P28370 · SMCA1_HUMAN
- ProteinProbable global transcription activator SNF2L1
- GeneSMARCA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1054 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Isoform 1
Acts as a negative regulator of chromatin remodelers by generating inactive complexes (PubMed:15310751).
Isoform 2
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).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | ATPase complex | |
Cellular Component | CERF complex | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | NURF complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent chromatin remodeler activity | |
Molecular Function | ATP-dependent DNA/DNA annealing activity | |
Molecular Function | DNA binding | |
Molecular Function | helicase activity | |
Molecular Function | hydrolase activity | |
Molecular Function | nucleosome binding | |
Molecular Function | RNA polymerase II-specific DNA-binding transcription factor binding | |
Biological Process | brain development | |
Biological Process | chromatin remodeling | |
Biological Process | neuron differentiation | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable global transcription activator SNF2L1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP28370
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 214 | No effect on neurite outgrowth. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_001242 | 656 | in dbSNP:rs1134838 | |||
Sequence: Q → R | ||||||
Natural variant | VAR_079028 | 978 | found in a patient with Rett syndrome-like phenotype; uncertain significance | |||
Sequence: G → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 879 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000074351 | 1-1054 | UniProt | Probable global transcription activator SNF2L1 | |||
Sequence: MEQDTAAVAATVAAADATATIVVIEDEQPGPSTSQEEGAAAAATEATAATEKGEKKKEKNVSSFQLKLAAKAPKSEKEMDPEYEEKMKADRAKRFEFLLKQTELFAHFIQPSAQKSPTSPLNMKLGRPRIKKDEKQSLISAGDYRHRRTEQEEDEELLSESRKTSNVCIRFEVSPSYVKGGPLRDYQIRGLNWLISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIKTDVEKSLPPKKEIKIYLGLSKMQREWYTKILMKDIDVLNSSGKMDKMRLLNILMQLRKCCNHPYLFDGAEPGPPYTTDEHIVSNSGKMVVLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREDKFLEVEFLGQREAIEAFNAPNSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLIDQQSNKLAKEEMLQMIRHGATHVFASKESELTDEDITTILERGEKKTAEMNERLQKMGESSLRNFRMDIEQSLYKFEGEDYREKQKLGMVEWIEPPKRERKANYAVDAYFREALRVSEPKIPKAPRPPKQPNVQDFQFFPPRLFELLEKEILYYRKTIGYKVPRNPDIPNPALAQREEQKKIDGAEPLTPEETEEKEKLLTQGFTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEYSAVFWERCNELQDIEKIMAQIERGEARIQRRISIKKALDAKIARYKAPFHQLRIQYGTSKGKNYTEEEDRFLICMLHKMGFDRENVYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISLIEKENMEIEERERAEKKKRATKTPMVKFSAFS | |||||||
Modified residue (large scale data) | 112 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 116 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 119 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 119 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 662 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 690 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 725 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 728 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 750 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 770 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 954 | UniProt | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Isoform 1
Component of the BPFT-SMARCA1 complex at least composed of SMARCA1, BPFT, RBBP4 and RBBP7; the complex is catalytically inactive and does not remodel chromatin (PubMed:15310751).
Within the complex interacts with BPTF, RBBP4 and RBBP7 (PubMed:15310751).
Component of the BAZ1A-1-SMARCA1 complex at least composed of SMARCA1 and BAZ1A; the complex is catalytically inactive and does not remodel chromatin (PubMed:28801535).
Component of the BAZ1B-1-SMARCA1 complex at least composed of SMARCA1 and BAZ1B; the complex is catalytically inactive and does not remodel chromatin (PubMed:28801535).
Isoform 2
Component of the ACF-1 ISWI chromatin remodeling complex at least composed of SMARCA1 and BAZ1A, which regulates the spacing of histone octamers on the DNA template to facilitate access to DNA (PubMed:28801535).
Within the complex interacts with BAZ1A; the interaction is direct (PubMed:28801535).
Component of the WICH-1 ISWI chromatin remodeling complex at least composed of SMARCA1 and BAZ1B/WSTF (PubMed:28801535).
Within the complex interacts with BAZ1B/WSTF (PubMed:28801535).
Component of the NoRC-1 ISWI chromatin remodeling complex at least composed of SMARCA1 and BAZ2A/TIP5 (PubMed:28801535).
Within the complex interacts with BAZ2A/TIP5 (PubMed:28801535).
Component of the BRF-1 ISWI chromatin remodeling complex at least composed of SMARCA1 and BAZ2B (PubMed:28801535).
