Paramormyrops_kingsleyaeFamily: KH_1 Number of Genes: 48
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
NOVA1
fmr1
fxr1
PCBP2 (1 of many)
hdlbpa
KHDRBS3
-
-
ddx43
khsrp
fubp3
KHSRP
nova2
-
-
hdlbpb
PCBP2 (1 of many)
-
-
ascc1
-
qkia
igf2bp2b
-
pcbp4
hnrpkl
qki2
-
khdrbs1a
sf1
-
igf2bp3
FXR1 (1 of many)
bicc2
MEX3C
akap1b
tdrkh
ankhd1
mex3b
MEX3D
pcbp3
-
-
-
PNPT1
hnrnpk
igf2bp1
khdrbs1b
fxr2
bicc1b

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.