Poecilia_formosaFamily: RRM_1 Number of Genes: 228
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
rbm24b (1 of many)
rbm24b (1 of many)
larp7
enox1
nifk
srsf3b
-
cpeb4a
rbm41
poldip3
-
rrp7a
-
zgc:123010
rbm46
-
ppargc1a
srsf4
si:dkey-93h22.8
eif3bb
ptbp3
alkbh8
-
myef2
-
-
-
-
-
enox2
nol8
eif4bb
rbm7
cnot4a
dazap1
ppie
hnrnpd
-
pabpc4
rbms2a
rbms2b
nelfe
rbm27
sfpq
scaf4b
-
celf5a
dazl
pspc1
ELAVL2
-
rbm14b
CPEB4 (1 of many)
trnau1apb
hnrnph1
ppil4
SCAF8
srsf10b
tardbpl
-
sltm
-
g3bp2
eif4h
elavl4
-
-
rbm10
-
-
-
rbm22
ptbp2b
-
-
sf3b4
pabpc1b
igf2bp3
-
grsf1
-
-
-
srsf6a
-
rbm45
a1cf
slirp
rbm4.3 (1 of many)
rbm4.3 (1 of many)
cpsf6
PABPN1L
-
raver1
TRA2B
-
-
igf2bp2b
-
ewsr1b
rbm42
safb
elavl3
htatsf1
-
hnrnpr
g3bp1
rbm47
trnau1apa
hnrnpaba
-
naa25
celf3a
srsf7b
celf4 (1 of many)
-
si:dkey-33c12.4
celf4 (1 of many)
-
rbfox1l
raver2
-
-
-
-
ssb
ELAVL1
tial1
-
rnpc3
RNPS1
sart3
pabpn1
ptbp1a
rbm8a
dnajc17
u2af2a
pabpc1a
snrpa
trmt2a
snrpb2
-
cpeb3
-
tnrc6c2
-
rbm38
-
zgc:163098
-
sf3b6
tnrc6c1
-
rbm4.1
-
rbm15
-
REXO5
-
-
mcm3ap
-
MSI1
rbm24a
rbmx
rbm39b
pabpc1l
rbm17
celf3b
ncoa5
hnrnpm
setd1a
-
hnrnpa3
elavl1a
rbfox2
-
syncripl
ncbp2
u2surp
pprc1
rbm15b
-
rbm19
HNRNPH3
-
rbm26
zcrb1
cirbpa
uhmk1
rbpms2b
rbms1a
tardbp
tut1
-
nono
-
si:dkey-205h23.2
snrnp70
rbm5 (1 of many)
CSTF2T
-
-
rbm5 (1 of many)
-
-
-
-
-
scaf4a
-
RBPMS
-
zrsr2
zgc:153215
-
RBMS1 (1 of many)
srsf5b
srsf7a
rbms3
rbm25a
-
si:ch1073-335m2.2
-
rbm28
rbfox3b
-
cpeb2
rbm25b
-
puf60b
MSI2 (1 of many)
igf2bp1
rbm18
setd1ba
srsf9
snrnp35
srsf2a
-
-
-
rbm12b
-
-
-
RALYL
-
tia1l
hnrnpl
-
-
-
taf15
alyref
srsf5a
eif3g
rbm12
-
-
rbm4.3 (1 of many)
ncl
-
-
-
-

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.