Within the complex interacts with BAZ2B (PubMed:28801535).
Component of the NURF-1 ISWI chromatin remodeling complex (also called the nucleosome-remodeling factor (NURF) complex) at least composed of SMARCA1, BPTF, RBBP4 and RBBP7 (PubMed:14609955, PubMed:15640247, PubMed:28801535).
Within the complex interacts with BPTF (PubMed:14609955, PubMed:15310751, PubMed:28801535).
Within the complex interacts with RBBP4 and RBBP7 (PubMed:14609955, PubMed:15310751).
Component of the CERF-1 ISWI chromatin remodeling complex (also called the CECR2-containing-remodeling factor (CERF) complex) at least composed of CECR2 and SMARCA1 (PubMed:15640247, PubMed:28801535).
Within the complex interacts with CECR2 (PubMed:28801535).
Component of the RSF-1 ISWI chromatin remodeling complex at least composed of SMARCA1 and RSF1 (PubMed:15640247, PubMed:28801535).
Within the complex interacts with RSF1 (PubMed:28801535).
Interacts with PRLR (PubMed:16740656).
Interacts with ERCC6 (PubMed:26030138).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P28370 | BAZ1B Q9UIG0 | 2 | EBI-2822460, EBI-927482 | |
BINARY | P28370 | BPTF Q12830 | 7 | EBI-2822460, EBI-1560273 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 25-82 | Disordered | ||||
Sequence: EDEQPGPSTSQEEGAAAAATEATAATEKGEKKKEKNVSSFQLKLAAKAPKSEKEMDPE | ||||||
Domain | 195-360 | Helicase ATP-binding | ||||
Sequence: ISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRVICFVGDKDARAAFIRDEMMPGEWDVCVTSYEMVIKEKSVFKKFHWRYLVIDEAHRIKNEKSKLSEIVREFKSTNRLLLTGTPLQNNLHELWALLNFLLPD | ||||||
Motif | 311-314 | DEAH box | ||||
Sequence: DEAH | ||||||
Domain | 490-653 | Helicase C-terminal | ||||
Sequence: VLDKLLAKLKEQGSRVLIFSQMTRLLDILEDYCMWRGYEYCRLDGQTPHEEREDKFLEVEFLGQREAIEAFNAPNSSKFIFMLSTRAGGLGINLASADVVILYDSDWNPQVDLQAMDRAHRIGQKKPVRVFRLITDNTVEERIVERAEIKLRLDSIVIQQGRLI | ||||||
Region | 819-849 | Disordered | ||||
Sequence: PDIPNPALAQREEQKKIDGAEPLTPEETEEK | ||||||
Compositional bias | 827-849 | Basic and acidic residues | ||||
Sequence: AQREEQKKIDGAEPLTPEETEEK | ||||||
Domain | 855-907 | SANT 1 | ||||
Sequence: QGFTNWTKRDFNQFIKANEKYGRDDIDNIAREVEGKSPEEVMEYSAVFWERCN | ||||||
Domain | 958-1022 | SANT 2 | ||||
Sequence: KGKNYTEEEDRFLICMLHKMGFDRENVYEELRQCVRNAPQFRFDWFIKSRTAMEFQRRCNTLISL | ||||||
Region | 1033-1054 | Disordered | ||||
Sequence: RERAEKKKRATKTPMVKFSAFS |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P28370-1
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.
- Name1
- SynonymsSMARCA1.13
- NoteInactive as an ATPase due to the presence of exon 13, but retains its ability to correctly fold and incorporate into complexes.
- Length1,054
- Mass (Da)122,605
- Last updated2006-09-19 v2
- ChecksumD3FBFCA177F7D3C0
P28370-2
- Name2
- NoteActive as an ATPase due to the absence of exon 13.
- Differences from canonical
- 543-554: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B7ZLQ5 | B7ZLQ5_HUMAN | SMARCA1 | 1070 | ||
A0A0A0MRP6 | A0A0A0MRP6_HUMAN | SMARCA1 | 1058 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020406 | 543-554 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 827-849 | Basic and acidic residues | ||||
Sequence: AQREEQKKIDGAEPLTPEETEEK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M88163 EMBL· GenBank· DDBJ | AAA80559.1 EMBL· GenBank· DDBJ | mRNA | ||
M89907 EMBL· GenBank· DDBJ | AAA80560.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL022577 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL138745 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC117447 EMBL· GenBank· DDBJ | AAI17448.1 EMBL· GenBank· DDBJ | mRNA |