Gambusia_affinisFamily: RRM_1 Number of Genes: 212
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
rbms3
-
rbmx2
-
-
-
-
-
snrpb2
-
rbm7
-
rbm25b
-
tial1
-
rbm15
-
-
-
-
-
-
-
rbm14b
-
rbm4.3
-
enox2
-
srsf7a
-
hnrnpl
-
dtwd2
-
nelfe
-
rbms2a
-
ssb
-
celf5a
-
srsf5b
-
rbpms2b
-
htatsf1
-
-
-
snrnp70
-
-
-
-
-
rbm45
-
hnrnpd
-
hnrnpr
-
u2surp
-
HNRNPA3
-
celf3a
-
-
-
-
-
-
-
grsf1
-
CPEB4 (1 of many)
-
rbm28
-
-
-
trnau1apa
-
-
-
rbm27
-
rbfox3b
-
HNRNPH3
-
RNPS1
-
brap
-
-
-
enox1
-
srsf2a
-
myef2
-
-
-
rbm24b
-
alyref
-
hnrnph1
-
pspc1
-
trmt2a
-
cpeb4a
-
trnau1apb
-
ptbp2b
-
-
-
-
-
msi2a
-
taf15
-
rbm12b
-
-
-
RBMS1 (1 of many)
-
-
-
rbm18
-
syncripl
-
zgc:153215
-
-
-
eif4bb
-
hnrnpaba
-
rbfox2
-
raver2
-
tut1
-
rbm22
-
cirbpa
-
setd1ba
-
srsf7b
-
rbm42
-
-
-
srsf9
-
-
-
esrp2
-
sf3b6
-
zgc:123010
-
ppil4
-
rbms2b
-
alkbh8
-
TRA2B
-
-
-
sf3b4
-
pabpc1b
-
ncbp2
-
si:dkey-205h23.2
-
igf2bp2b
-
mcm3ap
-
rbm5
-
rbm24a
-
slirp
-
REXO5
-
tardbp
-
rbm41
-
si:dkey-93h22.8
-
-
-
-
-
nono
-
nifk
-
-
-
PTBP1
-
rbms1a
-
setd1a
-
rbm26
-
rbm19
-
snrpa
-
PABPN1L
-
-
-
celf3b
-
rbfox1l
-
-
-
u2af2a
-
hnrnpm
-
-
-
-
-
sfpq
-
srsf10b
-
a1cf
-
-
-
ncl
-
larp7
-
ppargc1a
-
-
-
eif3g
-
raver1
-
elavl4
-
elavl3
-
safb
-
-
-
uhmk1
-
ELAVL2
-
RBPMS
-
g3bp2
-
-
-
-
-
-
-
-
-
-
-
-
-
pabpn1
-
-
-
rnpc3
-
zcrb1
-
-
-
poldip3
-
dnajc17
-
si:dkey-33c12.4
-
rbm34
-
-
-
dazl
-
SCAF8
-
rbm25a
-
sart3
-
ppie
-
pabpc4
-
srsf5a
-
ewsr1b
-
rbm15b
-
-
-
srsf4
-
RALYL
-
eif4h
-
ptbp1a
-
-
-
tnrc6c1
-
srsf6a
-
-
-
elavl1a
-
tardbpl
-
cpeb2
-
-
-
rbm4.1
-
scaf4a
-
-
-
dnd1
-
-
-
pabpc1a
-
g3bp1
-
rbm17
-
rbmx
-
-
-
cstf2
-
-
-
rbm46
-
-
-
-
-
rbm47
-
-
-
puf60b
-
pabpc1l
-
rbm39b
-
-
-
SRSF11 (1 of many)
-
celf4
-
MSI1
-
si:ch1073-335m2.2
-
srsf3b
-
-
-
rbm8a
-

Introduction

Pfam

The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.

InterPro

Many eukaryotic proteins containing one or more copies of a putative RNA-binding domain of about 90 amino acids are known to bind single-stranded RNAs [PUBMED:3072706, PUBMED:3192525, PUBMED:3313012]. The largest group of single strand RNA-binding proteins is the eukaryotic RNA recognition motif (RRM) family that contains an eight amino acid RNP-1 consensus sequence [PUBMED:2470643, PUBMED:2467746]. RRM proteins have a variety of RNA binding preferences and functions, and include heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing (SR, U2AF, Sxl), protein components of small nuclear ribonucleoproteins (U1 and U2 snRNPs), and proteins that regulate RNA stability and translation (PABP, La, Hu) [PUBMED:3192525, PUBMED:3313012, PUBMED:2467746]. The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor (U2AF) appears to have two RRM-like domains with specialised features for protein recognition [PUBMED:15231733]. The motif also appears in a few single stranded DNA binding proteins.

Reference

  1. Birney E., Kumar S., Krainer A.R. , Nucleic Acid Res 1993;21:5803-5816.: Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. PUBMED:8290338 EPMC:8290338.