PEX11B

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005778 peroxisomal membrane	IBA GO_REF:0000033	ACCEPT	Summary: PEX11B is an integral peroxisomal membrane protein. This is one of the best-established localizations for this protein, supported by multiple independent experimental studies including immunofluorescence and fractionation (PMID:9792670, PMID:10704444, PMID:20826455). IBA annotation is consistent with the phylogenetically conserved peroxisomal membrane localization of PEX11 family members. Reason: Core localization. PEX11B is an integral peroxisomal membrane protein with two transmembrane domains, confirmed by multiple experimental approaches. The IBA annotation is well-supported phylogenetically and experimentally. Supporting Evidence: PMID:9792670 Overexpression of the human PEX11beta gene alone was sufficient to induce peroxisome proliferation PMID:20826455 PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance file:human/PEX11B/PEX11B-deep-research-falcon.md PEX11B is the best-characterized isoform in mammals and the primary driver of constitutive peroxisome proliferation
GO:0016559 peroxisome fission	IBA GO_REF:0000033	ACCEPT	Summary: PEX11B is a key driver of peroxisome fission through the growth-and-division pathway. It mediates membrane elongation/tubulation that precedes DRP1-dependent scission. This is the core biological process for PEX11B, conserved across eukaryotes. IBA annotation reflects the phylogenetically conserved role. Reason: Core biological process. PEX11B drives peroxisome elongation and coordinates fission machinery recruitment. Multiple experimental studies demonstrate this role (PMID:9792670, PMID:17408615, PMID:20826455). Supporting Evidence: PMID:9792670 PEX11beta induces peroxisome proliferation through a multistep process involving peroxisome elongation and segregation of PEX11beta from other peroxisomal membrane proteins, followed by peroxisome division PMID:17408615 Fis1 plays important roles in peroxisome division and maintenance of peroxisome morphology in mammalian cells, possibly in a concerted manner with Pex11pbeta and DLP1
GO:0005778 peroxisomal membrane	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for peroxisomal membrane localization via combined automated methods. Consistent with the well-established experimental evidence for PEX11B localization. Reason: Correct and consistent with multiple experimental studies and the IBA annotation. Redundant with stronger evidence but not incorrect.
GO:0007031 peroxisome organization	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation based on UniProt keyword mapping. Peroxisome organization is a broad parent term that encompasses peroxisome fission, which is the more specific and accurate term for PEX11B function. Reason: While peroxisome fission (GO:0016559) is more specific and preferred, peroxisome organization is not wrong as a broader term. PEX11B is indeed involved in organizing peroxisomes through the growth-and-division pathway. Acceptable as a broader IEA annotation.
GO:0016559 peroxisome fission	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation based on InterPro-to-GO mapping. The PEX11 domain (IPR008733 / PF05648) maps to peroxisome fission, which is correct for PEX11B. Reason: Correct mapping. The PEX11 domain is functionally associated with peroxisome fission, well supported by experimental evidence.
