Mastacembelus_armatusFamily: KH_1 Number of Genes: 42
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
fmr1
igf2bp2b
-
igf2bp1
sf1
hnrnpk
hdlbpb
qki2
KHDRBS3
akap1b
khdrbs1b
fxr2
bicc2
-
qkia
fubp1
khdrbs1a
igf2bp3
hdlbpa
MEX3D
pcbp4
-
-
PCBP2
mex3b
-
ankhd1
-
khsrp
fxr1
fubp3
zgc:110045
khdrbs2
NOVA1
bicc1a
hnrpkl
-
ascc1
tdrkh
nova1
pcbp3
qkib
KHSRP
pcbp2

Introduction

Pfam

KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.

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

  1. Burd CG, Dreyfuss G; , Science 1994;265:615-621.: Conserved structures and diversity of functions of RNA-binding proteins. PUBMED:8036511 EPMC:8036511 .

  2. 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.