Astatotilapia_callipteraFamily: KH_1 Number of Genes: 42
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
igf2bp3
KHSRP
hnrpkl
khdrbs2
MEX3D
-
nova1
tdrkh
ankhd1
igf2bp1
-
khdrbs1a
ascc1
hdlbpb
fubp1
sf1
-
qkib
-
bicc2
-
fxr2
KHDRBS3
fubp3
pcbp3
khdrbs1b
pcbp4
igf2bp2a
-
hnrnpk
PCBP2
-
zgc:110045
bicc1a
khsrp
fmr1
akap1b
PNPT1
-
mex3b
fxr1
hdlbpa
ddx43
qki2

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.