ==Solution structure of the SH3 domain of the Protein arginine N-methyltransferase 2==
-<StructureSection load='1x2p' size='340' side='right'caption='[[1x2p]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1x2p' size='340' side='right'caption='[[1x2p]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1x2p]] 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=1X2P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X2P FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1x2p]] 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=1X2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X2P FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HRMT1L1 ([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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1x2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x2p OCA], [http://pdbe.org/1x2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x2p RCSB], [http://www.ebi.ac.uk/pdbsum/1x2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x2p ProSAT], [http://www.topsan.org/Proteins/RSGI/1x2p TOPSAN]</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=1x2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x2p OCA], [https://pdbe.org/1x2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x2p RCSB], [https://www.ebi.ac.uk/pdbsum/1x2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x2p ProSAT], [https://www.topsan.org/Proteins/RSGI/1x2p TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ANM2_HUMAN ANM2_HUMAN]] Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). May be involved in growth regulation.<ref>PMID:12039952</ref> <ref>PMID:16648481</ref> <ref>PMID:17587566</ref> <ref>PMID:19405910</ref>
+[https://www.uniprot.org/uniprot/ANM2_HUMAN ANM2_HUMAN] Arginine methyltransferase that methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1-dependent manner). May be involved in growth regulation.<ref>PMID:12039952</ref> <ref>PMID:16648481</ref> <ref>PMID:17587566</ref> <ref>PMID:19405910</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Chikayama, E]]
+[[Category: Chikayama E]]
-[[Category: Inoue, M]]
+[[Category: Inoue M]]
-[[Category: Kigawa, T]]
+[[Category: Kigawa T]]
-[[Category: Koshiba, S]]
+[[Category: Koshiba S]]
-[[Category: Structural genomic]]
+[[Category: Saito K]]
-[[Category: Saito, K]]
+[[Category: Yokoyama S]]
-[[Category: Yokoyama, S]]
-[[Category: National project on protein structural and functional analyse]]
-[[Category: Nppsfa]]
-[[Category: Protein arginine n-methyltransferase]]
-[[Category: Rsgi]]
-[[Category: Sh3 domain]]
-[[Category: Transferase]]

1x2p

From Proteopedia

Current revision

Solution structure of the SH3 domain of the Protein arginine N-methyltransferase 2

Structural highlights

Function

Evolutionary Conservation

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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