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0LY10_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSP140
DescriptionNuclear body protein sp140 (nuclear autoantigen sp-140) (speckled 140 kda) (lysp100 protein) (lymphoid-restricted homolog of sp100).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005635 nuclear membrane (TAS)
0005654 nucleoplasm (TAS)
0003700 transcription factor activity (TAS)
0006952 defense response (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The function of this domain is unknown. It is about 105 amino acid residues in length and is predicted to be predominantly alpha helical. This domain is usually found at the amino terminus of protein that contain a SAND domain .
  IPR004865:Sp100
The SAND domain (named after Sp100.IRE-1.ucP41/75.EAF-1) is a conserved~80 residue region found in a number of nuclear proteins.any of whichfunction in chromatin-dependent transcriptional control. These includeproteins linked to various human diseases.uch as the Sp100 (Speckled protein100 kDa).UDR (Nuclear DEAF-1 related).MEB (Glucocorticoid ModulatoryElement Binding) proteins and AIRE-1 (Autoimmune regulator 1) proteins.Proteins containing the SAND domain have a modular structure; the SAND domaincan be associated with a number of other modules.ncluding the bromodomain.he PHD finger and the MYND finger.Because no SAND domain has been found in yeast.t is thought that the SANDdomain could be restricted to animal phyla. Many SAND domain-containingproteins.ncluding NUDR.EAF-1 (Deformed epidermal autoregulatory factor-1)and GMEB.ave been shown to bind DNA sequences specifically. The SAND domainhas been proposed to mediate the DNA binding activity of these proteins .The resolution of the 3D structure of the SAND domain from Sp100b has revealedthat it consists of a novel alpha/beta fold. The SAND domainadopts a compact fold consisting of a strongly twisted.ive-strandedantiparallel beta-sheet with four alpha-helices packing against one side ofthe beta-sheet. The opposite side of the beta-sheet is solvent exposed. Thebeta-sheet and alpha-helical parts of the structure form two distinct regions.Multiple hydrophobic residues pack between these regions to form a structuralcore. A conserved KDWK sequence motif is found within the alpha-helical.ositively charged surface patch. The DNA binding surface has been mapped tothe alpha-helical region encompassing the KDWK motif .
  IPR000770:SAND
Bromodomains are found in a variety of mammalian.nvertebrate and yeast DNA-binding proteins . Bromodomains can interact withacetylated lysine .In some proteins.he classical bromodomain has diverged to such an extent that parts of the region are either missing or contain an insertion (e.g..ammalian protein HRX.aenorhabditis elegans hypothetical protein ZK783.4.east protein YTA7). The bromodomain may occur as a single copy.r in duplicate. The precise function of the domain is unclear.ut it may be involved in protein-protein interactions and may play a role in assembly or activity of multi-component complexes involved in transcriptional activation .
  IPR001487:Bromodomain
The homeodomain (PHD) finger .s a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of.ut distinct from the C3HC4 type RING finger.The function of this domain is not yet known but in analogy with the LIM domain it could be involved in protein-protein interaction and be important for the assembly or activity of multicomponent complexes involved in transcriptional activation or repression. Alternatively.he interactions could be intra-molecular and be important in maintaining the structural integrity of the protein. In similarity to the RING finger and the LIM domain.he PHD finger is thought to bind two zinc ions.
  IPR001965:Zinc finger, PHD-type
The SAND domain (named after Sp100.IRE-1.ucP41/75.EAF-1) is a conserved ~80 residue region found in a number of nuclear proteins.any of which function in chromatin-dependent transcriptional control. These include proteins linked to various human diseases.uch as the Sp100 (Speckled protein 100 kDa).UDR (Nuclear DEAF-1 related).MEB (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.ncluding the bromodomain.he PHD finger and the MYND finger. Because no SAND domain has been found in yeast.t is thought that the SAND domain could be restricted to animal phyla. Many SAND domain-containing proteins.ncluding NUDR.EAF-1 (Deformed epidermal autoregulatory factor-1) and GMEB.ave been shown to bind DNA sequences specifically. The SAND domain has been proposed to mediate the DNA binding activity of these proteins . Structurally.he SAND domain consists of a novel alpha/beta fold.hich has a core of three short helices packed against a barrel-like beta-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.hich is stabilised by a bound zinc atom.nd resembles a SAND domain.n 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.eading to the repression of TGF-beta.ctivin and BMP responses.esulting in the repression of TGF-signalling .
  IPR010919:SAND-like
Zinc finger domains (ZnFs) are common.elatively small protein motifs that fold around one or more zinc ions. In addition to their role as a DNA-binding module.nFs have recently been shown to mediate protein:protein and protein:lipid interactions. There are at least 14 different classes of Zn fingers.hich differ in the nature and arrangement of their zinc-binding residues .The FYVE zinc finger domain is conserved from yeast to man.nd is named after four proteins that it has been found in: Fab1.OTB/ZK632.12.ac1.nd EEA1. It functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P).hich is found mainly on endosomes .The plant homeodomain (PHD) zinc finger domain has a C4HC3-type motif.nd is widely distributed in eukaryotes.eing found in many chromatin regulatory factors .Both the FYVE and the PHD zinc finger motifs display strikingly similar dimetal(zinc)-bound alpha+beta folds.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011011:Zinc finger, FYVE/PHD-type
IPR004865:Sp100 
Evalue:-75.958610534668 
Location:36-139IPR000770:SAND 
Evalue:-53.5086364746094 
Location:580-661IPR001487:BROMO 
Evalue:-20.0409586076789 
Location:756-859IPR001965:PHD 
Evalue:-8.35654735565185 
Location:692-736IPR001487:BROMODOMAIN_1 
Evalue:0 
Location:0-0
SequencesProtein: LY10_HUMAN (882 aa)
mRNA: NM_007237
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 58 residues, 230798689-230798862Exon2: 61 residues, 230810041-230810219Exon3: 58 residues, 230811171-230811340Exon4: 30 residues, 230814362-230814446Exon5: 29 residues, 230816689-230816770Exon6: 33 residues, 230817946-230818039Exon7: 28 residues, 230818821-230818899Exon8: 52 residues, 230820874-230821024Exon9: 30 residues, 230821843-230821927Exon10: 29 residues, 230823939-230824020Exon11: 36 residues, 230826274-230826376Exon12: 29 residues, 230828410-230828491Exon13: 31 residues, 230842490-230842577Exon14: 41 residues, 230842795-230842912Exon15: 20 residues, 230843544-230843598Exon16: 24 residues, 230857304-230857370Exon17: 29 residues, 230858710-230858791Exon18: 27 residues, 230860850-230860925Exon19: 37 residues, 230863418-230863523Exon20: 49 residues, 230865604-230865747Exon21: 18 residues, 230867229-230867277Exon22: 16 residues, 230870379-230870421Exon23: 40 residues, 230882882-230882998Exon24: 38 residues, 230883701-230883810Exon25: 28 residues, 230884112-230884190Exon26: 50 residues, 230884410-230884554Exon27: 212 residues, 230885544-230886174Exon28: 2 residues, -Jump to LY10_HUMAN  
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