Cynoglossus_semilaevisFamily: KH_1 Number of Genes: 44
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
khdrbs1a
ddx43
-
PNPT1
pcbp3
hdlbpb
hnrpkl
fxr1
qkia
tdrkh
akap1b
bicc1a
khdrbs2
mex3b
-
NOVA1
bicc2
-
-
hdlbpa
zgc:110045
PCBP2
khsrp
-
-
-
igf2bp2b
khdrbs1b
-
igf2bp3
hnrnpk
KHDRBS3
qki2
fxr2
igf2bp1
MEX3D
-
sf1
-
pcbp4
ankhd1
fmr1
-
-
ascc1
nova1
FUBP3
PCBP4
fubp1
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.