|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 101 to 155 out of 155 for Sp110

<< First    < Previous  |  Next >    Last >>
0.026s
Type Details Score
DO Term
Protein
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
Protein Domain
Type: Family
Description: This entry includes a group of nuclear dot-associated proteins, including Sp110/Sp140/Sp140L from humans. They are proteins with a constituent of nuclear domains, also known as nuclear dots (NDs). Sequences similar to the Sp100 homodimerization/ND-targeting region occur in several other proteins and constitute a novel protein motif, termed HSR domain (for homogeneously-staining region) [].Sp110 is a leukocyte-specific component of the nuclear body []. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells []. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers [, ]. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population []. 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 [].This family also includes protein Sp140-like (SP140L) [].
Publication      
First Author: Mouse Genome Informatics and VEGA Genome Database Project
Year: 2006
Journal: Database Release
Title: Collaboration to Associate VEGA (Vertebrate Genome Annotation) Mouse Gene Models with MGI Markers
Protein
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 325  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 59  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
Publication
First Author: Sternsdorf T
Year: 1999
Journal: J Biol Chem
Title: The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers.
Volume: 274
Issue: 18
Pages: 12555-66
Publication
First Author: Zucchelli C
Year: 2014
Journal: FEBS J
Title: Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1.
Volume: 281
Issue: 1
Pages: 216-31
Publication
First Author: Yap KL
Year: 2010
Journal: Crit Rev Biochem Mol Biol
Title: Keeping it in the family: diverse histone recognition by conserved structural folds.
Volume: 45
Issue: 6
Pages: 488-505
Publication
First Author: Bloch DB
Year: 1996
Journal: J Biol Chem
Title: Identification and characterization of a leukocyte-specific component of the nuclear body.
Volume: 271
Issue: 46
Pages: 29198-204
Publication
First Author: Di Bernardo MC
Year: 2008
Journal: Nat Genet
Title: A genome-wide association study identifies six susceptibility loci for chronic lymphocytic leukemia.
Volume: 40
Issue: 10
Pages: 1204-10
Publication
First Author: Dent AL
Year: 1996
Journal: Blood
Title: LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies.
Volume: 88
Issue: 4
Pages: 1423-6
Publication  
First Author: Saare M
Year: 2015
Journal: J Immunol Res
Title: SP140L, an Evolutionarily Recent Member of the SP100 Family, Is an Autoantigen in Primary Biliary Cirrhosis.
Volume: 2015
Pages: 526518
Protein
Organism: Mus musculus/domesticus
Length: 482  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 418  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 283  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 494  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 482  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 397  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 302  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
Publication
First Author: Trost M
Year: 2009
Journal: Immunity
Title: The phagosomal proteome in interferon-gamma-activated macrophages.
Volume: 30
Issue: 1
Pages: 143-54
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89