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Protein

Transcription activator BRG1

Gene

SMARCA4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-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 a release of HDAC1 and recruitment of CREBBP. 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 post-mitotic 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 post-mitotic 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.By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1539 – 1540Required for binding to 'Lys-15'-acetylated histone 32

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi779 – 786ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • androgen receptor binding Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • DNA-dependent ATPase activity Source: BHF-UCL
  • DNA polymerase binding Source: BHF-UCL
  • helicase activity Source: ProtInc
  • lysine-acetylated histone binding Source: BHF-UCL
  • p53 binding Source: BHF-UCL
  • protein N-terminus binding Source: UniProtKB
  • RNA polymerase I CORE element sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II transcription coactivator activity Source: BHF-UCL
  • Tat protein binding Source: BHF-UCL
  • transcription coactivator activity Source: BHF-UCL
  • transcription corepressor activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • beta-catenin-TCF complex assembly Source: Reactome
  • chromatin modification Source: UniProtKB-KW
  • chromatin remodeling Source: UniProtKB
  • negative regulation of androgen receptor signaling pathway Source: BHF-UCL
  • negative regulation of cell growth Source: BHF-UCL
  • negative regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter during mitosis Source: BHF-UCL
  • nervous system development Source: UniProtKB-KW
  • neural retina development Source: BHF-UCL
  • nucleosome disassembly Source: BHF-UCL
  • positive regulation by host of viral transcription Source: BHF-UCL
  • positive regulation of glucose mediated signaling pathway Source: UniProtKB
  • positive regulation of pri-miRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProtKB
  • positive regulation of Wnt signaling pathway Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Helicase, Hydrolase, Repressor

Keywords - Biological processi

Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000092531-MONOMER.
ZFISH:ENSG00000127616-MONOMER.
BRENDAi3.6.4.11. 2681.
ReactomeiR-HSA-1266695. Interleukin-7 signaling.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-3247509. Chromatin modifying enzymes.
SignaLinkiP51532.
SIGNORiP51532.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription activator BRG1 (EC:3.6.4.-)
Alternative name(s):
ATP-dependent helicase SMARCA4
BRG1-associated factor 190A
Short name:
BAF190A
Mitotic growth and transcription activator
Protein BRG-1
Protein brahma homolog 1
SNF2-beta
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
Gene namesi
Name:SMARCA4
Synonyms:BAF190A, BRG1, SNF2B, SNF2L4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11100. SMARCA4.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • membrane Source: UniProtKB
  • nBAF complex Source: UniProtKB
  • npBAF complex Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
  • SWI/SNF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Rhabdoid tumor predisposition syndrome 2 (RTPS2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613325
Coffin-Siris syndrome 4 (CSS4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:614609
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068209546Missing in CSS4. 1 Publication1
Natural variantiVAR_068210859T → M in CSS4. 1 PublicationCorresponds to variant rs281875226dbSNPEnsembl.1
Natural variantiVAR_068211885R → C in CSS4. 1 PublicationCorresponds to variant rs281875227dbSNPEnsembl.1
Natural variantiVAR_068212921L → F in CSS4. 1 PublicationCorresponds to variant rs281875228dbSNPEnsembl.1
Natural variantiVAR_0682131011M → T in CSS4. 1 PublicationCorresponds to variant rs281875229dbSNPEnsembl.1
Natural variantiVAR_0682141157R → G in CSS4. 1 PublicationCorresponds to variant rs281875230dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1484V → A: No effect on binding to 'Lys-15'-acetylated histone H3. 1 Publication1
Mutagenesisi1539F → A: Abolishes binding to 'Lys-15'-acetylated histone H3. 1 Publication1
Mutagenesisi1540N → A: Abolishes binding to 'Lys-15'-acetylated histone H3. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi6597.
MalaCardsiSMARCA4.
MIMi613325. phenotype.
614609. phenotype.
OpenTargetsiENSG00000127616.
Orphaneti1465. Coffin-Siris syndrome.
231108. Familial rhabdoid tumor.
370396. Small cell carcinoma of the ovary.
PharmGKBiPA35950.

