Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0002183 | biological_process | cytoplasmic translational initiation |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003723 | molecular_function | RNA binding |
A | 0003724 | molecular_function | RNA helicase activity |
A | 0003725 | molecular_function | double-stranded RNA binding |
A | 0003743 | molecular_function | translation initiation factor activity |
A | 0004386 | molecular_function | helicase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006412 | biological_process | translation |
A | 0006413 | biological_process | translational initiation |
A | 0010494 | cellular_component | cytoplasmic stress granule |
A | 0016020 | cellular_component | membrane |
A | 0016281 | cellular_component | eukaryotic translation initiation factor 4F complex |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0097165 | cellular_component | nuclear stress granule |
Functional Information from PROSITE/UniProt
site_id | PS00039 |
Number of Residues | 9 |
Details | DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL |
Chain | Residue | Details |
A | VAL180-LEU188 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 171 |
Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 161 |
Details | Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | Motif: {"description":"Q motif"} |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Motif: {"description":"DEAD box"} |
site_id | SWS_FT_FI5 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI10 |
Number of Residues | 6 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P60842","evidenceCode":"ECO:0000250"}]} |