Rattus_norvegicusFamily: RRM_1 Number of Genes: 216
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
Syncrip
Srsf2
Nelfe
Srsf3
Sart3
Rbmx
Snrnp35
Elavl1
Msi1
Srsf9
Eif3b
Setd1b
-
Rbm19
Eif4h
Snrpa
Ncbp2
Tra2b
Scaf4
Hnrnpdl
Hnrnpd
LOC103689943
Rbm47
G3bp2
Rbfox1
Rbm25l1
Uhmk1
Rbms2
Pabpc5
Rbm31y
Rbfox3
Grsf1
Hnrnph1
LOC103689931
Nono
Ppargc1a
Rbfox2
Celf5
Snrpb2
Zcrb1
Cpeb2
-
AABR07051190.1
-
Myef2
Rbm3
Rbm28
Srsf5
AABR07061152.1
-
Cpsf6
Igf2bp1
Srsf6
Rbm38
Rbm18
Elavl2
Hnrnpll
Rbmx2
Hnrnpm
Srsf10
Ssb
AABR07055789.1
-
Rbm10
Rbms1
U2surp
Pabpc1
Rnps1
Igf2bp3
Tra2a
Ewsr1
Zrsr1
Puf60
Srsf4
Eif4b
Celf1
Ptbp1
Rbm45
Cnot4
Ptbp2
AABR07040947.1
-
Hnrnpa2b1
AABR07061825.1
-
LOC100911576
Hnrnph2
Hnrnpr
Rbmxl1
Slirp
Dnajc17
Tardbp
Pabpc1l
G3bp1
Rbpms
Elavl3
Rbm15b
Celf4
Rexo5
Pabpc2
Hnrnpf
Ppie
Ppil4
Pabpc4
Boll
Rbpms2
U2af2
Cirbp
Rbm12b
Ptbp3
Tia1
Dnd1
Scaf8
Rnpc3
Pabpc6
Raly
Ppargc1b
Rbm5
Ncl
Pprc1
Rbm17
Rbm22
Rbm12
Rbm39
Rbm34
Tut1
Hnrnpl
Tial1
Eif3g
Cpsf7
Cpeb3
Raver1
Rdm1
Snrnp70
Pspc1
Celf3
Sf3b4
Rbm8a
Tnrc6c
Poldip3
Fus
Dazl
Elavl4
Celf2
Raver2
Rbm42
U2af1l4
Alkbh8
Rbm44
Msi2
Nifk
Rbm46
Rbms3
Igf2bp2
LOC100911361
-
AABR07037800.1
-
Srsf7
Htatsf1
Smptb
AABR07035074.1
-
LOC100359930
Rbm11
Pabpn1l
Srsf11
Pabpc4l
Enox2
Dazap1
Srek1
Cpeb4
Zrsr2
A1cf
Spen
Alyref
Hnrnpa1
AABR07048397.1
-
LOC681410
Pabpn1
AABR07009224.1
-
Rbm14
Nol8
U2af1
Sf3b6
-
Hnrnpab
AABR07055878.1
-
Rbm24
-
LOC100912481
Nol8
Rbm15
Enox1
Cstf2
Hnrnph3
Ncbp2
-
Srsf8
-
Larp7
AABR07066522.1
-
AC109707.1
-
AABR07031533.1
-
LOC100910882
LOC100910990
Cstf2t
Srsf1
Safb
AABR07055875.1
-
Rbm4
Hnrnpc
Srsf12
AABR07060628.1
-
Celf6
Hnrnpa3
LOC108348134
Sltm
LOC103694865
Setd1a
LOC679087
Trnau1ap
-
Marf1
AABR07027799.1
-
Rbm41
Taf15
Sfpq
-
Rbmxl1b
-
Rbmy1j
Rbm4b

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.