2vxd
From Proteopedia
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==The structure of the C-terminal domain of Nucleophosmin== | ==The structure of the C-terminal domain of Nucleophosmin== | ||
| - | <StructureSection load='2vxd' size='340' side='right' caption='[[2vxd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2vxd' size='340' side='right'caption='[[2vxd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2vxd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VXD FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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=2vxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vxd OCA], [https://pdbe.org/2vxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vxd RCSB], [https://www.ebi.ac.uk/pdbsum/2vxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vxd ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location. |
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/NPM_HUMAN NPM_HUMAN]] Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication.<ref>PMID:16107701</ref> <ref>PMID:17015463</ref> <ref>PMID:18809582</ref> <ref>PMID:19188445</ref> <ref>PMID:20352051</ref> <ref>PMID:21084279</ref> <ref>PMID:22002061</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Bycroft, M]] | [[Category: Bycroft, M]] | ||
[[Category: Grummitt, C G]] | [[Category: Grummitt, C G]] | ||
Current revision
The structure of the C-terminal domain of Nucleophosmin
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