RBM4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RBM4_MOUSE
• UniProt AC: Q8C7Q4
• Protein Name: RNA-binding protein 4
• Gene Name: Rbm4
• Organism: Mus musculus (Mouse).
• Sequence Length: 361
• Subcellular Localization: Nucleus. Nucleus, nucleolus. Nucleus speckle. Cytoplasm. Cytoplasmic granule. Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases it
• Protein Description: 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..
• Protein Sequence: MVKLFIGNLPREATEQEIRSLFEQYGKVLECDIIKNYGFVHIEDKTAAEDAIRNLHHYKLHGVNINVEASKNKSKASTKLHVGNISPTCTNQELRAKFEEYGPVIECDIVKDYAFVHMERAEDAVEAIRGLDNTEFQGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPIDRSGRVADLTEQYNEQYGAVRTPYTMSYGDSLYYNNTYGALDAYYKRCRAARSYEAVAAAAASAYSNYAEQTLSQLPQVQNTAMASHLTSTSLDPYNRHLLPPSGAAAAAAAAAACTAASTSYYGRDRSPLRRATGPVLTVGEGYGYGHDSELSQASAAARNSLYDMARYEREQYADRARYSAF

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
86	Phosphorylation	KLHVGNISPTCTNQE EEEECCCCCCCCCHH	20.39	26824392
88	Phosphorylation	HVGNISPTCTNQELR EECCCCCCCCCHHHH	25.77	26239621
90	Phosphorylation	GNISPTCTNQELRAK CCCCCCCCCHHHHHH	42.27	26643407
152	Phosphorylation	LSTSRLRTAPGMGDQ EECCCCCCCCCCCCC	41.62	-
160	Phosphorylation	APGMGDQSGCYRCGK CCCCCCCCCCCCCCC	35.25	-
163	Phosphorylation	MGDQSGCYRCGKEGH CCCCCCCCCCCCCCC	16.68	-
306	Phosphorylation	SYYGRDRSPLRRATG CCCCCCCCCHHCCCC	32.35	26824392
340	Phosphorylation	ASAAARNSLYDMARY HHHHHHHHHHHHHHH	23.82	29176673

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RBM4_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
306	S	Phosphorylation	Phosphorylated in vitro on Ser-306 by SRPK1.	19801630
306	S	Phosphorylation	Phosphorylation on Ser-306 is induced upon cell muscle differentiation.	19801630
306	S	Phosphorylation	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).	19801630

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RBM4_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RBM4_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.