SMARCA4
entrez
6597
canonical
uniprot
P51532
canonical
ensembl
ENSG00000127616
resolver
ensp
ENSP00000343896
resolver
ensp
ENSP00000395654
resolver
ensp
ENSP00000445036
resolver
ensp
ENSP00000464778
resolver
ensp
ENSP00000466963
resolver
ensp
ENSP00000494353
resolver
ensp
ENSP00000494463
resolver
ensp
ENSP00000494676
resolver
ensp
ENSP00000494772
resolver
ensp
ENSP00000495368
resolver
ensp
ENSP00000495536
resolver
ensp
ENSP00000496498
resolver
ensp
ENSP00000518564
resolver
ensp
ENSP00000566402
resolver
ensp
ENSP00000594774
resolver
ensp
ENSP00000594775
resolver
ensp
ENSP00000594802
resolver
ensp
ENSP00000594807
resolver
ensp
ENSP00000594811
resolver
ensp
ENSP00000594815
resolver
enst
ENST00000642628
resolver
enst
ENST00000642726
resolver
enst
ENST00000646693
resolver
enst
ENST00000711079
resolver
enst
ENST00000896343
resolver
enst
ENST00000924743
resolver
enst
ENST00000924756
resolver
genesymbol
SMARCA4
resolver
genesymbol_syn
BAF190A
resolver
genesymbol_syn
BRG1
resolver
genesymbol_syn
SNF2B
resolver
genesymbol_syn
SNF2L4
resolver
hgnc
HGNC:11100
resolver
uniprot
A0A2R8Y7S2
resolver
uniprot
A7E2E1
resolver
uniprot
B1A8Z4
resolver
uniprot
B1A8Z5
resolver
uniprot
B1A8Z6
resolver
uniprot
B1A8Z7
resolver
uniprot
B3KNW7
resolver
uniprot
E9PBR8
resolver
uniprot
O95052
resolver
uniprot
Q9HBD3
resolver
uniprot
Q9HBD4
resolver
uniprot_entry
A0A2R8Y7S2_HUMAN
resolver
uniprot_entry
A7E2E1_HUMAN
resolver
uniprot_entry
B3KNW7_HUMAN
resolver
uniprot_entry
Q9HBD4_HUMAN
resolver
uniprot_entry
SMCA4_HUMAN
resolver
uniprot_sec
B1A8Z4
resolver
uniprot_sec
B1A8Z5
resolver
uniprot_sec
B1A8Z6
resolver
uniprot_sec
B1A8Z7
resolver
uniprot_sec
E9PBR8
resolver
uniprot_sec
O95052
resolver
uniprot_sec
Q9HBD3
resolver
activity_regulation
ACTIVITY REGULATION: Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and chromatin remodeling activities. {ECO:0000250|UniProtKB:Q3TKT4}.
uniprot
proteins
amino_acid_sequence
MSTPDPPLGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSMMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
uniprot
proteins
disease_involvement
DISEASE: Rhabdoid tumor predisposition syndrome 2 (RTPS2) [MIM:613325]: A familial cancer syndrome predisposing to renal or extrarenal malignant rhabdoid tumors and to a variety of tumors of the central nervous system, including choroid plexus carcinoma, medulloblastoma, and central primitive neuroectodermal tumors. Rhabdoid tumors are the most aggressive and lethal malignancies occurring in early childhood. {ECO:0000269|PubMed:20137775}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Coffin-Siris syndrome 4 (CSS4) [MIM:614609]: A form of Coffin-Siris syndrome, a congenital multiple malformation syndrome with broad phenotypic and genetic variability. Cardinal features are intellectual disability, coarse facial features, hypertrichosis, and hypoplastic or absent fifth digit nails or phalanges. Additional features include malformations of the cardiac, gastrointestinal, genitourinary, and/or central nervous systems. Sucking/feeding difficulties, poor growth, ophthalmologic abnormalities, hearing impairment, and spinal anomalies are common findings. Both autosomal dominant and autosomal recessive inheritance patterns have been reported. {ECO:0000269|PubMed:22426308}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Otosclerosis 12 (OTSC12) [MIM:620792]: A form of otosclerosis, a pathological condition of the ear characterized by formation of spongy bone in the labyrinth capsule, especially in front of and posterior to the footplate of the stapes, resulting in conductive hearing impairment. Cochlear otosclerosis may also develop, resulting in sensorineural hearing loss. OTSC12 is an autosomal dominant form with incomplete penetrance. {ECO:0000269|PubMed:37399313}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
FUNCTION: ATPase 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 (PubMed:15075294, PubMed:29374058, PubMed:30339381, PubMed:32459350). 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 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 (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1 (PubMed:20418909). 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 (By similarity). Binds to RNA in a promiscuous manner (By similarity). In brown adipose tissue, involved in the regulation of thermogenic genes expression (By similarity). {ECO:0000250|UniProtKB:Q3TKT4, ECO:0000250|UniProtKB:Q8K1P7, ECO:0000269|PubMed:15075294, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:20418909, ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:30339381, ECO:0000269|PubMed:32459350, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
uniprot
proteins
mass_dalton
184646
uniprot
proteins
mutagenesis
MUTAGEN 1484; /note="V->A: No effect on binding to 'Lys-15'-acetylated histone H3."; /evidence="ECO:0000269|PubMed:17274598"; MUTAGEN 1539; /note="F->A: Abolishes binding to 'Lys-15'-acetylated histone H3."; /evidence="ECO:0000269|PubMed:17274598"; MUTAGEN 1540; /note="N->A: Abolishes binding to 'Lys-15'-acetylated histone H3."; /evidence="ECO:0000269|PubMed:17274598
uniprot
proteins
protein_family
SNF2/RAD54 helicase family
uniprot
proteins
pubmed
10204490
uniprot
proteins
pubmed
11085541
uniprot
proteins
pubmed
11839798
uniprot
proteins
pubmed
12917342
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15075294
uniprot
proteins
pubmed
16051670
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17274598
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17582821
uniprot
proteins
pubmed
18386774
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18765789
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19571879
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20137775
uniprot
proteins
pubmed
20418909
uniprot
proteins
pubmed
20460684
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22426308
uniprot
proteins
pubmed
22952240
uniprot
proteins
pubmed
23071114
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
26601204
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28649782
uniprot
proteins
pubmed
29374058
uniprot
proteins
pubmed
29567837
uniprot
proteins
pubmed
30339381
uniprot
proteins
pubmed
32459350
uniprot
proteins
pubmed
37399313
uniprot
proteins
pubmed
8208605
uniprot
proteins
pubmed
8232556
uniprot
proteins
pubmed
9590696
uniprot
proteins
sequence_length
1647
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549, ECO:0000269|PubMed:20418909, ECO:0000269|PubMed:25593309}. Note=Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds (By similarity). Localizes to sites of DNA damage (PubMed:25593309). {ECO:0000250|UniProtKB:Q3TKT4, ECO:0000269|PubMed:25593309}.
uniprot
proteins