SMRC1_HUMAN
ID SMRC1_HUMAN Reviewed; 1105 AA.
AC Q92922; Q17RS0; Q6P172; Q8IWH2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=SWI/SNF complex subunit SMARCC1 {ECO:0000305};
DE AltName: Full=BRG1-associated factor 155;
DE Short=BAF155;
DE AltName: Full=SWI/SNF complex 155 kDa subunit;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1;
GN Name=SMARCC1 {ECO:0000312|HGNC:HGNC:11104}; Synonyms=BAF155;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8804307; DOI=10.1101/gad.10.17.2117;
RA Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.;
RT "Diversity and specialization of mammalian SWI/SNF complexes.";
RL Genes Dev. 10:2117-2130(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, and Testis;
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 [3]
RP PROTEIN SEQUENCE OF 2-32; 470-478; 483-491; 591-602; 653-663; 717-724 AND
RP 894-905, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION AT THE G2/M TRANSITION.
RX PubMed=9744861; DOI=10.1101/gad.12.18.2842;
RA Sif S., Stukenberg P.T., Kirschner M.W., Kingston R.E.;
RT "Mitotic inactivation of a human SWI/SNF chromatin remodeling complex.";
RL Genes Dev. 12:2842-2851(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-330; THR-335 AND
RP SER-357, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-345; LYS-346; LYS-354; LYS-359
RP AND LYS-948, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP INTERACTION WITH CEBPB.
RX PubMed=20111005; DOI=10.1038/emboj.2010.3;
RA Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
RT "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and
RT SWI/SNF/Mediator implies an indexing transcription factor code.";
RL EMBO J. 29:1105-1115(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-328; SER-330;
RP SER-357 AND SER-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-330; THR-335;
RP SER-350; THR-398; SER-822 AND SER-825, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310; SER-328; SER-330 AND
RP SER-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-359, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-359 AND LYS-592, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-359; LYS-592; LYS-739;
RP LYS-796; LYS-829 AND LYS-856, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP STIMULATION OF THE CHROMATIN-REMODELING ACTIVITY OF SMARCA4.
RX PubMed=10078207; DOI=10.1016/s1097-2765(00)80315-9;
RA Phelan M.L., Sif S., Narlikar G.J., Kingston R.E.;
RT "Reconstitution of a core chromatin remodeling complex from SWI/SNF
RT subunits.";
RL Mol. Cell 3:247-253(1999).
RN [22]
RP INTERACTION WITH CCNE1.
RX PubMed=9891079; DOI=10.1128/mcb.19.2.1460;
RA Shanahan F., Seghezzi W., Parry D., Mahony D., Lees E.;
RT "Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-
RT SNF complex, and alters the ability of BRG1 to induce growth arrest.";
RL Mol. Cell. Biol. 19:1460-1469(1999).
RN [23]
RP FUNCTION.
RX PubMed=11018012; DOI=10.1101/gad.828000;
RA Kadam S., McAlpine G.S., Phelan M.L., Kingston R.E., Jones K.A.,
RA Emerson B.M.;
RT "Functional selectivity of recombinant mammalian SWI/SNF subunits.";
RL Genes Dev. 14:2441-2451(2000).
RN [24]
RP INTERACTION WITH SIN3A.
RX PubMed=11238380; DOI=10.1101/gad.872801;
RA Sif S., Saurin A.J., Imbalzano A.N., Kingston R.E.;
RT "Purification and characterization of mSin3A-containing Brg1 and hBrm
RT chromatin remodeling complexes.";
RL Genes Dev. 15:603-618(2001).
RN [25]
RP INTERACTION WITH NR3C1 AND SMARD1.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
RN [26]
RP IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18765789; DOI=10.1101/gad.471408;
RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
RT "Regulation of muscle development by DPF3, a novel histone acetylation and
RT methylation reader of the BAF chromatin remodeling complex.";
RL Genes Dev. 22:2370-2384(2008).
