SMCE1_MOUSE - dbPTM
SMCE1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Methylation----MSKRPSYAPPP
----CCCCCCCCCCC
20.35-
21PhosphorylationAPATQMPSTPGFVGY
CCCCCCCCCCCCCCC
41.72-
22UbiquitinationPATQMPSTPGFVGYN
CCCCCCCCCCCCCCC
22.8927667366
40MethylationHLAYNNYRLGGNPGT
CEEECCCCCCCCCCC
29.04-
57UbiquitinationRVTASSGITIPKPPK
CEEECCCCCCCCCCC
3.2227667366
73PhosphorylationPDKPLMPYMRYSRKV
CCCCCCCCCHHCHHH
4.73-
92UbiquitinationKASNPDLKLWEIGKI
HHHCCCCHHHHHHHH
59.9627667366
146AcetylationYLAYINAKSRAEAAL
HHHHHCHHHHHHHHH
35.6722826441
157PhosphorylationEAALEEESRQRQSRM
HHHHHHHHHHHHHHH
36.67-
189UbiquitinationYDDGFSMKHTATARF
CCCCCCCCHHHHHHH
36.28-
201UbiquitinationARFQRNHRLISEILS
HHHHHHHHHHHHHHC
36.9527667366
204PhosphorylationQRNHRLISEILSESV
HHHHHHHHHHHCCCC
24.1529514104
236UbiquitinationRQVQSLMVHQRKLEA
HHHHHHHHHHHHHHH
4.1627667366
240UbiquitinationSLMVHQRKLEAELLQ
HHHHHHHHHHHHHHH
44.07-
262PhosphorylationKKRKFLESTDSFNNE
HHHHHHHCCHHHHHH
39.3929899451
263PhosphorylationKRKFLESTDSFNNEL
HHHHHHCCHHHHHHH
26.7026643407
265PhosphorylationKFLESTDSFNNELKR
HHHHCCHHHHHHHHH
29.9326643407
271UbiquitinationDSFNNELKRLCGLKV
HHHHHHHHHHHCCCE
36.8327667366
316PhosphorylationEQAERSQSSMAPEEE
HHHHHHHHCCCHHHH
24.2728973931
328AcetylationEEEQVANKAEEKKDE
HHHHHHHHHHHHCCC
47.6523236377
353PhosphorylationHLEDTAESQQNGEEG
HHHHHHHHHHCCCCC
34.3028285833
361PhosphorylationQQNGEEGTSTPEDKE
HHCCCCCCCCHHHHH
32.4826643407
362PhosphorylationQNGEEGTSTPEDKES
HCCCCCCCCHHHHHC
53.4725521595
363PhosphorylationNGEEGTSTPEDKESG
CCCCCCCCHHHHHCC
30.4527087446
369PhosphorylationSTPEDKESGQEGVDS
CCHHHHHCCCCCCCE
52.0625367039
376PhosphorylationSGQEGVDSMEVEGTS
CCCCCCCEEEEECCC
17.9025367039
382PhosphorylationDSMEVEGTSDSNTGS
CEEEEECCCCCCCCC
18.8225367039
383PhosphorylationSMEVEGTSDSNTGSE
EEEEECCCCCCCCCC
50.3125367039
385PhosphorylationEVEGTSDSNTGSESN
EEECCCCCCCCCCCC
35.7425367039
387PhosphorylationEGTSDSNTGSESNSA
ECCCCCCCCCCCCCC
46.1425367039
389PhosphorylationTSDSNTGSESNSATV
CCCCCCCCCCCCCCC
35.4925367039
391PhosphorylationDSNTGSESNSATVEE
CCCCCCCCCCCCCCC
37.4725367039
393PhosphorylationNTGSESNSATVEEPP
CCCCCCCCCCCCCCC
34.3025367039
395PhosphorylationGSESNSATVEEPPTD
CCCCCCCCCCCCCCC
28.4225367039
401PhosphorylationATVEEPPTDPVPEDE
CCCCCCCCCCCCHHH
64.7525367039

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 SMCE1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMCE1_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 SMCE1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOA1_HUMANNCOA1physical
12145209
NCOA2_HUMANNCOA2physical
12145209
ESR1_MOUSEEsr1physical
12145209
SMCA4_MOUSESmarca4physical
19781646
NCOA3_HUMANNCOA3physical
12145209

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMCE1_MOUSE

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Related Literatures of Post-Translational Modification

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