SMRC1_MOUSE - dbPTM
SMRC1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMRC1_MOUSE
UniProt AC P97496
Protein Name SWI/SNF complex subunit SMARCC1
Gene Name Smarcc1
Organism Mus musculus (Mouse).
Sequence Length 1104
Subcellular Localization Nucleus . Cytoplasm .
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. May stimulate the ATPase activity of the catalytic subunit of the complex. 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 MAATAGGGPGAAAGAVGAGGAAAASGLAVYRRKDGGPASKFWESPDTVSQLDSVRVWLGKHYKKYVHADAPTNKTLAGLVVQLLQFQEDAFGKHVTNPAFTKLPAKCFMDFKAGGTLCHILGAAYKYKNEQGWRRFDLQNPSRMDRNVEMFMNIEKTLVQNNCLTRPNIYLIPDIDLKLANKLKDIIKRHQGTFTDEKSKASHHIYPYPSSQEDEEWLRPVMRRDKQVLVHWGFYPDSYDTWVHSNDVDAEIEDAPIPEKPWKVHVKWILDTDVFNEWMNEEDYEVDENRKPVSFRQRISTKNEEPVRSPERRDRKASANSRKRKPSPSPPPPTATESRKKSGKKGQASLYGKRRSQKEEDEQEDLTKDMEDPTPVPNIEEVVLPKNVNPKKDSENTPVKGGTVADLDEQDEEAVTTGGKEDEDPSKGDPSRSVDPGEDNVTEQTNHIIIPSYASWFDYNCIHVIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLTGDVCAVMRVHAFLEQWGLVNYQVDPESRPMAMGPPPTPHFNVLADTPSGLVPLHLRSPQVPAAQQMLNFPEKNKEKPIDLQNFGLRTDIYSKKTLAKSKGASAGREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLENSDASLGPLAYQPVPFSQSGNPVMSTVAFLASVVDPRVASAAAKAALEEFSRVREEVPLELVEAHVKKVQEAARASGKVDPTYGLESSCIAGTGPDEPEKLEGSEEEKMETDPDGQQPEKAENKVENESDEGDKIQDRENEKNTEKEQDSDVSEDVKPEEKENEENKELTDTCKERESDAGKKKVEHEISEGNVATAAAAALASAATKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREKEALEQQRQQLLTERQNFHMEQLKYAELRARQQMEQQQQHGQTPQQAHQHTGGPGMAPLGATGHPGMMPHQQPPPYPLMHHQMPPPHPPQPGQIPGPGSMMPGQPMPGRMIPAVAANIHPTGSGPTPPGMPPMPGNILGPRVPLTAPNGMYPPPPQQQQPPPPADGVPPPPAPGPPASATP
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
4Phosphorylation----MAATAGGGPGA
----CCCCCCCCCCC		32.6629899451
25PhosphorylationAGGAAAASGLAVYRR
HHHHHHHHCCEEEEE		29.6120469934
30PhosphorylationAASGLAVYRRKDGGP
HHHCCEEEEECCCCC		10.0929899451
170PhosphorylationCLTRPNIYLIPDIDL
CCCCCCEEECCCCCH		12.76-
178UbiquitinationLIPDIDLKLANKLKD
ECCCCCHHHHHHHHH		41.6322790023
300PhosphorylationVSFRQRISTKNEEPV
CCHHHHHCCCCCCCC		35.2019144319
309PhosphorylationKNEEPVRSPERRDRK
CCCCCCCCHHHHHHH		31.2026824392
318PhosphorylationERRDRKASANSRKRK
HHHHHHHHCCCCCCC		30.9027555448
327PhosphorylationNSRKRKPSPSPPPPT
CCCCCCCCCCCCCCC		40.8327087446
329PhosphorylationRKRKPSPSPPPPTAT
CCCCCCCCCCCCCCC		55.1427087446
334PhosphorylationSPSPPPPTATESRKK
CCCCCCCCCCHHHHH		52.5721082442
336PhosphorylationSPPPPTATESRKKSG
CCCCCCCCHHHHHCC		36.6523375375
338PhosphorylationPPPTATESRKKSGKK
CCCCCCHHHHHCCCC		45.0722802335
344AcetylationESRKKSGKKGQASLY
HHHHHCCCCCCCHHH		61.90-
345AcetylationSRKKSGKKGQASLYG
HHHHCCCCCCCHHHC		60.8323806337
349PhosphorylationSGKKGQASLYGKRRS
CCCCCCCHHHCHHHC		17.7827149854
353AcetylationGQASLYGKRRSQKEE
CCCHHHCHHHCCCHH		30.95130111
356PhosphorylationSLYGKRRSQKEEDEQ
HHHCHHHCCCHHHHH		50.0321149613
358AcetylationYGKRRSQKEEDEQED
HCHHHCCCHHHHHHH		65.4022826441
374PhosphorylationTKDMEDPTPVPNIEE
HHCCCCCCCCCCCEE		49.60-
386AcetylationIEEVVLPKNVNPKKD
CEEEECCCCCCCCCC		70.1723236377