Chemistry databases

ChEMBLiCHEMBL3085620.
GuidetoPHARMACOLOGYi2740.

Polymorphism and mutation databases

BioMutaiSMARCA4.
DMDMi116242792.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000743531 – 1647Transcription activator BRG1Add BLAST1647

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11PhosphothreonineCombined sources1
Modified residuei188N6-acetyllysineCombined sources1
Modified residuei353PhosphothreonineCombined sources1
Modified residuei609PhosphothreonineCombined sources1
Modified residuei610PhosphoserineCombined sources1
Modified residuei613PhosphoserineCombined sources1
Modified residuei695PhosphoserineCombined sources1
Modified residuei699PhosphoserineCombined sources1
Modified residuei1382PhosphoserineCombined sources1
Modified residuei1423PhosphothreonineBy similarity1
Modified residuei1452PhosphoserineCombined sources1
Modified residuei1570PhosphoserineCombined sources1
Modified residuei1575PhosphoserineCombined sources1
Modified residuei1586PhosphoserineCombined sources1
Modified residuei1627PhosphoserineCombined sources1
Modified residuei1631PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP51532.
MaxQBiP51532.
PaxDbiP51532.
PeptideAtlasiP51532.
PRIDEiP51532.

PTM databases

iPTMnetiP51532.
PhosphoSitePlusiP51532.
SwissPalmiP51532.

Expressioni

Tissue specificityi

Colocalizes with ZEB1 in E-cadherin-negative cells from established lines, and stroma of normal colon as well as in de-differentiated epithelial cells at the invasion front of colorectal carcinomas (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000127616.
CleanExiHS_SMARCA4.
ExpressionAtlasiP51532. baseline and differential.
GenevisibleiP51532. HS.

Organism-specific databases

HPAiCAB004208.
HPA048340.

Interactioni

Subunit structurei

Component of the CREST-BRG1 complex, at least composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1 (By similarity). Interacts with NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, IKFZ1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. Interacts directly with IKFZ1 in the BAF complex. In muscle cells, the BAF complex also contains DPF3. Component of the BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially acetylates histone H4 (and H2A) within nucleosomes. Interacts with (via the bromodomain) with TERT; the interaction regulates Wnt-mediated signaling. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific chromatin remodeling complex (nBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. Interacts with PHF10/BAF45A (By similarity). Interacts with MYOG (By similarity). Interacts with ZEB1 (via N-terminus).By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARID1AO1449722EBI-302489,EBI-637887
ARID1BQ8NFD53EBI-302489,EBI-679921
ARID2Q68CP96EBI-302489,EBI-637818
ESR1P033723EBI-302489,EBI-78473
H2AFXP161049EBI-302489,EBI-494830
Nr3c1P065363EBI-302489,EBI-1187143From a different organism.
PBRM1Q86U864EBI-302489,EBI-637807
RESTQ131272EBI-302489,EBI-926706
SMARCB1Q1282422EBI-302489,EBI-358419
SMARCC1Q9292225EBI-302489,EBI-355653
SMARCD1Q96GM57EBI-302489,EBI-358489
SYT-SSX1A4PIV714EBI-302489,EBI-6901002

GO - Molecular functioni

  • androgen receptor binding Source: BHF-UCL
  • DNA polymerase binding Source: BHF-UCL
  • lysine-acetylated histone binding Source: BHF-UCL
  • p53 binding Source: BHF-UCL
  • protein N-terminus binding Source: UniProtKB
  • Tat protein binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112481. 216 interactors.
DIPiDIP-24249N.
IntActiP51532. 72 interactors.
MINTiMINT-204078.
STRINGi9606.ENSP00000350720.

Chemistry databases

BindingDBiP51532.

