Amphiprion_ocellarisFamily: RRM_1 Number of Genes: 236
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
rbpms2b
-
rbm24a
-
rbm28
CPEB4 (1 of many)
scaf4a
eif4bb
-
-
si:dkey-205h23.2
celf1
-
-
-
enox2
ncbp2
-
RNPS1
-
SCAF8
tardbp
sltm
srsf10b
rbm5
sfpq
srsf9
eif4h
ncl
-
-
u2surp
-
setd1a
MSI1
-
hnrnpa3
rrp7a
poldip3
rbm7
-
tial1
MARF1
enox1
elavl3
raver1
pspc1
-
-
eif3g
puf60b
srsf5b
zgc:123010
taf15
snrpa
srsf4
-
rbm34
-
rbm39b
snrpb2
safb
slirp
ppargc1a
rbm18
rbm22
-
rbm45
snrnp35
-
RBPMS
celf3b
rbm4.3 (1 of many)
rbm4.3 (1 of many)
trnau1apa
-
si:ch1073-335m2.2
si:dkey-93h22.8
rbfox1
-
rbms2a
hnrnph1
zgc:163098
hnrnpm
rbm19
rbm42
rbm14b
-
-
dnd1
rbm26
pprc1
trmt2a
-
-
raly
-
rbms1a
-
-
rbm15b
-
scaf4b
-
-
-
-
cnot4a
zgc:153215
-
-
-
rbm4.1
eif3bb
-
-
ewsr1b
pabpc1a
snrnp70
trnau1apb
hnrnph3
-
dnajc17
setd1ba (1 of many)
CPSF7
rbfox3b
g3bp1
RBM38
hnrnpaba
zgc:165603
-
nifk
-
srsf7a
ptbp3
sf3b6
-
-
-
rbm25a
rbfox2
fus
-
alyref
rnpc3
igf2bp1
hnrnpd
syncrip
-
-
ppil4
cpeb2
-
msi2a
-
rbm17
srsf5a
sart3
-
cpeb3
tra2a
-
-
-
u2af2a
-
zcrb1
pabpn1
cpeb4a
-
-
-
-
-
larp7
cirbpa
rbm27
TRA2B
rbm15
igf2bp2b
ptbp2a
nelfe
-
-
mcm3ap
myef2
-
tnrc6c2
alkbh8
esrp2
ncoa5
cpsf6
syncripl
tia1l
brap
nono
-
-
rbm25b
-
-
-
-
ELAVL2
rbm12
dazl
sf3b4
ptbp1a
pabpc1b
PABPN1L
-
-
elavl1a
si:dkey-33c12.4
dazap1
tardbpl
ssb
celf3a
celf4
-
cstf2
rbm41
rbmx
rbfox1l
htatsf1
-
rbms3
ppie
srsf7b
-
pabpc4
-
srsf2a
tut1
-
-
-
srsf3b
rbm47
-
-
-
elavl4 (1 of many)
-
rbm10
elavl4 (1 of many)
-
-
-
a1cf
-
rbm24b
g3bp2
rbm8a
hnrnpr
tnrc6c1
zrsr2
-
-
rbms2b
rbm12b
-
-
-
-
-
-
srek1
uhmk1

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.