SMRD1_MOUSE - dbPTM
SMRD1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
33PhosphorylationAALGPGGTPGPPVRM
HHCCCCCCCCCCCCC
30.8726643407
68MethylationPGMLPGSRMTPQGPS
CCCCCCCCCCCCCCC
38.62-
70PhosphorylationMLPGSRMTPQGPSMG
CCCCCCCCCCCCCCC
16.0226643407
88Asymmetric dimethylarginineYGGNPSVRPGLAQSG
CCCCCCCCCCCHHCC
24.73-
88MethylationYGGNPSVRPGLAQSG
CCCCCCCCCCCHHCC
24.7324129315
100DimethylationQSGMDQSRKRPAPQQ
HCCCCCCCCCCCHHH
33.11-
100MethylationQSGMDQSRKRPAPQQ
HCCCCCCCCCCCHHH
33.1154541477
187PhosphorylationRKLRIFISNTFNPAK
CCCEEEEECCCCCCC
21.0426643407
189PhosphorylationLRIFISNTFNPAKSD
CEEEEECCCCCCCCC
20.2826643407
195PhosphorylationNTFNPAKSDAEDGEG
CCCCCCCCCCCCCCC
44.1326643407
203PhosphorylationDAEDGEGTVASWELR
CCCCCCCCEEEEEEE
14.48-
223AcetylationLEDAALSKYDATKQK
ECHHHHHCCCCHHHH
48.2623806337
464UbiquitinationQSQCRDLKTMTDVVG
HHHHCCCCHHHHCCC
40.3122790023
515PhosphorylationQALGIRNT-------
HHHCCCCC-------
30.0924719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMRD1_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JUN_RATJunphysical
11053448
FOS_RATFosphysical
11053448
JUNB_HUMANJUNBphysical
11053448
SMCA2_MOUSESmarca2physical
11053448
TBX1_MOUSETbx1physical
22438823
P53_MOUSETrp53physical
18303029

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMRD1_MOUSE

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Related Literatures of Post-Translational Modification

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