394PhosphorylationNVNPKKDSENTPVKG
CCCCCCCCCCCCCCC		41.4425619855
397PhosphorylationPKKDSENTPVKGGTV
CCCCCCCCCCCCCEE		25.9627087446
403PhosphorylationNTPVKGGTVADLDEQ
CCCCCCCEECCCCCC		22.6125619855
416PhosphorylationEQDEEAVTTGGKEDE
CCCHHHHHCCCCCCC		27.1125619855
417PhosphorylationQDEEAVTTGGKEDED
CCHHHHHCCCCCCCC		37.0225619855
552PhosphorylationMAMGPPPTPHFNVLA
CCCCCCCCCCCEEEC		34.86-
572PhosphorylationLVPLHLRSPQVPAAQ
CEEEECCCCCCCHHH		26.5021082442
587UbiquitinationQMLNFPEKNKEKPID
HHHCCCHHHCCCCCC		73.8222790023
591UbiquitinationFPEKNKEKPIDLQNF
CCHHHCCCCCCHHHC		49.2122790023
627PhosphorylationREWTEQETLLLLEAL
CCCCHHHHHHHHHHH		23.5425338131
637PhosphorylationLLEALEMYKDDWNKV
HHHHHHHHHHCHHHH		11.2425338131
715UbiquitinationRVASAAAKAALEEFS
HHHHHHHHHHHHHHH		29.48-
722PhosphorylationKAALEEFSRVREEVP
HHHHHHHHHHHCCCC		32.9025266776
747PhosphorylationVQEAARASGKVDPTY
HHHHHHHCCCCCCCC		33.33-
753PhosphorylationASGKVDPTYGLESSC
HCCCCCCCCCCCCHH		26.2625619855
764PhosphorylationESSCIAGTGPDEPEK
CCHHCCCCCCCCHHH		36.2025619855
775PhosphorylationEPEKLEGSEEEKMET
CHHHCCCCHHHHCCC		32.2421082442
800PhosphorylationENKVENESDEGDKIQ
HHHCCCCCCCCCCCC		53.1727087446
815PhosphorylationDRENEKNTEKEQDSD
HHHHHHCCHHHHCCC		60.5525619855
821PhosphorylationNTEKEQDSDVSEDVK
CCHHHHCCCCCCCCC		39.3425521595
824PhosphorylationKEQDSDVSEDVKPEE
HHHCCCCCCCCCHHH		32.8225521595
881AcetylationASAATKAKHLAAVEE
HHHHHHHHHHHHHHH		40.4823806337
881UbiquitinationASAATKAKHLAAVEE
HHHHHHHHHHHHHHH		40.4822790023
905AcetylationLVETQMKKLEIKLRH
HHHHHHHHHHHHHHH		46.1121728379
909AcetylationQMKKLEIKLRHFEEL
HHHHHHHHHHHHHHH		30.0521728379
947AcetylationNFHMEQLKYAELRAR
HHCHHHHHHHHHHHH		41.95-
1064Asymmetric dimethylargininePGNILGPRVPLTAPN
CCCCCCCCCCCCCCC		40.67-
1064MethylationPGNILGPRVPLTAPN
CCCCCCCCCCCCCCC		40.6724129315
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 SMRC1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMRC1_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 SMRC1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WWP2_MOUSEWwp2physical
24365151
ACL6A_HUMANACTL6Aphysical
26496610
REQU_HUMANDPF2physical
26496610
SMCA2_HUMANSMARCA2physical
26496610
SMCA4_HUMANSMARCA4physical
26496610
SMRC2_HUMANSMARCC2physical
26496610
SMRD1_HUMANSMARCD1physical
26496610
SMRD2_HUMANSMARCD2physical
26496610
SMCE1_HUMANSMARCE1physical
26496610
ARI1A_HUMANARID1Aphysical
26496610
BICRL_HUMANGLTSCR1Lphysical
26496610
CALL5_HUMANCALML5physical
26496610
NSF1C_HUMANNSFL1Cphysical
26496610
ARID2_HUMANARID2physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMRC1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-329, ANDMASS SPECTROMETRY.
"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-300; SER-327 ANDSER-329, AND MASS SPECTROMETRY.
"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-309; SER-327; SER-329AND THR-336, 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-327 AND SER-329, ANDMASS SPECTROMETRY.

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