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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/G3BP1_HUMAN G3BP1_HUMAN] May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.<ref>PMID:9889278</ref> <ref>PMID:11604510</ref> | [https://www.uniprot.org/uniprot/G3BP1_HUMAN G3BP1_HUMAN] May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.<ref>PMID:9889278</ref> <ref>PMID:11604510</ref> | ||
==See Also== | |||
*[[3D structures of G3BP|3D structures of G3BP]] | |||
== References == | == References == | ||
<references/> | <references/> |
Latest revision as of 15:47, 9 May 2024
Crystal Structure of the G3BP1 NTF2-like domain bound to USP10 peptideCrystal Structure of the G3BP1 NTF2-like domain bound to USP10 peptide
Structural highlights
FunctionG3BP1_HUMAN May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.[1] [2] See AlsoReferences
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