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 |
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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 | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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