Acanthochromis_polyacanthusFamily: RRM_1 Number of Genes: 230
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
-
fus
-
-
rbm27
rbm39b
-
syncrip
PABPN1L
-
rbm24b
srsf6a
-
alkbh8
celf3b
raly
-
si:dkey-93h22.8
ppie
pabpc4
slirp
hnrnpm
msi2a
puf60b
-
-
tia1
-
rbm18
-
elavl1a
-
eif3bb
-
tardbp
-
raver2
scaf4a
rbm4.3 (1 of many)
celf4
rbm4.3 (1 of many)
MSI1
rbfox1
rbm38
HNRNPA0 (1 of many)
-
-
HNRNPA0 (1 of many)
-
-
ssb
cpeb3
hnrnpa3 (1 of many)
-
hnrnpa3 (1 of many)
-
rbm34
igf2bp2a
TRA2B
celf5a
cirbpa
-
rbfox2
dazl
-
RALYL
-
si:dkey-33c12.4
nifk
zgc:163098
cstf2
ppil4
-
celf3a
ncoa5
hnrnpd
hnrnpr
rbmx
ewsr1b
cpeb4a
hnrnpc
-
-
tia1l
rbm17
TRNAU1AP
-
-
sart3
-
-
rbms3
rbpms2b
srsf2b
a1cf
nelfe
REXO5
-
-
srsf5b
-
zgc:153215
-
-
-
hnrnpaba
rbm46
-
rbm45
-
ptbp1a
rbm8a
-
htatsf1
-
-
trnau1apb
rbm22
-
-
rbm19
ptbp2a
pabpc1l
rbm47
u2surp
eif4h
-
si:ch1073-335m2.2
sltm
rbm4.1
-
-
CPEB4 (1 of many)
grsf1
dnajc17
zcrb1
rbm7
tardbpl
pprc1
syncripl
srsf10b
srsf9
rbms1a
rbm12b
enox2
rbms2b
rbm15b
-
rbm26
-
larp7
-
-
-
-
-
setd1ba
myef2
pabpc1a
rbm42
snrpb2 (1 of many)
-
rbm25b
trmt2a
rbm28
SCAF8
tial1
-
-
pspc1
mcm3ap
ncbp2
-
-
cnot4a
rbfox1l
uhmk1
tut1
pabpn1
snrpa
hnrnph1
rbm5
-
-
-
PTBP3
MARF1
raver1
RNPS1
rnpc3
igf2bp3
srsf5a
tra2a
-
elavl3
-
sf3b4
eif3g
rbm25a
pabpc1b
srsf3b
setd1a
-
rbm10
ALYREF
rbmx2
-
ppargc1a
rbm15
si:dkey-205h23.2
g3bp1
-
-
rbm24a
scaf4b
zgc:123010
tnrc6c1
enox1
srsf4
-
elavl4
-
-
lin7b
-
poldip3
rrp7a
-
rbfox3b
-
-
rbm14b
hnrnph3
zgc:103564
-
dazap1
-
-
ELAVL2
RBPMS
-
safb
eif4bb
cpeb2
u2af2a
-
rbms2a
nono
-
-
hnrnpl2
srsf7a
srek1
-
sf3b6
ncl
celf1
HNRNPLL
-
snrpb2 (1 of many)
-
sfpq
g3bp2
srsf2a
-
-
-

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.