EPCAM encodes EpCAM/CD326, a single-pass epithelial cell-surface glycoprotein concentrated at lateral and basolateral membranes. It associates with claudin-7 and regulates the stability and distribution of claudin-containing membrane pools. In human intestinal epithelial cell models, it retains selected claudins outside tight junctions and affects their availability for junctional barrier function. Its effects on cadherin-mediated adhesion, proliferation and differentiation depend on cellular context; direct homophilic adhesion across opposing cells remains disputed. Proteolytic processing can release an extracellular fragment and a short intracellular product, EpICD, associated with nuclear regulatory complexes and gene-expression responses. Biallelic EPCAM defects cause congenital tufting enteropathy. Some 3-prime EPCAM deletions cause Lynch syndrome through transcriptional read-through and epigenetic silencing of neighboring MSH2, a genomic mechanism distinct from the molecular activities of EpCAM protein.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001657 ureteric bud development | IEA GO_REF:0000107 | UNDECIDED | Summary: The mouse ortholog source associates Epcam expression with the developing ureteric epithelium, but the specific developmental function remains unresolved. Reason: The actual Q99JW5 annotation is TAS from PMID:16545622; its verified abstract reports spatial gene-expression profiling in the E11.5 mouse metanephros. The complete original experiments were not recovered. PMID:18025791 establishes developmental localization, not by itself a step performed by EPCAM in ureteric bud development. Retain uncertainty about the asserted process without treating orthology or an expression-focused title as evidence of a curator error. |
| GO:0005515 protein binding | IPI PMID:16054130 The cell-cell adhesion molecule EpCAM interacts directly wit... | MODIFY | Summary: EPCAM binds the cell-junction adhesion protein claudin-7 and stabilizes a claudin-associated membrane pool. Reason: The 2005 cited paper remains abstract-only, but the same human EPCAM–CLDN7 association is independently demonstrated by endogenous co-immunoprecipitation in PMID:23486470, Figures 5–6. Figure 10 links physical association to claudin stabilization using human transmembrane-mutant and rescue experiments. Residual stabilization by the binding-impaired mutant leaves room for additional mechanisms. Replace generic binding with cell adhesion molecule binding; this does not assert that EPCAM forms a trans adhesion bond, that CLDN1 association is necessarily binary, or that the claudin-associated pool promotes cell adhesion. Proposed replacements: cell adhesion molecule binding |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: A human cDNA-fragment Y2H screen detects an EPCAM–CDH1 interaction; the native cadherin-binding role remains unresolved. Reason: PMID:32814053 Supplementary Table S2 (mmc3.xlsx, NN1.0, row 3072) contains the CDH1–EPCAM pair. The screen excluded reporter-autoactivating baits and used growth/reporter selection, so the construct interaction is positive experimental evidence. However, the gene-mapped row does not establish the boundaries of this pair’s fragments, pair-specific mammalian validation, or a native adhesive orientation. PMID:9382878 Figures 8–9 measure altered cadherin–cytoskeleton coupling rather than direct EPCAM–cadherin binding. PMID:23486470 Results preceding Figure 2 reports no tight EPCAM–E-cadherin association in T84 co-immunoprecipitation (Supplemental Figure 1B, described in the inspected main text). Retain the supported screen interaction as non-core while leaving the mature-protein cadherin-binding mechanism open; these limitations do not establish that the Y2H hit is false. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: A human Y2H screen supports interaction of EPCAM with calreticulin. Reason: The CALR–EPCAM pair is present in PMID:32814053 Supplementary Table S2, NN1.0 row 3071. Retain the reported construct interaction as non-core. The pair-specific evidence does not establish a chaperone function, calcium-binding activity, or endogenous intracellular localization of EPCAM. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: A human Y2H screen supports an EPCAM–DLST interaction. Reason: The DLST–EPCAM pair is present in PMID:32814053 Supplementary Table S2, NN1.0 row 3073. The screening interaction is supported, but a physiological mechanism or more specific EPCAM molecular function was not demonstrated. This does not transfer the catalytic activity or mitochondrial localization of DLST to EPCAM. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: A human Y2H screen supports interaction of EPCAM with CDK5R1. Reason: The EPCAM–CDK5R1 pair is present in PMID:32814053 Supplementary Table S2, NN1.0 row 2036. CDK5R1 is the regulatory partner rather than the CDK5 kinase itself; this pair does not establish kinase activity or a specific kinase-regulatory function for EPCAM. Retain the supported interaction as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | MODIFY | Summary: The human interaction screen detects EPCAM binding to the protein kinase NEK7. Reason: PMID:32814053 Supplementary Table S2, NN1.0 row 6916, identifies EPCAM and NEK7. Protein kinase binding captures the measured partner class more specifically. The Y2H construct result does not demonstrate that EPCAM activates or inhibits NEK7, is its substrate, or participates in an inflammasome. