hmga1, high mobility group AT-hook 1 - Creative Biogene
HMGA1; high mobility group AT-hook 1; high mobility group (nonhistone chromosomal) protein isoforms I and Y , HMGIY; high mobility group protein HMG-I/HMG-Y; HMG-I(Y); high mobility group protein R; high mobility group protein A1; nonhistone chromosomal h; nonhistone chromosomal high-mobility group protein HMG-I/HMG-Y; high-mobility group (nonhistone chromosomal) protein isoforms I and Y; HMG-R; HMGIY; HMGA1A; MGC4242; MGC4854; MGC12816 ...https://www.creative-biogene.com/symbolsearch_hmga1.html
"Biochemical characterization of mammalian high mobility group protein " by Lorraine Katy Edwards
The high mobility group protein HMGA2 is an architectural transcription factor, which is expressed during embryogenesis. Aberrant expression causes benign and malignant tumor formation. The protein possesses three 'AT hook' domains and an acidic Cterminal. HMGA2 is natively unstructured, however it forms a homodimer. In this study site-directed mutagenesis was used to create single methionine mutants, HMGA2Q37M, HMGA2I71M and HMGA2Q85M. These mutants were cross-linked using EDC and then cleaved using CNBr to determine which domains are involved in homodimer formation. Our results indicate that the second 'AT hook' domain may interact with the C-terminal. We then labeled a peptide containing the C-terminal (CTP) with tetramethylrhodamine-5- maleimide (TRM). We found that the CTP-TMR binds to HMGA2Α95-108, which lacks the C-terminal. These results suggest that the C-terminal is required for homodimer formation. The techniques used within this study can be ...http://digitalcommons.fiu.edu/etd/3118/
DNASU Plasmid | HMGN2 (Homo sapiens)...
high mobility group nucleosome-binding domain-containing protein 2,high mobility group protein N2,high-mobility group (nonhistone chromosomal) protein 17,high-mobility group nucleosomal binding domain 2,non-histone chromosomal protein HMG-17,nonhistone chromosomal protein HMG-17 ...http://dnasu.org/DNASU/GetCloneDetail.do?cloneid=329670
hmg20b, high mobility group 20B - Creative Biogene
HMG20B; high mobility group 20B; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related; BRAF25; BRAF35; HMG box domain containing 2; HMGX2; HMGXB2; SMARCE1r; SOXL; SMARCE1-related protein; high-mobility grou; high-mobility group 20B; BRCA2-associated factor 35; HMG box-containing protein 20B; HMG domain-containing protein 2; Sox-like transcriptional factor; HMG domain-containing protein HMGX2; structural DNA-binding protein BRAF35; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E, member 1-related; PP7706; pp8857; FLJ26127; SOXL, HMGX2, BRAF25, BRAF35, HMGXB2, PP7706, pp8857, SMARCE1r; fc85b02; wu:fc85b02; zgc:110001; si:dkey-110c1.6; high mobility group box domain containing ...https://www.creative-biogene.com/symbolsearch_hmg20b.html
High mobility group protein HMG-I/HMG-Y
This gene encodes a chromatin-associated protein involved in the regulation of gene transcription, integration of retroviruses into chromosomes, and the metastatic progression of cancer cells. The encoded protein preferentially binds to the minor groove of AT-rich regions in double-stranded DNA. Multiple transcript variants encoding different isoforms have been found for this gene. Pseudogenes of this gene have been identified on multiple chromosomes. [provided by RefSeq, Jan 2016 ...https://pharos.nih.gov/idg/targets/P17096
Collective mass spectrometry approaches reveal broad and combinatorial modification of high mobility group protein A1a |...
Transcriptional states are formed and maintained by the interaction and post-translational modification (PTM) of several chromatin proteins, such as histones and high mobility group (HMG) proteins. Amhttps://link.springer.com/article/10.1016/j.jasms.2010.01.020
NHP10 (YDL002C) Result Summary | BioGRID
Non-essential INO80 Chromatin Remodeling Complex Subunit; Preferentially Binds DNA Ends, Protecting Them From Exonucleatic Cleavage; Deletion Affects Telomere Maintenance Via Recombination; Related To Mammalian High Mobility Group Proteinshttps://thebiogrid.org/32052/protein/saccharomyces-cerevisiae/nhp10.html
PREDICTED: similar to High mobility group protein 1 (HMG-1) (High mobility group protein B1) (Amphoterin) (Heparin-binding protein p30) isoform 1 [Canis familiaris ...http://pede.dna.affrc.go.jp/seq_search/assembly_info.php?release=20110601&name=20110601C-000357
HMO1 - High mobility group protein 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) - HMO1 gene &...