GO:0005515 protein binding	IPI PMID:10704444 PEX19 binds multiple peroxisomal membrane proteins, is predo...	MARK AS OVER ANNOTATED	Summary: PMID:10704444 (Sacksteder et al. 2000) demonstrates that PEX19 binds PEX11B using yeast two-hybrid and blot overlay assays. PEX19 functions as a chaperone/import receptor for peroxisomal membrane proteins including PEX11B. The C-terminal region of PEX11B (aa 211-259) is required for PEX19 interaction. Reason: The interaction with PEX19 is real and well-characterized, but generic protein binding is uninformative. The biologically relevant annotation is PEX11B localization to the peroxisomal membrane via PEX19-dependent import, which is already captured by CC annotations. No specific GO MF term exists for PEX19-cargo binding that would be more informative. Supporting Evidence: PMID:10704444 PEX19 binds a broad spectrum of PMPs, displays saturable PMP binding, and interacts with regions of PMPs required for their targeting to peroxisomes
GO:0005515 protein binding	IPI PMID:12096124 Analysis of mammalian peroxin interactions using a non-trans...	MARK AS OVER ANNOTATED	Summary: PMID:12096124 (Fransen et al. 2002) used a bacterial two-hybrid system to analyze mammalian peroxin interactions. The study demonstrated PEX11B interactions with PEX19, showing that the CAAX motif of PEX19 enhances its affinity for PEX11B. Reason: This is a targeted two-hybrid study of peroxin interactions. The interaction with PEX19 is real and already captured by other annotations. Generic protein binding does not add useful information. The specific interaction partners (PEX19) are what matter. Supporting Evidence: PMID:12096124 the CAAXmotif, and not farnesylation, of Pex19p strongly enhances its affinity for Pex11pbeta
GO:0005515 protein binding	IPI PMID:14709540 PEX19 is a predominantly cytosolic chaperone and import rece...	MARK AS OVER ANNOTATED	Summary: PMID:14709540 (Jones et al. 2004) demonstrates that PEX19 is a chaperone and import receptor for class 1 PMPs, including PEX11B. PEX11B is classified as a class 1 PMP that requires PEX19 for targeting to peroxisomes. The study used deletion mutants to map PEX19 binding regions. Reason: Again captures the PEX19-PEX11B interaction. Protein binding is uninformative. The biologically relevant annotation is peroxisomal membrane localization via PEX19-dependent import, which is already captured. Supporting Evidence: PMID:14709540 PEX19 binds and stabilizes newly synthesized PMPs in the cytosol, binds to multiple PMP targeting signals (mPTSs), interacts with the hydrophobic domains of PMP targeting signals, and is essential for PMP targeting and import
GO:0005515 protein binding	IPI PMID:20531392 The peroxisomal receptor Pex19p forms a helical mPTS recogni...	MARK AS OVER ANNOTATED	Summary: PMID:20531392 (Schueller et al. 2010) determined the crystal structure of the Pex19p C-terminal domain and characterized its mPTS recognition. PEX11B is used as one of the cargo proteins to demonstrate mPTS binding by Pex19p. Reason: This again reflects the PEX19-PEX11B cargo-receptor interaction. The study is about PEX19 structure rather than PEX11B function per se. Generic protein binding is uninformative. Supporting Evidence: PMID:20531392 The crystal structure of the folded C-terminal part of the receptor reveals a globular domain that displays a bundle of three long helices in an antiparallel arrangement
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MARK AS OVER ANNOTATED	Summary: PMID:25416956 (Rolland et al. 2014) is a large-scale proteome-wide interactome mapping study. PEX11B interactions detected are from high-throughput yeast two-hybrid screens. No specific PEX11B interaction partners are highlighted in the abstract. Reason: High-throughput interactome study. Protein binding from large-scale screens provides no specific functional insight for PEX11B. The biologically relevant interactions (PEX19, FIS1, PEX11G, self-interaction) are captured by more targeted studies. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network.
GO:0005515 protein binding	IPI PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid tec...	MARK AS OVER ANNOTATED	Summary: PMID:29997244 (Trepte et al. 2018) describes the LuTHy technology for quantitative protein-protein interaction mapping. PEX11B is among proteins tested in this bioluminescence-based two-hybrid system as part of method validation. Reason: Technology paper using PEX11B as one of many test cases. Generic protein binding from a methods paper provides no specific functional annotation value. Supporting Evidence: PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.
