Pygocentrus_nattereriFamily: RRM_1 Number of Genes: 231
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
-
rbfox2
rbms2a
hnrnph1
hnrnpaba
hnrnph3
igf2bp3
tra2a
-
rnpc3
-
sf3b4
msi2b
syncripl
raver2
-
taf15
rbfox1l
u2surp
rbms3
eif4h
sart3
rbm14b
tardbp
celf5a
sfpq
ppil4
hnrnpl
brap
alyref
rbm4.1
rbm34
mcm3ap
rbm22
hnrnph1l
rbfox3a
tra2b
rbm26
tial1
rbm41
srsf9
elavl3
rbm24a
cpeb1a
srek1
rbpms2b
ncbp2
htatsf1
ncl
celf4
celf2
eif4ba
cpeb2
ppie
-
hnrnpl2
rbm15
zgc:123010
a1cf
hnrnpa1a
-
rbm39b
rbm39a
rbm47
rbm12b
nono
slirp
cnot4b
sf3b6
ewsr1a
rbm11
-
-
-
rbm42
-
rbms1a
cpeb4a
ppargc1a
srsf3b
srsf2a
rbm38
elavl1a
rbm10
igf2bp2b
TRA2B
srsf5b
uhmk1
si:ch1073-335m2.2
dazap1
ssb
nelfe
raly
ptbp1a
tut1
rbm25b
rbm19
rbm5
cpeb3
-
srsf3a
srsf7a
rbm14a
HNRNPLL
srsf7b
dazl
rbm7
-
-
rbm4.3
-
rbm4.2
dnd1
eif4bb
celf1
srsf6b
-
ewsr1b
-
-
rrp7a
srsf1b
pprc1
grsf1
msi2a
CPSF7
-
-
raver1
hnrnpc
-
igf2bp1
-
-
setd1ba
hnrnpd
hnrnpdl
tia1l
pspc1
trmt2a
ptbp3
scaf4a
eif3g
elavl4
enox2
enox1
celf3a
snrnp70
-
larp7
u2af2a
rbm18
-
nifk
celf3b
-
-
rbfox3b
-
si:dkey-33c12.4
-
rbm24b
-
cstf2
-
-
trnau1apb
setd1a
zgc:55733
msi1
puf60b
rbms2b
rbmx
puf60a
-
-
cirbpb
cnot4a
dnajc17
sltm
snrnp35
hnrnpm
spen
alkbh8
snrpb2
zgc:56304
pabpc1l
u2af1
-
srsf5a
HNRNPA3
-
pabpn1l
eif3ba
rbm45
safb
ptbp2b
ptbp2a
srsf1a
tardbpl
-
-
hnrnpr
poldip3
si:dkey-93h22.8
rbfox1
-
-
-
-
-
HNRNPA0
RBMS1 (1 of many)
pabpn1
srsf4
ppargc1b
zgc:163098
zcrb1
CPSF6
syncrip
pabpc4
elavl1b
ptbp1b
cirbpa
g3bp1
pabpc1b
SCAF8
trnau1apa
rbm46
rbm15b
-
RNPS1
zgc:153215
-
myef2
-
-
-
ncoa5
u2af2b
rbpms2a
celf5b
CPEB4 (1 of many)
snrpa
pabpc1a
rbm8a
hnrnpabb
ELAVL2
RBPMS
si:dkey-205h23.2
nol8
rbm17

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.