Nannospalax_galiliFamily: RRM_1 Number of Genes: 206
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
Rbm18
Srsf10
Poldip3
-
-
-
-
Eif4h
Spen
Puf60
Rbm17
Celf4
Sfpq
Raver2
Elavl3
Pabpc6
-
Pabpc1
-
-
Cirbp
-
Raly
-
Rbms2
Pabpc4l
-
Enox2
-
-
Tut1
Dnajc17
Cstf2t
-
Rbm47
Dazap1
Hnrnpm
-
-
Rbm46
Pabpc5
-
-
Cpsf7
Scaf4
-
-
-
-
-
-
-
Ppil4
Hnrnpa0
Rbm19
Dazl
-
-
-
-
-
Pabpc1l
Srsf11
Snrnp35
Rbm34
Cpeb4
G3bp1
-
Nono
Rnpc3
Rbpms
Rbm11
Pspc1
Rbm15
Srsf1
-
Tra2b
-
-
-
-
Ncbp2
-
Hnrnph3
Rbm5
-
-
Tia1
Zrsr1
Eif3g
Srsf4
Ewsr1
Sltm
Scaf8
Eif4b
-
-
Srsf9
-
-
Rbm3
-
Ptbp3
Ralyl
Hnrnpd
Marf1
Rbms1
-
U2surp
Rbm24
Rbm41
-
-
Rbms3
-
-
-
-
Uhmk1
G3bp2
Srsf7
Msi1
Elavl2
-
-
-
-
Hnrnph1
Sart3
Nifk
Cnot4
Ppargc1a
A1cf
-
Srsf3
Cpeb3
Igf2bp1
Hnrnpdl
Gm49396
Rbm12
-
Trnau1ap
Cpsf6
-
-
-
Pabpc2
-
Eif3b
Nelfe
Rbm4b
Sf3b4
Slirp
Pprc1
Rbm39
Hnrnpll
Ptbp2
-
-
Ppargc1b
Rbm44
-
-
-
Celf1
Alkbh8
Celf6
-
-
-
-
Srsf6
-
-
-
Msi2
Htatsf1
-
-
-
-
-
Rbfox3
Rbm22
Pabpc4
-
-
-
-
Rbm25
-
Srsf12
Rbm14
-
-
Gm20521
Elavl1
Rbm10
-
-
Rbm42
Safb
Rbmx2
Zcrb1
Sf3b6
U2af2
Tial1
Hnrnph2
Rbfox2
-
Syncrip
-
-
Celf2
-
-
Snrnp70
-
-
Celf3
U2af1
Hnrnpab
Snrpa
Srsf2
Hnrnpa3
Cstf2
-
-
-
Rbm15b
-
Hnrnpl
-
-
Ptbp1
Elavl4
Rbfox1
-
-
Rbpms2
Igf2bp3
Rnps1
-
-
Tra2a
-
-
Rbm45
Pabpn1l
Enox1

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.