RSMB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RSMB_MOUSE
• UniProt AC: P27048
• Protein Name: Small nuclear ribonucleoprotein-associated protein B
• Gene Name: Snrpb
• Organism: Mus musculus (Mouse).
• Sequence Length: 231
• Subcellular Localization: Cytoplasm, cytosol. Nucleus. SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes..
• Protein Description: Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing..
• Protein Sequence: MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGLPPGRGTPMGMPPPGMRPPPPGMRGLL

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
15	Phosphorylation	KMLQHIDYRMRCILQ HHHHHHCHHHHHEEC	13.00	-
32	Acetylation	RIFIGTFKAFDKHMN CEEEEECHHHHHCCC	48.24	23954790
32	Ubiquitination	RIFIGTFKAFDKHMN CEEEEECHHHHHCCC	48.24	-
54	Acetylation	EFRKIKPKNSKQAER HHHCCCCCCCHHHHH	69.70	19847537
88	Ubiquitination	TVEGPPPKDTGIARV EEECCCCCCCCEEEC	73.94	-
108	Asymmetric dimethylarginine	AGGPGIGRAAGRGIP CCCCCHHHHCCCCCC	21.24	-
108	Methylation	AGGPGIGRAAGRGIP CCCCCHHHHCCCCCC	21.24	24129315
112	Asymmetric dimethylarginine	GIGRAAGRGIPAGVP CHHHHCCCCCCCCCC	34.83	-
112	Methylation	GIGRAAGRGIPAGVP CHHHHCCCCCCCCCC	34.83	24129315
147	Methylation	QVMTPQGRGTVAAAA CCCCCCCHHHHHHHH	32.15	18935155
149	Phosphorylation	MTPQGRGTVAAAAAA CCCCCHHHHHHHHHH	12.95	25777480
158	Phosphorylation	AAAAAAATASIAGAP HHHHHHHHHHHCCCC	19.06	25777480
160	Phosphorylation	AAAAATASIAGAPTQ HHHHHHHHHCCCCCC	14.49	25777480
166	Phosphorylation	ASIAGAPTQYPPGRG HHHCCCCCCCCCCCC	39.95	25777480
168	Phosphorylation	IAGAPTQYPPGRGGP HCCCCCCCCCCCCCC	17.55	25777480
172	Methylation	PTQYPPGRGGPPPPM CCCCCCCCCCCCCCC	53.31	30761093

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
108	R	Methylation	Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine (By similarity).	24129315
112	R	Methylation	Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine (By similarity).	24129315

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of RSMB_MOUSE !!

Drug and Disease Associations

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