DNA-binding protein that is probably part of the rDNA transcription apparatus. Acts synergetically with the RPA49 subunit of RNA polymerase I during rDNA transcription. May participate in mutagenesis control.http://www.uniprot.org/uniprot/Q03973
The High Mobility Group (Hmg) Boxes of the Nuclear Protein Hmg1 Induce Chemotaxis and Cytoskeleton Reorganization in Rat Smooth...
High mobility group 1 (HMG1) protein is the archetypal protein of the HMG-box family, which is characterized by their DNA binding domains, called HMG boxes. HMG1 is a small 25-kD protein of 215 amino acids with a highly conserved sequence among mammals. The HMG1 molecule is organized into three domains: two DNA binding domains, HMG Box A and Box B, which are followed by an acidic COOH terminus composed of 30 glutamic and aspartic residues. The two HMG boxes, A and B, are similar 80 amino acid segments (29% identical, 65% similar) and form an L-shaped structure (Read et al. 1993; Weir et al. 1993; Hardman et al. 1995).. HMG1 has originally been identified as a ubiquitously expressed, abundant nuclear protein. It is present in ,1 million copies per single nucleus and binds double stranded DNA without apparent sequence specificity. Instead, HMG1 binds with high affinity to specific DNA structures like kinked or bent DNA and ...http://jcb.rupress.org/content/152/6/1197
Studies on the high-mobility-group non-histone proteins from hen oviduct | Biochemical Journal
Nuclear high-mobility-group (HMG) proteins were isolated from hen oviduct. These were proteins HMG-1, −2, −3, −14 and −17, which are equivalent to the classification of calf thymus HMG proteins. Hen oviduct proteins HMG-1 and −2 were individually isolated by HCIO4.extraction and CM-Sephadex chromatographic separation. Their mol.wts. were determined as 28 000 and 27 000, respectively. The proteins have a high content of acidic and basic amino acids. The association of proteins HMG-1 and −2 with the genome of hen oviduct nuclei was probed by a limited digestion with nucleases. Hen oviduct nuclei were incubated with deoxyribonuclease I or micrococcal nuclease until 10% of the DNA was digested. The nuclear suspension was centrifuged and the contents of proteins HMG-1 and −2 in the supernatant and sediment fractions were analysed ...http://www.biochemj.org/content/181/3/585
Abstract 18508: Exposure of Adipocytes to High Mobility Group Box 1 Impairs Insulin Signaling via RAGE, While Stimulating...
Background: Smokers show increased prevalence of insulin resistance for glucose and type 2 diabetes mellitus (T2DM). The underlying mechanisms, however, remain poorly understood. Tobacco smoke exposure increases tissue expression of high mobility group box 1 (HMGB1), a damage-associated molecular pattern (DAMP) that activates innate immunity. We recently reported that exposure of human macrophages to tobacco smoke extract (TSE) provokes the release of HMGB1 in two forms: as a soluble molecule and carried on membrane microvesicles (MV). Both soluble recombinant HMGB1 (rHMGB1) and MV-associated HMGB1 on TSE-induced MVs (TSE-MVs) mediate crucial crosstalk with adipocytes by impairing insulin signaling and by recruiting monocytes to the adipocytes -. GOAL- To identify the receptors on adipocytes that mediate the effects of HMGB1 on insulin signaling and monocyte recruitment.. Methods: Cultured 3T3-L1 adipocytes were incubated for 24h with rHMGB1 or TSE-MVs, in ...http://circ.ahajournals.org/content/128/Suppl_22/A18508
NHP2 (YDL208W) Result Summary | BioGRID
Protein Related To Mammalian High Mobility Group (HMG) Proteins; Nuclear Protein; Essential For Function Of H/ACA-type SnoRNPs, Which Are Involved In 18S RRNA Processinghttps://thebiogrid.org/31838/protein/saccharomyces-cerevisiae/nhp2.html
Monzen K et al. (2008), A crucial role of a high mobility group protein... - Xenbase Paper