GO:0005515 protein binding	IPI PMID:31467278 Maximizing binary interactome mapping with a minimal number ...	MARK AS OVER ANNOTATED	Summary: PMID:31467278 (Choi et al. 2019) is a large-scale binary interactome mapping study focused on maximizing coverage with minimal assays. PEX11B interactions are detected as part of a high-throughput effort. Reason: High-throughput interactome study. Generic protein binding from systematic screens is uninformative for PEX11B functional annotation. Supporting Evidence: PMID:31467278 Maximizing binary interactome mapping with a minimal number of assays.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: PMID:32814053 (Haenig et al. 2020) is an interactome mapping study focused on neurodegenerative disease proteins. PEX11B is included as a hit in interaction screens with disease-associated proteins. Reason: High-throughput interactome study focused on neurodegeneration. PEX11B is not a primary focus. Generic protein binding is uninformative. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
GO:0005515 protein binding	IPI PMID:37398436 AI-guided pipeline for protein-protein interaction drug disc...	MARK AS OVER ANNOTATED	Summary: PMID:37398436 (Trepte et al. 2023) is an AI-guided pipeline for PPI drug discovery targeting SARS-CoV-2. PEX11B appears as part of the reference interaction set used to validate the approach. Reason: PEX11B is used as part of a reference set for a drug discovery method paper. No specific functional insight for PEX11B. Generic protein binding is uninformative. Supporting Evidence: PMID:37398436 AI-guided pipeline for protein-protein interaction drug discovery identifies a SARS-CoV-2 inhibitor.
GO:0005739 mitochondrion	IEA GO_REF:0000107	REMOVE	Summary: This IEA annotation from Ensembl Compara suggests mitochondrial localization. While peroxisomal and mitochondrial fission machineries share components (DRP1, FIS1), and Lismont et al. (2019) showed PEX11B deficiency can cause partial mislocalization of peroxisomal proteins to mitochondria, PEX11B itself is not established as a mitochondrial protein. UniProt mass spectrometry detection from the mitochondrial proteome (PMID:25944712) may reflect contamination or the physical proximity of peroxisomes and mitochondria. Reason: PEX11B is established as a peroxisomal membrane protein. No experimental evidence supports bona fide mitochondrial localization. The Ensembl Compara transfer is likely erroneous, possibly driven by the shared fission machinery between peroxisomes and mitochondria, or contamination in proteomics studies. Supporting Evidence: PMID:20826455 PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance
GO:0042802 identical protein binding	IPI PMID:17408615 Fis1, DLP1, and Pex11p coordinately regulate peroxisome morp...	ACCEPT	Summary: PMID:17408615 (Kobayashi et al. 2007) demonstrated that Pex11pbeta interacts with itself (homo-oligomerization). The highly conserved N-terminal domain was required for this self-interaction and was indispensable for peroxisome-proliferating activity. This is functionally important as oligomerization is required for membrane remodeling. Reason: PEX11B homo-oligomerization is well-established and functionally important for membrane elongation/tubulation. This is more informative than generic protein binding and represents a core molecular function aspect. Supporting Evidence: PMID:17408615 Pex11pbeta also interacted with each other, whereas the binding of Pex11pbeta to DLP1 was not detectable PMID:17408615 the highly conserved N-terminal domain of Pex11pbeta was required for the homo-oligomerization of Pex11pbeta and indispensable for the peroxisome-proliferating activity
GO:0005778 peroxisomal membrane	TAS Reactome:R-HSA-9603775	ACCEPT	Summary: Reactome annotation from R-HSA-9603775 (PEX3:PEX19:class I PMP dissociates). This represents the Reactome model of PEX11B (as a class I PMP) being delivered to the peroxisomal membrane by the PEX19-PEX3 import pathway. PEX11B is released at the peroxisomal membrane. Reason: Correct localization. PEX11B is delivered to and resides in the peroxisomal membrane. Reactome pathway accurately models PEX11B as a class I PMP imported via PEX19/PEX3.
GO:0005829 cytosol	TAS Reactome:R-HSA-9603775	KEEP AS NON CORE	Summary: Reactome annotation from R-HSA-9603775 (PEX3:PEX19:class I PMP dissociates). This reflects the transient cytosolic state of PEX11B as a newly synthesized PMP before it is chaperoned by PEX19 to the peroxisomal membrane. Reason: PEX11B transiently passes through the cytosol as a newly synthesized protein before being imported to peroxisomes. This is not its functional localization but rather a transit compartment. Acceptable as non-core since it reflects the PMP import pathway.
