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). Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt Endoplasmic reticulum
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. 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). Supporting Evidence: file:human/SRP72/SRP72-uniprot.txt affects protein localization to
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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