SMRC2_MOUSE - dbPTM
SMRC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMRC2_MOUSE
UniProt AC Q6PDG5
Protein Name SWI/SNF complex subunit SMARCC2
Gene Name Smarcc2
Organism Mus musculus (Mouse).
Sequence Length 1213
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. Can stimulate the ATPase activity of the catalytic subunit of these complexes. May be required for CoREST dependent repression of neuronal specific gene promoters in non-neuronal cells. 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 Critical regulator of myeloid differentiation, controlling granulocytopoiesis and the expression of genes involved in neutrophil granule formation]
Protein Sequence MAVRKKDGGPNVKYYEAADTVTQFDNVRLWLGKNYKKYIQAEPPTNKSLSSLVVQLLQFQEEVFGKHVSNAPLTKLPIKCFLDFKAGGSLCHILAAAYKFKSDQGWRRYDFQNPSRMDRNVEMFMTIEKSLVQNNCLSRPNIFLCPEIEPKLLGKLKDIVKRHQGTISEDKSNASHVVYPVPGNLEEEEWVRPVMKRDKQVLLHWGYYPDSYDTWIPASEIEASVEDAPTPEKPRKVHAKWILDTDTFNEWMNEEDYEVSDDKSPVSRRKKISAKTLTDEVNSPDSDRRDKKGGNYKKRKRSPSPSPTPEAKKKNAKKGPSTPYTKSKRGHREEEQEDLTKDMDEPSPVPNVEEVTLPKTVNTKKDSESAPVKGGTMTDLDEQDDESMETTGKDEDENSTGNKGEQTKNPDLHEDNVTEQTHHIIIPSYAAWFDYNSVHAIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQVDAESRPTPMGPPPTSHFHVLADTPSGLVPLQPKPPQQSSASQQMLNFPEKGKEKPADMQNFGLRTDMYTKKNVPSKSKAAASATREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLEDSEASLGPLAYQPIPFSQSGNPVMSTVAFLASVVDPRVASAAAKSALEEFSKMKEEVPTALVEAHVRKVEEAAKVTGKADPAFGLESSGIAGTASDEPERIEESGTEEARPEGQAADEKKEPKEPREGGGAVEEEAKEEISEVPKKDEEKGKEGDSEKESEKSDGDPIVDPEKDKEPTEGQEEVLKEVAEPEGERKTKVERDIGEGNLSTAAAAALAAAAVKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREREALEYQRQQLLADRQAFHMEQLKYAEMRARQQHFQQMHQQQQQQPPTLPPGSQPIPPTGAAGPPTVHGLAVPPAAVASAPPGSGAPPGSLGPSEQIGQAGTTAGPQQPQQAGAPQPGAVPPGVPPPGPHGPSPFPNQPTPPSMMPGAVPGSGHPGVAGNAPLGLPFGMPPPPPAAPSVIPFGSLADSISINLPPPPNLHGHHHHLPFAPGTIPPPNLPVSMANPLHPNLPATTTMPSSLPLGPGLGSAAAQSPAIVAAVQGNLLPSASPLPDPGTPLPPDPTAPSPGTVTPVPPPQ
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
14PhosphorylationDGGPNVKYYEAADTV
CCCCCCEEEECCCCC		11.4021454597
20PhosphorylationKYYEAADTVTQFDNV
EEEECCCCCCHHHCE		22.2621454597
22PhosphorylationYEAADTVTQFDNVRL
EECCCCCCHHHCEEE		26.1321454597
33UbiquitinationNVRLWLGKNYKKYIQ
CEEEECCCCHHHHHC		55.7422790023
37MalonylationWLGKNYKKYIQAEPP
ECCCCHHHHHCCCCC		36.9126320211
69PhosphorylationEVFGKHVSNAPLTKL
HHHCCCCCCCCCCCC		27.3028066266
273PhosphorylationVSRRKKISAKTLTDE
CCHHHCCCCEECCCC		32.3720139300
276PhosphorylationRKKISAKTLTDEVNS
HHCCCCEECCCCCCC		34.3125619855
278PhosphorylationKISAKTLTDEVNSPD
CCCCEECCCCCCCCC		35.0325168779
283PhosphorylationTLTDEVNSPDSDRRD
ECCCCCCCCCCCCCC		34.9527087446
286PhosphorylationDEVNSPDSDRRDKKG
CCCCCCCCCCCCCCC		36.0825521595
302PhosphorylationNYKKRKRSPSPSPTP
CCCCCCCCCCCCCCH		32.5327087446
304PhosphorylationKKRKRSPSPSPTPEA
CCCCCCCCCCCCHHH		38.9827087446
306PhosphorylationRKRSPSPSPTPEAKK
CCCCCCCCCCHHHHH		45.8225521595
308PhosphorylationRSPSPSPTPEAKKKN
CCCCCCCCHHHHHHC		37.7925521595
318MalonylationAKKKNAKKGPSTPYT
HHHHCCCCCCCCCCC		73.9026320211
321PhosphorylationKNAKKGPSTPYTKSK
HCCCCCCCCCCCCCC		51.1626745281
322PhosphorylationNAKKGPSTPYTKSKR