GO:0005829 cytosol	TAS Reactome:R-HSA-9603784	KEEP AS NON CORE	Summary: Reactome annotation from R-HSA-9603784 (PEX19:class I PMP binds PEX3). This again reflects the cytosolic complex formation between PEX19-PEX11B before docking at PEX3 on the peroxisomal membrane. Reason: Redundant with annotation 18. Reflects the same transient cytosolic state during PMP import pathway. Not the functional localization of PEX11B.
GO:0005829 cytosol	TAS Reactome:R-HSA-9603804	KEEP AS NON CORE	Summary: Reactome annotation from R-HSA-9603804 (PEX19 binds class I peroxisomal membrane proteins). This reflects initial PEX19 recognition of PEX11B in the cytosol. Reason: Same as annotations 18 and 19. Transient cytosolic localization during PMP import. Not the functional localization.
GO:0016020 membrane	HDA PMID:19946888 Defining the membrane proteome of NK cells.	ACCEPT	Summary: PMID:19946888 (Ghosh et al. 2010) is a proteomics study of NK cell membranes. PEX11B was detected in membrane fractions by mass spectrometry. This is a very generic localization term; PEX11B is specifically a peroxisomal membrane protein. Reason: Not incorrect - PEX11B is indeed a membrane protein - but overly generic. The more specific term (peroxisomal membrane) is already well-annotated. This HDA annotation from a proteomics study simply confirms membrane association without adding specificity. Acceptable as a broader supporting annotation from high-throughput data. Supporting Evidence: PMID:19946888 Mass spectrometric analysis identified 1843 proteins with high confidence scores.
GO:0005515 protein binding	IPI PMID:18782765 Targeting of hFis1 to peroxisomes is mediated by Pex19p.	MARK AS OVER ANNOTATED	Summary: PMID:18782765 (Delille and Schrader 2008) demonstrates that hFis1 targeting to peroxisomes is mediated by Pex19p. PEX11B is mentioned in the context of the peroxisomal targeting pathway and PEX19 interactions, but the paper primarily focuses on hFis1-Pex19p interaction rather than PEX11B specifically. Reason: This paper is primarily about FIS1 targeting, not PEX11B function. PEX11B is mentioned in context of PEX19 interactions but is not the focus. Generic protein binding annotation is uninformative. Supporting Evidence: PMID:18782765 peroxisomal targeting of hFis1 depends on Pex19p, a peroxisomal membrane protein import factor
GO:0032991 protein-containing complex	IDA PMID:17408615 Fis1, DLP1, and Pex11p coordinately regulate peroxisome morp...	ACCEPT	Summary: PMID:17408615 (Kobayashi et al. 2007) detected ternary complexes of Fis1, Pex11pbeta, and DLP1 by chemical cross-linking. PEX11B forms homo-oligomers and is part of multi-protein complexes involved in peroxisome fission. Reason: PEX11B is indeed part of protein complexes - it homo-oligomerizes and forms ternary complexes with FIS1 and DLP1. The annotation is supported by cross-linking experiments. Supporting Evidence: PMID:17408615 ternary complexes comprising Fis1, Pex11pbeta, and DLP1 were detected by chemical cross-linking
GO:0005515 protein binding	IPI PMID:17408615 Fis1, DLP1, and Pex11p coordinately regulate peroxisome morp...	MARK AS OVER ANNOTATED	Summary: PMID:17408615 (Kobayashi et al. 2007) demonstrated direct binding of PEX11B to FIS1, involving the C-terminal region of PEX11B. This is a functionally important interaction for coordinating peroxisome fission. The paper also showed PEX11B self-interaction. Reason: The interaction with FIS1 is biologically important and well-characterized, but generic protein binding is uninformative. The self-interaction is already captured by identical protein binding (GO:0042802) and protein homodimerization activity (GO:0042803). The FIS1 interaction is captured in the process annotation for peroxisome fission. Supporting Evidence: PMID:17408615 Fis1 interacted with Pex11pbeta, by direct binding apparently involving the C-terminal region of Pex11pbeta in the interaction
