| UniProt ID | SMRD1_MOUSE | |
|---|---|---|
| UniProt AC | Q61466 | |
| Protein Name | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1 | |
| Gene Name | Smarcd1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 515 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (By similarity). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. [PubMed: 17640523 Has a strong influence on vitamin D-mediated transcriptional activity from an enhancer vitamin D receptor element (VDRE May be a link between mammalian SWI-SNF-like chromatin remodeling complexes and the vitamin D receptor (VDR) heterodimer. Mediates critical interactions between nuclear receptors and the BRG1/SMARCA4 chromatin-remodeling complex for transactivation (By similarity] | |
| Protein Sequence | MAARAGFQSVAPSGGAGASGGAGVAAALGPGGTPGPPVRMGPAPGQGLYRSPMPGAAYPRPGMLPGSRMTPQGPSMGPPGYGGNPSVRPGLAQSGMDQSRKRPAPQQIQQVQQQAVQNRNHNAKKKKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRLDIQEALKRPIKQKRKLRIFISNTFNPAKSDAEDGEGTVASWELRVEGRLLEDAALSKYDATKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTATTQETDGFQVKRPGDVNVRCTVLLMLDYQPPQFKLDPRLARLLGIHTQTRPVIIQALWQYIKTHKLQDPHEREFVLCDKYLQQIFESQRMKFSEIPQRLHALLMPPEPIIINHVISVDPNDQKKTACYDIDVEVDDTLKTQMNSFLLSTASQQEIATLDNKIHETIETINQLKTQREFMLSFARDPQGFINDWLQSQCRDLKTMTDVVGNPEEERRAEFYFQPWAQEAVCRYFYSKVQQRRQELEQALGIRNT | |
| 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 |
|---|---|---|---|---|---|
| 33 | Phosphorylation | AALGPGGTPGPPVRM HHCCCCCCCCCCCCC | 30.87 | 26643407 | |
| 68 | Methylation | PGMLPGSRMTPQGPS CCCCCCCCCCCCCCC | 38.62 | - | |
| 70 | Phosphorylation | MLPGSRMTPQGPSMG CCCCCCCCCCCCCCC | 16.02 | 26643407 | |
| 88 | Asymmetric dimethylarginine | YGGNPSVRPGLAQSG CCCCCCCCCCCHHCC | 24.73 | - | |
| 88 | Methylation | YGGNPSVRPGLAQSG CCCCCCCCCCCHHCC | 24.73 | 24129315 | |
| 100 | Dimethylation | QSGMDQSRKRPAPQQ HCCCCCCCCCCCHHH | 33.11 | - | |
| 100 | Methylation | QSGMDQSRKRPAPQQ HCCCCCCCCCCCHHH | 33.11 | 54541477 | |
| 187 | Phosphorylation | RKLRIFISNTFNPAK CCCEEEEECCCCCCC | 21.04 | 26643407 | |
| 189 | Phosphorylation | LRIFISNTFNPAKSD CEEEEECCCCCCCCC | 20.28 | 26643407 | |
| 195 | Phosphorylation | NTFNPAKSDAEDGEG CCCCCCCCCCCCCCC | 44.13 | 26643407 | |
| 203 | Phosphorylation | DAEDGEGTVASWELR CCCCCCCCEEEEEEE | 14.48 | - | |
| 223 | Acetylation | LEDAALSKYDATKQK ECHHHHHCCCCHHHH | 48.26 | 23806337 | |
| 464 | Ubiquitination | QSQCRDLKTMTDVVG HHHHCCCCHHHHCCC | 40.31 | 22790023 | |
| 515 | Phosphorylation | QALGIRNT------- HHHCCCCC------- | 30.09 | 24719451 |
| 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 SMRD1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMRD1_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 SMRD1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| JUN_RAT | Jun | physical | 11053448 | |
| FOS_RAT | Fos | physical | 11053448 | |
| JUNB_HUMAN | JUNB | physical | 11053448 | |
| SMCA2_MOUSE | Smarca2 | physical | 11053448 | |
| TBX1_MOUSE | Tbx1 | physical | 22438823 | |
| P53_MOUSE | Trp53 | physical | 18303029 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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