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P51532

- SMCA4_HUMAN

UniProt

P51532 - SMCA4_HUMAN

Protein

Transcription activator BRG1

Gene

SMARCA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    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 binding Source: UniProtKB
    9. protein N-terminus binding Source: UniProtKB
    10. RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl
    11. RNA polymerase II transcription coactivator activity Source: BHF-UCL
    12. Tat protein binding Source: BHF-UCL
    13. transcription coactivator activity Source: BHF-UCL
    14. 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. liver development Source: Ensembl
    21. methylation-dependent chromatin silencing Source: Ensembl
    22. negative regulation of androgen receptor signaling pathway Source: BHF-UCL
    23. negative regulation of cell growth Source: BHF-UCL
    24. negative regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
    25. negative regulation of transcription, DNA-templated Source: BHF-UCL
    26. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    27. negative regulation of transcription from RNA polymerase II promoter during mitosis Source: BHF-UCL
    28. neural retina development Source: BHF-UCL
    29. nucleosome disassembly Source: BHF-UCL
    30. positive regulation by host of viral transcription Source: BHF-UCL
    31. positive regulation of DNA binding Source: Ensembl
    32. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    33. positive regulation of transcription, DNA-templated Source: BHF-UCL
    34. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    35. regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    36. stem cell maintenance Source: Ensembl
    37. vasculogenesis Source: Ensembl

    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

    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.
    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

    ArrayExpressiP51532.
    BgeeiP51532.
    CleanExiHS_SMARCA4.
    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. 183 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 – 147116
    Turni1475 – 14773
    Helixi1481 – 14855
    Turni1491 – 14933
    Helixi1495 – 15006
    Helixi1507 – 15159
    Helixi1522 – 153918
    Beta strandi1542 – 15443
    Helixi1545 – 156723

    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.
    HOGENOMiHOG000172363.
    HOVERGENiHBG056636.
    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

    MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP     50
    SAGHPIPTQG PGGYPQDNMH QMHKPMESMH EKGMSDDPRY NQMKGMGMRS 100
    GGHAGMGPPP SPMDQHSQGY PSPLGGSEHA SSPVPASGPS SGPQMSSGPG 150
    GAPLDGADPQ ALGQQNRGPT PFNQNQLHQL RAQIMAYKML ARGQPLPDHL 200
    QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP GPGPAPPNYS 250
    RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ 300
    KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PMVPLHQKQS 350
    RITPIQKPRG LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA 400
    TIELKALRLL NFQRQLRQEV VVCMRRDTAL ETALNAKAYK RSKRQSLREA 450
    RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL QHAKDFKEYH RSVTGKIQKL 500
    TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK LIDQKKDKRL 550
    AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG 600
    PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE 650
    VAPRSDSEES GSEEEEEEEE EEQPQAAQPP TLPVEEKKKI PDPDSDDVSE 700
    VDARHIIENA KQDVDDEYGV SQALARGLQS YYAVAHAVTE RVDKQSALMV 750
    NGVLKQYQIK GLEWLVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK 800
    RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA RRAFVPQLRS 850
    GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH 900
    YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT 950
    GEKVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM 1000
    SALQRVLYRH MQAKGVLLTD GSEKDKKGKG GTKTLMNTIM QLRKICNHPY 1050
    MFQHIEESFS EHLGFTGGIV QGLDLYRASG KFELLDRILP KLRATNHKVL 1100
    LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK TFNEPGSEYF 1150
    IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR 1200
    VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI 1250
    LEHEEQDESR HCSTGSGSAS FAHTAPPPAG VNPDLEEPPL KEEDEVPDDE 1300
    TVNQMIARHE EEFDLFMRMD LDRRREEARN PKRKPRLMEE DELPSWIIKD 1350
    DAEVERLTCE EEEEKMFGRG SRHRKEVDYS DSLTEKQWLK AIEEGTLEEI 1400
    EEEVRQKKSS RKRKRDSDAG SSTPTTSTRS RDKDDESKKQ KKRGRPPAEK 1450
    LSPNPPNLTK KMKKIVDAVI KYKDSSSGRQ LSEVFIQLPS RKELPEYYEL 1500
    IRKPVDFKKI KERIRNHKYR SLNDLEKDVM LLCQNAQTFN LEGSLIYEDS 1550
    IVLQSVFTSV RQKIEKEDDS EGEESEEEEE GEEEGSESES RSVKVKIKLG 1600
    RKEKAQDRLK GGRRRPSRGS RAKPVVSDDD SEEEQEEDRS GSGSEED 1647
    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]
    ENST00000413806; ENSP00000414727; ENSG00000127616. [P51532-4]
    ENST00000429416; ENSP00000395654; ENSG00000127616. [P51532-1]
    ENST00000444061; ENSP00000392837; ENSG00000127616. [P51532-5]
    ENST00000450717; ENSP00000397783; ENSG00000127616. [P51532-3]
    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. 183 interactions.
    DIPi DIP-24249N.
    IntActi P51532. 56 interactions.
    MINTi MINT-204078.
    STRINGi 9606.ENSP00000350720.

    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 ]
    ENST00000413806 ; ENSP00000414727 ; ENSG00000127616 . [P51532-4 ]
    ENST00000429416 ; ENSP00000395654 ; ENSG00000127616 . [P51532-1 ]
    ENST00000444061 ; ENSP00000392837 ; ENSG00000127616 . [P51532-5 ]
    ENST00000450717 ; ENSP00000397783 ; ENSG00000127616 . [P51532-3 ]
    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.
    PharmGKBi PA35950.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000172363.
    HOVERGENi HBG056636.
    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

    ArrayExpressi P51532.
    Bgeei P51532.
    CleanExi HS_SMARCA4.
    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

    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 1, 2014
    This is version 169 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