GO:0016559 peroxisome fission	IDA PMID:17408615 Fis1, DLP1, and Pex11p coordinately regulate peroxisome morp...	ACCEPT	Summary: PMID:17408615 (Kobayashi et al. 2007) provides direct experimental evidence for PEX11B's role in peroxisome fission. Overexpression induces peroxisome proliferation. The N-terminal domain is required for homo-oligomerization and peroxisome-proliferating activity. PEX11B coordinates with Fis1 and DLP1 in peroxisome morphogenesis. Reason: Core function. Strong experimental evidence from a targeted study demonstrating PEX11B's role in coordinating peroxisome fission with FIS1 and DLP1. Supporting Evidence: PMID:17408615 Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis PMID:17408615 the highly conserved N-terminal domain of Pex11pbeta was required for the homo-oligomerization of Pex11pbeta and indispensable for the peroxisome-proliferating activity
GO:0005515 protein binding	IPI PMID:20826455 PEX11 family members are membrane elongation factors that co...	MARK AS OVER ANNOTATED	Summary: PMID:20826455 (Koch et al. 2010) established homo- and heterodimerization properties of PEX11 proteins and their interaction with hFis1. PEX11B interacts with PEX11G (heterodimerization) and FIS1. Reason: The specific interactions (self, PEX11G, FIS1) are functionally important but already captured by more specific annotations (identical protein binding, protein homodimerization activity, protein-containing complex). Generic protein binding is uninformative. Supporting Evidence: PMID:20826455 We established the homo- and heterodimerization properties of the human PEX11 proteins and their interaction with the fission factor hFis1
GO:0005777 peroxisome	IDA PMID:20826455 PEX11 family members are membrane elongation factors that co...	ACCEPT	Summary: PMID:20826455 (Koch et al. 2010) confirms peroxisomal localization of PEX11B through microscopy and functional studies. PEX11B expression leads to juxtaposed elongated peroxisomes (JEPs). Reason: Correct localization. The more specific term peroxisomal membrane (GO:0005778) is also annotated, but peroxisome (GO:0005777) is acceptable as a broader compartment annotation. Supporting Evidence: PMID:20826455 Ectopic expression of proteins of the PEX11 family from yeast, plant or human lead to the formation of juxtaposed elongated peroxisomes (JEPs)
GO:0016559 peroxisome fission	IDA PMID:20826455 PEX11 family members are membrane elongation factors that co...	ACCEPT	Summary: PMID:20826455 (Koch et al. 2010) demonstrates PEX11B's role in peroxisome membrane elongation and fission. Excess hFis1 is sufficient to fragment PEX11-induced JEPs, demonstrating that PEX11B drives the elongation step while FIS1/DRP1 drive scission. Reason: Core function. Strong experimental evidence showing PEX11B as a membrane elongation factor that initiates the fission pathway. Complements PMID:17408615 and PMID:9792670. Supporting Evidence: PMID:20826455 PEX11-induced JEPs represent intermediates in the process of peroxisome membrane proliferation and that hFis1 is the limiting factor for progression
GO:0032991 protein-containing complex	IDA PMID:20826455 PEX11 family members are membrane elongation factors that co...	ACCEPT	Summary: PMID:20826455 (Koch et al. 2010) demonstrates PEX11B forms homo- and heterodimers (with PEX11G) and interacts with FIS1. This multiprotein complex assembly is critical for coordinating peroxisome fission. Reason: PEX11B forms functional complexes as demonstrated by dimerization and interaction studies. Consistent with PMID:17408615 cross-linking data showing ternary complexes. Supporting Evidence: PMID:20826455 We established the homo- and heterodimerization properties of the human PEX11 proteins and their interaction with the fission factor hFis1
GO:0042803 protein homodimerization activity	IDA PMID:20826455 PEX11 family members are membrane elongation factors that co...	ACCEPT	Summary: PMID:20826455 (Koch et al. 2010) demonstrated PEX11B homodimerization. This is functionally important as oligomerization is required for membrane remodeling activity. The paper showed this using FRET-based approaches and co-immunoprecipitation. Reason: Core molecular function. PEX11B homodimerization/oligomerization is essential for its membrane elongation activity. Well-supported by both Koch et al. 2010 and Kobayashi et al. 2007, and Bonekamp et al. 2013 (self-interaction study). Supporting Evidence: PMID:20826455 We established the homo- and heterodimerization properties of the human PEX11 proteins PMID:17408615 the highly conserved N-terminal domain of Pex11pbeta was required for the homo-oligomerization of Pex11pbeta and indispensable for the peroxisome-proliferating activity