RN [27]
RP INTERACTION WITH TRIP12.
RX PubMed=20829358; DOI=10.1074/jbc.m110.173997;
RA Keppler B.R., Archer T.K.;
RT "Ubiquitin-dependent and ubiquitin-independent control of subunit
RT stoichiometry in the SWI/SNF complex.";
RL J. Biol. Chem. 285:35665-35674(2010).
RN [28]
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 [29]
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 [30]
RP STRUCTURE BY NMR OF 607-676.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SANT domain of human SWI/SNF-related matrix-
RT associated actin-dependent regulator of chromatin subfamily C member 1.";
RL Submitted (APR-2008) to the PDB data bank.
RN [31]
RP INTERACTION WITH MKKS, AND SUBCELLULAR LOCATION.
RX PubMed=28753627; DOI=10.1371/journal.pgen.1006936;
RA Scott C.A., Marsden A.N., Rebagliati M.R., Zhang Q., Chamling X.,
RA Searby C.C., Baye L.M., Sheffield V.C., Slusarski D.C.;
RT "Nuclear/cytoplasmic transport defects in BBS6 underlie congenital heart
RT disease through perturbation of a chromatin remodeling protein.";
RL PLoS Genet. 13:E1006936-E1006936(2017).
RN [32]
RP INTERACTION WITH DPF2.
RX PubMed=28533407; DOI=10.1073/pnas.1700328114;
RA Huber F.M., Greenblatt S.M., Davenport A.M., Martinez C., Xu Y., Vu L.P.,
RA Nimer S.D., Hoelz A.;
RT "Histone-binding of DPF2 mediates its repressive role in myeloid
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6016-6021(2017).
RN [33]
RP FUNCTION, AND 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 [34]
RP INTERACTION WITH PRDM1.
RX PubMed=32417234; DOI=10.1016/j.bbagrm.2020.194577;
RA Fong H.T., Hagen T., Inoue T.;
RT "LDB1 and the SWI/SNF complex participate in both transcriptional
RT activation and repression by Caenorhabditis elegans BLIMP1/PRDM1.";
RL Biochim. Biophys. Acta 1863:194577-194577(2020).
RN [35]
RP INTERACTION WITH HDGFL2 AND DPF3.
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 [36]
RP VARIANTS 179-LYS--PRO-1105 DEL AND PRO-526.
RX PubMed=29983323; DOI=10.1016/j.neuron.2018.06.019;
RA Furey C.G., Choi J., Jin S.C., Zeng X., Timberlake A.T.,
RA Nelson-Williams C., Mansuri M.S., Lu Q., Duran D., Panchagnula S.,
RA Allocco A., Karimy J.K., Khanna A., Gaillard J.R., DeSpenza T., Antwi P.,
RA Loring E., Butler W.E., Smith E.R., Warf B.C., Strahle J.M., Limbrick D.D.,
RA Storm P.B., Heuer G., Jackson E.M., Iskandar B.J., Johnston J.M.,
RA Tikhonova I., Castaldi C., Lopez-Giraldez F., Bjornson R.D., Knight J.R.,
RA Bilguvar K., Mane S., Alper S.L., Haider S., Guclu B., Bayri Y., Sahin Y.,
RA Apuzzo M.L.J., Duncan C.C., DiLuna M.L., Guenel M., Lifton R.P.,
RA Kahle K.T.;
RT "De Novo Mutation in Genes Regulating Neural Stem Cell Fate in Human
RT Congenital Hydrocephalus.";
RL Neuron 99:302-314.e4(2018).
