SRP72

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0006614 SRP-dependent cotranslational protein targeting to membrane	IBA GO_REF:0000033	ACCEPT	Summary: SRP72 is an SRP subunit and participates in the defining SRP biological process, co-translational targeting of secretory/membrane proteins to the ER membrane. Phylogenetic (IBA) inference is consistent with experimental evidence on the SRP complex. Reason: Core biological process of SRP and of SRP72 as one of its subunits; consistent with UniProt FUNCTION and structural studies. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt mediates the cotranslational targeting
GO:0008312 7S RNA binding	IBA GO_REF:0000033	ACCEPT	Summary: SRP72 binds the 7SL (7S) RNA, threading along the 5e/5f loops of the SRP RNA; this RNA-binding scaffold activity is a core molecular function. Phylogenetic inference matches experimental IMP evidence (PMID:27899666). Reason: Core molecular function; SRP72 directly contacts the 7SL RNA (RNA-binding region 545-617) and binds it in presence of SRP68. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Binds the signal recognition particle RNA (7SL RNA) in presence of PMID:27899666 flexible peptide crawling along the 5e- and 5f-loops of SRP RNA
GO:0043022 ribosome binding	IBA GO_REF:0000033	ACCEPT	Summary: SRP72 (within SRP68/72) makes multiple contacts with the ribosome, and SRP72-mediated remodeling of the 5f-loop affects ribosome binding. The contributes_to qualifier appropriately reflects that ribosome binding is a property of the assembled SRP to which SRP72 contributes. Reason: Supported by structural evidence that SRP68/72 contacts the ribosome and that SRP72 remodels the ribosome-binding 5f-loop; contributes_to qualifier is correct for a subunit-level contribution. Supporting Evidence: PMID:27899666 reveals multiple contact sites between SRP68/72 and the ribosome
GO:0005786 signal recognition particle, endoplasmic reticulum targeting	IBA GO_REF:0000033	ACCEPT	Summary: SRP72 is a constitutive subunit of the ER-targeting SRP. This is a core cellular component annotation, corroborated by direct (IDA) evidence. Reason: SRP72 is part of the SRP complex; phylogenetic assignment agrees with experimental IDA annotations. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt six protein subunits: SRP72, SRP68, SRP54,
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: SRP72 is cytoplasmic, consistent with the cytosolic SRP. Electronic transfer from the UniProt subcellular location, redundant with experimental EXP evidence (PMID:22541560). Reason: Correct compartment; SRP operates in the cytosol. The more specific cytosol/SRP terms better localize the function but cytoplasm is accurate. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0005783 endoplasmic reticulum	IEA GO_REF:0000044	ACCEPT	Summary: SRP delivers nascent chains to the ER membrane and SRP72 localizes to the ER; the BMFS1 R207H variant disrupts ER localization. Electronic transfer from UniProt subcellular location, redundant with IDA/EXP evidence. Reason: Correct compartment for SRP72 during co-translational targeting; consistent with experimental IDA (PMID:22541560) and EXP (PMID:28369529). ORGANELLES check (2026-11-06): the GO_REF:0000044 mapping rests on a curated UniProt line (Endoplasmic reticulum, ECO:0000269 from PMID:22541560 and PMID:28369529), not a prediction, so the root claim is sourced. SRP72 is a soluble SRP subunit with no signal peptide or TM segment; its ER pool is the SRP docked at the cytosolic face of the ER membrane through the SRP receptor, so the row stays at the root and no ER membrane or lumen row is added (a recruited surface pool, like TRAF3 on mitochondria). ACCEPT rather than KEEP_AS_NON_CORE because handing the ribosome-nascent chain to the ER is the particle's core activity; KEEP_AS_NON_CORE would be the call if the ER pool were read as transient docking only. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Endoplasmic reticulum {ECO:0000269\|PubMed:22541560, ECO:0000269\|PubMed:28369529}. PMID:28369529 Both wild-type SRP72 and SRP68 showed uniform coincidence with an ER marker
