SRPRB

UniProt ID: Q9Y5M8
Organism: Homo sapiens
Review Status: COMPLETE
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Gene Description

SRPRB (signal recognition particle receptor subunit beta, SR-beta; also APMCF1) is a 271 aa single-pass ER membrane protein and a small Ras-superfamily GTPase closely related to Arf and Sar1. It is the membrane-anchored beta subunit of the heterodimeric signal recognition particle (SRP) receptor (SR), assembling with the soluble alpha subunit SRPRA via a Longin-domain interface and tethering SRPRA to the ER membrane. The SRP receptor docks the SRP-ribosome-nascent chain complex at the ER so that signal-sequence-bearing nascent secretory and membrane proteins are delivered to the Sec61 translocon for cotranslational translocation and insertion. SRP-dependent targeting is driven by a GTPase cycle in which the SR (SRPRA and SRPRB) and the SRP54 GTPase reciprocally activate one another; GTP binding and hydrolysis by SRPRB regulate ribosome-nascent chain handover and receptor recycling. SRPRB is broadly expressed and localizes to the ER membrane.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005785 signal recognition particle receptor complex
IBA
GO_REF:0000033
ACCEPT
Summary: SRPRB is the beta subunit of the heterodimeric SRP receptor; phylogenetic assignment of SR-complex membership is consistent with direct structural and biochemical evidence. Core structural identity.
Reason: SRP receptor complex membership is the core cellular-component identity of SRPRB; SRPRB heterodimerizes with SRPRA.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
Component of the signal recognition particle (SRP) complex receptor (SR)
GO:0045047 protein targeting to ER
IBA
GO_REF:0000033
ACCEPT
Summary: As part of the SRP receptor, SRPRB participates in targeting nascent secretory/membrane proteins to the ER. Core biological process.
Reason: Core SR-mediated process; the SRP receptor ensures correct targeting of nascent proteins to the ER membrane.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
the correct targeting of the nascent secretory proteins to the
GO:0005525 GTP binding
IEA
GO_REF:0000002
ACCEPT
Summary: SRPRB is a small GTPase of the Ras superfamily (Arf/Sar1-related) with conserved GTP-binding motifs; GTP binding and hydrolysis drive the SRP-targeting cycle. Core molecular function.
Reason: Core molecular function; SRPRB binds GTP (structure solved in the Mg2+-GTP-bound state) and its GTPase activity regulates targeting.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
GTP-binding
GO:0005789 endoplasmic reticulum membrane
IEA
GO_REF:0000044
ACCEPT
Summary: Electronic transfer of the ER membrane subcellular location from UniProt; the correct and core compartment for the membrane-anchored SR-beta subunit.
Reason: Correct core location; SRPRB is a single-pass ER membrane protein.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0005515 protein binding
IPI
PMID:16169070
A human protein-protein interaction network: a resource for ...
KEEP AS NON CORE
Summary: High-throughput protein-protein interaction capture. SRPRB's functionally informative interaction is with SRPRA (the SR heterodimer), but bare protein binding is uninformative.
Reason: Real but the bare protein binding term is uninformative per curation guidelines; the SR-complex term captures the informative content.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
Heterodimer with SRPRA
GO:0005515 protein binding
IPI
PMID:33961781
Dual proteome-scale networks reveal cell-specific remodeling...
KEEP AS NON CORE
Summary: BioPlex affinity-MS interactome capture. Bare protein binding is uninformative.
Reason: High-throughput interaction; bare protein binding is uninformative and not core.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
Heterodimer with SRPRA
GO:0005515 protein binding
IPI
PMID:40205054
Multimodal cell maps as a foundation for structural and func...
KEEP AS NON CORE
Summary: Multimodal cell-map interactome capture. Bare protein binding is uninformative.
Reason: High-throughput interaction; bare protein binding is uninformative and not core.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
Heterodimer with SRPRA
GO:0005785 signal recognition particle receptor complex
EXP
PMID:16439358
The structure of the mammalian signal recognition particle (...
ACCEPT
Summary: Crystal structure of mammalian SR-beta in complex with the SRalpha (SRPRA) binding domain (SRX); direct experimental evidence that SRPRB is part of the heterodimeric SRP receptor. Core structural identity.
Reason: Experimentally demonstrated core SR membership; SRPRB-SRPRA heterodimer structure.
Supporting Evidence:
PMID:16439358
The SR is a heterodimeric complex assembled by the two GTPases SRalpha and SRbeta
GO:0006617 SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition
NAS
PMID:16439358
The structure of the mammalian signal recognition particle (...
ACCEPT
Summary: SRPRB, as part of the SR, participates in SRP-dependent cotranslational targeting of nascent chains to the ER membrane. Core biological process.
Reason: Core SR-mediated process; the SRP receptor mediates SRP-dependent cotranslational targeting at the ER.
Supporting Evidence:
PMID:16439358
co-translational targeting of secretory and membrane proteins to the endoplasmic reticulum
GO:0016020 membrane
NAS
PMID:16439358
The structure of the mammalian signal recognition particle (...
KEEP AS NON CORE
Summary: The SR is membrane-anchored via SRPRB; a generic membrane localization that is a parent of the specific ER membrane term.
Reason: Correct but generic; the ER membrane term captures the informative localization.
Supporting Evidence:
PMID:16439358
which is membrane-anchored
GO:0005789 endoplasmic reticulum membrane
ISS
GO_REF:0000024
ACCEPT
Summary: Curator ISS transfer of ER membrane localization from an ortholog; the correct and core compartment for SRPRB.
Reason: Correct core location; redundant with other ER membrane evidence.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0016020 membrane
IDA
PMID:22375059
Different effects of Sec61Ξ±, Sec62 and Sec63 depletion on tr...
KEEP AS NON CORE
Summary: Direct evidence of membrane localization from a study of Sec61/Sec62/Sec63-dependent ER translocation; a generic membrane term, parent of ER membrane.
Reason: Correct but generic; the ER membrane term captures the informative localization.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0005789 endoplasmic reticulum membrane
TAS
Reactome:R-HSA-1791060
ACCEPT
Summary: Reactome TAS annotation of ER membrane localization for SRPRB, consistent with the core compartment.
Reason: Correct core location; consistent with experimental and ISS evidence.
Supporting Evidence:
file:human/SRPRB/SRPRB-uniprot.txt
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0005881 cytoplasmic microtubule
IDA
PMID:23264731
MTR120/KIAA1383, a novel microtubule-associated protein, pro...
REMOVE
Summary: Wrong-gene citation. PMID:23264731 characterizes MTR120/KIAA1383 as a microtubule-associated protein; the now-cached full text never mentions or assays SRPRB (no occurrence of SRPRB / SR-beta / SRP receptor). SRPRB is an ER-membrane GTPase, for which a cytoplasmic microtubule localization is biologically implausible.
Reason: The full text of PMID:23264731 is now available and confirms the paper is entirely about MTR120/KIAA1383 and does not assay SRPRB, so this GO:0005881 IDA is a wrong-gene mis-attribution. This matches the sibling SERP1 review, where the same PMID:23264731 cytoplasmic-microtubule annotation was REMOVED after full-text confirmation; previously this row was held UNDECIDED only because the full text was unavailable.
Supporting Evidence:
PMID:23264731
a novel microtubule-associated protein, promotes microtubule stability and ensures cytokinesis
GO:0005737 cytoplasm
IDA
PMID:19664239
Subcellular localization of APMCF1 and its biological signif...
KEEP AS NON CORE
Summary: GFP-APMCF1 (SRPRB) overexpression showed a generally cytoplasmic distribution in COS-7 cells. A diffuse cytoplasmic signal is consistent with an ER-membrane protein (the ER is in the cytoplasm), but cytoplasm is imprecise relative to the ER membrane and the signal derives from overexpression of a GFP fusion.
Reason: Plausible but imprecise (and overexpression-based); the informative core localization is the ER membrane.
Supporting Evidence:
PMID:19664239
EGFP-APMCF1 was generally localized in the cytoplasm of COS-7 cell