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. May stimulate the ATPase activity of the catalytic subunit of
CC the complex (PubMed:10078207, PubMed:29374058). Belongs to the neural
CC progenitors-specific chromatin remodeling complex (npBAF complex) and
CC the neuron-specific chromatin remodeling complex (nBAF complex). During
CC neural development a switch from a stem/progenitor to a postmitotic
CC chromatin remodeling mechanism occurs as neurons exit the cell cycle
CC and become committed to their adult state. The transition from
CC proliferating neural stem/progenitor cells to postmitotic neurons
CC requires a switch in subunit composition of the npBAF and nBAF
CC complexes. As neural progenitors exit mitosis and differentiate into
CC neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A,
CC are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
CC or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF
CC complex is essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth
CC (By similarity). {ECO:0000250|UniProtKB:P97496,
CC ECO:0000269|PubMed:10078207, ECO:0000269|PubMed:11018012,
CC ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
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 combinations developmentally and tissue
CC specific (Probable). Component of the BAF complex, which includes at
CC least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC SMARCA4/BRG1, 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 (PubMed:18765789). Component of neural
CC progenitors-specific chromatin remodeling complex (npBAF complex)
CC composed of at 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 (By similarity). Component of the
CC 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 (PubMed:22952240, PubMed:26601204). Component of SWI/SNF (GBAF)
CC subcomplex, which includes at least BICRA or BICRAL (mutually
CC exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A,
CC ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). May
CC also interact with the SIN3A histone deacetylase transcription
CC repressor complex in conjunction with SMARCA2 and SMARCA4
CC (PubMed:11238380). The minimal complex composed of SMARCC1 and SMARCA4
CC seems to be able to associate with cyclin such as CCNE1 or
CC transcription factors such as KLF1 or GATA1 (PubMed:9891079). Interacts
CC with NR3C1 and SMARD1 (PubMed:12917342). Interacts with TRIP12; leading
CC to disrupt interaction between TRIP12 and SMARCE1 and prevent SMARCE1
CC ubiquitination (PubMed:20111005). Interacts with CEBPB (when not
CC methylated) (PubMed:20829358). Interacts with KDM6B (By similarity).
CC Interacts with MKKS; the interaction takes place predominantly in the
CC cytoplasm and may modulate SMARCC1 location (PubMed:28753627).
CC Interacts with DPF2 (PubMed:28533407). Interacts with PRDM1/BLIMP1
CC (PubMed:32417234). Interacts with DPF3a (isoform 2 of DPF3/BAF45C) and
CC with HDGFL2 in a DPF3a-dependent manner (PubMed:32459350).
CC {ECO:0000250|UniProtKB:P97496, ECO:0000269|PubMed:11238380,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:18765789,
CC ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:20829358,
CC ECO:0000269|PubMed:28533407, ECO:0000269|PubMed:28753627,
CC ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:32417234,
CC ECO:0000269|PubMed:32459350, ECO:0000269|PubMed:9891079,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC Q92922; Q6UY14-3: ADAMTSL4; NbExp=6; IntAct=EBI-355653, EBI-10173507;
CC Q92922; Q86X55: CARM1; NbExp=4; IntAct=EBI-355653, EBI-2339854;
CC Q92922; P27918: CFP; NbExp=3; IntAct=EBI-355653, EBI-9038570;
CC Q92922; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-355653, EBI-7062247;
CC Q92922; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-355653, EBI-3867333;
CC Q92922; O76003: GLRX3; NbExp=3; IntAct=EBI-355653, EBI-374781;
CC Q92922; Q9H4Y5: GSTO2; NbExp=3; IntAct=EBI-355653, EBI-10194609;
CC Q92922; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-355653, EBI-10241252;