GO:0044375 regulation of peroxisome size	IDA PMID:20826455 PEX11 family members are membrane elongation factors that co...	ACCEPT	Summary: PMID:20826455 (Koch et al. 2010) demonstrated that PEX11B expression affects peroxisome size and morphology, specifically causing membrane elongation and formation of juxtaposed elongated peroxisomes (JEPs). Overexpression increased peroxisome number to ~405 per cell vs ~187 in controls. Reason: PEX11B directly regulates peroxisome size through its membrane elongation activity. This is a core function. The regulation of peroxisome size is a consequence of PEX11B's membrane remodeling activity. Supporting Evidence: PMID:20826455 we propose a model for a conserved role of PEX11 proteins in peroxisome maintenance through peroxisome polarization, membrane elongation and segregation
GO:0005778 peroxisomal membrane	IDA PMID:14709540 PEX19 is a predominantly cytosolic chaperone and import rece...	ACCEPT	Summary: PMID:14709540 (Jones et al. 2004) classifies PEX11B as a class 1 PMP that is imported to the peroxisomal membrane via PEX19. The study demonstrates PEX19-dependent targeting of PEX11B to the peroxisomal membrane. Reason: Core localization confirmed by direct experimental observation. PEX11B is a class 1 peroxisomal membrane protein. Supporting Evidence: PMID:14709540 PEX19 functions as both a chaperone and an import receptor for newly synthesized PMPs
GO:0005778 peroxisomal membrane	IDA PMID:9792670 Expression of PEX11beta mediates peroxisome proliferation in...	ACCEPT	Summary: PMID:9792670 (Schrader et al. 1998) is the foundational paper characterizing PEX11B. It identifies PEX11B as a peroxisomal membrane protein and demonstrates that its overexpression induces peroxisome proliferation through membrane elongation and division. Reason: Foundational experimental evidence for PEX11B peroxisomal membrane localization. Supporting Evidence: PMID:9792670 identification and characterization of two novel human peroxisomal membrane proteins, PEX11alpha and PEX11beta
GO:0007031 peroxisome organization	IDA PMID:9792670 Expression of PEX11beta mediates peroxisome proliferation in...	ACCEPT	Summary: PMID:9792670 (Schrader et al. 1998) demonstrates PEX11B's role in peroxisome organization - specifically that overexpression induces peroxisome proliferation through elongation and division. PEX11B is implicated in constitutive control of peroxisome abundance. Reason: Peroxisome organization is a parent term of peroxisome fission and accurately describes PEX11B's broader role. Supported by the foundational paper on PEX11B function. Supporting Evidence: PMID:9792670 PEX11beta induces peroxisome proliferation through a multistep process involving peroxisome elongation and segregation of PEX11beta from other peroxisomal membrane proteins, followed by peroxisome division PMID:9792670 these data implicate PEX11beta in the constitutive control of peroxisome abundance
GO:0016559 peroxisome fission	IDA PMID:9792670 Expression of PEX11beta mediates peroxisome proliferation in...	ACCEPT	Summary: PMID:9792670 (Schrader et al. 1998) provides the original evidence that PEX11B mediates peroxisome proliferation through elongation followed by division. Time course studies demonstrated the multistep nature of this process. Reason: Foundational experimental evidence for PEX11B's role in peroxisome fission. Core function. Supporting Evidence: PMID:9792670 PEX11beta induces peroxisome proliferation through a multistep process involving peroxisome elongation and segregation of PEX11beta from other peroxisomal membrane proteins, followed by peroxisome division
GO:0005778 peroxisomal membrane	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation transferred from ortholog by curator judgment. Consistent with extensive experimental evidence for PEX11B peroxisomal membrane localization. Reason: Correct. Peroxisomal membrane localization is the best-established feature of PEX11B, conserved across species.
