Stegastes_partitusFamily: KH_1 Number of Genes: 42
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
IGF2BP2
zgc:110045
khdrbs1b
nova1
-
qki2
-
igf2bp3
-
akap1b
MEX3D
fmr1
tdrkh
ddx43
hnrnpk
fxr2
KHSRP
NOVA1
khsrp
igf2bp1
hdlbpa
ankhd1
fubp1
fxr1
hnrpkl
mex3b
-
-
bicc1a
ascc1
PNPT1
bicc2
hdlbpb
pcbp2
qkia
KHDRBS3
-
fubp3
-
-
sf1
khdrbs1a
-
PCBP2 (1 of many)
-

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.