Structurei

Secondary structure

11647
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1456 – 1471Combined sources16
Turni1475 – 1477Combined sources3
Helixi1481 – 1485Combined sources5
Turni1491 – 1493Combined sources3
Helixi1495 – 1500Combined sources6
Helixi1507 – 1515Combined sources9
Helixi1522 – 1539Combined sources18
Beta strandi1542 – 1544Combined sources3
Helixi1545 – 1567Combined sources23
Helixi1571 – 1577Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GRCX-ray1.50A1448-1575[»]
2H60NMR-A1452-1570[»]
3UVDX-ray1.85A1448-1569[»]
5DKDX-ray2.00A/B1451-1569[»]
5EA1X-ray2.00A/B/C1451-1580[»]
ProteinModelPortaliP51532.
SMRiP51532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51532.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini171 – 206QLQPROSITE-ProRule annotationAdd BLAST36
Domaini460 – 532HSAPROSITE-ProRule annotationAdd BLAST73
Domaini766 – 931Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST166
Domaini1084 – 1246Helicase C-terminalPROSITE-ProRule annotationAdd BLAST163
Domaini1477 – 1547BromoPROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 282Necessary for interaction with SS18L1/CRESTBy similarityAdd BLAST282

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi881 – 884DEGH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi578 – 588Poly-LysAdd BLAST11
Compositional biasi663 – 672Poly-Glu10
Compositional biasi1360 – 1364Poly-Glu5
Compositional biasi1571 – 1584Poly-GluAdd BLAST14

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 HSA domain.PROSITE-ProRule annotation
Contains 1 QLQ domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiKOG0386. Eukaryota.
COG0553. LUCA.
COG5076. LUCA.
GeneTreeiENSGT00550000074659.
HOGENOMiHOG000172363.
HOVERGENiHBG056636.
InParanoidiP51532.
KOiK11647.
PhylomeDBiP51532.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR030100. BRG1.
IPR006576. BRK_domain.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014978. Gln-Leu-Gln_QLQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014012. HSA_dom.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF76. PTHR10799:SF76. 4 hits.
PfamiPF07533. BRK. 1 hit.
PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF08880. QLQ. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00592. BRK. 1 hit.
SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
SM00951. QLQ. 1 hit.
SM01314. SnAC. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS51666. QLQ. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P51532-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP
60 70 80 90 100
SAGHPIPTQG PGGYPQDNMH QMHKPMESMH EKGMSDDPRY NQMKGMGMRS
110 120 130 140 150
GGHAGMGPPP SPMDQHSQGY PSPLGGSEHA SSPVPASGPS SGPQMSSGPG
160 170 180 190 200
GAPLDGADPQ ALGQQNRGPT PFNQNQLHQL RAQIMAYKML ARGQPLPDHL
210 220 230 240 250
QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP GPGPAPPNYS
260 270 280 290 300
RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ
310 320 330 340 350
KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PMVPLHQKQS
360 370 380 390 400
RITPIQKPRG LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA
410 420 430 440 450
TIELKALRLL NFQRQLRQEV VVCMRRDTAL ETALNAKAYK RSKRQSLREA
460 470 480 490 500
RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL QHAKDFKEYH RSVTGKIQKL
510 520 530 540 550
TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK LIDQKKDKRL
560 570 580 590 600
AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG
610 620 630 640 650
PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE
660 670 680 690 700
VAPRSDSEES GSEEEEEEEE EEQPQAAQPP TLPVEEKKKI PDPDSDDVSE
710 720 730 740 750
VDARHIIENA KQDVDDEYGV SQALARGLQS YYAVAHAVTE RVDKQSALMV
760 770 780 790 800
NGVLKQYQIK GLEWLVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK
810 820 830 840 850
RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA RRAFVPQLRS
860 870 880 890 900
GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH
910 920 930 940 950
YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT
960 970 980 990 1000
GEKVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM
1010 1020 1030 1040 1050
SALQRVLYRH MQAKGVLLTD GSEKDKKGKG GTKTLMNTIM QLRKICNHPY
1060 1070 1080 1090 1100
MFQHIEESFS EHLGFTGGIV QGLDLYRASG KFELLDRILP KLRATNHKVL
1110 1120 1130 1140 1150
LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK TFNEPGSEYF
1160 1170 1180 1190 1200
IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR
1210 1220 1230 1240 1250
VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI
1260 1270 1280 1290 1300
LEHEEQDESR HCSTGSGSAS FAHTAPPPAG VNPDLEEPPL KEEDEVPDDE
1310 1320 1330 1340 1350
TVNQMIARHE EEFDLFMRMD LDRRREEARN PKRKPRLMEE DELPSWIIKD
1360 1370 1380 1390 1400
DAEVERLTCE EEEEKMFGRG SRHRKEVDYS DSLTEKQWLK AIEEGTLEEI
1410 1420 1430 1440 1450
EEEVRQKKSS RKRKRDSDAG SSTPTTSTRS RDKDDESKKQ KKRGRPPAEK
1460 1470 1480 1490 1500
LSPNPPNLTK KMKKIVDAVI KYKDSSSGRQ LSEVFIQLPS RKELPEYYEL
1510 1520 1530 1540 1550
IRKPVDFKKI KERIRNHKYR SLNDLEKDVM LLCQNAQTFN LEGSLIYEDS
1560 1570 1580 1590 1600
IVLQSVFTSV RQKIEKEDDS EGEESEEEEE GEEEGSESES RSVKVKIKLG
1610 1620 1630 1640
RKEKAQDRLK GGRRRPSRGS RAKPVVSDDD SEEEQEEDRS GSGSEED
Length:1,647
Mass (Da):184,646
Last modified:October 17, 2006 - v2
Checksum:iABDA5EDBF10D7D28
GO
Isoform 2 (identifier: P51532-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1291: Missing.

