Q03532 · HAS1_YEAST
- ProteinATP-dependent RNA helicase HAS1
- GeneHAS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids505 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Miscellaneous
Transcription depends partially on SET1.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
450 μM | ATP |
pH Dependence
Optimum pH is 6.5. Active from pH 5 to 8.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 90S preribosome | |
Cellular Component | nuclear envelope | |
Cellular Component | nucleolus | |
Cellular Component | preribosome, large subunit precursor | |
Cellular Component | small-subunit processome | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent activity, acting on RNA | |
Molecular Function | identical protein binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Biological Process | maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) | |
Biological Process | maturation of SSU-rRNA | |
Biological Process | maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) | |
Biological Process | ribosomal large subunit biogenesis | |
Biological Process | ribosomal small subunit biogenesis | |
Biological Process | rRNA processing | |
Biological Process | snoRNA release from pre-rRNA |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent RNA helicase HAS1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ03532
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 92 | Lethal in vivo and impairs ATPase with 2-5% of wild-type ATPase activity, a 20-fold higher KM for ATP and prevents RNA/DNA heteroduplexes unwinding activity in vitro. Leads to 13% of wild-type ATPase activity and higher RNA/DNA heteroduplexes unwinding activity in vitro; when associated with A-389. | ||||
Sequence: K → A | ||||||
Mutagenesis | 105 | Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with S-315 and S-393. | ||||
Sequence: H → Y | ||||||
Mutagenesis | 228 | Slow growth at 18 and 16 degrees Celsius, no growth at 14 degrees Celsius and drastic decrease of the amount of 40S ribosomal subunits at 30 degrees Celsius in vivo. Leads to 70-80% of wild-type ATPase activity, a 2-fold lower KM for ATP and a slightly reduced RNA/DNA heteroduplexes unwinding activity in vitro. | ||||
Sequence: S → A | ||||||
Mutagenesis | 230 | Lethal in vivo and leads to 70-80% of wild-type ATPase activity, a 2-fold lower KM for ATP and a reduced RNA/DNA heteroduplexes unwinding activity in vitro. | ||||
Sequence: T → A | ||||||
Mutagenesis | 315 | Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with Y-105 and S-393. | ||||
Sequence: P → S | ||||||
Mutagenesis | 375 | Lethal in vivo and leads to 70-80% of wild-type ATPase activity, a 2-fold lower KM for ATP and a reduced RNA/DNA heteroduplexes unwinding activity in vitro. | ||||
Sequence: H → E | ||||||
Mutagenesis | 376 | Lethal in vivo and leads to less than 30% of wild-type ATPase activity and a 2-fold lower KM for ATP in vitro. | ||||
Sequence: R → A | ||||||
Mutagenesis | 389 | Increases 3-fold the ATPase activity and a higher RNA/DNA heteroduplexes unwinding activity in vitro. Leads to 13% of wild-type ATPase activity and lower RNA/DNA heteroduplexes unwinding activity in vitro; when associated with A-92. | ||||
Sequence: K → A | ||||||
Mutagenesis | 393 | Decreases the amount of 40S ribosomal subunits at 37 degrees Celsius; when associated with Y-105 and S-315. | ||||
Sequence: F → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000055046 | 1-505 | ATP-dependent RNA helicase HAS1 | |||
Sequence: MATPSNKRSRDSESTEEPVVDEKSTSKQNNAAPEGEQTTCVEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGIIVITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEDEMRQIIKILPNEDRQSMLFSATQTTKVEDLARISLRPGPLFINVVPETDNSTADGLEQGYVVCDSDKRFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKGKGKSLMFLTPNELGFLRYLKASKVPLNEYEFPENKIANVQSQLEKLIKSNYYLHQTAKDGYRSYLQAYASHSLKTVYQIDKLDLAKVAKSYGFPVPPKVNITIGASGKTPNTKRRKTHK | ||||||
Modified residue | 12 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by CDK1.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with RRP1. Associates in the nucleolus with the 60S and pre-60S ribosomal subunits. It has also been isolated with the nuclear pore complex.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q03532 | DBP10 Q12389 | 5 | EBI-8170, EBI-5644 | |
BINARY | Q03532 | EBP2 P36049 | 3 | EBI-8170, EBI-6289 | |
BINARY | Q03532 | ERB1 Q04660 | 6 | EBI-8170, EBI-28098 | |
BINARY | Q03532 | ESF2 P53743 | 2 | EBI-8170, EBI-28537 | |
BINARY | Q03532 | HAS1 Q03532 | 3 | EBI-8170, EBI-8170 | |
BINARY | Q03532 | HCA4 P20448 | 3 | EBI-8170, EBI-5612 | |
BINARY | Q03532 | LOC1 P43586 | 6 | EBI-8170, EBI-22906 | |
BINARY | Q03532 | MAK21 Q12176 | 4 | EBI-8170, EBI-10944 | |
BINARY | Q03532 | MAK5 P38112 | 4 | EBI-8170, EBI-10394 | |
BINARY | Q03532 | MPP10 P47083 | 3 | EBI-8170, EBI-11168 | |
BINARY | Q03532 | NOC2 P39744 | 4 | EBI-8170, EBI-29259 | |
BINARY | Q03532 | NOG1 Q02892 | 3 | EBI-8170, EBI-12105 | |
BINARY | Q03532 | NOP15 P53927 | 5 | EBI-8170, EBI-28853 | |
BINARY | Q03532 | NOP4 P37838 | 5 | EBI-8170, EBI-12122 | |
BINARY | Q03532 | NSA2 P40078 | 4 | EBI-8170, EBI-22681 | |
BINARY | Q03532 | RLP7 P40693 | 4 | EBI-8170, EBI-15415 | |
BINARY | Q03532 | RRP36 Q12481 | 2 | EBI-8170, EBI-31770 | |
BINARY | Q03532 | SAS10 Q12136 | 2 | EBI-8170, EBI-36084 | |
BINARY | Q03532 | SQS1 P53866 | 3 | EBI-8170, EBI-29168 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-37 | Disordered | ||||
Sequence: MATPSNKRSRDSESTEEPVVDEKSTSKQNNAAPEGEQ | ||||||
Compositional bias | 9-23 | Basic and acidic residues | ||||
Sequence: SRDSESTEEPVVDEK | ||||||
Motif | 42-70 | Q motif | ||||
Sequence: EKFEELKLSQPTLKAIEKMGFTTMTSVQA | ||||||
Domain | 73-249 | Helicase ATP-binding | ||||
Sequence: IPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGIIVITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEDEMRQIIKILPNEDRQSMLFSATQTTKVEDLARISLRPGPLF | ||||||
Motif | 196-199 | DEAD box | ||||
Sequence: DEAD | ||||||
Domain | 263-433 | Helicase C-terminal | ||||
Sequence: GLEQGYVVCDSDKRFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKGKGKSLMFLTPNELGFLRYLKASKVPLNEYEFPENKIANVQSQLEKLI | ||||||
Motif | 275-291 | Bipartite nuclear localization signal | ||||
Sequence: KRFLLLFSFLKRNQKKK |
Domain
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence similarities
Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length505
- Mass (Da)56,717
- Last updated1997-11-01 v1
- ChecksumEE15D51A7F6BE1A2
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-23 | Basic and acidic residues | ||||
Sequence: SRDSESTEEPVVDEK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X80836 EMBL· GenBank· DDBJ | CAA56799.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA10191.1 EMBL· GenBank· DDBJ | Genomic DNA |