Seriola_dumeriliFamily: KH_1 Number of Genes: 44
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
KHDRBS3
khdrbs1b
-
KHSRP
khsrp
bicc2
sf1
igf2bp3
-
-
fubp1
-
ankhd1
khdrbs1a
pcbp3
qkib
-
mex3b
tdrkh
qki2
fmr1
-
MEX3D
-
qkia
fxr1
bicc1a
igf2bp2b
pcbp4
-
fxr2
PNPT1
PCBP2 (1 of many)
zgc:110045
-
akap1b
ascc1
ddx43
hdlbpb
nova1
pcbp2
hnrnpk
-
hdlbpa
igf2bp1
fubp3
khdrbs2
hnrpkl

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.