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Search results 201 to 300 out of 415 for Sp100

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Type Details Score
Publication
24275490 | -
First Author: Perniola R
Year: 2014
Journal: Biochim Biophys Acta
Title: The biophysical and biochemical properties of the autoimmune regulator (AIRE) protein.
Volume: 1842
Issue: 2
Pages: 326-37
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Protein Domain
IPR004865 | HSR_dom
Type: Domain
Description: The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots (NDs). An ND-targeting region that coincides with a homodimerisation domain was mapped in Sp100. 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) []. This domain can also be found in Vertebrate AutoImmune REgulator (AIRE) protein, a transcription regulator predominantly expressed in thymus medullary epithelial cells which also localises to nuclear dots []. The HSR domain, which has also been named ASS (AIRE, Sp-100 and Sp140) domain [], can be found alone or in association with other domains, such as SAND , PHD finger and Bromo , The HSR domain is predicted to be predominantly α-helical [, , ].
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Publication
17245429 | J:196105
First Author: Milovic-Holm K
Year: 2007
Journal: EMBO J
Title: FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies.
Volume: 26
Issue: 2
Pages: 391-401
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Protein Coding Gene
MGI:1917193 | Lrch4
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
22519587 | J:184866
First Author: Yang CY
Year: 2012
Journal: Clin Exp Immunol
Title: Epitope-specific anti-nuclear antibodies are expressed in a mouse model of primary biliary cirrhosis and are cytokine-dependent.
Volume: 168
Issue: 3
Pages: 261-7
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Publication
21831885 | J:176678
First Author: De Vos WH
Year: 2011
Journal: Hum Mol Genet
Title: Repetitive disruptions of the nuclear envelope invoke temporary loss of cellular compartmentalization in laminopathies.
Volume: 20
Issue: 21
Pages: 4175-86
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Publication
24586165 | J:246216
First Author: DaÄŸ F
Year: 2014
Journal: PLoS Pathog
Title: Reversible silencing of cytomegalovirus genomes by type I interferon governs virus latency.
Volume: 10
Issue: 2
Pages: e1003962
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Protein
Q99388
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
E0CXN9
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: true
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Protein
Q3UTB2
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: false
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Protein
Q3TQS4
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
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Protein
Q3TZR7
Organism: Mus musculus/domesticus
Length: 325  
Fragment?: false
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Protein
E9PV05
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
E9Q422
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: false
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Protein
Q4KKY3
Organism: Mus musculus/domesticus
Length: 59  
Fragment?: false
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Protein
E9Q4Y0
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
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Protein
Q52KL8
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: false
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Protein
E9Q3M7
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: true
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Protein
Q8BNW8
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: true
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Protein
Q8BS13
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
Q8C9H3
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
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Protein
Q3UT50
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
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Protein
Q7TSS9
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
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Protein
D6RIJ4
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: false
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Protein
E0CXL1
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
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Protein
Q3UKD8
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
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Protein
E0CY74
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
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Protein
Q3KNJ6
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
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Protein
Q8C9T1
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false
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Protein
Q8C898
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
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Publication
10212234 | -
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
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Publication
9697411 | -
First Author: Gibson TJ
Year: 1998
Journal: Trends Biochem Sci
Title: The APECED polyglandular autoimmune syndrome protein, AIRE-1, contains the SAND domain and is probably a transcription factor.
Volume: 23
Issue: 7
Pages: 242-4
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Protein Coding Gene
MGI:1923257 | Zmym2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1915689 | Lrrc28
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q8BVK9
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
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Protein
Q3U876
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
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Protein
A0A1B0GX24
Organism: Mus musculus/domesticus
Length: 418  
Fragment?: true
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Protein
E9QA05
Organism: Mus musculus/domesticus
Length: 494  
Fragment?: false
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Protein
Q3U5P2
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: true
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Protein
Q922J2
Organism: Mus musculus/domesticus
Length: 397  
Fragment?: false
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Protein
A0A668KM38
Organism: Mus musculus/domesticus
Length: 332  
Fragment?: false
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Protein
Q3U0D6
Organism: Mus musculus/domesticus
Length: 332  
Fragment?: false
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Protein Coding Gene
MGI:2183446 | Agap3
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
9773984 | J:50207
First Author: Huggenvik JI
Year: 1998
Journal: Mol Endocrinol
Title: Characterization of a nuclear deformed epidermal autoregulatory factor-1 (DEAF-1)-related (NUDR) transcriptional regulator protein.
