Ictalurus_punctatusFamily: KH_1 Number of Genes: 40
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
igf2bp1
HDLBP
akap1b
zgc:110045
-
zgc:110045
-
qkia
khdrbs3
igf2bp3
mex3a
pcbp3
khsrp
pcbp4
bicc1
bicc2
HNRNPK
tdrkh
fubp1
ascc1
qki
hdlbp
-
-
Khdrbs1
fmr1-b
PNPT1
qki2
khdrbs2
hnrpkl
nova1
FUBP3
MEX3D
-
nova2
khdrbs1a
ankhd1
Igf2bp2
sf1
fxr2
mex3b
ddx43
fxr1
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.