ID SMCA4_MOUSE Reviewed; 1613 AA. AC Q3TKT4; Q3TUD7; Q6AXG8; DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Transcription activator BRG1; DE EC=3.6.4.-; DE AltName: Full=ATP-dependent helicase SMARCA4; DE AltName: Full=BRG1-associated factor 190A; DE Short=BAF190A; DE AltName: Full=Protein brahma homolog 1; DE AltName: Full=SNF2-beta; DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4; GN Name=Smarca4; Synonyms=Baf190a, Brg1, Snf2b, Snf2l4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS RP SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND RP INTERACTION WITH PHF10. RX PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019; RA Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H., RA Aebersold R., Graef I.A., Crabtree G.R.; RT "An essential switch in subunit composition of a chromatin remodeling RT complex during neural development."; RL Neuron 55:201-215(2007). RN [5] RP INTERACTION WITH MYOG. RX PubMed=16424906; DOI=10.1038/sj.emboj.7600943; RA Ohkawa Y., Marfella C.G., Imbalzano A.N.; RT "Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF ATPase RT Brg1."; RL EMBO J. 25:490-501(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-613, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610; SER-613; SER-695; RP SER-699; THR-1390; SER-1536; SER-1541 AND SER-1552, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [9] RP INTERACTION WITH KDM6A; KDM6B AND TBX21. RX PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028; RA Miller S.A., Mohn S.E., Weinmann A.S.; RT "Jmjd3 and UTX play a demethylase-independent role in chromatin remodeling RT to regulate T-box family member-dependent gene expression."; RL Mol. Cell 40:594-605(2010). RN [10] RP INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION. RX PubMed=22162999; DOI=10.1371/journal.pone.0028049; RA Vizlin-Hodzic D., Runnberg R., Ryme J., Simonsson S., Simonsson T.; RT "SAF-A forms a complex with BRG1 and both components are required for RNA RT polymerase II mediated transcription."; RL PLoS ONE 6:E28049-E28049(2011). RN [11] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=22952240; DOI=10.1074/jbc.r111.309302; RA Euskirchen G., Auerbach R.K., Snyder M.; RT "SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse RT functions."; RL J. Biol. Chem. 287:30897-30905(2012). RN [12] RP FUNCTION, INTERACTION WITH DLX1, SUBCELLULAR LOCATION, AND RNA-BINDING RP REGION. RX PubMed=26138476; DOI=10.1242/dev.126318; RA Cajigas I., Leib D.E., Cochrane J., Luo H., Swyter K.R., Chen S., RA Clark B.S., Thompson J., Yates J.R. III, Kingston R.E., Kohtz J.D.; RT "Evf2 lncRNA/BRG1/DLX1 interactions reveal RNA-dependent inhibition of RT chromatin remodeling."; RL Development 142:2641-2652(2015). RN [13] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=26601204; DOI=10.1126/sciadv.1500447; RA Kadoch C., Crabtree G.R.; RT "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic RT insights gained from human genomics."; RL Sci. Adv. 1:E1500447-E1500447(2015). RN [14] RP IDENTIFICATION IN THE GBAF COMPLEX. RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065; RA Alpsoy A., Dykhuizen E.C.; RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes."; RL J. Biol. Chem. 293:3892-3903(2018). RN [15] RP INTERACTION WITH HDGFL2. RX PubMed=32459350; DOI=10.1093/nar/gkaa441; RA Zhu X., Lan B., Yi X., He C., Dang L., Zhou X., Lu Y., Sun Y., Liu Z., RA Bai X., Zhang K., Li B., Li M.J., Chen Y., Zhang L.; RT "HRP2-DPF3a-BAF complex coordinates histone modification and chromatin RT remodeling to regulate myogenic gene transcription."; RL Nucleic Acids Res. 48:6563-6582(2020). RN [16] RP FUNCTION, INTERACTION WITH SMARCA4, AND SUBCELLULAR LOCATION. RX PubMed=34910916; DOI=10.1016/j.celrep.2021.110104; RA Choi K.M., Kim J.H., Kong X., Isik M., Zhang J., Lim H.W., Yoon J.C.; RT "Defective brown adipose tissue thermogenesis and impaired glucose RT metabolism in mice lacking Letmd1."; RL Cell Rep. 37:110104-110104(2021). CC -!