GO:0007031 peroxisome organization	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation transferred from ortholog. Consistent with the well-established role of PEX11B in peroxisome organization across eukaryotes. Reason: Correct. PEX11B's role in peroxisome organization is conserved and well-supported.
GO:0007165 signal transduction	ISS GO_REF:0000024	REMOVE	Summary: ISS annotation for signal transduction transferred from ortholog. PEX11B is a membrane remodeling protein involved in peroxisome fission, not a classical signal transduction component. While there are recent reports linking PEX11B to PPARgamma and SIRT1 pathways (Esmaeili et al. 2024), PEX11B itself is not a signal transduction molecule. It is a downstream effector of peroxisome proliferation signals, not a signal transducer. Reason: PEX11B is a structural/membrane-remodeling protein, not a signal transduction component. While peroxisome proliferation can be regulated by signaling pathways (PPARs, etc.), PEX11B functions as an effector of peroxisome division, not as a signal transducer itself. This annotation likely results from overly broad inference. PEX11B's constitutive expression pattern further argues against a primary signaling role (PMID:9792670). Supporting Evidence: PMID:9792670 Levels of PEX11beta mRNA were similar in all tissues examined and were unaffected by peroxisome-proliferating agents
GO:0005777 peroxisome	IDA PMID:9922452 Peroxisome synthesis in the absence of preexisting peroxisom...	ACCEPT	Summary: PMID:9922452 (South and Gould 1999) describes peroxisome synthesis in the absence of preexisting peroxisomes. PEX11B is mentioned in the context of the PEX11-mediated division pathway. PEX11Bmyc is used as a peroxisomal membrane marker to assess peroxisome formation in PEX16-deficient cells. Reason: PEX11B's peroxisomal localization is used as a functional readout in this study. The broader peroxisome term is correct, though peroxisomal membrane is more specific. Supporting Evidence: PMID:9922452 peroxisomes may form by either of two pathways: one that involves PEX11-mediated division of preexisting peroxisomes, and another that involves PEX16-mediated formation of peroxisomes in the absence of preexisting peroxisomes
GO:0005777 peroxisome	IDA PMID:10704444 PEX19 binds multiple peroxisomal membrane proteins, is predo...	ACCEPT	Summary: PMID:10704444 (Sacksteder et al. 2000) demonstrates PEX11B is targeted to peroxisomes via PEX19. PEX11B deletion mutants were used to map the PEX19 binding/targeting region. Immunofluorescence confirms peroxisomal localization. Reason: Correct localization. PEX11B is targeted to peroxisomes in a PEX19-dependent manner. Supporting Evidence: PMID:10704444 PEX19 binds a broad spectrum of PMPs, displays saturable PMP binding, and interacts with regions of PMPs required for their targeting to peroxisomes

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

Falcon

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