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P51532

- SMCA4_HUMAN

UniProt

P51532 - SMCA4_HUMAN

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Protein

Transcription activator BRG1

Gene

SMARCA4

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene. Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1539 – 15402Required for binding to 'Lys-15'-acetylated histone 3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi779 – 7868ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. androgen receptor binding Source: BHF-UCL
  2. ATP binding Source: UniProtKB-KW
  3. chromatin binding Source: Ensembl
  4. DNA-dependent ATPase activity Source: BHF-UCL
  5. helicase activity Source: ProtInc
  6. lysine-acetylated histone binding Source: BHF-UCL
  7. p53 binding Source: BHF-UCL
  8. protein N-terminus binding Source: UniProtKB
  9. RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl
  10. RNA polymerase II transcription coactivator activity Source: BHF-UCL
  11. Tat protein binding Source: BHF-UCL
  12. transcription coactivator activity Source: BHF-UCL
  13. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. aortic smooth muscle cell differentiation Source: Ensembl
  2. ATP catabolic process Source: GOC
  3. ATP-dependent chromatin remodeling Source: UniProt
  4. blastocyst growth Source: Ensembl
  5. blastocyst hatching Source: Ensembl
  6. cell morphogenesis Source: Ensembl
  7. chromatin remodeling Source: BHF-UCL
  8. definitive erythrocyte differentiation Source: Ensembl
  9. DNA methylation on cytosine within a CG sequence Source: Ensembl
  10. embryonic hindlimb morphogenesis Source: Ensembl
  11. embryonic organ morphogenesis Source: Ensembl
  12. epidermis morphogenesis Source: Ensembl
  13. extracellular matrix organization Source: Ensembl
  14. forebrain development Source: Ensembl
  15. glial cell fate determination Source: Ensembl
  16. heart trabecula formation Source: Ensembl
  17. hindbrain development Source: Ensembl
  18. histone H3 acetylation Source: Ensembl
  19. keratinocyte differentiation Source: Ensembl
  20. lens fiber cell development Source: Ensembl
  21. liver development Source: Ensembl
  22. methylation-dependent chromatin silencing Source: Ensembl
  23. negative regulation of androgen receptor signaling pathway Source: BHF-UCL
  24. negative regulation of cell growth Source: BHF-UCL
  25. negative regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
  26. negative regulation of transcription, DNA-templated Source: BHF-UCL
  27. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  28. negative regulation of transcription from RNA polymerase II promoter during mitosis Source: BHF-UCL
  29. neural retina development Source: BHF-UCL
  30. nucleosome disassembly Source: BHF-UCL
  31. positive regulation by host of viral transcription Source: BHF-UCL
  32. positive regulation of DNA binding Source: Ensembl
  33. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  34. positive regulation of transcription, DNA-templated Source: BHF-UCL
  35. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  36. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  37. stem cell maintenance Source: Ensembl
  38. vasculogenesis Source: Ensembl
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

ReactomeiREACT_200753. formation of the beta-catenin:TCF transactivating complex.
SignaLinkiP51532.

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
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:11100. SMARCA4.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. extracellular space Source: UniProt
  2. heterochromatin Source: Ensembl
  3. membrane Source: UniProtKB
  4. nBAF complex Source: UniProtKB
  5. npBAF complex Source: UniProtKB
  6. nuclear chromatin Source: BHF-UCL
  7. nuclear euchromatin Source: Ensembl
  8. nucleolus Source: HPA
  9. nucleus Source: UniProtKB
  10. perichromatin fibrils Source: Ensembl
  11. protein complex Source: UniProt
  12. SWI/SNF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Mental retardation, autosomal dominant 16 (MRD16) [MIM:614609]: A disease characterized by multiple congenital anomalies and mental retardation. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD16 patients manifest developmental delay, absent or hypoplastic fifth fingernails or toenails, thick eyebrows and long eyelashes, hirsutism. Additional findings include hypotonia, microcephaly, seizures, a Dandy-Walker malformation, and vision and hearing problems.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti546 – 5461Missing in MRD16. 1 Publication
VAR_068209
Natural varianti859 – 8591T → M in MRD16. 1 Publication
Corresponds to variant rs281875226 [ dbSNP | Ensembl ].
VAR_068210
Natural varianti885 – 8851R → C in MRD16. 1 Publication
Corresponds to variant rs281875227 [ dbSNP | Ensembl ].
VAR_068211
Natural varianti921 – 9211L → F in MRD16. 1 Publication
Corresponds to variant rs281875228 [ dbSNP | Ensembl ].
VAR_068212
Natural varianti1011 – 10111M → T in MRD16. 1 Publication
Corresponds to variant rs281875229 [ dbSNP | Ensembl ].
VAR_068213
Natural varianti1157 – 11571R → G in MRD16. 1 Publication
Corresponds to variant rs281875230 [ dbSNP | Ensembl ].
VAR_068214

