UniProt ID | SMCE1_MOUSE | |
---|---|---|
UniProt AC | O54941 | |
Protein Name | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 | |
Gene Name | Smarce1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 411 | |
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. [PubMed: 12110891 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] | |
Protein Sequence | MSKRPSYAPPPTPAPATQMPSTPGFVGYNPYSHLAYNNYRLGGNPGTNSRVTASSGITIPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQSSMAPEEEQVANKAEEKKDEESIPMETEETHLEDTAESQQNGEEGTSTPEDKESGQEGVDSMEVEGTSDSNTGSESNSATVEEPPTDPVPEDEKKE | |
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 |
---|---|---|---|---|---|
4 | Methylation | ----MSKRPSYAPPP ----CCCCCCCCCCC | 20.35 | - | |
21 | Phosphorylation | APATQMPSTPGFVGY CCCCCCCCCCCCCCC | 41.72 | - | |
22 | Ubiquitination | PATQMPSTPGFVGYN CCCCCCCCCCCCCCC | 22.89 | 27667366 | |
40 | Methylation | HLAYNNYRLGGNPGT CEEECCCCCCCCCCC | 29.04 | - | |
57 | Ubiquitination | RVTASSGITIPKPPK CEEECCCCCCCCCCC | 3.22 | 27667366 | |
73 | Phosphorylation | PDKPLMPYMRYSRKV CCCCCCCCCHHCHHH | 4.73 | - | |
92 | Ubiquitination | KASNPDLKLWEIGKI HHHCCCCHHHHHHHH | 59.96 | 27667366 | |
146 | Acetylation | YLAYINAKSRAEAAL HHHHHCHHHHHHHHH | 35.67 | 22826441 | |
157 | Phosphorylation | EAALEEESRQRQSRM HHHHHHHHHHHHHHH | 36.67 | - | |
189 | Ubiquitination | YDDGFSMKHTATARF CCCCCCCCHHHHHHH | 36.28 | - | |
201 | Ubiquitination | ARFQRNHRLISEILS HHHHHHHHHHHHHHC | 36.95 | 27667366 | |
204 | Phosphorylation | QRNHRLISEILSESV HHHHHHHHHHHCCCC | 24.15 | 29514104 | |
236 | Ubiquitination | RQVQSLMVHQRKLEA HHHHHHHHHHHHHHH | 4.16 | 27667366 | |
240 | Ubiquitination | SLMVHQRKLEAELLQ HHHHHHHHHHHHHHH | 44.07 | - | |
262 | Phosphorylation | KKRKFLESTDSFNNE HHHHHHHCCHHHHHH | 39.39 | 29899451 | |
263 | Phosphorylation | KRKFLESTDSFNNEL HHHHHHCCHHHHHHH | 26.70 | 26643407 | |
265 | Phosphorylation | KFLESTDSFNNELKR HHHHCCHHHHHHHHH | 29.93 | 26643407 | |
271 | Ubiquitination | DSFNNELKRLCGLKV HHHHHHHHHHHCCCE | 36.83 | 27667366 | |
316 | Phosphorylation | EQAERSQSSMAPEEE HHHHHHHHCCCHHHH | 24.27 | 28973931 | |
328 | Acetylation | EEEQVANKAEEKKDE HHHHHHHHHHHHCCC | 47.65 | 23236377 | |
353 | Phosphorylation | HLEDTAESQQNGEEG HHHHHHHHHHCCCCC | 34.30 | 28285833 | |
361 | Phosphorylation | QQNGEEGTSTPEDKE HHCCCCCCCCHHHHH | 32.48 | 26643407 | |
362 | Phosphorylation | QNGEEGTSTPEDKES HCCCCCCCCHHHHHC | 53.47 | 25521595 | |
363 | Phosphorylation | NGEEGTSTPEDKESG CCCCCCCCHHHHHCC | 30.45 | 27087446 | |
369 | Phosphorylation | STPEDKESGQEGVDS CCHHHHHCCCCCCCE | 52.06 | 25367039 | |
376 | Phosphorylation | SGQEGVDSMEVEGTS CCCCCCCEEEEECCC | 17.90 | 25367039 | |
382 | Phosphorylation | DSMEVEGTSDSNTGS CEEEEECCCCCCCCC | 18.82 | 25367039 | |
383 | Phosphorylation | SMEVEGTSDSNTGSE EEEEECCCCCCCCCC | 50.31 | 25367039 | |
385 | Phosphorylation | EVEGTSDSNTGSESN EEECCCCCCCCCCCC | 35.74 | 25367039 | |
387 | Phosphorylation | EGTSDSNTGSESNSA ECCCCCCCCCCCCCC | 46.14 | 25367039 | |
389 | Phosphorylation | TSDSNTGSESNSATV CCCCCCCCCCCCCCC | 35.49 | 25367039 | |
391 | Phosphorylation | DSNTGSESNSATVEE CCCCCCCCCCCCCCC | 37.47 | 25367039 | |
393 | Phosphorylation | NTGSESNSATVEEPP CCCCCCCCCCCCCCC | 34.30 | 25367039 | |
395 | Phosphorylation | GSESNSATVEEPPTD CCCCCCCCCCCCCCC | 28.42 | 25367039 | |
401 | Phosphorylation | ATVEEPPTDPVPEDE CCCCCCCCCCCCHHH | 64.75 | 25367039 |
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 SMCE1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMCE1_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 SMCE1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NCOA1_HUMAN | NCOA1 | physical | 12145209 | |
NCOA2_HUMAN | NCOA2 | physical | 12145209 | |
ESR1_MOUSE | Esr1 | physical | 12145209 | |
SMCA4_MOUSE | Smarca4 | physical | 19781646 | |
NCOA3_HUMAN | NCOA3 | physical | 12145209 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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