CC Q92922; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-355653, EBI-12196745;
CC Q92922; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-355653, EBI-18395721;
CC Q92922; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-355653, EBI-3957672;
CC Q92922; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-355653, EBI-9996449;
CC Q92922; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-355653, EBI-751260;
CC Q92922; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-355653, EBI-3957694;
CC Q92922; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-355653, EBI-12111050;
CC Q92922; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-355653, EBI-11962084;
CC Q92922; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-355653, EBI-18394498;
CC Q92922; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-355653, EBI-18273118;
CC Q92922; P32242: OTX1; NbExp=3; IntAct=EBI-355653, EBI-740446;
CC Q92922; O15162: PLSCR1; NbExp=3; IntAct=EBI-355653, EBI-740019;
CC Q92922; O43314-2: PPIP5K2; NbExp=3; IntAct=EBI-355653, EBI-12906508;
CC Q92922; Q03431: PTH1R; NbExp=3; IntAct=EBI-355653, EBI-2860297;
CC Q92922; Q16348: SLC15A2; NbExp=3; IntAct=EBI-355653, EBI-12806032;
CC Q92922; P51532: SMARCA4; NbExp=28; IntAct=EBI-355653, EBI-302489;
CC Q92922; Q96GM5: SMARCD1; NbExp=5; IntAct=EBI-355653, EBI-358489;
CC Q92922; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-355653, EBI-10696971;
CC Q92922; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-355653, EBI-5235829;
CC Q92922; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-355653, EBI-12068150;
CC Q92922; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-355653, EBI-11957216;
CC Q92922; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-355653, EBI-745520;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28753627}. Cytoplasm
CC {ECO:0000269|PubMed:28753627}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, muscle, placenta, lung,
CC liver, muscle, kidney and pancreas.
CC -!- PTM: Phosphorylated on undefined residues at the G2/M transition by
CC ERK1 and other kinases. This may contribute to cell cycle specific
CC inactivation of remodeling complexes containing the phosphorylated
CC protein. {ECO:0000269|PubMed:9744861}.
CC -!- SIMILARITY: Belongs to the SMARCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39843.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH65253.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={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; U66615; AAC50693.1; -; mRNA.
DR EMBL; BC039843; AAH39843.1; ALT_SEQ; mRNA.
DR EMBL; BC065253; AAH65253.1; ALT_SEQ; mRNA.
DR EMBL; BC113465; AAI13466.1; -; mRNA.
DR EMBL; BC117213; AAI17214.1; -; mRNA.
DR CCDS; CCDS2758.1; -.
DR RefSeq; NP_003065.3; NM_003074.3.
DR PDB; 2YUS; NMR; -; A=610-675.
DR PDB; 5GJK; X-ray; 2.05 A; A=447-540.
DR PDB; 6KZ7; X-ray; 2.28 A; A/C=449-542.
DR PDB; 6YXO; X-ray; 2.00 A; A/B=28-302.
DR PDB; 6YXP; X-ray; 1.60 A; A/B=28-305.
DR PDBsum; 2YUS; -.
DR PDBsum; 5GJK; -.
DR PDBsum; 6KZ7; -.
DR PDBsum; 6YXO; -.
DR PDBsum; 6YXP; -.
DR AlphaFoldDB; Q92922; -.
DR BMRB; Q92922; -.
DR SMR; Q92922; -.
DR BioGRID; 112483; 241.
DR ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4223; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4224; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR CORUM; Q92922; -.
DR DIP; DIP-27545N; -.
DR DIP; DIP-33044N; -.
DR IntAct; Q92922; 114.
DR MINT; Q92922; -.
DR STRING; 9606.ENSP00000254480; -.
DR GlyGen; Q92922; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92922; -.
DR MetOSite; Q92922; -.
DR PhosphoSitePlus; Q92922; -.
DR SwissPalm; Q92922; -.
DR BioMuta; SMARCC1; -.
DR DMDM; 209572723; -.
DR EPD; Q92922; -.
DR jPOST; Q92922; -.
DR MassIVE; Q92922; -.
DR MaxQB; Q92922; -.
DR PaxDb; Q92922; -.
DR PeptideAtlas; Q92922; -.
DR PRIDE; Q92922; -.
DR ProteomicsDB; 75605; -.
DR Antibodypedia; 3168; 252 antibodies from 36 providers.
DR DNASU; 6599; -.
