Chrysemys_picta_belliiFamily: zf-CCCH Number of Genes: 33
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
ZC3H15
U2AF1L4
-
ZC3H4
-
ZFP36L2
TOE1
ZC3H7A
ZMAT5
-
-
HELZ
RC3H2
-
-
MKRN1
ZRSR2
-
ZC3H10
-
U2AF1
PARP12
RC3H1
-
-
ZFP36
MBNL1
PPP1R10
ZC3H3
ZC3H7B
CPSF4
ZFP36L1
MBNL2
DHX57
MBNL3
MKRN2
-
UNK

Introduction

Pfam

No Pfam abstract.

InterPro

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [PUBMED:10529348, PUBMED:15963892, PUBMED:15718139, PUBMED:17210253, PUBMED:12665246]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [PUBMED:11179890]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

Reference

  1. No References