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| | ==AIDA-1 SAM domain tandem== | | ==AIDA-1 SAM domain tandem== |
| - | <StructureSection load='2kiv' size='340' side='right'caption='[[2kiv]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kiv' size='340' side='right'caption='[[2kiv]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kiv]] 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=2KIV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KIV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kiv]] 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=2KIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KIV FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AIDA-1b, ANKS1B ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kiv OCA], [http://pdbe.org/2kiv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kiv RCSB], [http://www.ebi.ac.uk/pdbsum/2kiv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kiv ProSAT]</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=2kiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kiv OCA], [https://pdbe.org/2kiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kiv RCSB], [https://www.ebi.ac.uk/pdbsum/2kiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kiv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ANS1B_HUMAN ANS1B_HUMAN]] Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> Isoform 3 can regulate global protein synthesis by altering nucleolar numbers (By similarity).<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing.<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> | + | [https://www.uniprot.org/uniprot/ANS1B_HUMAN ANS1B_HUMAN] Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> Isoform 3 can regulate global protein synthesis by altering nucleolar numbers (By similarity).<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing.<ref>PMID:15862129</ref> <ref>PMID:15347684</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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Donaldson, L W]] | + | [[Category: Donaldson LW]] |
| - | [[Category: Kurabi, A]] | + | [[Category: Kurabi A]] |
| - | [[Category: Alternative splicing]]
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| - | [[Category: Ank repeat]]
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| - | [[Category: Cell junction]]
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| - | [[Category: Cell membrane]]
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| - | [[Category: Cell projection]]
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| - | [[Category: Cytoplasm]]
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| - | [[Category: Membrane]]
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| - | [[Category: Nucleus]]
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| - | [[Category: Phosphoprotein]]
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| - | [[Category: Postsynaptic cell membrane]]
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| - | [[Category: Sam domain]]
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| - | [[Category: Signaling protein]]
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| - | [[Category: Synapse]]
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| - | [[Category: Tandem]]
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| Structural highlights
Function
ANS1B_HUMAN Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.[1] [2] Isoform 3 can regulate global protein synthesis by altering nucleolar numbers (By similarity).[3] [4] Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing.[5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The neuronal scaffolding protein AIDA-1 is believed to act as a convener of signals arising at postsynaptic densities. Among the readily identifiable domains in AIDA-1, two closely juxtaposed sterile alpha motif (SAM) domains and a phosphotyrosine binding domain are located within the C-terminus of the longest splice variant and exclusively in four shorter splice variants. As a first step towards understanding the possible emergent properties arising from this assembly of ligand binding domains, we have used NMR methods to solve the first structure of a SAM domain tandem. Separated by a 15-aa linker, the two SAM domains are fused in a head-to-tail orientation that has been observed in other hetero- and homotypic SAM domain structures. The basic nuclear import signal for AIDA-1 is buried at the interface between the two SAM domains. An observed disparity between the thermal stabilities of the two SAM domains suggests a mechanism whereby the second SAM domain decouples from the first SAM domain to facilitate translocation of AIDA-1 to the nucleus.
A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import.,Kurabi A, Brener S, Mobli M, Kwan JJ, Donaldson LW J Mol Biol. 2009 Oct 9;392(5):1168-77. Epub 2009 Aug 8. PMID:19666031[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu H, Hebert MD. A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin. BMC Cell Biol. 2005 Apr 29;6(1):23. PMID:15862129 doi:http://dx.doi.org/10.1186/1471-2121-6-23
- ↑ Ghersi E, Noviello C, D'Adamio L. Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner. J Biol Chem. 2004 Nov 19;279(47):49105-12. Epub 2004 Sep 3. PMID:15347684 doi:http://dx.doi.org/10.1074/jbc.M405329200
- ↑ Xu H, Hebert MD. A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin. BMC Cell Biol. 2005 Apr 29;6(1):23. PMID:15862129 doi:http://dx.doi.org/10.1186/1471-2121-6-23
- ↑ Ghersi E, Noviello C, D'Adamio L. Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner. J Biol Chem. 2004 Nov 19;279(47):49105-12. Epub 2004 Sep 3. PMID:15347684 doi:http://dx.doi.org/10.1074/jbc.M405329200
- ↑ Xu H, Hebert MD. A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin. BMC Cell Biol. 2005 Apr 29;6(1):23. PMID:15862129 doi:http://dx.doi.org/10.1186/1471-2121-6-23
- ↑ Ghersi E, Noviello C, D'Adamio L. Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner. J Biol Chem. 2004 Nov 19;279(47):49105-12. Epub 2004 Sep 3. PMID:15347684 doi:http://dx.doi.org/10.1074/jbc.M405329200
- ↑ Kurabi A, Brener S, Mobli M, Kwan JJ, Donaldson LW. A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import. J Mol Biol. 2009 Oct 9;392(5):1168-77. Epub 2009 Aug 8. PMID:19666031 doi:10.1016/j.jmb.2009.08.004
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