SMCA4_MOUSE - dbPTM
SMCA4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMCA4_MOUSE
UniProt AC Q3TKT4
Protein Name Transcription activator BRG1
Gene Name Smarca4
Organism Mus musculus (Mouse).
Sequence Length 1613
Subcellular Localization Nucleus . Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds.
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. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP (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 in regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues. Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1 (By similarity). Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2. [PubMed: 26138476 Binds to RNA in a promiscuous manner]
Protein Sequence MSTPDPPLGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSMMGPSPGPPSAGHPMPTQGPGGYPQDNMHQMHKPMESMHEKGMPDDPRYNQMKGMGMRSGAHTGMAPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGSDPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPLVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFREYHRSVTGKLQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQPAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDEEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSEAGSSTPTTSTRSRDKDEESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
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
2Phosphorylation------MSTPDPPLG
------CCCCCCCCC		61.0129233185
3Phosphorylation-----MSTPDPPLGG
-----CCCCCCCCCC		43.5026824392
11PhosphorylationPDPPLGGTPRPGPSP
CCCCCCCCCCCCCCC		17.8329233185
17PhosphorylationGTPRPGPSPGPGPSP
CCCCCCCCCCCCCCC		48.6925338131
78PhosphorylationQMHKPMESMHEKGMP
HCCCCHHHHHHCCCC		21.1326745281
188AcetylationRAQIMAYKMLARGQP
HHHHHHHHHHHCCCC		20.21-
296PhosphorylationMANAAAPTSTPQKLI
CCCCCCCCCCCCCCC		40.2726643407
297PhosphorylationANAAAPTSTPQKLIP
CCCCCCCCCCCCCCC		36.7126643407
298PhosphorylationNAAAPTSTPQKLIPP
CCCCCCCCCCCCCCC		32.0126643407
308PhosphorylationKLIPPQPTGRPSPAP
CCCCCCCCCCCCCCC		40.3423140645
312PhosphorylationPQPTGRPSPAPPAVP
CCCCCCCCCCCCCCC		32.1221183079
323PhosphorylationPAVPPAASPVMPPQT
CCCCCCCCCCCCCCC		21.8229233185
330PhosphorylationSPVMPPQTQSPGQPA
CCCCCCCCCCCCCCC		36.4721183079
332PhosphorylationVMPPQTQSPGQPAQP
CCCCCCCCCCCCCCC		34.0929233185
353PhosphorylationHQKQSRITPIQKPRG
CCCCCCCCCCCCCCC		17.1528066266
405 (in isoform 2)Ubiquitination-32.3622790023
405UbiquitinationTKATIELKALRLLNF
CCHHHHHHHHHHHHH		32.3622790023
492PhosphorylationDFREYHRSVTGKLQK
HHHHHHHHHHHHHHH		15.66-
494PhosphorylationREYHRSVTGKLQKLT
HHHHHHHHHHHHHHH		29.82-
596PhosphorylationAENAEGQTPAIGPDG
HHCCCCCCCCCCCCC		26.0825619855
609PhosphorylationDGEPLDETSQMSDLP
CCCCCCCCCCCCCCC		24.7526824392
610PhosphorylationGEPLDETSQMSDLPV
CCCCCCCCCCCCCCE		23.1027087446
613PhosphorylationLDETSQMSDLPVKVI
CCCCCCCCCCCEEEE		28.4927087446
626AcetylationVIHVESGKILTGTDA
EEEEECCCEEECCCC		43.7723236377
655PhosphorylationGYEVAPRSDSEESGS
CCCCCCCCCCCCCCC		44.4220531401
657PhosphorylationEVAPRSDSEESGSEE
CCCCCCCCCCCCCHH		44.5020531401
660PhosphorylationPRSDSEESGSEEEEE
CCCCCCCCCCHHHHH		43.5020531401
662PhosphorylationSDSEESGSEEEEEEE
CCCCCCCCHHHHHHH		51.6320531401
695PhosphorylationKKIPDPDSDDVSEVD
CCCCCCCCCCCCHHH		40.8927087446
699PhosphorylationDPDSDDVSEVDARHI
CCCCCCCCHHHHHHH		38.6127087446
718PhosphorylationKQDVDDEYGVSQALA
HHCCCCCCHHHHHHH		29.8025159016
850PhosphorylationAFVPQLRSGKFNVLL
HHHHHHHCCCCCEEE		55.73-
935PhosphorylationLLPTIFKSCSTFEQW
HHHHHHHHCHHHHHH		11.5323375375
937PhosphorylationPTIFKSCSTFEQWFN
HHHHHHCHHHHHHHC		43.1323375375
950PhosphorylationFNAPFAMTGEKVDLN
HCCCCCCCCCCCCCC		38.4723375375
1022PhosphorylationGVLLTDGSEKDKKGK
CEEECCCCCCCCCCC		44.2622871156
1032PhosphorylationDKKGKGGTKTLMNTI
CCCCCCCHHHHHHHH		29.53-
1325PhosphorylationDAEVERLTCEEEEEK
CHHCEECCCHHHHHH		24.8829550500
1338PhosphorylationEKMFGRGSRHRKEVD
HHHCCCCCCCCCCCC		24.4529176673
1346PhosphorylationRHRKEVDYSDSLTEK
CCCCCCCCCCCCCHH		21.3928833060
1347PhosphorylationHRKEVDYSDSLTEKQ
CCCCCCCCCCCCHHH		19.0928833060
1349PhosphorylationKEVDYSDSLTEKQWL