- FUNCTION: Involved in transcriptional activation and repression of CC select genes by chromatin remodeling (alteration of DNA-nucleosome CC topology). Component of SWI/SNF chromatin remodeling complexes that CC carry out key enzymatic activities, changing chromatin structure by CC altering DNA-histone contacts within a nucleosome in an ATP-dependent CC manner. Component of the CREST-BRG1 complex, a multiprotein complex CC that regulates promoter activation by orchestrating the calcium- CC dependent release of a repressor complex and the recruitment of an CC activator complex. In resting neurons, transcription of the c-FOS CC promoter is inhibited by SMARCA4-dependent recruitment of a phospho- CC RB1-HDAC repressor complex. Upon calcium influx, RB1 is CC dephosphorylated by calcineurin, which leads to release of the CC repressor complex. At the same time, there is increased recruitment of CC CREBBP to the promoter by a CREST-dependent mechanism, which leads to CC transcriptional activation. The CREST-BRG1 complex also binds to the CC NR2B promoter, and activity-dependent induction of NR2B expression CC involves the release of HDAC1 and recruitment of CREBBP (By CC similarity). Belongs to the neural progenitors-specific chromatin CC remodeling complex (npBAF complex) and the neuron-specific chromatin CC remodeling complex (nBAF complex). During neural development, a switch CC from a stem/progenitor to a postmitotic chromatin remodeling mechanism CC occurs as neurons exit the cell cycle and become committed to their CC adult state. The transition from proliferating neural stem/progenitor CC cells to postmitotic neurons requires a switch in subunit composition CC of the npBAF and nBAF complexes. As neural progenitors exit mitosis and CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A CC and PHF10/BAF45A, are exchanged for homologous alternative CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- CC specific complexes (nBAF). The npBAF complex is essential for the self- CC renewal/proliferative capacity of the multipotent neural stem cells. CC The nBAF complex along with CREST plays a role in regulating the CC activity of genes essential for dendrite growth. SMARCA4/BAF190A may CC promote neural stem cell self-renewal/proliferation by enhancing Notch- CC dependent proliferative signals, while concurrently making the neural CC stem cell insensitive to SHH-dependent differentiating cues. Acts as a CC corepressor of ZEB1 to regulate E-cadherin transcription and is CC required for induction of epithelial-mesenchymal transition (EMT) by CC ZEB1 (By similarity). Binds via DLX1 to enhancers located in the CC intergenic region between DLX5 and DLX6 and this binding is stabilized CC by the long non-coding RNA (lncRNA) Evf2 (PubMed:26138476). Binds to CC RNA in a promiscuous manner (PubMed:26138476). Binding to RNAs CC including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and CC chromatin remodeling activities (PubMed:26138476). In brown adipose CC tissue, involved in the regulation of thermogenic genes expression CC (PubMed:34910916). {ECO:0000250|UniProtKB:P51532, CC ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:26138476, CC ECO:0000269|PubMed:34910916}. CC -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes CC SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The CC canonical complex contains a catalytic subunit (either CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. CC Other subunits specific to each of the complexes may also be present CC permitting several possible developmental- and tissue-specific CC combinations (Probable). Component of the BAF complex, which includes CC at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the CC BAF complex also contains DPF3. Component of neural progenitors- CC specific chromatin remodeling complex (npBAF complex) composed of at CC least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, CC PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific CC chromatin remodeling complex (nBAF complex) composed of at least, CC ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, CC SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, CC SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, CC DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of CC the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of CC SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, CC SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, CC SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin. CC Component of SWI/SNF (GBAF) subcomplex, which includes at least BICRA CC or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM, CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A CC (PubMed:29374058). Component of the BAF53 complex, at least composed of CC BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially CC acetylates histone H4 (and H2A) within nucleosomes (By similarity). CC Component of the CREST-BRG1 complex, at least composed of CC SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1 (By similarity). CC Interacts with PHF10/BAF45A (PubMed:17640523). Interacts with MYOG CC (PubMed:16424906). Interacts directly with IKFZ1; the interaction CC associates IKFZ1 with the BAF complex. Interacts with ZEB1 (via N- CC terminus). Interacts with NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7. CC Interacts with (via the bromodomain) with TERT; the interaction CC regulates Wnt-mediated signaling (By similarity). Interacts with KDM6A CC and KDM6B (PubMed:21095589). Interacts with TBX21 in a KDM6B-dependent CC manner (PubMed:21095589). Interacts with HNRNPU; this interaction CC occurs in embryonic stem cells and stimulates global Pol II-mediated CC transcription (PubMed:22162999). Interacts with ACTL6A (By similarity). CC Interacts with DLX1 (PubMed:26138476). Interacts with DPF2 (By CC similarity). Interacts with DPF3a (isoform 2 of DPF3/BAF45C) (By CC similarity). Interacts with HDGFL2 in a DPF3a-dependent manner CC (PubMed:32459350). May interact with ADNP2 (By similarity). Interacts CC with LETMD1 (via C-terminal); the interaction regulates transcriptional CC expression of thermogenic genes in brown adipose tissue CC (PubMed:34910916). Interacts (via KIKL motif) with BRD3 (via NET CC domain) (By similarity). {ECO:0000250|UniProtKB:P51532, CC ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:17640523, CC ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:22162999, CC ECO:0000269|PubMed:26138476, ECO:0000269|PubMed:29374058, CC ECO:0000269|PubMed:32459350, ECO:0000269|PubMed:34910916, CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. CC -!- INTERACTION: CC Q3TKT4; A2BH40: Arid1a; NbExp=7; IntAct=EBI-1210244, EBI-371499; CC Q3TKT4; E9Q4N7: Arid1b; NbExp=5; IntAct=EBI-1210244, EBI-6900614; CC Q3TKT4; O09106: Hdac1; NbExp=2; IntAct=EBI-1210244, EBI-301912; CC Q3TKT4; P70288: Hdac2; NbExp=4; IntAct=EBI-1210244, EBI-302251; CC Q3TKT4; O88895: Hdac3; NbExp=2; IntAct=EBI-1210244, EBI-302263; CC Q3TKT4; Q99N13: Hdac9; NbExp=3; IntAct=EBI-1210244, EBI-645361; CC Q3TKT4; Q8VEK3: Hnrnpu; NbExp=3; IntAct=EBI-1210244, EBI-529674; CC Q3TKT4; Q9Z2D6: Mecp2; NbExp=2; IntAct=EBI-1210244, EBI-1188816; CC Q3TKT4; Q01705: Notch1; NbExp=2; IntAct=EBI-1210244, EBI-1392707; CC Q3TKT4; P11103: Parp1; NbExp=2; IntAct=EBI-1210244, EBI-642213; CC Q3TKT4; P13405: Rb1; NbExp=3; IntAct=EBI-1210244, EBI-971782; CC Q3TKT4; P97496: Smarcc1; NbExp=7; IntAct=EBI-1210244, EBI-648047; CC Q3TKT4; Q6P9Z1: Smarcd3; NbExp=3; IntAct=EBI-1210244, EBI-7525857; CC Q3TKT4; O70372: Tert; NbExp=2; IntAct=EBI-1210244, EBI-9662790; CC Q3TKT4; Q01320: Top2a; NbExp=3; IntAct=EBI-1210244, EBI-642809; CC Q3TKT4; Q6P1E1: Zmiz1; NbExp=2; IntAct=EBI-1210244, EBI-647033; CC Q3TKT4; Q62908: Csrp2; Xeno; NbExp=3; IntAct=EBI-1210244, EBI-918425; CC Q3TKT4; P06400: RB1; Xeno; NbExp=4; IntAct=EBI-1210244, EBI-491274; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549, CC ECO:0000269|PubMed:26138476}. Note=Colocalizes with long non-coding RNA CC Evf2 in nuclear RNA clouds (PubMed:26138476). Localizes to sites of DNA CC damage (By similarity). {ECO:0000250|UniProtKB:P51532, CC ECO:0000269|PubMed:26138476}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q3TKT4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3TKT4-2; Sequence=VSP_038696; CC -!- DOMAIN: The KIKL motif recognizes and binds the NET domain of BRD3. CC {ECO:0000250|UniProtKB:P51532}. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK147285; BAE27821.1; -; mRNA. DR EMBL; AK160825; BAE36034.1; -; mRNA. DR EMBL; AK166837; BAE39059.1; -; mRNA. DR EMBL; BC079560; AAH79560.1; -; mRNA. DR EMBL; CH466522; EDL25209.1; -; Genomic_DNA. DR CCDS; CCDS22909.1; -. [Q3TKT4-2] DR CCDS; CCDS57662.1; -. [Q3TKT4-1] DR RefSeq; NP_001167549.1; NM_001174078.1. DR RefSeq; NP_001167550.1; NM_001174079.1. [Q3TKT4-1] DR RefSeq; NP_035547.2; NM_011417.3. [Q3TKT4-2] DR RefSeq; XP_006510180.2; XM_006510117.2. DR RefSeq; XP_006510182.2; XM_006510119.2. [Q3TKT4-2] DR RefSeq; XP_006510183.2; XM_006510120.2. [Q3TKT4-1] DR AlphaFoldDB; Q3TKT4; -. DR SMR; Q3TKT4; -. DR BioGRID; 203336; 92. DR ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant. DR ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant. DR ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex. DR ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1262; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1264; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant. DR ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant. DR ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant. DR ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant. DR CORUM; Q3TKT4; -. DR DIP; DIP-40650N; -. DR DIP; DIP-59249N; -. DR IntAct; Q3TKT4; 50. DR MINT; Q3TKT4; -. DR STRING; 10090.ENSMUSP00000096547; -. DR GlyGen; Q3TKT4; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q3TKT4; -. DR PhosphoSitePlus; Q3TKT4; -. DR SwissPalm; Q3TKT4; -. DR EPD; Q3TKT4; -. DR jPOST; Q3TKT4; -. DR MaxQB; Q3TKT4; -. DR PaxDb; 10090-ENSMUSP00000034707; -. DR PeptideAtlas; Q3TKT4; -. DR ProteomicsDB; 261524; -. [Q3TKT4-1] DR ProteomicsDB; 261525; -. [Q3TKT4-2] DR Pumba; Q3TKT4; -. DR Antibodypedia; 3778; 679 antibodies from 45 providers. DR DNASU; 20586; -. DR Ensembl; ENSMUST00000034707.15; ENSMUSP00000034707.9; ENSMUSG00000032187.17. [Q3TKT4-2] DR Ensembl; ENSMUST00000174008.8; ENSMUSP00000133922.2; ENSMUSG00000032187.17. [Q3TKT4-1] DR GeneID; 20586; -. DR KEGG; mmu:20586; -. DR UCSC; uc009omd.2; mouse. [Q3TKT4-2] DR UCSC; uc009ome.2; mouse. [Q3TKT4-1] DR AGR; MGI:88192; -. DR CTD; 6597; -. DR MGI; MGI:88192; Smarca4. DR VEuPathDB; HostDB:ENSMUSG00000032187; -. DR eggNOG; KOG0386; Eukaryota. DR GeneTree; ENSGT00940000156887; -. DR HOGENOM; CLU_000315_15_0_1; -. DR InParanoid; Q3TKT4; -. DR OMA; YGPGHKL; -. DR OrthoDB; 5482994at2759; -. DR PhylomeDB; Q3TKT4; -. DR TreeFam; TF300785; -. DR Reactome; R-MMU-1266695; Interleukin-7 signaling. DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-MMU-3214858; RMTs methylate histone arginines. DR Reactome; R-MMU-3247509; Chromatin modifying enzymes. DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR BioGRID-ORCS; 20586; 21 hits in 88 CRISPR screens. DR ChiTaRS; Smarca4; mouse. DR PRO; PR:Q3TKT4; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q3TKT4; Protein. DR Bgee; ENSMUSG00000032187; Expressed in rostral migratory stream and 316 other cell types or tissues. DR ExpressionAtlas; Q3TKT4; baseline and differential. DR GO; GO:0140092; C:bBAF complex; NAS:ComplexPortal. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0000791; C:euchromatin; IDA:MGI. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0140288; C:GBAF complex; NAS:ComplexPortal. DR GO; GO:0000792; C:heterochromatin; IDA:MGI. DR GO; GO:0000776; C:kinetochore; NAS:ComplexPortal. DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI. DR GO; GO:0071565; C:nBAF complex; IDA:UniProtKB. DR GO; GO:0071564; C:npBAF complex; IDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005726; C:perichromatin fibrils; IDA:MGI. DR GO; GO:0016586; C:RSC-type complex; NAS:ComplexPortal. DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:MGI. DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI. DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:UniProt. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0106222; F:lncRNA binding; IPI:MGI. DR GO; GO:0070577; F:lysine-acetylated histone binding; ISO:MGI. DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI. DR GO; GO:0002039; F:p53 binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0030957; F:Tat protein binding; ISO:MGI. DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI. DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI. DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB. DR GO; GO:0035904; P:aorta development; IMP:MGI. DR GO; GO:0035887; P:aortic smooth muscle cell differentiation; IMP:MGI. DR GO; GO:0001832; P:blastocyst growth; IMP:MGI. DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI. DR GO; GO:0001568; P:blood vessel development; IMP:MGI. DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI. DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI. DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI. DR GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI. DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IMP:MGI. DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; IDA:MGI. DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI. DR GO; GO:0048562; P:embryonic organ morphogenesis; IMP:MGI. DR GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI. DR GO; GO:0030900; P:forebrain development; IMP:MGI. DR GO; GO:0010467; P:gene expression; IDA:MGI. DR GO; GO:0007403; P:glial cell fate determination; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0060347; P:heart trabecula formation; IGI:MGI. DR GO; GO:0030902; P:hindbrain development; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI. DR GO; GO:0070307; P:lens fiber cell development; IMP:MGI. DR GO; GO:0001889; P:liver development; IMP:MGI. DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI. DR GO; GO:0045596; P:negative regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB. DR GO; GO:0022008; P:neurogenesis; IDA:MGI. DR GO; GO:0006334; P:nucleosome assembly; TAS:MGI. DR GO; GO:0006337; P:nucleosome disassembly; ISO:MGI. DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI. DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IMP:MGI. DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI. DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IDA:UniProt. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; ISO:MGI. DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:MGI. DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IEA:GOC. DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IDA:UniProt. DR GO; GO:0001570; P:vasculogenesis; IMP:MGI. DR GO; GO:0003281; P:ventricular septum development; IMP:MGI. DR CDD; cd05516; Bromo_SNF2L2; 1. DR CDD; cd18062; DEXHc_SMARCA4; 1. DR CDD; cd18793; SF2_C_SNF; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 3.40.5.120; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1. DR InterPro; IPR030100; BRG1_ATP-bd. DR InterPro; IPR006576; BRK_domain. DR InterPro; IPR037259; BRK_sf. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR014978; Gln-Leu-Gln_QLQ. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR014012; HSA_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR029295; SnAC. DR InterPro; IPR038718; SNF2-like_sf. DR InterPro; IPR049730; SNF2/RAD54-like_C. DR InterPro; IPR000330; SNF2_N. DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1. DR PANTHER; PTHR10799:SF76; TRANSCRIPTION ACTIVATOR BRG1; 1. DR Pfam; PF07533; BRK; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF07529; HSA; 1. DR Pfam; PF08880; QLQ; 1. DR Pfam; PF14619; SnAC; 1. DR Pfam; PF00176; SNF2-rel_dom; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00592; BRK; 1. DR SMART; SM00297; BROMO; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00573; HSA; 1. DR SMART; SM00951; QLQ; 1. DR SMART; SM01314; SnAC; 1. DR SUPFAM; SSF160481; BRK domain-like; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51204; HSA; 1. DR PROSITE; PS51666; QLQ; 1. DR Genevisible; Q3TKT4; MM. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; ATP-binding; Bromodomain; KW Chromatin regulator; Helicase; Hydrolase; Isopeptide bond; Neurogenesis; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..1613 FT /note="Transcription activator BRG1" FT /id="PRO_0000391343" FT DOMAIN 171..206 FT /note="QLQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001" FT DOMAIN 460..532 FT /note="HSA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549" FT DOMAIN 766..931 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 1084..1246 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT DOMAIN 1443..1513 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT REGION 1..282 FT /note="Necessary for interaction with SS18L1/CREST" FT /evidence="ECO:0000250" FT REGION 1..