Volume: 12
Issue: 10
Pages: 1619-39
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Protein
E9Q441
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
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Protein
Q3ZB72
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
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Protein
Q8C405
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein Coding Gene
MGI:2137356 | Trim16
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2442599 | Simc1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2684975 | Ciart
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1333839 | Magea4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:3588211 | Magea10
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:105113 | Gcna
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1333793 | Magea2
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
10049735 | J:53032
First Author: Mittaz L
Year: 1999
Journal: Biochem Biophys Res Commun
Title: Isolation and characterization of the mouse Aire gene.
Volume: 255
Issue: 2
Pages: 483-90
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Protein
Q9JL60
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Protein
P58929
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
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Protein
Q3UYV4
Organism: Mus musculus/domesticus
Length: 563  
Fragment?: false
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Protein
A0A1B0GSY7
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: true
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Protein
A2AS07
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: true
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Protein
Q3TYJ5
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
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Protein
Q80V49
Organism: Mus musculus/domesticus
Length: 450  
Fragment?: false
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Protein
A0A1B0GRZ5
Organism: Mus musculus/domesticus
Length: 575  
Fragment?: false
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Protein
D6RGU7
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: false
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Protein
D6RDQ5
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: false
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Protein
Q6ZPV0
Organism: Mus musculus/domesticus
Length: 411  
Fragment?: true
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Publication
11427895 | -
First Author: Bottomley MJ
Year: 2001
Journal: Nat Struct Biol
Title: The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation.
Volume: 8
Issue: 7
Pages: 626-33
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Protein
Q8C308
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: false
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Protein
F6V9G0
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
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Publication
16803959 | -
First Author: Tosh K
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Variants in the SP110 gene are associated with genetic susceptibility to tuberculosis in West Africa.
Volume: 103
Issue: 27
Pages: 10364-10368
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Publication
21222611 | -
First Author: Cai L
Year: 2011
Journal: Med Chem
Title: Identification of proteins interacting with human SP110 during the process of viral infections.
Volume: 7
Issue: 2
Pages: 121-6
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Publication
10913195 | -
First Author: Bloch DB
Year: 2000
Journal: Mol Cell Biol
Title: Sp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivator.
Volume: 20
Issue: 16
Pages: 6138-46
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Publication
16648851 | -
First Author: Roscioli T
Year: 2006
Journal: Nat Genet
Title: Mutations in the gene encoding the PML nuclear body protein Sp110 are associated with immunodeficiency and hepatic veno-occlusive disease.
Volume: 38
Issue: 6
Pages: 620-2
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Protein Domain
IPR043563 | Sp110/Sp140/Sp140L
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) [].