The high mobility group (HMG) of nuclear proteins regulates expression of many genes through architectural remodelling of the chromatin structure, and formation of multiprotein complexes on promoter/enhancer regions. This leads to the active transcription of their target genes. Here we show that HMGA2, a member of the HMGA sub-family of HMG proteins, has a critical function in cardiogenesis. Overexpression of HMGA2 enhanced, whereas siRNA-mediated knockdown of HMGA2 blocked, cardiomyocyte differentiation of the embryonal carcinoma cell line P19CL6. Moreover, overexpression of a dominant-negative HMGA2 or morpholino-mediated knockdown of HMGA2 expression blocked normal heart formation in Xenopus laevis embryos, suggesting that HMGA2 has an important role in cardiogenesis both in vitro and in vivo. Mechanistically, HMGA2 associated with Smad1/4 and showed synergistic trans-activation of the gene for a cardiac transcription ...http://www.xenbase.org/literature/article.do?method=display&articleId=37615
Abstract 487: Heart fibroblasts mediate the effect of High Mobility Group Box 1 Protein on cardiac stem cells | Circulation
Introduction. We have previously shown that High Mobility Group Box-1 Protein (HMGB1) injection into the infarcted mouse heart induces resident cardiac c-kit+ stem cell (CSC) proliferation and differentiation toward the myocardial lineage. However, in contrast to the in vivo studies, in vitro experiments have shown no effect of HMGB1 on CSC proliferation. Here we examined whether HMGB1 modulates CSC proliferation and differentiation in a paracrine manner through cardiac fibroblasts (cFb) activation.. Methods and Results. cFbs were obtained from human auricle and identified for the expression of vimentin and smooth muscle actin. CSC, magnetically sorted for c-kit antigen, were obtained from adult CD1 mice. Western blot analysis revealed that cFbs expressed the HMGB1 receptors RAGE and Toll-like receptors 2 and 4. HMGB1 (5, 10, 100, 200 ng/ml) induced a dose-dependent chemotactic effect on cFbs but had no effect on proliferation. Moreover, HMGB1 was not a ...http://circ.ahajournals.org/content/116/Suppl_16/II_83.3
HMG1 and 2: architectural DNA-binding proteins | Biochemical Society Transactions
HMG1 and 2 (high mobility group proteins 1 and 2; renamed HMGB1 and 2) contain two DNA-binding HMG-box domains (A and B) and a long acidic C-terminal domain. They bind DNA without sequence specificity, but have a high affinity for bent or distorted DNA, and bend linear DNA. The individual A and B boxes (which, although broadly similar, show both structural and functional differences) exhibit many of the structure-specific properties of the whole protein. The acidic tail modulates the affinity of the tandem HMG boxes in HMG1 and 2 for a variety of DNA targets, including four-way junctions, but not distorted DNA minicircles, to which the proteins bind with very high affinity. HMG1 and 2 appear to play important architectural roles in the assembly of nucleoprotein complexes in a variety of biological processes, for example V(D)J recombination, the initiation of transcription, and DNA repair. ...http://www.biochemsoctrans.org/content/29/4/395
interspecies promoter evolution
In article ,2834 at alsys1.aecom.yu.edu,, ,burk at alsys1.aecom.yu.edu., writes: , There has been considerable interest and work on the evolution of , proteins between species. Does anyone know of work on analyses of , promoter sequences between species for a given gene? Not to blow my own horn too much. ;-} Take a look at my paper: Evolutionary Conserved Motifs and Protein Binding Elements in the 5' Region of the Chromosomal Protein HMG-14 Gene. DNA and Cell Biology, 12(8):753-761. IMHO, comparitive sequence analysis between promoter elements is the best way of identifying regions that important for promoter function ...http://www.bio.net/bionet/mm/mol-evol/1994-June/001719.html
Three distinct sub-nuclear populations of HMG-I protein of different properties revealed by co-localization image analysis |...
