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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 03 Oct 2014.

High mobility group box 3

HMGB3, HMG4, HMG2a
HMGB3 belongs to the high mobility group (HMG) protein superfamily. Like HMG1 (MIM 163905) and HMG2 (MIM 163906), HMGB3 contains DNA-binding HMG box domains and is classified into the HMG box subfamily. Members of the HMG box subfamily are thought to play a fundamental role in DNA replication, nucleosome assembly and transcription (Wilke et al., 1997 [PubMed 9370291]; Nemeth et al., 2006 [PubMed 16945912]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: HMG2, HMGB1, ACID, HAD, iMpact
Papers on HMGB3
Characterization of spermatogonial markers in the mature testis of the dogfish (Scyliorhinus canicula L.).
New
Sourdaine et al., Caen, France. In Reproduction, Jan 2014
Moreover, hmgb3 and mcm6 have been identified as new markers of differentiated spermatogonia.
Two novel homologs of high mobility group box 3 gene in grass carp (Ctenopharyngodon idella): potential roles in innate immune responses.
New
Rao et al., Taiwan. In Fish Shellfish Immunol, Nov 2013
High mobility group box 3 (HMGB3) protein is a universal sentinel in the activation of innate antiviral immune responses in mammalian cells of limited tissues.
Prognostic value of HMGB3 expression in patients with non-small cell lung cancer.
New
Zhang et al., Shijiazhuang, China. In Tumour Biol, Oct 2013
HMGB3 overexpression has been reported in a variety of human cancers.
Localization and functional analysis of HmgB3p, a novel protein containing high-mobility-group-box domain from Tetrahymena thermophila.
New
Liang et al., Taiyuan, China. In Gene, Oct 2013
In this study, we identified the gene HMGB3 in Tetrahymena thermophila.
Multiple promoters and targeted microRNAs direct the expressions of HMGB3 gene transcripts in dairy cattle.
New
Zhong et al., Jinan, China. In Anim Genet, Jun 2013
HMGB3 (high-mobility group box 3) is an X-linked member of a family of sequence-independent chromatin-binding proteins and functions as a universal sentinel for nucleic acid-mediated innate immune responses.
High mobility group-box 3 overexpression is associated with poor prognosis of resected gastric adenocarcinoma.
Wu et al., Zhenjiang, China. In World J Gastroenterol, 2013
AIM: To elucidate high mobility group-box 3 (HMGB3) protein expression in gastric adenocarcinoma, its potential prognostic relevance, and possible mechanism of action.
Tumor suppressive function of mir-205 in breast cancer is linked to HMGB3 regulation.
Schmittgen et al., Columbus, United States. In Plos One, 2012
Two predicted binding sites for miR-205 were identified in the 3' untranslated region of the high mobility group box 3 gene, HMGB3.
HMGB3 characterization in gastric cancer.
Wu et al., Beijing, China. In Genet Mol Res, 2012
However, HMGB3 has been little studied.
High mobility group B proteins regulate mesoderm formation and dorsoventral patterning during zebrafish and Xenopus early development.
Shi et al., Jinan, China. In Mech Dev, 2012
Overexpression of hmgb3 blocks the expression of the pan-mesoderm gene no tail/Xbra and other ventrolateral mesoderm genes, and results in embryos with shortened anteroposterior axis, while overexpression of hmgb3EnR, which contains the engrailed repressor domain, most potently repressed no tail expression and mesoderm formation.
Regulation of transcription factor Twist expression by the DNA architectural protein high mobility group A2 during epithelial-to-mesenchymal transition.
GeneRIF
Moustakas et al., Uppsala, Sweden. In J Biol Chem, 2012
Regulation of transcription factor Twist expression by the DNA architectural protein high mobility group A2 during epithelial-to-mesenchymal transition.
Proteomic profiling of the human T-cell nucleolus.
Gautier et al., Dublin, Ireland. In Mol Immunol, 2011
Furthermore, among our dataset, we identified proteins known to functionally participate in T-cell biology, including RUNX1, ILF3, ILF2, STAT3, LSH, TCF-1, SATB1, CTCF, HMGB3, BCLAF1, FX4L1, ZAP70, TIAM1, RAC2, THEMIS, LCP1, RPL22, TOPK, RETN, IFI-16, MCT-1, ISG15, and 14-3-3τ, which support cell-specific composition of the Jurkat nucleolus.
