Carlito_syrichtaFamily: KH_1 Number of Genes: 34
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
FUBP1
HNRNPK
FXR1
HDLBP
-
IGF2BP2
DDX43
IGF2BP1
KHDRBS3
BICC1
FXR2
ANKRD17
KHDRBS1
PCBP3
-
PNPT1
KHDRBS2
-
PCBP4
PCBP2
TDRKH
KHSRP
-
ASCC1
IGF2BP3
NOVA1
FMR1
MEX3B
-
MEX3A
-
PCBP1
FUBP3
-
-
-
-
-
-
SF1
-
-
-
QKI

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.