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005576 extracellular region | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: A shed EPCAM extracellular fragment can occur outside the cell. Reason: The actual PTN008351906 assertion lies above the EPCAM/TACSTD2 duplication and is ancestral to human EPCAM; its mouse Tacstd2 evidence is not a misidentified human ortholog. Independently, PMID:19136966 Figure 1d detects EpEX in cell-free human-cell supernatants, supporting extracellular occurrence of a released product. This does not mean the intact transmembrane precursor is a soluble extracellular protein, and the extracellular domain alone would not establish this location. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: EPCAM is a plasma-membrane protein. Reason: The PTN008351906 IBD is ancestral to the human target and includes experimental human evidence among its descendants. Direct human surface flow cytometry and microscopy in PMID:19785009 Figure 2, together with human intestinal localization in PMID:23486470 Figure 1, establish the conserved location. Target self-inclusion in the PAINT evidence is expected. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: Human Protein Atlas immunofluorescence supports EPCAM at the plasma membrane. Reason: The current official HPA subcellular record reports supported plasma-membrane localization; the listed HPA067463 experiment is positive in MCF-7 cells, with no staining in the other displayed cell lines. Independent human microscopy and surface FACS corroborate the location. This review does not treat absent staining in a cell line as absence from all human cells. |
| GO:0005886 plasma membrane | IDA PMID:15195135 The carcinoma-associated antigen EpCAM upregulates c-myc and... | ACCEPT | Summary: Plasma-membrane localization is independently established for human EPCAM. Reason: The complete original PMID:15195135 was not recovered. Its localization claim is nevertheless clearly supported by independent original human-cell surface FACS and microscopy in PMID:19785009 Figure 2 and human epithelial membrane staining in PMID:23486470 Figure 1. Preserve the original citation and do not claim its unread experiments were inspected. |
| GO:0005886 plasma membrane | IDA PMID:19785009 Characterization of epithelial cell adhesion molecule as a s... | ACCEPT | Summary: EPCAM is detected on the surface of undifferentiated human embryonic stem cells. Reason: PMID:19785009 Figure 2 shows EpCAM membrane/intercellular staining and positive flow cytometry in human HES cultures, with diminished surface signal after differentiation. The original Methods and main figure were inspected. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS PMID:1729376 A murine cDNA encodes a pan-epithelial glycoprotein that is ... | ACCEPT | Summary: The human EPCAM plasma-membrane location is established despite the older reference emphasizing a murine cDNA. Reason: The actual abstract of PMID:1729376 includes FACS experiments on human myeloma cells as well as murine cloning; its title is not evidence of a wrong-species attribution. The main original remains unavailable, but human surface expression is independently established in PMID:19785009 Figure 2 and PMID:23486470 Figure 1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867240 | ACCEPT | Summary: The plasma membrane is the location of membrane-anchored EPCAM. Reason: The Reactome event places EPCAM at the plasma membrane, consistent with direct human surface studies. Accept this compartment annotation without importing the event title’s stronger homophilic trans-adhesion model, which has been challenged by the direct tests in PMID:30185875. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9638571 | ACCEPT | Summary: Cell-surface EPCAM is compatible with the plasma-membrane location of the Reactome host-binding event. Reason: The event concerns bacterial FimH binding to mannose on host glycoproteins. The EPCAM compartment is independently established by human cell-surface experiments. This location annotation does not assign FimH lectin activity, glycan synthesis, or a bacterial pathogenic process to the EPCAM protein. |
| GO:0005923 bicellular tight junction | IBA GO_REF:0000033 | UNDECIDED | Summary: Tight-junction residency is unresolved across the relevant epithelial contexts. Reason: PTN002680918 is a verified ancestor of human EPCAM, and its rat/human descendant evidence is legitimate. However, the supporting 2005 localization experiments could not be inspected in full. Later human T84/Caco-2 and intestinal tissue imaging places EPCAM below rather than within the tight junction (PMID:23486470, Figure 1). This is a context-specific discrepancy requiring the original tissue/marker comparison, not a reason to reject the phylogeny or globally exclude tight-junction localization. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN002680918 · PTN002680918 UNRESOLVED Verified ancestral IBD node for human EPCAM, supported by rat/human descendants. Exact 2005 tissue localization remains inaccessible; later human intestinal imaging places EPCAM below tight junctions. The unresolved issue is tissue/compartment scope, not ancestry or donor count. |