CCCCCCCCCCHHHHH		31.1125521595
1351PhosphorylationVDYSDSLTEKQWLKA
CCCCCCCCHHHHHHH		45.1228833060
1363PhosphorylationLKAIEEGTLEEIEEE
HHHHHHCCHHHHHHH		33.99-
1384PhosphorylationSRKRKRDSEAGSSTP
HHHHHCCCCCCCCCC		33.1228833060
1388PhosphorylationKRDSEAGSSTPTTST
HCCCCCCCCCCCCCC		37.7825521595
1389PhosphorylationRDSEAGSSTPTTSTR
CCCCCCCCCCCCCCC		37.1727087446
1390PhosphorylationDSEAGSSTPTTSTRS
CCCCCCCCCCCCCCC		26.7625521595
1392PhosphorylationEAGSSTPTTSTRSRD
CCCCCCCCCCCCCCC		33.2027742792
1393PhosphorylationAGSSTPTTSTRSRDK
CCCCCCCCCCCCCCC		29.3328833060
1394PhosphorylationGSSTPTTSTRSRDKD
CCCCCCCCCCCCCCC		25.0525521595
1395PhosphorylationSSTPTTSTRSRDKDE
CCCCCCCCCCCCCCH		30.4828833060
1419PhosphorylationRPPAEKLSPNPPNLT
CCCHHHCCCCCCCHH		33.4327087446
1426PhosphorylationSPNPPNLTKKMKKIV
CCCCCCHHHHHHHHH		34.9525619855
1484UbiquitinationKERIRNHKYRSLNDL
HHHHHHCCCCCHHHH		46.0022790023
1484 (in isoform 2)Ubiquitination-46.0022790023
1485 (in isoform 2)Ubiquitination-9.62-
1487PhosphorylationIRNHKYRSLNDLEKD
HHHCCCCCHHHHHHH		28.5627149854
1516PhosphorylationGSLIYEDSIVLQSVF
CCEEECCCHHHHHHH		11.5822802335
1521PhosphorylationEDSIVLQSVFTSVRQ
CCCHHHHHHHHHHHH		18.2922802335
1536PhosphorylationKIEKEDDSEGEESEE
HHHHCCCCCCCCCHH		60.8827087446
1541PhosphorylationDDSEGEESEEEEEGE
CCCCCCCCHHHHHCC		46.1127087446
1552PhosphorylationEEGEEEGSESESRSV
HHCCCCCCCCCCCCE		41.0327087446
1554PhosphorylationGEEEGSESESRSVKV
CCCCCCCCCCCCEEE		42.4425159016
1556PhosphorylationEEGSESESRSVKVKI
CCCCCCCCCCEEEEE		38.8529550500
1593PhosphorylationSRAKPVVSDDDSEEE
CCCCCCCCCCCCHHH		35.2423684622
1597PhosphorylationPVVSDDDSEEEQEED
CCCCCCCCHHHHHHH		54.6323684622
1605MethylationEEEQEEDRSGSGSEE
HHHHHHHCCCCCCCC		46.3116186125
1606PhosphorylationEEQEEDRSGSGSEED
HHHHHHCCCCCCCCC		50.0229895711
1608PhosphorylationQEEDRSGSGSEED--
HHHHCCCCCCCCC--		40.1529895711
1610PhosphorylationEDRSGSGSEED----
HHCCCCCCCCC----		39.2429895711
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 SMCA4_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMCA4_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 SMCA4_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
7923370
NR1H4_MOUSENr1h4physical
19805516
ANM5_MOUSEPrmt5physical
17043109
CREST_MOUSESs18l1physical
19279220
SFPQ_MOUSESfpqphysical
19279220
NONO_MOUSENonophysical
19279220
MBB1A_MOUSEMybbp1aphysical
19279220
SRRM2_MOUSESrrm2physical
19279220
BRD9_MOUSEBrd9physical
19279220
BRD7_MOUSEBrd7physical
19279220
BCL7A_MOUSEBcl7aphysical
19279220
ACTG_MOUSEActg1physical
19279220
REQU_MOUSEDpf2physical
19279220
PHF10_MOUSEPhf10physical
19279220
ACL6A_MOUSEActl6aphysical
19279220
SNF5_MOUSESmarcb1physical
19279220
SMCE1_MOUSESmarce1physical
19279220
SMRD3_MOUSESmarcd3physical
19279220
SMRD1_MOUSESmarcd1physical
19279220
SMRC1_MOUSESmarcc1physical
19279220
SMRC2_MOUSESmarcc2physical
19279220
ARI1A_MOUSEArid1aphysical
19279220
SMCA2_MOUSESmarca2physical
19279220
ETS2_MOUSEEts2physical
12637547
ACL6B_MOUSEActl6bphysical
12368262
ARI1A_MOUSEArid1aphysical
12368262
SMCA4_MOUSESmarca4physical
12368262
SMRC2_MOUSESmarcc2physical
12368262
SMRC1_MOUSESmarcc1physical
12368262
SMRD2_MOUSESmarcd2physical
12368262
SMCE1_MOUSESmarce1physical
12368262
SNF5_MOUSESmarcb1physical
12368262
RPB1_MOUSEPolr2aphysical
15999204
NF1_MOUSENf1physical
15999204
CDX2_MOUSECdx2physical
20485553
STAT6_MOUSEStat6physical
21262765
SMCE1_MOUSESmarce1physical
19781646
KDM6B_MOUSEKdm6bphysical
21095589
KDM6A_MOUSEKdm6aphysical
21095589
TBX5_MOUSETbx5genetic
21304516
NKX25_MOUSENkx2-5genetic
21304516
TBX20_MOUSETbx20genetic
21304516
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMCA4_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-1419, 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-695, AND MASSSPECTROMETRY.
"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-610 AND SER-613, ANDMASS SPECTROMETRY.
"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-695, AND MASSSPECTROMETRY.

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