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Protein Domain
IPR000770 | SAND_dom
Type: Domain
Description: The SAND domain (named after Sp100, AIRE-1, NucP41/75, DEAF-1) is a conserved ~80 residue region found in a number of nuclear proteins, many of which function in chromatin-dependent transcriptional control. These include proteins linked to various human diseases, such as the Sp100 (Speckled protein 100kDa) [], NUDR (Nuclear DEAF-1 related), GMEB (Glucocorticoid Modulatory Element Binding) proteins []and AIRE-1 (Autoimmune regulator 1) proteins.Proteins containing the SAND domain have a modular structure; the SAND domain can be associated with a number of other modules, including the bromodomain, the PHD finger and the MYND finger. Because no SAND domain has been found in yeast, it is thought that the SAND domain could be restricted to animal phyla. Many SAND domain-containing proteins, including NUDR, DEAF-1 (Deformed epidermal autoregulatory factor-1)and GMEB, have been shown to bind DNA sequences specifically. The SAND domain has been proposed to mediate the DNA binding activity of these proteins [, ].The resolution of the 3D structure of the SAND domain from Sp100b has revealed that it consists of a novel alpha/beta fold. The SAND domain adopts a compact fold consisting of a strongly twisted, five-stranded antiparallel β-sheet with four α-helices packing against one side of the β-sheet. The opposite side of the β-sheet is solvent exposed. The β-sheet and α-helical parts of the structure form two distinct regions.Multiple hydrophobic residues pack between these regions to form a structural core. A conserved KDWK sequence motif is found within the α-helical, positively charged surface patch. The DNA binding surface has been mapped to the α-helical region encompassing the KDWK motif [].
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Protein Domain
IPR010919 | SAND-like_dom_sf
Type: Homologous_superfamily
Description: The SAND domain (named after Sp100, AIRE-1, NucP41/75, DEAF-1) is a conserved ~80 residue region found in a number of nuclear proteins, many of which function in chromatin-dependent transcriptional control. These include proteins linked to various human diseases, such as the Sp100 (Speckled protein 100kDa), NUDR (Nuclear DEAF-1 related), GMEB (Glucocorticoid Modulatory Element Binding) proteins and AIRE-1 (Autoimmune regulator 1) proteins.Proteins containing the SAND domain have a modular structure; the SAND domain can be associated with a number of other modules, including the bromodomain, the PHD finger and the MYND finger. Because no SAND domain has been found in yeast, it is thought that the SAND domain could be restricted to animal phyla. Many SAND domain-containing proteins, including NUDR, DEAF-1 (Deformed epidermal autoregulatory factor-1) and GMEB, have been shown to bind DNA sequences specifically. The SAND domain has been proposed to mediate the DNA binding activity of these proteins [, ]. Structurally, the SAND domain consists of a novel alpha/beta fold, which has a core of three short helices packed against a barrel-like β-sheet; it is structurally similar to the SH3-like fold.Other proteins display domains that are structurally similar to the SAND domain. One such example is the SMAD4-binding domain of the oncoprotein Ski, which is stabilised by a bound zinc atom, and resembles a SAND domain, in which the corresponding I loop is responsible for DNA binding. Ski is able to disrupt the formation of a functional complex between the Co- and R-SMADs, leading to the repression of TGF-beta, Activin and BMP responses, resulting in the repression of TGF-signalling [].
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Protein
A0A1B0GT08
Organism: Mus musculus/domesticus
Length: 283  
Fragment?: true
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Protein
A0A1B0GRR4
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: false
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Protein Coding Gene
MGI:1336201 | Sumo3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1343177 | Calcoco2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1891307 | Ubn1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1860606 | Akap8l
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2147679 | Patl1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1914120 | Serbp1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1919943 | Zcchc12
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1333832 | Magea3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1333838 | Magea5
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
10894151 | -
First Author: Kaul S
Year: 2000
Journal: Mol Endocrinol
Title: Properties of the glucocorticoid modulatory element binding proteins GMEB-1 and -2: potential new modifiers of glucocorticoid receptor transactivation and members of the family of KDWK proteins.
Volume: 14
Issue: 7
Pages: 1010-27
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Publication
24267382 | -
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
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Publication
20923397 | -
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
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Publication
8910577 | -
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
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Publication
18758461 | -
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
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Publication
8695863 | -
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
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Protein Coding Gene
MGI:2137896 | Zfp451
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1352465 | Nr2c1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1916973 | Rpain
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913849 | Rdm1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1860486 | Tdp2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:99430 | Hira
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2136841 | Morc3
Type: protein_coding_gene
Organism: mouse, laboratory
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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