Note: No experimental confirmation available.
Show »
Length:1,614
Mass (Da):181,348
Checksum:iCB7C83C8DC7109CA
GO
Isoform 3 (identifier: P51532-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1291: Missing.
     1388-1388: W → WLKT
     1475-1475: Missing.

Show »
Length:1,616
Mass (Da):181,603
Checksum:i94455AEA6678D1CC
GO
Isoform 4 (identifier: P51532-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1291: Missing.
     1388-1388: W → WLKT

Show »
Length:1,617
Mass (Da):181,690
Checksum:i33F65B2C4F6CCCEC
GO
Isoform 5 (identifier: P51532-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1291: Missing.
     1475-1475: Missing.

Show »
Length:1,613
Mass (Da):181,261
Checksum:i9E9DBE797BBDF774
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti569R → P in AAB40977 (PubMed:8232556).Curated1
Sequence conflicti569R → P in BAA05143 (PubMed:8208605).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_068209546Missing in CSS4. 1 Publication1
Natural variantiVAR_028215561V → E.Corresponds to variant rs1804579dbSNPEnsembl.1
Natural variantiVAR_068210859T → M in CSS4. 1 PublicationCorresponds to variant rs281875226dbSNPEnsembl.1
Natural variantiVAR_068211885R → C in CSS4. 1 PublicationCorresponds to variant rs281875227dbSNPEnsembl.1
Natural variantiVAR_068212921L → F in CSS4. 1 PublicationCorresponds to variant rs281875228dbSNPEnsembl.1
Natural variantiVAR_0682131011M → T in CSS4. 1 PublicationCorresponds to variant rs281875229dbSNPEnsembl.1
Natural variantiVAR_0282161036M → I.Corresponds to variant rs1801514dbSNPEnsembl.1
Natural variantiVAR_0682141157R → G in CSS4. 1 PublicationCorresponds to variant rs281875230dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0431371259 – 1291Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_0436771388W → WLKT in isoform 3 and isoform 4. 1 Publication1
Alternative sequenceiVSP_0436781475Missing in isoform 3 and isoform 5. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29175 mRNA. Translation: AAB40977.1.
D26156 mRNA. Translation: BAA05143.1.
AF254822 Genomic DNA. Translation: AAG24789.1.
EU430756 mRNA. Translation: ACA09750.1.
EU430757 mRNA. Translation: ACA09751.1.
EU430758 mRNA. Translation: ACA09752.1.
EU430759 mRNA. Translation: ACA09753.1.
AC006127 Genomic DNA. Translation: AAC97986.1.
AC006127 Genomic DNA. Translation: AAC97987.1.
AC011442 Genomic DNA. No translation available.
AC011485 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84167.1.
CCDSiCCDS12253.1. [P51532-1]
CCDS45972.1. [P51532-4]
CCDS45973.1. [P51532-3]
CCDS54217.1. [P51532-2]
