The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane (Q24672874)

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Language	Label	Description	Also known as
English	The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane	scientific article

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scholarly article

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The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane (English)

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endoplasmic reticulum

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transmembrane protein

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Signal recognition particle receptor subunit alpha YDR292C

1 reference

GOA release 2020-03-11

Signal recognition particle receptor subunit beta YKL154W

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GOA release 2020-03-11

author name string

J D Miller

1

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S Tajima

2

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L Lauffer

3

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P Walter

4

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language of work or name

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publication date

February 1995

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Journal of Cell Biology

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128

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3

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273-82

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GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120348

7 April 2017

Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle

1 reference

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7 April 2017

The signal recognition particle receptor is a complex that contains two distinct polypeptide chains

1 reference

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Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin

1 reference

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Protein translocation across the ER requires a functional GTP binding site in the alpha subunit of the signal recognition particle receptor

1 reference

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Basic local alignment search tool

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The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S

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Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein

1 reference

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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis

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The GTPase superfamily: conserved structure and molecular mechanism

1 reference

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Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression

1 reference

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Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum

1 reference

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Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum

1 reference

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The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide

1 reference

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Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle

1 reference

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Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains

1 reference

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7 April 2017

The GTPase superfamily: a conserved switch for diverse cell functions

1 reference

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Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum

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Phase separation of integral membrane proteins in Triton X-114 solution

1 reference

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Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation

1 reference

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1 reference

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Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane

1 reference

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Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane

1 reference

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Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor

1 reference

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1 reference

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Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle

1 reference

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1 reference

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1 reference

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1 reference

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Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore.

1 reference

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1 reference

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1 reference

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Computerised version of the Chou and Fasman protein secondary structure predictive method.

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Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocation

1 reference

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https://pubmed.ncbi.nlm.nih.gov/7844142

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A structural and functional analysis of the docking protein. Characterization of active domains by proteolysis and specific antibodies

1 reference

https://pubmed.ncbi.nlm.nih.gov/7844142

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based on heuristic

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1 reference

https://pubmed.ncbi.nlm.nih.gov/7844142

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1083/JCB.128.3.273

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