Search by BoMiProt ID - Bomi2688


Primary Information

BoMiProt ID Bomi2688
Protein Name Rhophilin-2
Organism Bos taurus
Uniprot IDA4FUC9
Milk FractionExosome
Ref Sequence ID NP_001076939.1
Aminoacid Length 686
Molecular Weight 77105
FASTA Sequence Download
Gene Name RHPN2
Gene ID 533687
Protein Existence Status Reveiwed:Experimental evidence at transcript level

Secondary Information

Protein Function RHPN2, a member of rhophilin family of rho-binding proteins, regulates actin cytoskeleton and vesicular trafficking, and promotes mesenchymal transformation in cancer. 
Biochemical Properties RHPN2 protein contains several protein interacting domains including an N-terminal HR-1,a centralBro1-like, and a C-terminal PDZ domains. The HR-1 domain binds to Rho GTPase, and the Bro1-like domain is required for its recruitment to the late endosome in the presence of activated RhoB. The PDZ domain mediates the interaction between RHPN2 and other proteins like KRT18, a component of cytoskeleton. 
PTMs Phosphorylation at Thr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments RHPN2 is overexpressed in tumors from LUAD( lung adenocarcinoma), and high levels of RHPN2 are associated with poor prognosis of LUAD patients.
Bibliography 1.Xiao D, He J, Guo Z, He H, Yang S, Huang L, Pan H, He J. Rhophilin-2 Upregulates Glutamine Synthetase by Stabilizing c-Myc Protein and Confers Resistance to Glutamine Deprivation in Lung Cancer. Front Oncol. 2021 Jan 20;10:571384. doi: 10.3389/fonc.2020.571384. PMID: 33552953; PMCID: PMC7855701. 2.Peck JW, Oberst M, Bouker KB, Bowden E, Burbelo PD. The RhoA-binding protein, rhophilin-2, regulates actin cytoskeleton organization. J Biol Chem (2002) 277(46):43924–32. 10.1074/jbc.M203569200. 3.Mircescu H, Steuve S, Savonet V, Degraef C, Mellor H, Dumont JE, et al. Identification and characterization of a novel activated RhoB binding protein containing a PDZ domain whose expression is specifically modulated in thyroid cells by cAMP. Eur J Biochem (2002) 269(24):6241–9. 10.1046/j.1432-1033.2002.03343.x