Mus_musculusFamily: RRM_1 Number of Genes: 224
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
Hnrnpd
Celf2
Puf60
Elavl3
Hnrnpa2b1
Celf1
Rbm14
Ptbp1
Hnrnpa0
Hnrnph1
Snrpb2
Elavl2
Rbfox1
Ewsr1
Raver1
Rdm1
Dazl
Rbm25
Pabpc4
Igf2bp1
Hnrnpl
Ppil4
Srsf6
Srsf1
G3bp1
Sart3
Hnrnph3
Cpeb4
Hnrnpab
Taf15
Slirp
Srsf5
Nol8
Pspc1
Enox1
Pabpn1
Pabpc1
Zcrb1
Ncbp2
Tra2b
Scaf4
Hnrnpll
Srsf7
Celf4
Nelfe
Rbm22
Alyref
Tnrc6c
Rbfox3
Alkbh8
Boll
Ncl
Nifk
Uhmk1
Rbm18
Rbms1
Myef2
Rbm38
Raly
Rbm39
Larp7
Rnpc3
Ptbp2
Celf3
Ptbp3
Elavl4
Ppie
Srsf10
Sfpq
Trnau1ap
Srsf4
Ppargc1a
Hnrnpdl
Snrnp35
G3bp2
Srsf9
Rbm19
Rbm28
Igf2bp3
Tra2a
U2af2
Fus
Tial1
Rexo5
Rbm10
Rbmx2
Enox2
Rbmx
Rbm3
Cstf2
Nono
Zrsr2
Rbm41
Rbpms
Sltm
Celf6
Rbpms2
U2surp
Syncrip
Rbm5
Srek1
Rbm11
Rbfox2
Igf2bp2
Rbm4b
Ppargc1b
Rbm46
Rbm34
Srsf2
Dnajc17
Rnps1
Pabpc5
Celf5
Cpsf7
Raver2
Rbm42
Rbmxl1
Rbm17
Sf3b6
Rbm24
Rbm8a
Setd1b
Cnot4
Rbms3
Cpeb3
Ralyl
Cpeb2
Elavl1
Rbms2
Eif4h
Spen
Tardbp
Poldip3
Hnrnpf
Setd1a
Rbm45
Rbm7
Safb2
Zrsr1
Grsf1
Dnd1
Cirbp
Hnrnph2
Pabpc6
Scaf8
Hnrnpa1
Rbm12b1
Rbm15
Rbm33
Gm9833
Gm7324
-
Pabpc2
Rbm12b2
A1cf
Cstf2t
Msi1
Pabpc1l
Srsf12
Srsf11
Pprc1
Cpsf6
Eif3b
Eif4b
Hnrnpa3
Hnrnpm
Alyref2
Hnrnpc
4930595M18Rik
Snrpa
U2af1
Snrnp70
Hnrnpr
Gm12666
-
Htatsf1
Sf3b4
Ssb
Dazap1
Msi2
Pabpn1l
Eif3g
Rbm44
Rbm47
Safb
Srsf3
Tia1
Tut1
Rbmxl2
Rbm15b
Gm12355
-
Rbm8a2
-
U2af1l4
4931428L18Rik
Rbm12
Gm4340
Pabpc4l
Gm4302
Gm21293
Gm10352
Gm6793
Gm20521
-
Gm21677
Gm21704
Gm21312
Gm4301
Gm21693
Rbmy
Rbm4
Gm20765
Rbm31y
Gm10256
Gm21708
Gm21992
Gm3376
Gm4312
Gm4307
Gm6763
Gm21304
Gm8764
Gm17190
-
Gm29289
-
Gm4064
Gm4305
Gm4303
AC153137.1
-

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.