GO:0005829 cytosol	IEA GO_REF:0000117	ACCEPT	Summary: Cytosol is a core compartment for the SRP, where it scans translating ribosomes. ARBA machine-learning electronic annotation, consistent with TAS (Reactome) cytosol annotation. Reason: Correct and core compartment; SRP is cytosolic. Redundant with Reactome TAS. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0006614 SRP-dependent cotranslational protein targeting to membrane	IEA GO_REF:0000002	ACCEPT	Summary: InterPro-based electronic assignment of the core SRP-dependent targeting process, consistent with the IBA/experimental evidence. Reason: Correct core biological process; redundant with IBA annotation. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt mediates the cotranslational targeting
GO:0008312 7S RNA binding	IEA GO_REF:0000002	ACCEPT	Summary: InterPro-based electronic assignment of 7S RNA binding (the SRP72 RNA-binding domain, IPR013699), consistent with the experimental IMP evidence. Reason: Correct core molecular function; redundant with IMP/IBA. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Binds the signal recognition particle RNA (7SL RNA) in presence of
GO:0048500 signal recognition particle	IEA GO_REF:0000002	ACCEPT	Summary: InterPro-based electronic assignment to the SRP complex, consistent with the experimental IDA annotation (PMID:27899666). Reason: Correct core cellular component; SRP72 is a defining SRP subunit. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt six protein subunits: SRP72, SRP68, SRP54,
GO:0005515 protein binding	IPI PMID:16672232 Protein SRP68 of human signal recognition particle: identifi...	KEEP AS NON CORE	Summary: IntAct capture of the physiological SRP72-SRP68 heterodimer interaction. The bare protein binding term is uninformative; the informative version is captured by signal recognition particle binding (GO:0005047) and the SUBUNIT description. Reason: Records the real SRP68-SRP72 heterodimer interaction, but bare protein binding is uninformative per curation guidelines; the heterodimer scaffolding role is captured by more specific terms. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Heterodimer with SRP68
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	KEEP AS NON CORE	Summary: High-throughput binary interactome (HuRI) capture; the recorded partner is SULT2B1 (O00204). Bare protein binding is uninformative and the partner does not reflect SRP72's core SRP function. Reason: Real high-throughput interaction record, but bare protein binding is uninformative and not elevated to core per guidelines. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt O76094; O00204: SULT2B1
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: High-throughput affinity-purification interactome (BioPlex) capturing the SRP72-SRP68 (Q9UHB9) interaction. Bare protein binding is uninformative. Reason: Captures the SRP68 partner via high-throughput screen, but bare protein binding is uninformative; the heterodimer is better described by specific terms. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Heterodimer with SRP68
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	KEEP AS NON CORE	Summary: OpenCell endogenous-tagging interactome capturing the SRP72-SRP68 (Q9UHB9) interaction. Bare protein binding is uninformative. Reason: Real interactome capture of the SRP68 partner, but bare protein binding is uninformative; not core per guidelines. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Heterodimer with SRP68
GO:0005786 signal recognition particle, endoplasmic reticulum targeting	NAS PMID:34208095 SRPassing Co-translational Targeting: The Role of the Signal...	ACCEPT	Summary: Review-based (ComplexPortal NAS) assertion of SRP72 as a component of the ER-targeting SRP, consistent with experimental IDA evidence. Reason: Correct core cellular component; consistent with the SRP review and IDA annotations. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt six protein subunits: SRP72, SRP68, SRP54,
GO:0006617 SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition	NAS PMID:34208095 SRPassing Co-translational Targeting: The Role of the Signal...	KEEP AS NON CORE	Summary: ComplexPortal NAS annotation for the signal-sequence-recognition step of SRP-dependent targeting. SRP recognizes the signal sequence of nascent chains; SRP72 participates as a complex subunit, though signal-sequence binding itself is performed by SRP54. Reason: Accurate at the complex level (SRP recognizes signal sequences) but the actual signal-sequence recognition is mediated by SRP54, not SRP72; kept as a non-core process-level annotation for SRP72. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins
GO:0005737 cytoplasm	EXP PMID:22541560 Exome sequencing identifies autosomal-dominant SRP72 mutatio...	ACCEPT	Summary: Experimental (EXP) cytoplasmic localization from the BMFS1 disease study, which examined SRP72 localization in transfected cells. Consistent with the cytosolic SRP. Reason: Correct compartment; experimentally supported localization consistent with SRP biology. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0005783 endoplasmic reticulum	EXP PMID:28369529 Human apo-SRP72 and SRP68/72 complex structures reveal the m...	ACCEPT	Summary: Experimental ER localization from the SRP68/72 structural study, which showed cancer-associated mutations disrupt co-localization with the ER. Consistent with SRP's site of action. Reason: Correct compartment for SRP72 during co-translational targeting; experimentally supported. ORGANELLES check (2026-11-06): the full text shows GFP-SRP72 (pEGFP-C1, transfected HeLa cells) co-localising with ER-Tracker Red, a whole-organelle stain that cannot resolve the membrane face from the lumen; overexpressed tagged protein, so weaker than endogenous staining, but it agrees with SRP biology (SRP docks on the ER through its receptor). The direct-evidence row is ACCEPT at the root under rule 2; no sub-compartment is asserted because SRP72 is soluble and peripheral to the cytosolic face. Supporting Evidence: PMID:28369529 disrupt the SRP68-SRP72 interaction and their co-localization with ER in
GO:0008312 7S RNA binding	IMP PMID:27899666 Structures of human SRP72 complexes provide insights into SR...	ACCEPT	Summary: Direct experimental (IMP) evidence that SRP72 binds the 7SL RNA; the SRP72-RBD crawls along the 5e/5f loops and a conserved tryptophan forms an RNA kink-turn. This is a core molecular function. Reason: Core molecular function with direct experimental and structural support (PDB 5M73; RNA-binding mutagenesis). Supporting Evidence: PMID:27899666 flexible peptide crawling along the 5e- and 5f-loops of SRP RNA
GO:0030911 TPR domain binding	IPI PMID:27899666 Structures of human SRP72 complexes provide insights into SR...	KEEP AS NON CORE	Summary: The SRP72 protein-binding domain is a TPR that binds an extended linear motif of SRP68 with high affinity. The annotation records that SRP72's TPR mediates the SRP68 interaction; the WITH/FROM partner is SRP68 (Q9UHB9). Reason: Mechanistically accurate (SRP72 TPR-PBD binds SRP68), but this is the structural means by which the SRP68-SRP72 heterodimer forms; the heterodimer/scaffold role is better captured by signal recognition particle binding and complex membership. Supporting Evidence: PMID:27899666 The SRP72-PBD is a tetratricopeptide repeat, which binds an
GO:0043022 ribosome binding	IMP PMID:27899666 Structures of human SRP72 complexes provide insights into SR...	ACCEPT	Summary: SRP72 remodels the 5f-loop of the 7SL RNA involved in ribosome binding, and SRP68/72 makes multiple contacts with the ribosome. The contributes_to qualifier reflects SRP72's subunit-level contribution to SRP-ribosome interaction. Reason: Supported by structural/functional evidence; contributes_to is the appropriate qualifier for a subunit contributing to a complex-level binding activity. Supporting Evidence: PMID:27899666 SRP72-RBD remodels the 5f-loop involved in ribosome binding
GO:0048500 signal recognition particle	IDA PMID:27899666 Structures of human SRP72 complexes provide insights into SR...	ACCEPT	Summary: Direct experimental demonstration that SRP72 is part of the SRP S-domain (crystal structures of SRP72 bound to SRP RNA, SRP19 and SRP68). Core cellular component. Reason: Core cellular component; SRP72 is a defining SRP subunit, directly demonstrated structurally. Supporting Evidence: PMID:27899666 SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68)
GO:0005515 protein binding	IPI PMID:24965446 Host factors that interact with the pestivirus N-terminal pr...	KEEP AS NON CORE	Summary: SRP72 co-purified with the pestivirus N-terminal protease (Npro) in an interactome of ribosomal/ribonucleoprotein components. Bare protein binding is uninformative and the viral partner does not reflect SRP72's core function. Reason: Records a real (host-virus) interaction capture, but bare protein binding is uninformative and the partner is unrelated to SRP72's core SRP role. Supporting Evidence: PMID:24965446 components of the ribonucleoprotein complex
