Q8C7Q4 (RBM4_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified November 13, 2013. Version 92. History...
Names and origin
|Protein names||Recommended name:|
RNA-binding protein 4
RNA-binding motif protein 4
RNA-binding motif protein 4a
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||361 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro. Ref.4
Interacts with TNPO3; the interaction mediates nuclear import of the protein and is disrupted by nuclear Ran bound to GTP. Interacts with EIF4G1 and WT1. Interacts with EIF4A1; the interaction is modulated under stress-induced conditions. Interacts with AGO1. Interacts with AGO2; the interaction occurs under both cell proliferation and differentiation conditions and in a RNA- and phosphorylation-independent manner. Interacts with DDX5; the interaction occurs in a RNA-independent manner By similarity.
Nucleus By similarity. Nucleus › nucleolus By similarity. Nucleus speckle By similarity. Cytoplasm By similarity. Cytoplasmic granule By similarity. Note: Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases its subcellular relocalization from the nucleus to the cytoplasm and to cytoplasmic stress granules (SG) via a p38 MAPK signaling pathway. Primarily localized in nucleus and nucleoli under cell growth conditions and accumulated in the cytoplasm and cytoplasm perinuclear granules upon muscle cell differentiation By similarity. Ref.5
Expressed in the suprachiasmatic nucleus (SCN). Expressed in myocytes; expression gradually increases during muscle cell differentiation (at protein level). Expressed in the suprachiasmatic nucleus (SCN). Ref.4 Ref.5 Ref.6
Accumulates according to a circadian rhythm in the SCN. Ref.4
Phosphorylated. Phosphorylated in vitro on Ser-306 by SRPK1. Phosphorylation on Ser-306 is induced upon cell stress signaling, which alters its subcellular localization and may modulate its activity on IRES-mediated mRNA translation By similarity. Phosphorylated. Phosphorylation on Ser-306 is induced upon cell muscle differentiation. Ref.5
Contains 1 CCHC-type zinc finger.
Contains 2 RRM (RNA recognition motif) domains.
|This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]|
|Isoform 1 (identifier: Q8C7Q4-1) |
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
|Isoform 2 (identifier: Q8C7Q4-2) |
The sequence of this isoform differs from the canonical sequence as follows:
139-168: KRMHVQLSTSRLRTAPGMGDQSGCYRCGKE → ESLFWSAQYKAVRNELVEKRKALGWKDFAG
|Note: May be due to an intron retention. No experimental confirmation available.|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 361||361||RNA-binding protein 4||PRO_0000081755|
|Domain||2 – 72||71||RRM 1|
|Domain||78 – 148||71||RRM 2|
|Zinc finger||160 – 177||18||CCHC-type|
|Region||196 – 361||166||Interaction with TNPO3 By similarity|
|Compositional bias||233 – 241||9||Poly-Ala|
|Compositional bias||283 – 292||10||Poly-Ala|
Amino acid modifications
|Modified residue||306||1||Phosphoserine By similarity|
|Alternative sequence||139 – 168||30||KRMHV…RCGKE → ESLFWSAQYKAVRNELVEKR KALGWKDFAG in isoform 2.||VSP_013417|
|Alternative sequence||169 – 361||193||Missing in isoform 2.||VSP_013418|
|Sequence conflict||243||1||S → N in AAC53171. Ref.1|
|Sequence conflict||292||1||A → AAAAA in AAC53171. Ref.1|
|Sequence conflict||299||1||S → P in AAC53171. Ref.1|
|Sequence conflict||316||1||L → P in AAC53171. Ref.1|
|||"A novel zinc finger-containing RNA-binding protein conserved from fruitflies to humans."|
Jackson F.R., Banfi S., Guffanti A., Rossi E.
Genomics 41:444-452(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
|||"The transcriptional landscape of the mammalian genome."|
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Eye and Spinal cord.
|||"Exon selection in alpha-tropomyosin mRNA is regulated by the antagonistic action of RBM4 and PTB."|
Lin J.C., Tarn W.Y.
Mol. Cell. Biol. 25:10111-10121(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
|||"LARK activates posttranscriptional expression of an essential mammalian clock protein, PERIOD1."|
Kojima S., Matsumoto K., Hirose M., Shimada M., Nagano M., Shigeyoshi Y., Hoshino S., Ui-Tei K., Saigo K., Green C.B., Sakaki Y., Tei H.
Proc. Natl. Acad. Sci. U.S.A. 104:1859-1864(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
|||"RNA-binding motif protein 4 translocates to cytoplasmic granules and suppresses translation via argonaute2 during muscle cell differentiation."|
Lin J.C., Tarn W.Y.
J. Biol. Chem. 284:34658-34665(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
|||"RBM4 down-regulates PTB and antagonizes its activity in muscle cell-specific alternative splicing."|
Lin J.C., Tarn W.Y.
J. Cell Biol. 193:509-520(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
|+||Additional computationally mapped references.|
|U89506 mRNA. Translation: AAC53171.1. Frameshift.|
AK049659 mRNA. Translation: BAC33862.1.
AK087488 mRNA. Translation: BAC39895.1.
|RefSeq||NP_033058.2. NM_009032.2. |
3D structure databases
|SMR||Q8C7Q4. Positions 1-155. |
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000006628; ENSMUSP00000006628; ENSMUSG00000096370. |
ENSMUST00000180248; ENSMUSP00000137345; ENSMUSG00000094936.
|UCSC||uc008gau.1. mouse. |
|MGI||MGI:1100865. Rbm4. |
Gene expression databases
Family and domain databases
|Gene3D||22.214.171.1240. 2 hits. |
126.96.36.199. 1 hit.
|InterPro||IPR012677. Nucleotide-bd_a/b_plait. |
|Pfam||PF00076. RRM_1. 2 hits. |
PF00098. zf-CCHC. 1 hit.
|SMART||SM00360. RRM. 2 hits. |
SM00343. ZnF_C2HC. 1 hit.
|PROSITE||PS50102. RRM. 2 hits. |
PS50158. ZF_CCHC. 1 hit.
|Accession||Primary (citable) accession number: Q8C7Q4|
Secondary accession number(s): O08752, Q8BN66
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|