UniProt ID | RBM39_MOUSE | |
---|---|---|
UniProt AC | Q8VH51 | |
Protein Name | RNA-binding protein 39 | |
Gene Name | Rbm39 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 530 | |
Subcellular Localization | Nucleus . | |
Protein Description | Transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1. May be involved in pre-mRNA splicing process.. | |
Protein Sequence | MADDIDIEAMLEAPYKKDENKLNSANGHEERSKKRKKSKSRSRSHERKRSKSKERKRSRDRERKKSKSRERKRSRSKERRRSRSRSRDRRFRGRYRSPYSGPKFNSAIRGKIGLPHSIKLSRRRSRSKSPFRKDKSPVREPIDNLTPEERDARTVFCMQLAARIRPRDLEEFFSTVGKVRDVRMISDRNSRRSKGIAYVEFVDVSSVPLAIGLTGQRVLGVPIIVQASQAEKNRAAAMANNLQKGSAGPMRLYVGSLHFNITEDMLRGIFEPFGRIESIQLMMDSETGRSKGYGFITFSDSECAKKALEQLNGFELAGRPMKVGHVTERTDASSASSFLDSDELERTGIDLGTTGRLQLMARLAEGTGLQIPPAAQQALQMSGSLAFGAVAEFSFVIDLQTRLSQQTEASALAAAASVQPLATQCFQLSNMFNPQTEEEVGWDTEIKDDVIEECNKHGGVIHIYVDKNSAQGNVYVKCPSIAAAIAAVNALHGRWFAGKMITAAYVPLPTYHNLFPDSMTATQLLVPSRR | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MADDIDIEA ------CCCCCCHHH | 24.15 | - | |
24 | Phosphorylation | KDENKLNSANGHEER CCCCCCCCCCCCHHH | 33.28 | 27841257 | |
40 | Phosphorylation | KKRKKSKSRSRSHER HHHHHHHHHHHHHHH | 42.45 | 19367708 | |
42 | Phosphorylation | RKKSKSRSRSHERKR HHHHHHHHHHHHHHH | 45.27 | 19367708 | |
44 | Phosphorylation | KSKSRSRSHERKRSK HHHHHHHHHHHHHHH | 30.83 | 19367708 | |
95 | Phosphorylation | DRRFRGRYRSPYSGP HHHHHCCCCCCCCCC | 20.47 | 27087446 | |
97 | Phosphorylation | RFRGRYRSPYSGPKF HHHCCCCCCCCCCCH | 21.18 | 27087446 | |
99 | Phosphorylation | RGRYRSPYSGPKFNS HCCCCCCCCCCCHHH | 27.75 | 23984901 | |
100 | Phosphorylation | GRYRSPYSGPKFNSA CCCCCCCCCCCHHHH | 52.59 | 25521595 | |
106 | Phosphorylation | YSGPKFNSAIRGKIG CCCCCHHHHHHCCCC | 28.36 | 29514104 | |
109 | Methylation | PKFNSAIRGKIGLPH CCHHHHHHCCCCCCC | 39.82 | 12019205 | |
117 | Phosphorylation | GKIGLPHSIKLSRRR CCCCCCCCHHHHCCC | 21.34 | 26824392 | |
121 | Phosphorylation | LPHSIKLSRRRSRSK CCCCHHHHCCCCCCC | 20.81 | 26824392 | |
125 | Phosphorylation | IKLSRRRSRSKSPFR HHHHCCCCCCCCCCC | 38.81 | 23684622 | |
127 | Phosphorylation | LSRRRSRSKSPFRKD HHCCCCCCCCCCCCC | 38.44 | 23684622 | |
129 | Phosphorylation | RRRSRSKSPFRKDKS CCCCCCCCCCCCCCC | 30.43 | 23684622 | |
136 | Phosphorylation | SPFRKDKSPVREPID CCCCCCCCCCCCCCC | 38.47 | 24925903 | |
146 | Phosphorylation | REPIDNLTPEERDAR CCCCCCCCHHHHHHH | 34.60 | 24925903 | |
174 | Phosphorylation | RDLEEFFSTVGKVRD CCHHHHHHHCCCHHE | 27.75 | 29550500 | |
175 | Phosphorylation | DLEEFFSTVGKVRDV CHHHHHHHCCCHHEE | 28.28 | 29550500 | |
178 | Ubiquitination | EFFSTVGKVRDVRMI HHHHHCCCHHEEEEE | 29.75 | 22790023 | |
232 | Ubiquitination | VQASQAEKNRAAAMA EECHHHHHHHHHHHH | 55.54 | 22790023 | |
306 | Ubiquitination | SDSECAKKALEQLNG CCHHHHHHHHHHCCC | 39.41 | 22790023 | |
330 | Phosphorylation | VGHVTERTDASSASS CCCCEECCCCCHHHH | 29.68 | 25619855 | |
333 | Phosphorylation | VTERTDASSASSFLD CEECCCCCHHHHHCC | 29.28 | 25619855 | |
334 | Phosphorylation | TERTDASSASSFLDS EECCCCCHHHHHCCH | 33.61 | 22942356 | |
336 | Phosphorylation | RTDASSASSFLDSDE CCCCCHHHHHCCHHH | 24.46 | 25521595 | |
337 | Phosphorylation | TDASSASSFLDSDEL CCCCHHHHHCCHHHH | 29.55 | 25521595 | |
341 | Phosphorylation | SASSFLDSDELERTG HHHHHCCHHHHHHHC | 34.82 | 27149854 | |
347 | Phosphorylation | DSDELERTGIDLGTT CHHHHHHHCCCCCHH | 29.16 | 19854140 | |
353 | Phosphorylation | RTGIDLGTTGRLQLM HHCCCCCHHHHHHHH | 33.12 | 22942356 | |
354 | Phosphorylation | TGIDLGTTGRLQLMA HCCCCCHHHHHHHHH | 20.64 | 22817900 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of RBM39_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RBM39_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 RBM39_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NCOA6_HUMAN | NCOA6 | physical | 11704680 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-136, 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-97 AND SER-136, AND MASSSPECTROMETRY. | |
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY. | |
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-337, ANDMASS SPECTROMETRY. |