DR Ensembl; ENST00000254480.10; ENSP00000254480.5; ENSG00000173473.11.
DR GeneID; 6599; -.
DR KEGG; hsa:6599; -.
DR MANE-Select; ENST00000254480.10; ENSP00000254480.5; NM_003074.4; NP_003065.3.
DR UCSC; uc003crq.3; human.
DR CTD; 6599; -.
DR DisGeNET; 6599; -.
DR GeneCards; SMARCC1; -.
DR HGNC; HGNC:11104; SMARCC1.
DR HPA; ENSG00000173473; Low tissue specificity.
DR MIM; 601732; gene.
DR neXtProt; NX_Q92922; -.
DR OpenTargets; ENSG00000173473; -.
DR PharmGKB; PA35954; -.
DR VEuPathDB; HostDB:ENSG00000173473; -.
DR eggNOG; KOG1279; Eukaryota.
DR GeneTree; ENSGT00940000156347; -.
DR HOGENOM; CLU_004447_0_1_1; -.
DR InParanoid; Q92922; -.
DR OMA; CLTRPSI; -.
DR OrthoDB; 683891at2759; -.
DR PhylomeDB; Q92922; -.
DR TreeFam; TF314710; -.
DR PathwayCommons; Q92922; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; Q92922; -.
DR SIGNOR; Q92922; -.
DR BioGRID-ORCS; 6599; 59 hits in 1095 CRISPR screens.
DR ChiTaRS; SMARCC1; human.
DR EvolutionaryTrace; Q92922; -.
DR GeneWiki; SMARCC1; -.
DR GenomeRNAi; 6599; -.
DR Pharos; Q92922; Tbio.
DR PRO; PR:Q92922; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q92922; protein.
DR Bgee; ENSG00000173473; Expressed in ventricular zone and 213 other tissues.
DR ExpressionAtlas; Q92922; baseline and differential.
DR Genevisible; Q92922; HS.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR030087; BAF155.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR032451; SMARCC_C.
DR InterPro; IPR032450; SMARCC_N.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR032448; SWIRM-assoc.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12802:SF9; PTHR12802:SF9; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF16495; SWIRM-assoc_1; 1.
DR Pfam; PF16496; SWIRM-assoc_2; 1.
DR Pfam; PF16498; SWIRM-assoc_3; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromatin regulator; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Methylation; Neurogenesis;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT CHAIN 2..1105
FT /note="SWI/SNF complex subunit SMARCC1"
FT /id="PRO_0000197115"
FT DOMAIN 449..546
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 618..669
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 296..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 914..946
FT /evidence="ECO:0000255"
FT COMPBIAS 296..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1019
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1061
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 345
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 346
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 354
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 359
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 948
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1064
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P97496"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 739
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 796
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 829
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 856
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 179..1105
FT /note="Missing (probable disease-associated variant found
FT in a patient with obstructive congenitalhydrocephalus with
FT aqueductal stenosis)"
FT /evidence="ECO:0000269|PubMed:29983323"
FT /id="VAR_083428"
FT VARIANT 526
FT /note="H -> P (probable disease-associated variant found in
