Search Results
Overview
| Uniprot ID | P28370 |
|---|---|
| Protein Name | SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1 |
| Gene Name | SMARCA1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 59 | KGEKKKEKNVSSFQL |
| 67 | NVSSFQLKLAAKAPK |
| 71 | FQLKLAAKAPKSEKE |
Function
ATPase that possesses intrinsic ATP-dependent chromatin-remodeling activity (PubMed:14609955, PubMed:15310751, PubMed:15640247, PubMed:28801535). ATPase activity is substrate-dependent, and is increased when nucleosomes are the substrate, but is also catalytically active when DNA alone is the substrate (PubMed:14609955, PubMed:15310751, PubMed:15640247). Catalytic subunit of ISWI chromatin-remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair (PubMed:14609955, PubMed:15310751, PubMed:15640247, PubMed:28801535). Within the ISWI chromatin-remodeling complexes, slides edge- and center-positioned histone octamers away from their original location on the DNA template (PubMed:28801535). Catalytic activity and histone octamer sliding propensity is regulated and determined by components of the ISWI chromatin-remodeling complexes (PubMed:28801535). The BAZ1A-, BAZ1B-, BAZ2A- and BAZ2B-containing ISWI chromatin-remodeling complexes regulate the spacing of nucleosomes along the chromatin and have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). The CECR2- and RSF1-containing ISWI chromatin-remodeling complexes do not have the ability to slide mononucleosomes to the center of a DNA template (PubMed:28801535). Within the NURF-1 and CERF-1 ISWI chromatin remodeling complexes, nucleosomes are the preferred substrate for its ATPase activity (PubMed:14609955, PubMed:15640247). Within the NURF-1 ISWI chromatin-remodeling complex, binds to the promoters of En1 and En2 to positively regulate their expression and promote brain development (PubMed:14609955). May promote neurite outgrowth (PubMed:14609955). May be involved in the development of luteal cells (PubMed:16740656). Facilitates nucleosome assembly during DNA replication, ensuring replication fork progression and genomic stability by preventing replication stress and nascent DNA gaps (PubMed:39413208)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0090537 | CERF complex |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0016589 | NURF complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0140658 | ATP-dependent chromatin remodeler activity |
| Molecular Function | GO:0036310 | ATP-dependent DNA/DNA annealing activity |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0004386 | helicase activity |
| Molecular Function | GO:0140750 | nucleosome array spacer activity |
| Molecular Function | GO:0031491 | nucleosome binding |
| Molecular Function | GO:0061629 | RNA polymerase II-specific DNA-binding transcription factor binding |
| Biological Process | GO:0007420 | brain development |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:0030182 | neuron differentiation |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.