Maylandia_zebraFamily: KH_1 Number of Genes: 45
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
-
bicc2
akap1b
khdrbs1b
hnrpkl
ascc1
KHDRBS3
mex3b
qkia
hnrnpk
qki2
-
fmr1
khdrbs2
PCBP2
tdrkh
FXR2
dcaf15
igf2bp2a
pcbp4
pcbp3
igf2bp3
sf1
hdlbpa
KHSRP
zgc:110045
-
fxr1
-
qkib
hdlbpb
-
-
igf2bp1
nova1
-
fubp1
-
MEX3D
pcbp2
-
-
khdrbs1a
ddx43
PNPT1
bicc1a
fxr2

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.