Ictalurus_punctatusFamily: RRM_1 Number of Genes: 227
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
rbfox1l
-
ralyl
rrp7a
poldip3
rbm5
cirbpb
-
tnrc6c1
-
celf5
RBM12B
CPEB2
G3BP
elavl4
Ppargc1b
rbms2a
msi1
-
-
hnrnpa1a
-
puf60a
igf2bp1
tra2b
rnpc3
srsf5a
g3bp2
SSB
msi2b
-
SRSF2
RBM15
rbm26
puf60b
rbm47
-
-
eif3g
tardbp
uhmk1
srsf9
cpeb4
-
-
syncripl
si:dkey-33c12.4
igf2bp3
dazl
cnot4
rbm8a
PPIL4
mthfsd
-
-
-
-
-
-
eif4b
dazap1
raver2
RBM3
rbm28
-
-
-
rbmx2
si:dkey-16l2.17
-
rbm41
setd1a
Rbm17
u2af2a
u2surp
-
-
hnrnpl
pprc1
PABPN1
celf3a
hnrnpr
rbm15b
ptbp1a
celf2
zgc:55733
srsf1b
snrpa
tsp1l
pabpc1a
u2af2
rbm14b
ptbp2a
rbm7
alyref
enox2
-
-
-
RBMS1
SLIRP
cpeb4a
a1cf
si:dkey-205h23.2
grsf1
dnd1
-
-
celf4
-
nol8
hnrnpc
scaf4
hnrnpll
srsf7
rnps1
rbfox3a
rbm39b
Sf3b4
rbm27
elavl2
RBPMS
pabpc1l
elavl3
SFPQ
raver1
pspc1
u2af1
snrnp70
RBPMS
elavl1a
rbm10
-
rbm12
RBMS1 (1 of many)
rbm24
rbfox1
syncrip
ptbp1
elavl1b
hnrnph3
snrnp35
nelfe
ewsr1b
ppie
pabpc4
tia1
trmt2a
srek1
SRSF6
-
rbfox2
cnot4b
zcrb1
-
srsf1a
srsf3
tut1
rbms3
-
htatsf1
cstf2
celf5b
rbm11
-
si:ch1073-335m2.2
HNRNPAB
hnrnph1
nono
eif3b
cpeb3
myef2
-
-
ptbp2b
srsf7a
hnrnpl
-
dnajc17
-
-
-
-
RBM45
zgc:163098
zgc:153215
rbm22
-
RO32
larp7
-
-
-
-
EIF4B
PTBP3
hnrnpab
ppargc1a
-
eif4h
RBPMS
zgc:77262
msi2a
sart3
-
rbm14a
tial1
RBMS2
boll
rbm18
si:dkey-93h22.8
spen
rbm34
rbfox3b
-
-
Igf2bp2
TRA2B (1 of many)
rbmx
enox1
-
rbm42
hnrnpa1b
-
-
-
tnrc6c2
rbm4.1
rbm4.2
RBM4B
-
-
sltm
PABPN1L
-
nifk
celf1
sf3b6
TARDBP
rbm19
rbm46
hnrnph1l
ewsr1a
-
-
-
-
snrpb2
-
-
ncl
-
rbm39
ncoa5
setd1b
safb2
hnrnpdl
hnrnpd
hnrnpm

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.