Reviewed,
UniProtKB/Swiss-Prot P51532 (SMCA4_HUMAN)
Last modified
November 25, 2008.
Version 98.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable global transcription activator SNF2L4 EC=3.6.1.- Alternative name(s): ATP-dependent helicase SMARCA4 SNF2-beta BRG-1 protein Mitotic growth and transcription activator Brahma protein homolog 1 SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1647 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Transcriptional coactivator cooperating with nuclear hormone receptors to potentiate transcriptional activation. |
| Subunit structure | 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, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of the BAF53 complex, at least composed of BAF53A, RUVBL1, SMARCA4/BRG1, and TRRAP, which preferentially acetylates histone H4 (and H2A) within nucleosomes. |
| Subcellular location | |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. |
| Sequence similarities | Belongs to the SNF2/RAD54 helicase family. Contains 1 bromo domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HSA domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Coding sequence diversity | Polymorphism |
| Domain | Bromodomain |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Activator Helicase Hydrolase |
| PTM | Phosphoprotein |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | regulation of transcription from RNA polymerase II promoter Ref.3 Traceable author statement. Source: ProtInc |
| Cellular component | SWI/SNF complex Inferred from direct assay. Source: UniProtKB |
| Molecular function | ATP binding Inferred from electronic annotation. Source: InterPro helicase activity Ref.3Traceable author statement. Source: ProtInc identical protein binding Ref.8Inferred from physical interaction. Source: IntAct protein N-terminus binding Ref.8Inferred from physical interaction. Source: UniProtKB transcription coactivator activity Ref.3Traceable author statement. Source: ProtInc transcription factor activity Ref.3Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 1 | EBI-302489,EBI-302489 | ||
| ARID1A | O14497 | 4 | EBI-302489,EBI-637887 | |
| ARID1B | Q8NFD5 | 2 | EBI-302489,EBI-679921 | |
| ARID2 | Q68CP9 | 1 | EBI-302489,EBI-637818 | |
| MPHOSPH6 | Q99547 | 1 | EBI-302489,EBI-373187 | |
| NR3C1 | P04150 | 1 | EBI-302489,EBI-493507 | |
| Nr3c1 | P06536 | 3 | EBI-302489,EBI-1187143 | From a different organism. |
| PBRM1 | Q86U86 | 1 | EBI-302489,EBI-637807 | |
| PPARG | P37231 | 1 | EBI-302489,EBI-781384 | |
| RCOR1 | Q9UKL0 | 1 | EBI-302489,EBI-926563 | |
| REST | Q13127 | 1 | EBI-302489,EBI-926706 | |
| SMARCC1 | Q92922 | 1 | EBI-302489,EBI-355653 | |
| SMARCD1 | Q96GM5 | 2 | EBI-302489,EBI-358489 | |
| SMARCE1 | Q969G3-1 | 1 | EBI-302489,EBI-455091 | |
| SMARCE1 | Q969G3-2 | 1 | EBI-302489,EBI-455096 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1647 | 1647 | Probable global transcription activator SNF2L4 | PRO_0000074353 | |||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||
| Domain | 460 – 532 | 73 | HSA | ||||||||||||||||||||||||
| Domain | 766 – 931 | 166 | Helicase ATP-binding | ||||||||||||||||||||||||
| Domain | 1084 – 1246 | 163 | Helicase C-terminal | ||||||||||||||||||||||||
| Domain | 1477 – 1547 | 71 | Bromo | ||||||||||||||||||||||||
| Nucleotide binding | 779 – 786 | 8 | ATP Potential | ||||||||||||||||||||||||
| Motif | 881 – 884 | 4 | DEGH box | ||||||||||||||||||||||||
| Compositional bias | 578 – 588 | 11 | Poly-Lys | ||||||||||||||||||||||||
| Compositional bias | 663 – 672 | 10 | Poly-Glu | ||||||||||||||||||||||||
| Compositional bias | 1360 – 1364 | 5 | Poly-Glu | ||||||||||||||||||||||||
| Compositional bias | 1571 – 1584 | 14 | Poly-Glu | ||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||
| Modified residue | 11 | 1 | Phosphothreonine | ||||||||||||||||||||||||
| Modified residue | 610 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 613 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 655 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 657 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 660 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 662 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 695 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 721 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1382 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1452 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1570 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1575 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1586 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1627 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1631 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1640 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1642 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 1644 | 1 | Phosphoserine | ||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||
| Natural variant | 561 | 1 | V → E: dbSNP rs1804579. | VAR_028215 | |||||||||||||||||||||||
| Natural variant | 1036 | 1 | M → I: dbSNP rs1801514. | VAR_028216 | |||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||
| Sequence conflict | 569 | 1 | R → P in AAB40977. Ref.1 | ||||||||||||||||||||||||
| Sequence conflict | 569 | 1 | R → P in BAA05143. Ref.3 | ||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Helix | 1462 – 1471 | 10 | |||||||||||||||||||||||||
| Turn | 1475 – 1478 | 4 | |||||||||||||||||||||||||
| Helix | 1481 – 1485 | 5 | |||||||||||||||||||||||||
| Turn | 1491 – 1493 | 3 | |||||||||||||||||||||||||
| Helix | 1495 – 1500 | 6 | |||||||||||||||||||||||||
| Helix | 1507 – 1514 | 8 | |||||||||||||||||||||||||
| Turn | 1515 – 1517 | 3 | |||||||||||||||||||||||||
| Helix | 1522 – 1539 | 18 | |||||||||||||||||||||||||
| Beta strand | 1542 – 1544 | 3 | |||||||||||||||||||||||||
| Helix | 1545 – 1564 | 20 | |||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 8232556] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [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: 8208605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 11085541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [5] | "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. Lucas S.M.Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex." Fryer C.J., Archer T.K. Nature 393:88-91(1998) [PubMed: 9590696] [Abstract] Cited for: INTERACTION WITH NR3C1 AND PGR. |
| [7] | "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: 11839798] [Abstract] Cited for: IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND TRRAP. |
| [8] | "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: 12917342] [Abstract] Cited for: INTERACTION WITH NR3C1 AND SMARD1. |
| [9] | "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: 15075294] [Abstract] Cited for: INTERACTION WITH TOPBP1. |
| [10] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-1382, MASS SPECTROMETRY. Tissue: Epithelium. |
| [11] | "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: 16051670] [Abstract] Cited for: INTERACTION WITH ZMIM2. |
| [12] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-655; SER-657; SER-660; SER-662 AND SER-1452, MASS SPECTROMETRY. Tissue: Epithelium. |
| [13] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-721, MASS SPECTROMETRY. |
| [14] | "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: 18765789] [Abstract] Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY. |
| [15] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1382; SER-1452; SER-1570; SER-1575; SER-1586; SER-1627; SER-1631; SER-1640; SER-1642 AND SER-1644, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| U29175 mRNA. Translation: AAB40977.1. D26156 mRNA. Translation: BAA05143.1. AF254822 Genomic DNA. Translation: AAG24789.1. AC006127 Genomic DNA. Translation: AAC97986.1. AC006127 Genomic DNA. Translation: AAC97987.1. AC011442 Genomic DNA. No translation available. AC011485 Genomic DNA. No translation available. | |||||||||||||||||||
| PIR | S45252. | ||||||||||||||||||
| RefSeq | NP_001122316.1. NP_003063.2. | ||||||||||||||||||
| UniGene | Hs.327527 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP:24249N. | ||||||||||||||||||
| IntAct | P51532. | ||||||||||||||||||
PTM databases | |||||||||||||||||||

Clusters with