InterPro : IPR006861

Name  Hyaluronan/mRNA-binding protein Short Name  HABP4_PAIRBP1-bd
Type  Domain Description  This entry includes the HABP4 protein family of hyaluronan-binding proteins, and the PAI-1 mRNA-binding protein, PAI-RBP1. HABP4 has been observed to bind hyaluronan (a glucosaminoglycan), but it is not known whether this is its primary role in vivo. It has also been observed to bind RNA, but with a lower affinity than that for hyaluronan []. PAI-1 mRNA-binding protein specifically binds the mRNA of type-1 plasminogen activator inhibitor (PAI-1), and is thought to be involved in regulation of mRNA stability []. However, in both cases, the sequence motifs predicted to be important for ligand binding are not conserved throughout the family, so it is not known whether members of this family share a common function.Hyaluronan/mRNA-binding protein may be involved in nuclear functions such as the remodeling of chromatin and the regulation of transcription [, ].
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Proteins

InterPro protein domain ID --> Contigs

 

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4 Publications

First Author Title Year Journal Volume Pages
Huang L Molecular characterization of a novel intracellular hyaluronan-binding protein. 2000 J Biol Chem 275 29829-39
Heaton JH Identification and cDNA cloning of a novel RNA-binding protein that interacts with the cyclic nucleotide-responsive sequence in the Type-1 plasminogen activator inhibitor mRNA. 2001 J Biol Chem 276 3341-7
Nery FC Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by phorbol 12-myristate 13-acetate-activated protein kinase C. 2004 J Biol Chem 279 11444-55
Nery FC Evidence for the interaction of the regulatory protein Ki-1/57 with p53 and its interacting proteins. 2006 Biochem Biophys Res Commun 341 847-55



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)