Core Functions

Membrane-anchored beta subunit of the heterodimeric signal recognition particle (SRP) receptor; a Ras-superfamily GTPase that, together with SRPRA, docks the SRP-ribosome-nascent chain complex at the ER membrane to enable SRP-dependent cotranslational protein targeting.

Supporting Evidence:
  • file:human/SRPRB/SRPRB-uniprot.txt
    Component of the signal recognition particle (SRP) complex receptor (SR)
  • PMID:16439358
    The SR is a heterodimeric complex assembled by the two GTPases SRalpha and SRbeta
  • PMID:29567807
  • PMID:37643813

References

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Suggested Questions for Experts

Q: Is the reported cytoplasmic-microtubule localization of SRPRB a genuine secondary localization or a mis-attribution from the MTR120 study, and does SRPRB have any verified function outside the SRP receptor?

Q: How do the GTPase cycles of SRPRB, SRPRA, and SRP54 coordinate ribosome-nascent chain handover to the Sec61 translocon, and what is the specific catalytic contribution of SRPRB GTP hydrolysis?

Suggested Experiments

Experiment: Use endogenous tagging plus proximity labeling and super-resolution microscopy to test whether SRPRB localizes to microtubules under any condition, distinguishing genuine localization from overexpression or co-purification artifacts.

Experiment: Reconstitute SRP-dependent targeting with wild-type and GTPase-dead SRPRB to quantify the role of SRPRB GTP hydrolysis in receptor recycling and nascent-chain delivery to Sec61.

Deep Research

Falcon

(SRPRB-deep-research-falcon.md)

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πŸ“š Additional Documentation

Notes

(SRPRB-notes.md)

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Pn Notes

(SRPRB-pn-notes.md)

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