CCCCCCCCCCCCCCC		24.3724453211
324PhosphorylationKKGPSTPYTKSKRGH
CCCCCCCCCCCCCCC		27.2123608596
325PhosphorylationKGPSTPYTKSKRGHR
CCCCCCCCCCCCCCC		30.0028066266
326AcetylationGPSTPYTKSKRGHRE
CCCCCCCCCCCCCCH		48.41-
340PhosphorylationEEEQEDLTKDMDEPS
HHHHHHHHCCCCCCC		37.0025159016
347PhosphorylationTKDMDEPSPVPNVEE
HCCCCCCCCCCCCEE		36.1624925903
356PhosphorylationVPNVEEVTLPKTVNT
CCCCEEEECCCEECC		40.3925619855
367PhosphorylationTVNTKKDSESAPVKG
EECCCCCCCCCCCCC		42.1826824392
369PhosphorylationNTKKDSESAPVKGGT
CCCCCCCCCCCCCCC		41.6529550500
376PhosphorylationSAPVKGGTMTDLDEQ
CCCCCCCCCCCCHHC		26.0925521595
378PhosphorylationPVKGGTMTDLDEQDD
CCCCCCCCCCHHCCC		32.9925521595
387PhosphorylationLDEQDDESMETTGKD
CHHCCCHHHHHCCCC		28.9825521595
390PhosphorylationQDDESMETTGKDEDE
CCCHHHHHCCCCCCC		32.0123737553
391PhosphorylationDDESMETTGKDEDEN
CCHHHHHCCCCCCCC		29.0023737553
399PhosphorylationGKDEDENSTGNKGEQ
CCCCCCCCCCCCCCC		35.3325521595
400PhosphorylationKDEDENSTGNKGEQT
CCCCCCCCCCCCCCC		57.2523737553
486S-palmitoylationEYLTSTACRRNLAGD
HHHHHHHHHHHCCHH		4.2126165157
568UbiquitinationFPEKGKEKPADMQNF
CCCCCCCCCCHHHHC		49.3322790023
606PhosphorylationREWTEQETLLLLEAL
CHHHHHHHHHHHHHH		23.5425338131
616PhosphorylationLLEALEMYKDDWNKV
HHHHHHHHHHCHHHH		11.2425338131
635S-palmitoylationGSRTQDECILHFLRL
CCCCHHHHHHHHHHC		5.5826165157
635GlutathionylationGSRTQDECILHFLRL
CCCCHHHHHHHHHHC		5.5824333276
694UbiquitinationRVASAAAKSALEEFS
HHHHHHHHHHHHHHH		31.3822790023
704UbiquitinationLEEFSKMKEEVPTAL
HHHHHHHHHHCCHHH		55.2322790023
743PhosphorylationESSGIAGTASDEPER
CCCCCCCCCCCCHHH		17.6128066266
745PhosphorylationSGIAGTASDEPERIE
CCCCCCCCCCHHHHH		42.2028066266
754PhosphorylationEPERIEESGTEEARP
CHHHHHHCCCCCCCC		37.9227841257
806PhosphorylationEKGKEGDSEKESEKS
HCCCCCCCHHHHHCC		62.5225521595
810PhosphorylationEGDSEKESEKSDGDP
CCCCHHHHHCCCCCC		62.4825521595
813PhosphorylationSEKESEKSDGDPIVD
CHHHHHCCCCCCCCC		42.6525521595
825UbiquitinationIVDPEKDKEPTEGQE
CCCCCCCCCCCCCHH		76.3422790023
872UbiquitinationALAAAAVKAKHLAAV
HHHHHHHHHHHHHHH		47.1722790023
874UbiquitinationAAAAVKAKHLAAVEE
HHHHHHHHHHHHHHH		33.1722790023
898AcetylationLVETQMKKLEIKLRH
HHHHHHHHHHHHHHC		46.1130795595
902AcetylationQMKKLEIKLRHFEEL
HHHHHHHHHHCHHHH		30.0524613203
940UbiquitinationAFHMEQLKYAEMRAR
HHHHHHHHHHHHHHH		41.9522790023
1192PhosphorylationSPLPDPGTPLPPDPT
CCCCCCCCCCCCCCC		27.3425338131
1202PhosphorylationPPDPTAPSPGTVTPV
CCCCCCCCCCCCCCC		33.2325338131
1207PhosphorylationAPSPGTVTPVPPPQ-
CCCCCCCCCCCCCC-		20.5725338131
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 SMRC2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMRC2_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 SMRC2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SMRC2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMRC2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-302; SER-304;SER-806 AND SER-810, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-347, ANDMASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-304, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASSSPECTROMETRY.

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