Esox_luciusFamily: RRM_1 Number of Genes: 245
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
snrnp35
-
rbfox2
-
mcm3ap
-
rbm15b
nono
rbm22
msi2b
si:ch1073-296d18.1
-
-
-
rbm39b
pabpc1l
si:dkey-33c12.4
u2surp
rnpc3
-
srsf3a
ptbp2a
dnd1
SCAF8
rbms3
-
rbm26
a1cf
ppie
pabpc4
hnrnpd
ptbp1b
hnrnpdl
-
rbmx
uhmk1
pabpc1a
myef2
pspc1
HNRNPLL (1 of many)
-
-
-
-
-
-
rbm14b
dnajc17
-
-
cpeb4a
-
-
htatsf1
-
cpeb2
nelfe
tra2a
-
-
rbm18
igf2bp3
ncl
-
celf3a
rbm47
dazl
tia1
rbm17
hnrnpr
puf60b
ptbp1a
hnrnph1
-
-
trmt2a
rbm24a
tnrc6c2
-
-
celf5b
rbm41
-
nifk
si:ch1073-335m2.2
rbm25b
srsf10b
rbms2b
enox1
elavl1a
elavl4
-
rbm46
srek1
-
cnot4a
-
poldip3
rrp7a
zgc:153215
tardbp
-
rbpms
-
-
cirbpa
scaf4a
ELAVL2
dazap1
sf3b6
-
igf2bp2a
-
tra2b
-
raly
tut1
cnot4b
-
msi2a
snrpb2
eif4bb
u2af1
rbm8a
eif4ba
rbm19
SRSF9 (1 of many)
sf3b4
sart3
rbfox1
-
rbm4.1
tardbpl
sltm
celf3b
SRSF6 (1 of many)
syncripl
ewsr1b
ptbp3
RO21
SRSF3
-
-
-
-
RBM15 (1 of many)
HNRNPR
snrpa
ppargc1b
igf2bp1
RNPS1
-
ncoa5
-
rbfox1l
nol8
-
larp7
-
-
hnrnpaba
g3bp2
rbm34
PTBP2 (1 of many)
u2af2a
taf15
rbm15
-
si:dkey-205h23.2
syncrip
trnau1apb
enox2
slirp
-
srsf7a
-
eif4h
ppargc1a
SRSF10
alyref
hnrnpl2
-
srsf4
-
srsf2b
trnau1apa
rbm7
rbfox3b
zgc:163098
srsf7b
HNRNPLL (1 of many)
pigs
PABPN1L
hnrnph3
-
-
ppil4
-
rbms1a
ncbp2
celf5a
cpeb3
RBMS1 (1 of many)
-
cirbpb
-
osbp2
rbms2a
rbm10
srsf5b
-
setd1a
rbm39a
srsf5a
rbm28
hnrnpabb
setd1ba
zcrb1
-
ssb
-
tial1
hnrnpm
-
-
-
srsf1a
pprc1
srsf9
eif3bb
rbpms2b
rbm25a
-
zgc:123010
rbm4.3 (1 of many)
rbm4.3 (1 of many)
rbm4.3 (1 of many)
g3bp1
u2af2b
safb
raver2
rbm42
rbm5
pabpn1
-
-
-
CPEB4 (1 of many)
-
-
elavl3
hnrnpa3
sfpq
rbm27
celf1
MSI1
rbm45
-
raver1
srsf2a
rbm14a
eif3g
RBPMS
srsf11
-
SRSF6 (1 of many)
-

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.