Kryptolebias_marmoratusFamily: KH_1 Number of Genes: 42
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
-
-
bicc1a
khdrbs1b
pcbp3
fxr1
sf1
-
-
fmr1
MEX3D
-
hdlbpa
qki2
bicc2
-
qkia
-
PCBP2
igf2bp2b
hnrpkl
akap1b
nova1
pcbp4
fxr2
ascc1
khdrbs1a
-
-
-
ddx43
-
hdlbpb
tdrkh
igf2bp1
fubp3
-
PNPT1
-
khdrbs2
-
khsrp
ankhd1
fubp1
igf2bp3
hnrnpk
-
MEX3B

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.