The HMGB protein gene family in zebrafish: Evolution and embryonic expression patterns.
Beltrame et al., Milano, Italy. In Gene Expr Patterns, 2011
In mammals, three family members are present: HMGB1, HMGB2 and HMGB3.
Nucleocytoplasmic distribution of the Arabidopsis chromatin-associated HMGB2/3 and HMGB4 proteins.
GeneRIF
Grasser et al., Aalborg, Denmark. In Plant Physiol, 2010
results show that, in contrast to other Arabidopsis HMGB proteins such as HMGB1 and HMGB5, the HMGB2/3 and HMGB4 proteins occur preferentially in the cell nucleus, but to various extents also in the cytoplasm
Sumoylation controls retinal progenitor proliferation by repressing cell cycle exit in Xenopus laevis.
Furukawa et al., Suita, Japan. In Dev Biol, 2010
Ubc9 physically and functionally associates with Xenopus hmgb3, which is required for retinal cell proliferation, and prolonged expression of ubc9 and hmgb3 results in suppression of the cell cycle exit of retinal progenitors in a sumoylation-dependent manner.
Secreted phosphoprotein 1 upstream invasive network construction and analysis of lung adenocarcinoma compared with human normal adjacent tissues by integrative biocomputation.
Wolfl et al., Beijing, China. In Cell Biochem Biophys, 2010
SPP1 skeletal development module appears in human normal adjacent tissues (COL11A1_1 activation; COL10A1 inhibition), whereas in lung adenocarcinoma (COL11A1_2, COL1A2 activation); signal module appears in human normal adjacent tissues (COL11A1_1, CXCL13, MMP11, SPINK1 activation; COL10A1, COL3A1 inhibition), whereas in lung adenocarcinoma (COL11A1_2, COL1A2, MMP12 activation; CDH3, CXCL13, GREM1_2, MMP11, SPINK1 inhibition); biological regulation module appears in human normal adjacent tissues (CXCL13, MKI67, PYCR1 activation; NEK2, SPDEF, TOP2A_2, TOX3_1 inhibition), whereas in lung adenocarcinoma (HMGB3, MKI67, NMU, PYCR1, TOX3_2 activation; CXCL13, SPDEF, TOP2A_2 inhibition); sequence variant module appears in human normal adjacent tissues (COL11A1_1, MKI67, MMP11 activation; ASPM, COL10A1, COL3A1, NEK2, TMPRSS4, TOP2A_2 inhibition), whereas in lung adenocarcinoma (COL11A1_2, COL1A2, HMMR, MKI67, MMP12 activation; ABCC3, ASPM, CDH3, MMP11, TOP2A_2 inhibition).
Photoaffinity isolation and identification of proteins in cancer cell extracts that bind to platinum-modified DNA.
Lippard et al., Cambridge, United States. In Chembiochem, 2009
Proteins identified in this manner include the DNA repair factors RPA1, Ku70, Ku80, Msh2, DNA ligase III, PARP-1, and DNA-PKcs, as well as HMG-domain proteins HMGB1, HMGB2, HMGB3, and UBF1.
Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens.
Grasser et al., Aalborg, Denmark. In Gene, 2008
The structurally similar HMGB2 and HMGB3 proteins display the typical overall structure of higher plant HMGB proteins consisting of a central HMG-box DNA-binding domain that is flanked by a basic N-terminal and an acidic C-terminal domain.
Hmgb3 regulates the balance between hematopoietic stem cell self-renewal and differentiation.
GeneRIF
Bodine et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2006
Hmgb3 is required for the proper balance between hematopoietic stem cell self-renewal and differentiation.
Nucleosome regulator Xhmgb3 is required for cell proliferation of the eye and brain as a downstream target of Xenopus rax/Rx1.
GeneRIF
Furukawa et al., Suita, Japan. In Dev Biol, 2006
Xhmgb3 is required for cell proliferation of the eye and brain as a downstream target of Xenopus rax/Rx1.
Hmgb3 deficiency deregulates proliferation and differentiation of common lymphoid and myeloid progenitors.
GeneRIF
Bodine et al., Bethesda, United States. In Blood, 2005
Hmgb3 deficiency leads to a failure of hematopoietic stem cells to expand into normal numbers of lymphoid progenitor and myeloid progenitors
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