| UniProt ID | RBPMS_HUMAN | |
|---|---|---|
| UniProt AC | Q93062 | |
| Protein Name | RNA-binding protein with multiple splicing | |
| Gene Name | RBPMS | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 196 | |
| Subcellular Localization | Nucleus . Cytoplasm . Cytoplasm, P-body . Translocates into cytoplasmic stress granules that probably correspond to P-bodies in response to oxidative stress. | |
| Protein Description | Acts as a coactivator of transcriptional activity. Required to increase TGFB1/Smad-mediated transactivation. Acts through SMAD2, SMAD3 and SMAD4 to increase transcriptional activity. Increases phosphorylation of SMAD2 and SMAD3 on their C-terminal SSXS motif, possibly through recruitment of TGFBR1. Promotes the nuclear accumulation of SMAD2, SMAD3 and SMAD4 proteins. [PubMed: 26347403 Binds to poly(A) RNA] | |
| Protein Sequence | MNNGGKAEKENTPSEANLQEEEVRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQTLRLEFAKANTKMAKNKLVGTPNPSTPLPNTVPQFIAREPYELTVPALYPSSPEVWAPYPLYPAELAPALPPPAFTYPASLHAQMRWLPPSEATSQGWKSRQFC | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MNNGGKAE -------CCCCCCCC | 8.74 | 22814378 | |
| 9 | Ubiquitination | NNGGKAEKENTPSEA CCCCCCCCCCCCCHH | 62.21 | - | |
| 9 | Acetylation | NNGGKAEKENTPSEA CCCCCCCCCCCCCHH | 62.21 | 26051181 | |
| 12 | Phosphorylation | GKAEKENTPSEANLQ CCCCCCCCCCHHHCC | 29.32 | 25849741 | |
| 14 | Phosphorylation | AEKENTPSEANLQEE CCCCCCCCHHHCCHH | 47.50 | 22199227 | |
| 25 | Phosphorylation | LQEEEVRTLFVSGLP CCHHHHHHHHHCCCC | 29.71 | - | |
| 29 | Phosphorylation | EVRTLFVSGLPLDIK HHHHHHHCCCCCCCC | 27.55 | - | |
| 36 | Ubiquitination | SGLPLDIKPRELYLL CCCCCCCCHHHEEEE | 37.38 | - | |
| 53 | Phosphorylation | PFKGYEGSLIKLTSK CCCCCCCCEEEEECC | 18.25 | 24719451 | |
| 60 | Ubiquitination | SLIKLTSKQPVGFVS CEEEEECCCCEEEEE | 54.08 | - | |
| 100 | Ubiquitination | TLRLEFAKANTKMAK HHHHHHHHCCCHHHH | 47.71 | - | |
| 109 | Ubiquitination | NTKMAKNKLVGTPNP CCHHHHCCCCCCCCC | 43.79 | - | |
| 113 | Phosphorylation | AKNKLVGTPNPSTPL HHCCCCCCCCCCCCC | 16.65 | 25159151 | |
| 117 | Phosphorylation | LVGTPNPSTPLPNTV CCCCCCCCCCCCCCC | 49.66 | 25159151 | |
| 118 | Phosphorylation | VGTPNPSTPLPNTVP CCCCCCCCCCCCCCC | 30.06 | 25159151 | |
| 118 (in isoform 4) | Phosphorylation | - | 30.06 | 25159151 | |
| 123 | Phosphorylation | PSTPLPNTVPQFIAR CCCCCCCCCCHHHHC | 31.46 | 26699800 | |
| 143 | Phosphorylation | TVPALYPSSPEVWAP ECCEECCCCCCCCCC | 44.99 | 24275569 | |
| 144 | Phosphorylation | VPALYPSSPEVWAPY CCEECCCCCCCCCCC | 22.15 | 24275569 | |
| 190 (in isoform 2) | Phosphorylation | - | 6.44 | 27251275 | |
| 193 (in isoform 2) | Phosphorylation | - | 29.84 | 28348404 | |
| 196 (in isoform 2) | Phosphorylation | - | 4.05 | 28348404 |
| 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 RBPMS_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RBPMS_HUMAN !! | ||||||
* 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 RBPMS_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113 AND THR-118, ANDMASS SPECTROMETRY. | |