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1484 – 14841V → A: No effect on binding to 'Lys-15'-acetylated histone H3. 1 Publication
Mutagenesisi1539 – 15391F → A: Abolishes binding to 'Lys-15'-acetylated histone H3. 1 Publication
Mutagenesisi1540 – 15401N → A: Abolishes binding to 'Lys-15'-acetylated histone H3. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16471647Transcription activator BRG1PRO_0000074353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphothreonine1 Publication
Modified residuei188 – 1881N6-acetyllysine1 Publication
Modified residuei353 – 3531Phosphothreonine1 Publication
Modified residuei609 – 6091Phosphothreonine1 Publication
Modified residuei610 – 6101Phosphoserine1 Publication
Modified residuei613 – 6131Phosphoserine3 Publications
Modified residuei695 – 6951Phosphoserine3 Publications
Modified residuei699 – 6991Phosphoserine3 Publications
Modified residuei1382 – 13821Phosphoserine2 Publications
Modified residuei1452 – 14521Phosphoserine2 Publications
Modified residuei1570 – 15701Phosphoserine3 Publications
Modified residuei1575 – 15751Phosphoserine3 Publications
Modified residuei1586 – 15861Phosphoserine1 Publication
Modified residuei1627 – 16271Phosphoserine2 Publications
Modified residuei1631 – 16311Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51532.
PaxDbiP51532.
PRIDEiP51532.

PTM databases

PhosphoSiteiP51532.

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

BgeeiP51532.
CleanExiHS_SMARCA4.
ExpressionAtlasiP51532. baseline and differential.
GenevestigatoriP51532.

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. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. 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 similarity12 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

Protein-protein interaction databases

BioGridi112481. 184 interactions.
DIPiDIP-24249N.
IntActiP51532. 56 interactions.
MINTiMINT-204078.
STRINGi9606.ENSP00000350720.

Structurei

Secondary structure

1
1647
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1456 – 147116Combined sources
Turni1475 – 14773Combined sources
Helixi1481 – 14855Combined sources
Turni1491 – 14933Combined sources
Helixi1495 – 15006Combined sources
Helixi1507 – 15159Combined sources
Helixi1522 – 153918Combined sources
Beta strandi1542 – 15443Combined sources
Helixi1545 – 156723Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GRCX-ray1.50A1448-1575[»]
2H60NMR-A1452-1570[»]
3UVDX-ray1.85A1448-1569[»]
ProteinModelPortaliP51532.
SMRiP51532. Positions 749-1265, 1449-1569.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51532.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 20636QLQPROSITE-ProRule annotationAdd
BLAST
Domaini460 – 53273HSAPROSITE-ProRule annotationAdd
BLAST
Domaini766 – 931166Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1084 – 1246163Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini1477 – 154771BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 282282Necessary for interaction with SS18L1/CRESTBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi881 – 8844DEGH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi578 – 58811Poly-LysAdd
BLAST
Compositional biasi663 – 67210Poly-Glu
Compositional biasi1360 – 13645Poly-Glu
Compositional biasi1571 – 158414Poly-GluAdd
BLAST

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

eggNOGiCOG0553.
GeneTreeiENSGT00550000074659.
HOGENOMiHOG000172363.
HOVERGENiHBG056636.
InParanoidiP51532.
KOiK11647.
OrthoDBiEOG771265.
PhylomeDBiP51532.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR006576. BRK_domain.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014978. Gln-Leu-Gln_QLQ.
IPR013999. HAS_subgr.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view]
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.
[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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti569 – 5691R → P in AAB40977. (PubMed:8232556)Curated
Sequence conflicti569 – 5691R → P in BAA05143. (PubMed:8208605)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti546 – 5461Missing in MRD16. 1 Publication
VAR_068209
Natural varianti561 – 5611V → E.
Corresponds to variant rs1804579 [ dbSNP | Ensembl ].
VAR_028215
Natural varianti859 – 8591T → M in MRD16. 1 Publication
Corresponds to variant rs281875226 [ dbSNP | Ensembl ].
VAR_068210
Natural varianti885 – 8851R → C in MRD16. 1 Publication
Corresponds to variant rs281875227 [ dbSNP | Ensembl ].
VAR_068211
Natural varianti921 – 9211L → F in MRD16. 1 Publication
Corresponds to variant rs281875228 [ dbSNP | Ensembl ].
VAR_068212
Natural varianti1011 – 10111M → T in MRD16. 1 Publication
Corresponds to variant rs281875229 [ dbSNP | Ensembl ].
VAR_068213
Natural varianti1036 – 10361M → I.
Corresponds to variant rs1801514 [ dbSNP | Ensembl ].
VAR_028216
Natural varianti1157 – 11571R → G in MRD16. 1 Publication
Corresponds to variant rs281875230 [ dbSNP | Ensembl ].
VAR_068214

