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Rhomboid, veinlet-like 2

RHBDL2
The protein encoded by this gene is a member of the rhomboid family of integral membrane proteins. This family contains proteins that are related to Drosophila rhomboid protein. Members of this family are found in both prokaryotes and eukaryotes and are thought to function as intramembrane serine proteases. The encoded protein is thought to release soluble growth factors by proteolytic cleavage of certain membrane-bound substrates, including ephrin B2 and ephrin B3. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: Epidermal Growth Factor, thrombomodulin, EGFR, Inactive, PARL
Papers on RHBDL2
Rhomboid family gene expression profiling in breast normal tissue and tumor samples.
Abba et al., La Plata, Argentina. In Tumour Biol, 2014
In addition, we found that RHBDL2 and PARL mRNA expression was associated with a low/intermediate histologic tumor grade (p = 0.024 and p = 0.015, respectively).
RHBDL2 is a critical membrane protease for anoikis resistance in human malignant epithelial cells.
Wu et al., Kao-hsiung, Taiwan. In Scientificworldjournal, 2013
Rhomboid-like-2 (RHBDL2), an evolutionally conserved intramembrane serine protease, can cleave the EGF ligand and thus trigger EGFR activation.
Rhomboid proteins: a role in keratinocyte proliferation and cancer.
Review
Blaydon et al., London, United Kingdom. In Cell Tissue Res, 2013
EGF is moreover a substrate of RHBDL2, their active Rhomboid relative.
Evaluating GWAS-identified SNPs for age at natural menopause among chinese women.
Long et al., Nashville, United States. In Plos One, 2012
Eight SNPs were nominally statistically significant with P≤0.05: rs4246511 (RHBDL2), rs12461110 (NLRP11), rs2307449 (POLG), rs12611091 (BRSK1), rs1172822 (BRSK1), rs365132 (UIMC1), rs2720044 (ASH2L), and rs7246479 (TMEM150B).
Functions of rhomboid family protease RHBDL2 and thrombomodulin in wound healing.
GeneRIF
Wu et al., Tainan City, Taiwan. In J Invest Dermatol, 2011
Thrombomodulin and RHBDL2 are upregulated in human HaCaT cells stimulated by scratch wounds; furthermore, increased solulbe thrombomodulin was found in culture medium.
Mammalian EGF receptor activation by the rhomboid protease RHBDL2.
GeneRIF
Freeman et al., Cambridge, United Kingdom. In Embo Rep, 2011
RHBDL2 cleaves epidermal growth factor just outside its transmembrane domain, thereby facilitating its secretion and triggering activation of the epidermal growth factor receptor.
The processing of human rhomboid intramembrane serine protease RHBDL2 is required for its proteolytic activity.
GeneRIF
Li et al., New York City, United States. In J Mol Biol, 2010
Here, the authors show that RHBDL2 is produced as a proenzyme and that the processing of RHBDL2 is required for its cellular protease activity.
Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2.
GeneRIF
Brown et al., Cambridge, United Kingdom. In Biochem Biophys Res Commun, 2004
The encoded protein is thought to release soluble growth factors by proteolytic cleavage of certain membrane-bound substrates, including ephrin B2 and ephrin B3.
Diverse substrate recognition mechanisms for rhomboids; thrombomodulin is cleaved by Mammalian rhomboids.
Freeman et al., Cambridge, United Kingdom. In Curr Biol, 2004
The thrombomodulin transmembrane domain (TMD) is cleaved only by vertebrate RHBDL2-like rhomboids.
Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain.
GeneRIF
Freeman et al., Cambridge, United Kingdom. In Mol Cell, 2003
Substrate specificity of RHBDL2 intramembrane protease is governed by helix-breaking residues in the transmembrane domain.
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