UniProt ID | RBM5_MOUSE | |
---|---|---|
UniProt AC | Q91YE7 | |
Protein Name | RNA-binding protein 5 | |
Gene Name | Rbm5 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 815 | |
Subcellular Localization | Nucleus. | |
Protein Description | Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate apoptosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes production of a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes production of a catalytically active form of CASP2/Caspase-2 that induces apoptosis (By similarity).. | |
Protein Sequence | MGSDKRVSRTERSGRYGSIIDRDDRDERESRSRRRDSDYKRSSDDRRGDRYDDYRDYDSPERERERRNSDRSEDGYHSDGDYGEHDYRHDISDERESKTIMLRGLPITITESDIREMMESFEGPQPADVRLMKRKTGVSRGFAFVEFYHLQDATSWMEANQKKLVIQGKHIAMHYSNPRPKFEDWLCNKCCLNNFRKRLKCFRCGADKFDSEQEVPPGTTESAQSVDYYCDTIILRNIAPHTVVDSIMTALSPYASLAVNNIRLIKDKQTQQNRGFAFVQLSSAMDASQLLQILQSLHPPLKIDGKTIGVDFAKSARKDLVLPDGNRVSAFSVASTAIAAAQWSSTQSQSGEGGSVDYSYMQPGQDGYTQYTQYSQDYQQFYQQQAGGLESDTSATSGTTVTTTSAAVVSQSPQLYNQTSNPPGSPTEEAQPSTSTSTQAPAASPTGVVPGTKYAVPDTSTYQYDESSGYYYDPTTGLYYDPNSQYYYNSLTQQYLYWDGEKETYVPAAEASSNQQTGLPSTKEGKEKKEKPKSKTAQQIAKDMERWAKSLNKQKENFKNSFQPVNSLREEERRESAAADAGFALFEKKGALAERQQLLPELVRNGDEENPLKRGLVAAYSGDSDNEEELVERLESEEEKLADWKKMACLLCRRQFPNRDALVRHQQLSDLHKQNMDIYRRSRLSEQELEALELREREMKYRDRAAERREKYGIPEPPEPKRKKQFDAGTVNYEQPTKDGIDHSNIGNKMLQAMGWREGSGLGRKCQGITAPIEAQVRLKGAGLGAKGSAYGLSGADSYKDAVRKAMFARFTEME | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
18 | Phosphorylation | ERSGRYGSIIDRDDR CCCCCCCCCCCCCCC | 13.87 | 27600695 | |
37 | Phosphorylation | SRSRRRDSDYKRSSD HHHHHCCHHCCCCCC | 40.82 | 29899451 | |
51 | Phosphorylation | DDRRGDRYDDYRDYD CCCCCCCCCCCCCCC | 20.22 | 25777480 | |
54 | Phosphorylation | RGDRYDDYRDYDSPE CCCCCCCCCCCCCHH | 11.50 | 25159016 | |
57 | Phosphorylation | RYDDYRDYDSPERER CCCCCCCCCCHHHHH | 14.88 | 25159016 | |
59 | Phosphorylation | DDYRDYDSPERERER CCCCCCCCHHHHHHH | 23.56 | 25521595 | |
69 | Phosphorylation | RERERRNSDRSEDGY HHHHHHCCCCCCCCC | 32.37 | 27087446 | |
72 | Phosphorylation | ERRNSDRSEDGYHSD HHHCCCCCCCCCCCC | 45.06 | 27087446 | |
76 | Phosphorylation | SDRSEDGYHSDGDYG CCCCCCCCCCCCCCC | 15.52 | 25619855 | |
78 | Phosphorylation | RSEDGYHSDGDYGEH CCCCCCCCCCCCCCC | 34.50 | 25521595 | |
82 | Phosphorylation | GYHSDGDYGEHDYRH CCCCCCCCCCCCCCC | 29.91 | 25619855 | |
87 | Phosphorylation | GDYGEHDYRHDISDE CCCCCCCCCCCCCCH | 16.26 | 21149613 | |
92 | Phosphorylation | HDYRHDISDERESKT CCCCCCCCCHHHCCE | 39.20 | 23684622 | |
249 | Phosphorylation | TVVDSIMTALSPYAS HHHHHHHHHHHHHHH | 23.83 | 22802335 | |
252 | Phosphorylation | DSIMTALSPYASLAV HHHHHHHHHHHHHHH | 17.25 | 22802335 | |
444 | Phosphorylation | STQAPAASPTGVVPG CCCCCCCCCCCCCCC | 25.71 | - | |
528 | Acetylation | STKEGKEKKEKPKSK CCCCCHHCCCCCCCH | 70.49 | 7613431 | |
531 | Acetylation | EGKEKKEKPKSKTAQ CCHHCCCCCCCHHHH | 67.63 | 7613441 | |
542 | Acetylation | KTAQQIAKDMERWAK HHHHHHHHHHHHHHH | 60.27 | 23806337 | |
576 | Phosphorylation | REEERRESAAADAGF CHHHHHHHHHHHHHH | 22.77 | 28833060 | |
620 | Phosphorylation | KRGLVAAYSGDSDNE CCCCEEEECCCCCCH | 11.93 | 26239621 | |
621 | Phosphorylation | RGLVAAYSGDSDNEE CCCEEEECCCCCCHH | 31.25 | 25521595 | |
623 (in isoform 2) | Phosphorylation | - | 47.05 | 19144319 | |
624 | Phosphorylation | VAAYSGDSDNEEELV EEEECCCCCCHHHHH | 45.95 | 27087446 | |
636 | Phosphorylation | ELVERLESEEEKLAD HHHHHHHHHHHHHHH | 55.70 | 25159016 | |
682 | Phosphorylation | NMDIYRRSRLSEQEL CHHHHHHHCCCHHHH | 28.68 | 28833060 | |
685 | Phosphorylation | IYRRSRLSEQELEAL HHHHHCCCHHHHHHH | 35.80 | 28833060 | |
787 | Acetylation | KGAGLGAKGSAYGLS CCCCCCCCCCCCCCC | 52.15 | 22826441 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of RBM5_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of RBM5_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of RBM5_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of RBM5_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND MASSSPECTROMETRY. | |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-621, AND MASSSPECTROMETRY. | |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND MASSSPECTROMETRY. |