CCDS54218.1. [P51532-5]
PIRiS45252.
RefSeqiNP_001122316.1. NM_001128844.1. [P51532-1]
NP_001122317.1. NM_001128845.1. [P51532-4]
NP_001122318.1. NM_001128846.1. [P51532-3]
NP_001122319.1. NM_001128847.1. [P51532-2]
NP_001122320.1. NM_001128848.1. [P51532-5]
NP_003063.2. NM_003072.3. [P51532-1]
XP_016882654.1. XM_017027165.1. [P51532-4]
XP_016882655.1. XM_017027166.1. [P51532-3]
XP_016882656.1. XM_017027167.1. [P51532-2]
XP_016882657.1. XM_017027168.1. [P51532-5]
UniGeneiHs.327527.

Genome annotation databases

EnsembliENST00000344626; ENSP00000343896; ENSG00000127616. [P51532-1]
ENST00000429416; ENSP00000395654; ENSG00000127616. [P51532-1]
ENST00000444061; ENSP00000392837; ENSG00000127616. [P51532-5]
ENST00000541122; ENSP00000445036; ENSG00000127616. [P51532-4]
ENST00000589677; ENSP00000464778; ENSG00000127616. [P51532-3]
ENST00000590574; ENSP00000466963; ENSG00000127616. [P51532-2]
GeneIDi6597.
KEGGihsa:6597.
UCSCiuc002mqf.5. human. [P51532-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Mendelian genes SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29175 mRNA. Translation: AAB40977.1.
D26156 mRNA. Translation: BAA05143.1.
AF254822 Genomic DNA. Translation: AAG24789.1.
EU430756 mRNA. Translation: ACA09750.1.
EU430757 mRNA. Translation: ACA09751.1.
EU430758 mRNA. Translation: ACA09752.1.
EU430759 mRNA. Translation: ACA09753.1.
AC006127 Genomic DNA. Translation: AAC97986.1.
AC006127 Genomic DNA. Translation: AAC97987.1.
AC011442 Genomic DNA. No translation available.
AC011485 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84167.1.
CCDSiCCDS12253.1. [P51532-1]
CCDS45972.1. [P51532-4]
CCDS45973.1. [P51532-3]
CCDS54217.1. [P51532-2]
CCDS54218.1. [P51532-5]
PIRiS45252.
RefSeqiNP_001122316.1. NM_001128844.1. [P51532-1]
NP_001122317.1. NM_001128845.1. [P51532-4]
NP_001122318.1. NM_001128846.1. [P51532-3]
NP_001122319.1. NM_001128847.1. [P51532-2]
NP_001122320.1. NM_001128848.1. [P51532-5]
NP_003063.2. NM_003072.3. [P51532-1]
XP_016882654.1. XM_017027165.1. [P51532-4]
XP_016882655.1. XM_017027166.1. [P51532-3]
XP_016882656.1. XM_017027167.1. [P51532-2]
XP_016882657.1. XM_017027168.1. [P51532-5]
UniGeneiHs.327527.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GRCX-ray1.50A1448-1575[»]
2H60NMR-A1452-1570[»]
3UVDX-ray1.85A1448-1569[»]
5DKDX-ray2.00A/B1451-1569[»]
5EA1X-ray2.00A/B/C1451-1580[»]
ProteinModelPortaliP51532.
SMRiP51532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112481. 216 interactors.
DIPiDIP-24249N.
IntActiP51532. 72 interactors.
MINTiMINT-204078.
STRINGi9606.ENSP00000350720.

