InterPro : IPR030411

Name  Nuclear body protein SP140 Short Name  SP140
Type  Family Description  The function of nuclear protein SP140 is not known, though it contains several chromatin related modules such as plant homeodomain (PHD), bromodomain (BRD) and SAND domain, which suggests a role in chromatin-mediated regulation of gene expression []. It also harbours a nuclear localisation signal, and a dimerisation domain (HSR or CARD domain). The PHD finger of Sp140 presents an atypical fold which does not bind to histone H3 tails but binds to peptidylprolyl isomerase Pin1. Pin1 catalyses the isomerisation of a phospho-Threonine-Proline bond in Sp140-PHD and thus may modulate Sp140 function [].Human Sp140 is an interferon inducible nuclear leukocyte-specific protein that may be involved in the pathogenesis of acute promyelocytic leukemia and viral infection []. It localises to LYSP100-associated nuclear dots and is also a component of the promyelocytic leukemia nuclear body (PML-NBs) [, ]. The Sp140 locus has been identified as a lymphocytic leukemia (CLL) risk locus [].
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Proteins

InterPro protein domain ID --> Contigs

 

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5 Publications

First Author Title Year Journal Volume Pages
Zucchelli C Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1. 2014 FEBS J 281 216-31
Yap KL Keeping it in the family: diverse histone recognition by conserved structural folds. 2010 Crit Rev Biochem Mol Biol 45 488-505
Bloch DB Identification and characterization of a leukocyte-specific component of the nuclear body. 1996 J Biol Chem 271 29198-204
Di Bernardo MC A genome-wide association study identifies six susceptibility loci for chronic lymphocytic leukemia. 2008 Nat Genet 40 1204-10
Dent AL LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies. 1996 Blood 88 1423-6



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)