FT a patient with obstructive congenitalhydrocephalus with
FT aqueductal stenosis; dbSNP:rs1576408057)"
FT /evidence="ECO:0000269|PubMed:29983323"
FT /id="VAR_083429"
FT VARIANT 1075
FT /note="P -> H (in dbSNP:rs3772406)"
FT /id="VAR_020883"
FT CONFLICT 19..22
FT /note="SGIA -> FGDS (in Ref. 1; AAC50693)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="T -> S (in Ref. 1; AAC50693)"
FT /evidence="ECO:0000305"
FT CONFLICT 528..529
FT /note="FL -> GG (in Ref. 1; AAC50693)"
FT /evidence="ECO:0000305"
FT CONFLICT 564..570
FT /note="SGLVPLH -> LACASD (in Ref. 1; AAC50693)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="E -> G (in Ref. 1; AAC50693)"
FT /evidence="ECO:0000305"
FT CONFLICT 842..843
FT /note="TD -> SS (in Ref. 1; AAC50693)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="E -> G (in Ref. 1; AAC50693)"
FT /evidence="ECO:0000305"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:6YXP"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6YXP"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 74..92
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6YXO"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:6YXP"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6YXP"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:6YXP"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:6YXP"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6YXP"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6YXP"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:6YXP"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:5GJK"
FT HELIX 465..470
FT /evidence="ECO:0007829|PDB:5GJK"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:5GJK"
FT HELIX 484..500
FT /evidence="ECO:0007829|PDB:5GJK"
FT HELIX 508..512
FT /evidence="ECO:0007829|PDB:5GJK"
FT HELIX 519..531
FT /evidence="ECO:0007829|PDB:5GJK"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5GJK"
FT HELIX 625..637
FT /evidence="ECO:0007829|PDB:2YUS"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:2YUS"
FT HELIX 642..649
FT /evidence="ECO:0007829|PDB:2YUS"
FT HELIX 654..661
FT /evidence="ECO:0007829|PDB:2YUS"
SQ SEQUENCE 1105 AA; 122867 MW; EDA6FF5B0472AEA9 CRC64;
MAAAAGGGGP GTAVGATGSG IAAAAAGLAV YRRKDGGPAT KFWESPETVS QLDSVRVWLG
KHYKKYVHAD APTNKTLAGL VVQLLQFQED AFGKHVTNPA FTKLPAKCFM DFKAGGALCH
ILGAAYKYKN EQGWRRFDLQ NPSRMDRNVE MFMNIEKTLV QNNCLTRPNI YLIPDIDLKL
ANKLKDIIKR HQGTFTDEKS KASHHIYPYS SSQDDEEWLR PVMRKEKQVL VHWGFYPDSY
DTWVHSNDVD AEIEDPPIPE KPWKVHVKWI LDTDIFNEWM NEEDYEVDEN RKPVSFRQRI
STKNEEPVRS PERRDRKASA NARKRKHSPS PPPPTPTESR KKSGKKGQAS LYGKRRSQKE
EDEQEDLTKD MEDPTPVPNI EEVVLPKNVN LKKDSENTPV KGGTVADLDE QDEETVTAGG
KEDEDPAKGD QSRSVDLGED NVTEQTNHII IPSYASWFDY NCIHVIERRA LPEFFNGKNK
SKTPEIYLAY RNFMIDTYRL NPQEYLTSTA CRRNLTGDVC AVMRVHAFLE QWGLVNYQVD
PESRPMAMGP PPTPHFNVLA DTPSGLVPLH LRSPQVPAAQ QMLNFPEKNK EKPVDLQNFG
LRTDIYSKKT LAKSKGASAG REWTEQETLL LLEALEMYKD DWNKVSEHVG SRTQDECILH
FLRLPIEDPY LENSDASLGP LAYQPVPFSQ SGNPVMSTVA FLASVVDPRV ASAAAKAALE
EFSRVREEVP LELVEAHVKK VQEAARASGK VDPTYGLESS CIAGTGPDEP EKLEGAEEEK
MEADPDGQQP EKAENKVENE TDEGDKAQDG ENEKNSEKEQ DSEVSEDTKS EEKETEENKE
LTDTCKERES DTGKKKVEHE ISEGNVATAA AAALASAATK AKHLAAVEER KIKSLVALLV
ETQMKKLEIK LRHFEELETI MDREKEALEQ QRQQLLTERQ NFHMEQLKYA ELRARQQMEQ
QQHGQNPQQA HQHSGGPGLA PLGAAGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP
GSMMPGQHMP GRMIPTVAAN IHPSGSGPTP PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ
QPPPPPPADG VPPPPAPGPP ASAAP