GO:0003723 RNA binding	HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi...	ACCEPT	Summary: High-throughput mRNA-interactome capture (HeLa) identifying SRP72 as an RNA-binding protein. Consistent with SRP72's bona fide RNA-binding activity, though this assay reports general mRNA crosslinking rather than the specific 7SL RNA interaction. Reason: SRP72 is a genuine RNA-binding protein; the general term is correct, with the more specific 7S RNA binding (GO:0008312) capturing the core physiological function. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Binds the signal recognition particle RNA (7SL RNA) in presence of
GO:0003723 RNA binding	HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ...	ACCEPT	Summary: Second high-throughput mRNA-bound proteome study identifying SRP72 as RNA-binding. Consistent with its RNA-binding scaffold role in SRP. Reason: Correct general molecular function; the specific 7S RNA binding term better captures the core function. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Binds the signal recognition particle RNA (7SL RNA) in presence of
GO:0005829 cytosol	TAS Reactome:R-HSA-1799332	ACCEPT	Summary: Reactome curation of SRP72 cytosolic localization within the SRP-targeting reaction. Core compartment. Reason: Correct and core compartment; SRP scans translating ribosomes in the cytosol. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0005783 endoplasmic reticulum	IDA PMID:22541560 Exome sequencing identifies autosomal-dominant SRP72 mutatio...	ACCEPT	Summary: Direct (IDA) ER localization of SRP72 from the BMFS1 study; the disease-associated R207H variant affects protein localization to the ER. Consistent with SRP's ER-targeting role. Reason: Correct compartment; experimentally supported and mechanistically relevant (variant disrupts ER localization). ORGANELLES check (2026-11-06): the cached paper is abstract-only (transfected constructs that "localize incorrectly within the cell"); the follow-up study that used the same protocol (PMID:28369529) shows wild-type GFP-SRP72 co-localising with an ER marker, and UniProt curates the ER location from this paper (ECO:0000269). Root ACCEPT on that basis and curator deference; SRP72 is a soluble, peripheral SRP subunit, so no ER membrane row. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt affects protein localization to PMID:28369529 Both wild-type SRP72 and SRP68 showed uniform coincidence with an ER marker
GO:0005047 signal recognition particle binding	IPI PMID:17254600 Protein-induced conformational changes of RNA during the ass...	ACCEPT	Summary: SRP72 (with SRP68) binds the assembling SRP and the 7SL RNA, rearranging it into an SRP54-binding-competent state. This is the informative molecular function capturing SRP72's association with the particle. Reason: Informative molecular function for SRP72's role in SRP assembly/binding; supported by the RNA conformational-change assembly study and the heterodimer/RNA interactions. Supporting Evidence: PMID:17254600 SRP68/72, together with SRP19, rearranges the 7SL RNA in an SRP54 binding
GO:0005786 signal recognition particle, endoplasmic reticulum targeting	IDA PMID:18089836 A new mechanism of 6-((2-(dimethylamino)ethyl)amino)-3-hydro...	ACCEPT	Summary: SRP72 annotated as part of the ER-targeting SRP based on a study identifying SRP as the cellular target of TAS-103. The abstract foregrounds SRP54, but the work assays the intact SRP complex of which SRP72 is a subunit; the CC localization is accurate. Reason: SRP72 is a constitutive SRP subunit; the SRP complex localization is correct. Per guidelines, an experimental annotation is not removed because the abstract emphasizes another subunit. Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt six protein subunits: SRP72, SRP68, SRP54,

Gene Description

Existing Annotations Review

Core Functions

RNA-binding scaffold subunit of the signal recognition particle that binds the 7SL (7S) RNA, threading along its 5e/5f loops to remodel the RNA and modulate ribosome contacts.

Structural subunit of the SRP that forms a heterodimer with SRP68 (via its N-terminal TPR region) and binds/assembles into the signal recognition particle, contributing to its architecture and ribosome interaction.

As an integral SRP subunit, participates in SRP-dependent co-translational targeting of secretory and membrane proteins to the endoplasmic reticulum membrane.

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