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1259 – 129133Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 1 PublicationVSP_043137Add
BLAST
Alternative sequencei1388 – 13881W → WLKT in isoform 3 and isoform 4. 1 PublicationVSP_043677
Alternative sequencei1475 – 14751Missing in isoform 3 and isoform 5. 1 PublicationVSP_043678

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005260089.1. XM_005260032.1. [P51532-4]
XP_005260090.1. XM_005260033.1. [P51532-3]
XP_005260091.1. XM_005260034.1. [P51532-2]
XP_005260092.1. XM_005260035.1. [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.4. human. [P51532-1]
uc002mqj.4. human. [P51532-4]
uc010dxq.3. human. [P51532-2]
uc010dxr.3. human. [P51532-5]
uc010dxs.3. human. [P51532-3]

Polymorphism databases

DMDMi116242792.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS12253.1. [P51532-1 ]
CCDS45972.1. [P51532-4 ]
CCDS45973.1. [P51532-3 ]
CCDS54217.1. [P51532-2 ]
CCDS54218.1. [P51532-5 ]
PIRi S45252.
RefSeqi NP_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_005260089.1. XM_005260032.1. [P51532-4 ]
XP_005260090.1. XM_005260033.1. [P51532-3 ]
XP_005260091.1. XM_005260034.1. [P51532-2 ]
XP_005260092.1. XM_005260035.1. [P51532-5 ]
UniGenei Hs.327527.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GRC X-ray 1.50 A 1448-1575 [» ]
2H60 NMR - A 1452-1570 [» ]
3UVD X-ray 1.85 A 1448-1569 [» ]
ProteinModelPortali P51532.
SMRi P51532. Positions 749-1265, 1449-1569.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112481. 184 interactions.
DIPi DIP-24249N.
IntActi P51532. 56 interactions.
MINTi MINT-204078.
STRINGi 9606.ENSP00000350720.

Chemistry

ChEMBLi CHEMBL3085620.

PTM databases

PhosphoSitei P51532.

Polymorphism databases

DMDMi 116242792.

Proteomic databases

MaxQBi P51532.
PaxDbi P51532.
PRIDEi P51532.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344626 ; 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 ]
GeneIDi 6597.
KEGGi hsa:6597.
UCSCi uc002mqf.4. human. [P51532-1 ]
uc002mqj.4. human. [P51532-4 ]
uc010dxq.3. human. [P51532-2 ]
uc010dxr.3. human. [P51532-5 ]
uc010dxs.3. human. [P51532-3 ]

Organism-specific databases

CTDi 6597.
GeneCardsi GC19P011071.
GeneReviewsi SMARCA4.
HGNCi HGNC:11100. SMARCA4.
HPAi CAB004208.
HPA048340.
MIMi 603254. gene.
613325. phenotype.
614609. phenotype.
neXtProti NX_P51532.
Orphaneti 1465. Coffin-Siris syndrome.
231108. Familial rhabdoid tumor.
370396. Small cell carcinoma of the ovary.
PharmGKBi PA35950.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00550000074659.
HOGENOMi HOG000172363.
HOVERGENi HBG056636.
InParanoidi P51532.
KOi K11647.
OrthoDBi EOG771265.
PhylomeDBi P51532.

Enzyme and pathway databases

Reactomei REACT_200753. formation of the beta-catenin:TCF transactivating complex.
SignaLinki P51532.

Miscellaneous databases

ChiTaRSi SMARCA4. human.
EvolutionaryTracei P51532.
GeneWikii SMARCA4.
GenomeRNAii 6597.
NextBioi 25661.
PROi P51532.
SOURCEi Search...