Chemistry databases

BindingDBiP51532.
ChEMBLiCHEMBL3085620.
GuidetoPHARMACOLOGYi2740.

PTM databases

iPTMnetiP51532.
PhosphoSitePlusiP51532.
SwissPalmiP51532.

Polymorphism and mutation databases

BioMutaiSMARCA4.
DMDMi116242792.

Proteomic databases

EPDiP51532.
MaxQBiP51532.
PaxDbiP51532.
PeptideAtlasiP51532.
PRIDEiP51532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344626; ENSP00000343896; ENSG00000127616. [P51532-1]
ENST00000429416; ENSP00000395654; ENSG00000127616. [P51532-1]
ENST00000444061; ENSP00000392837; ENSG00000127616. [P51532-5]
ENST00000541122; ENSP00000445036; ENSG00000127616. [P51532-4]
ENST00000589677; ENSP00000464778; ENSG00000127616. [P51532-3]
ENST00000590574; ENSP00000466963; ENSG00000127616. [P51532-2]
GeneIDi6597.
KEGGihsa:6597.
UCSCiuc002mqf.5. human. [P51532-1]

Organism-specific databases

CTDi6597.
DisGeNETi6597.
GeneCardsiSMARCA4.
GeneReviewsiSMARCA4.
HGNCiHGNC:11100. SMARCA4.
HPAiCAB004208.
HPA048340.
MalaCardsiSMARCA4.
MIMi603254. gene.
613325. phenotype.
614609. phenotype.
neXtProtiNX_P51532.
OpenTargetsiENSG00000127616.
Orphaneti1465. Coffin-Siris syndrome.
231108. Familial rhabdoid tumor.
370396. Small cell carcinoma of the ovary.
PharmGKBiPA35950.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0386. Eukaryota.
COG0553. LUCA.
COG5076. LUCA.
GeneTreeiENSGT00550000074659.
HOGENOMiHOG000172363.
HOVERGENiHBG056636.
InParanoidiP51532.
KOiK11647.
PhylomeDBiP51532.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000092531-MONOMER.
ZFISH:ENSG00000127616-MONOMER.
BRENDAi3.6.4.11. 2681.
ReactomeiR-HSA-1266695. Interleukin-7 signaling.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-3247509. Chromatin modifying enzymes.
SignaLinkiP51532.
SIGNORiP51532.

Miscellaneous databases

ChiTaRSiSMARCA4. human.
EvolutionaryTraceiP51532.
GeneWikiiSMARCA4.
GenomeRNAii6597.
PROiP51532.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000127616.
CleanExiHS_SMARCA4.
ExpressionAtlasiP51532. baseline and differential.
GenevisibleiP51532. HS.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR030100. BRG1.
IPR006576. BRK_domain.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014978. Gln-Leu-Gln_QLQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014012. HSA_dom.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
PANTHERiPTHR10799:SF76. PTHR10799:SF76. 4 hits.
PfamiPF07533. BRK. 1 hit.
PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF08880. QLQ. 1 hit.
PF14619. SnAC. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00592. BRK. 1 hit.
SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
SM00951. QLQ. 1 hit.
SM01314. SnAC. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS51666. QLQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSMCA4_HUMAN
AccessioniPrimary (citable) accession number: P51532
Secondary accession number(s): B1A8Z4
, B1A8Z5, B1A8Z6, B1A8Z7, E9PBR8, O95052, Q9HBD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: November 2, 2016
This is version 192 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.