We have studied the nuclear distribution of the non-histone HMG-I protein by indirect immunofluorescence in several human and murine somatic cell lines and in growing mouse oocytes. We show that HMG-I, a high mobility-group protein which interacts in vitro with the minor groove of AT-rich B-DNA, is found exclusively in the nucleus and that this localization corresponds to a complex distribution. By comparing the HMG-I-dependent fluorescence signal with the chromatin density determined by Hoechst 33342 or propidium iodide staining, we present evidence for the existence of three HMG-I sub-populations whose contribution to the total fluorescence can be determined using a newly developed quantitative co-localization image analysis program: foci that correspond to regions of heterochromatin, intense dots located within decondensed chromatin, and a more diffuse component extending throughout the nucleoplasm. In addition, we show that these sub-populations differ ...http://jcs.biologists.org/content/111/23/3551
SPRINT==| Query Results
High mobility group (HMG)I proteins bind preferentially to the minor groove of A.T-rich regions in double-stranded DNA [1,2]. DNA-binding of these, and several related, proteins is effected by an 11-residue domain known as an A.T-hook . Within known HMG-I proteins are found three highly conserved regions, closely related to the consensus sequence TPKRPRGRPKK . A synthetic oligopeptide with this sequence specifically binds to substrate DNA in a manner reminiscent of intact HMG-I proteins. Structure predictions suggest that the peptide has a secondary structure similar to the anti-tumour and anti-viral drugs netropsin and distamycin, and to the dye Hoechst 33258 . These ligands, which also preferentially bind to A.T-rich DNA, effectively compete with both the synthetic peptide and the HMG-I proteins for DNA binding . The peptide also contains novel ...http://126.96.36.199/cgi-bin/dbbrowser/sprint/searchprintss.cgi?display_opts=Prints&category=None&queryform=false&prints_accn=PR00929
hmg-3 - FACT complex subunit ssrp1-B - Caenorhabditis elegans - hmg-3 gene & protein
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to double-stranded DNA (By similarity).http://www.uniprot.org/uniprot/O01683
amphoterin - oi
A high mobility group protein (HMGB1, 215 aa) considered a structural protein in chromatin. It can be released from endotoxin or cytokine-stimulated macrophages and is toxic (levels are high in patients with sepsis). It is bound by RAGE (receptor for advanced glycation end products ) and inhibition of the RAGE-amphoterin interaction suppresses various systems linked to tumour proliferation, invasion, and expression of matrix metalloproteinases. ...http://oxfordindex.oup.com/view/10.1093/oi/authority.20110803095409663
Update: Hepatoma derived growth factor in neurosurgery | Neurocirugia.com
Hepatoma derived growth factor Hepatoma-derived growth factor (HDGF) also known as high mobility group protein 1-like 2 (HMG-1L2) is a protein that in humans is encoded by the HDGF gene. Hepatoma-derived growth factor (HDGF), a potential predictive and prognostic marker in several human cancers, is the firstly reportedhttp://neurocirugia.com/2015/08/03/hepatoma-derived-growth-factor/
The high mobility group (HMG) proteins I and Y are well characterized nonhistone chromosomal proteins which bind to A·T-rich regions of DNA, and may regulate gene expression and/or DNA replication. We utilized a series of mouse mammary epithelial preneoplastic and tumor cell lines to explore the relationship between neoplastic transformation and HMG-I(Y) gene expression. The cell lines used in this study were originally derived from a single hyperplastic outgrowth, and exhibit a distinct gradient of preneoplastic to highly metastatic transformation states. We measured the levels of HMG-I(Y) gene expression in these cell lines during the different phases of cell growth in culture. At both subconfluent and confluent cell densities, elevated levels of HMG-I(Y) mRNA were directly correlated with the relative degree of neoplastic transformation and metastatic progression of these cells. HMG-I(Y) mRNA levels were ...http://cancerres.aacrjournals.org/content/53/11/2655
SRY-Box 18 - CAGS
The SOX18 gene localizes to the long arm of chromosome 20. It spans a length of about 3.3 Kb and encodes a protein of 468 amino acids. Like all other SOX genes, SOX18 also carries a characteristic conserved DNA sequence that codes for an approximately 80 amino acid DNA binding domain having homology with the High Mobility Group (HMG) box domain. Another vital domain in Sox18 is the transactivation domain, which is a 92 amino acid domain immediately C terminal of the HMG DNA binding region. Only a handful of mutations in SOX18 leading to HLTS are known. These include both missense as well as nonsense mutations. The missense mutations tend to affect the HMG box and result in a phenotype with a dominant mode of transmission. The nonsense mutations, on the other hand, tend to terminate the transactivation domain, and result in a phenotype that is transmitted in an autosomal recessive manner. ...http://cags.org.ae/ctga/details.aspx?id=2213
SRY-Box 18 - CAGS
The SOX18 gene localizes to the long arm of chromosome 20. It spans a length of about 3.3 Kb and encodes a protein of 468 amino acids. Like all other SOX genes, SOX18 also carries a characteristic conserved DNA sequence that codes for an approximately 80 amino acid DNA binding domain having homology with the High Mobility Group (HMG) box domain. Another vital domain in Sox18 is the transactivation domain, which is a 92 amino acid domain immediately C terminal of the HMG DNA binding region. Only a handful of mutations in SOX18 leading to HLTS are known. These include both missense as well as nonsense mutations. The missense mutations tend to affect the HMG box and result in a phenotype with a dominant mode of transmission. The nonsense mutations, on the other hand, tend to terminate the transactivation domain, and result in a phenotype that is transmitted in an autosomal recessive manner. ...http://cags.org.ae/ctga/details.aspx?id=2213&se=Latest