Gene expression databases

Bgeei P51532.
CleanExi HS_SMARCA4.
ExpressionAtlasi P51532. baseline and differential.
Genevestigatori P51532.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR006576. BRK_domain.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014978. Gln-Leu-Gln_QLQ.
IPR013999. HAS_subgr.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR029295. SnAC.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF07533. 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 ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00592. BRK. 1 hit.
SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
SM00951. QLQ. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS00633. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription."
    Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.
    Nature 366:170-174(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor."
    Chiba H., Muramatsu M., Nomoto A., Kato H.
    Nucleic Acids Res. 22:1815-1820(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  4. "BRG1, a component of the SWI-SNF complex, is mutated in multiple human tumor cell lines."
    Wong A.K.C., Shanahan F., Chen Y., Lian L., Ha P., Hendricks K., Ghaffari S., Iliev D., Penn B., Woodland A.-M., Smith R., Salada G., Carillo A., Laity K., Gupte J., Swedlund B., Tavtigian S.V., Teng D.H.-F., Lees E.
    Cancer Res. 60:6171-6177(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Frequent BRG1/SMARCA4-inactivating mutations in human lung cancer cell lines."
    Medina P.P., Romero O.A., Kohno T., Montuenga L.M., Pio R., Yokota J., Sanchez-Cespedes M.
    Hum. Mutat. 29:617-622(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
    Tissue: Lung.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex."
    Fryer C.J., Archer T.K.
    Nature 393:88-91(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR3C1 AND PGR.
  9. "Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes."
    Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.
    Immunity 10:345-355(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKZF1 IN THE BAF COMPLEX.
  10. "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation."
    Park J., Wood M.A., Cole M.D.
    Mol. Cell. Biol. 22:1307-1316(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND TRRAP.
  11. "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
    Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
    Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
  12. "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
    Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
    Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR3C1 AND SMARD1.
  13. "TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival."
    Liu K., Luo Y., Lin F.-T., Lin W.-C.
    Genes Dev. 18:673-686(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOPBP1.
  14. "hZimp7, a novel PIAS-like protein, enhances androgen receptor-mediated transcription and interacts with SWI/SNF-like BAF complexes."
    Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B., Sun Z.
    Mol. Endocrinol. 19:2915-2929(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZMIM2.
  15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND SER-1452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  18. "Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
    Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
    Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1382; SER-1452; SER-1570; SER-1575 AND SER-1586, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: INTERACTION WITH TERT, FUNCTION.
  22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353; THR-609; SER-610; SER-613; SER-695; SER-699; SER-1570; SER-1575; SER-1627 AND SER-1631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Germline nonsense mutation and somatic inactivation of SMARCA4/BRG1 in a family with rhabdoid tumor predisposition syndrome."
    Schneppenheim R., Fruhwald M.C., Gesk S., Hasselblatt M., Jeibmann A., Kordes U., Kreuz M., Leuschner I., Martin Subero J.I., Obser T., Oyen F., Vater I., Siebert R.
    Am. J. Hum. Genet. 86:279-284(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RTPS2.
  25. "ZEB1 represses E-cadherin and induces an EMT by recruiting the SWI/SNF chromatin-remodeling protein BRG1."
    Sanchez-Tillo E., Lazaro A., Torrent R., Cuatrecasas M., Vaquero E.C., Castells A., Engel P., Postigo A.
    Oncogene 29:3490-3500(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZEB1, TISSUE SPECIFICITY.
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-699; SER-1570 AND SER-1575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-695; SER-699; SER-1382; SER-1627 AND SER-1631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Solution structure of human Brg1 bromodomain and its specific binding to acetylated histone tails."
    Shen W., Xu C., Huang W., Zhang J., Carlson J.E., Tu X., Wu J., Shi Y.
    Biochemistry 46:2100-2110(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1452-1570 IN COMPLEX WITH ACETYLATED HISTONES, MUTAGENESIS OF VAL-1484; PHE-1539 AND ASN-1540.
  30. "Structural ramification for acetyl-lysine recognition by the bromodomain of human BRG1 protein, a central ATPase of the SWI/SNF remodeling complex."
    Singh M., Popowicz G.M., Krajewski M., Holak T.A.
    ChemBioChem 8:1308-1316(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1448-1575 IN COMPLEX WITH ACETYLATED HISTONE 3.
  31. Cited for: VARIANTS MRD16 LYS-546 DEL; MET-859; CYS-885; PHE-921; THR-1011 AND GLY-1157.

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: October 29, 2014
This is version 170 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

External Data

Dasty 3