EuRBPDB

Mus_musculus_dba2jFamily: KH_2 Number of Genes: 10

Ensembl ID	Symbol	Entrez ID
MGP_DBA2J_G0017228	Pcbp3	-
MGP_DBA2J_G0018594	Eral1	-
MGP_DBA2J_G0019545	Nova1	-
MGP_DBA2J_G0020465	Hnrnpk	-
MGP_DBA2J_G0022248	Pcbp2	-
MGP_DBA2J_G0023776	Khsrp	-
MGP_DBA2J_G0025431	Fubp3	-
MGP_DBA2J_G0027804	Fubp1	-
MGP_DBA2J_G0032370	Rps3	-
MGP_DBA2J_G0035044	Pcbp4	-

Introduction

Pfam

No Pfam abstract.

InterPro

The K homology (KH) domain was first identified in the human heterogeneous nuclear ribonucleoprotein (hnRNP) K. It is a domain of around 70 amino acids that is present in a wide variety of quite diverse nucleic acid-binding proteins [PUBMED:8036511]. It has been shown to bind RNA [PUBMED:9302998, PUBMED:10369774]. Like many other RNA-binding motifs, KH motifs are found in one or multiple copies (14 copies in chicken vigilin) and, at least for hnRNP K (three copies) and FMR-1 (two copies), each motif is necessary for in vitro RNA binding activity, suggesting that they may function cooperatively or, in the case of single KH motif proteins (for example, Mer1p), independently [PUBMED:8036511].

Reference

Burd CG, Dreyfuss G; , Science 1994;265:615-621.: Conserved structures and diversity of functions of RNA-binding proteins. PUBMED:8036511 EPMC:8036511 .
Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A; , Cell 1996;85:237-245.: Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. PUBMED:8612276 EPMC:8612276.