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 198..353 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 462..728 FT /note="RNA-binding region which is sufficient for binding FT to lncRNA Evf2" FT /evidence="ECO:0000269|PubMed:26138476" FT REGION 577..610 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 647..699 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 837..916 FT /note="Sufficient for interaction with DLX1" FT /evidence="ECO:0000269|PubMed:26138476" FT REGION 1247..1413 FT /note="Sufficient for interaction with DLX1" FT /evidence="ECO:0000269|PubMed:26138476" FT REGION 1366..1427 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1530..1613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 881..884 FT /note="DEGH box" FT /evidence="ECO:0000250" FT MOTIF 1562..1565 FT /note="KIKL" FT /evidence="ECO:0000250|UniProtKB:P51532" FT COMPBIAS 1..31 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 73..88 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 133..147 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 159..177 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 215..288 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..340 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 659..674 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 685..699 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1366..1386 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1395..1415 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1535..1552 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1553..1579 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1595..1613 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 779..786 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT SITE 1505..1506 FT /note="Required for binding to 'Lys-15'-acetylated histone FT 3" FT /evidence="ECO:0000250" FT MOD_RES 11 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P51532" FT MOD_RES 188 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P51532" FT MOD_RES 353 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P51532" FT MOD_RES 609 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P51532" FT MOD_RES 610 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 613 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 626 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6DIC0" FT MOD_RES 695 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 699 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1349 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51532" FT MOD_RES 1390 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51532" FT MOD_RES 1536 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1541 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1552 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1593 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51532" FT MOD_RES 1597 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51532" FT CROSSLNK 1332 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P51532" FT VAR_SEQ 1441 FT /note="D -> DS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072" FT /id="VSP_038696" FT CONFLICT 1355 FT /note="W -> WLKT (in Ref. 1; BAE36034)" FT /evidence="ECO:0000305" SQ SEQUENCE 1613 AA; 181427 MW; C23804ED858F98FE CRC64; MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPTQG PGGYPQDNMH QMHKPMESMH EKGMPDDPRY NQMKGMGMRS GAHTGMAPPP SPMDQHSQGY PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGSDPQ ALGQQNRGPT PFNQNQLHQL RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PLVPLHQKQS RITPIQKPRG LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL QHAKDFREYH RSVTGKLQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES GSEEEEEEEE EEQPQPAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDEEE DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR KRDSEAGSST PTTSTRSRDK DEESKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK DSSGRQLSEV FIQLPSRKEL PEYYELIRKP VDFKKIKERI RNHKYRSLND LEKDVMLLCQ NAQTFNLEGS LIYEDSIVLQ SVFTSVRQKI EKEDDSEGEE SEEEEEGEEE GSESESRSVK VKIKLGRKEK AQDRLKGGRR RPSRGSRAKP VVSDDDSEEE QEEDRSGSGS EED //