| GO:0005923 bicellular tight junction | IDA PMID:16054130 The cell-cell adhesion molecule EpCAM interacts directly wit... | UNDECIDED | Summary: The exact tight-junction localization reported in the 2005 study remains source-specific uncertainty. Reason: The verified abstract of PMID:16054130 reports tissue-dependent basolateral and tight-junction colocalization, including human material, but the complete images and methods remain inaccessible. PMID:23486470 Figure 1 demonstrates a distinct below-junction lateral pool in human intestinal contexts. Preserve uncertainty rather than overrule the older experimental annotation from its abstract or extrapolate one tissue result to all epithelia. |
| GO:0005923 bicellular tight junction | IEA GO_REF:0000044 | UNDECIDED | Summary: The electronic tight-junction assertion inherits an unresolved localization boundary. Reason: Official UniProt SL-0265 correctly maps to GO:0005923. The issue is the biological scope of EPCAM localization: the older tissue experiments are not fully accessible, whereas human intestinal imaging in PMID:23486470 Figure 1 separates lateral EPCAM from occludin/ZO-1-defined tight junctions. Association with claudin-7 and regulation of junctions alone do not settle physical residency in the junction. |
| GO:0008284 positive regulation of cell population proliferation | IDA PMID:15195135 The carcinoma-associated antigen EpCAM upregulates c-myc and... | KEEP AS NON CORE | Summary: EPCAM can promote proliferation in particular human cellular contexts. Reason: The original PMID:15195135 main text is unavailable, but its direction is independently supported by human hESC knockdown and viable-cell counts in PMID:19785009 Figures 3 and 5, and EpICD-related loss/rescue experiments in PMID:19136966 Figure 4f. This is context dependent: intestinal cell lines in PMID:23486470 respond differently. Retain a supported regulatory phenotype as non-core without asserting a universal proliferative effect or a single mechanism in every cell type. |
| GO:0009986 cell surface | IEA GO_REF:0000107 | ACCEPT | Summary: EPCAM is exposed on the human cell surface. Reason: The ortholog transfer from mouse Q99JW5 is consistent with direct human surface flow cytometry in PMID:19785009 Figure 2 and the displayed single-pass membrane topology. This target evidence establishes the compartment without pretending the mouse donor’s complete experimental paper was read. |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: The EPCAM/Trop-2 family membrane inference can be refined to plasma membrane for human EPCAM. Reason: IPR043406 is the verified transmembrane EPCAM/Trop-2 family and its broad membrane mapping is biologically sound. The existing plasma-membrane rows and independent direct human surface measurements in PMID:19785009 Figure 2 and PMID:23486470 Figure 1 provide a more informative compartment. Proposed replacements: plasma membrane |
| GO:0016323 basolateral plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Basolateral plasma-membrane localization is conserved and directly observed in human epithelia. Reason: The actual PTN002680918 assertion is ancestral to human EPCAM and includes human experimental evidence. PMID:18025791 Figure 7E is adult human kidney basolateral staining, distinct from the transgenic-mouse panels. Human intestinal imaging in PMID:23486470 also identifies the lateral/basolateral pool. |
| GO:0016323 basolateral plasma membrane | IDA PMID:18025791 Spatial and temporal expression patterns of the epithelial c... | ACCEPT | Summary: Adult human kidney epithelia show basolateral EPCAM. Reason: The original PMID:18025791 Methods distinguish human tissues from human-EpCAM transgenic mice. Figure 7E specifically shows basolateral labeling in adult human collecting ducts and distal tubules. Retain the direct human localization without substituting the mouse transgene for the human evidence. Supporting Evidence: |
| GO:0016324 apical plasma membrane | IDA PMID:18025791 Spatial and temporal expression patterns of the epithelial c... | KEEP AS NON CORE | Summary: Apical EPCAM occurs in the developmental kidney context examined. Reason: PMID:18025791 Figure 7D specifically shows apical staining in 20-week human fetal kidney, whereas Figure 7E shows adult human basolateral staining. This is a developmental and tissue-dependent compartment, not a contradictory universal topology or the default location in mature epithelia. Supporting Evidence: |
| GO:0016328 lateral plasma membrane | EXP PMID:15195135 The carcinoma-associated antigen EpCAM upregulates c-myc and... | ACCEPT | Summary: Human EPCAM occurs at lateral cell interfaces. Reason: The original PMID:15195135 main text remains inaccessible, but the location is independently demonstrated by human intestinal and cell-line imaging in PMID:23486470 Figure 1, and human hESC intercellular staining in PMID:19785009 Figure 2. Accept the established location while keeping the original-source access limitation explicit. |
| GO:0016328 lateral plasma membrane | EXP PMID:19785009 Characterization of epithelial cell adhesion molecule as a s... | ACCEPT | Summary: EPCAM is enriched at interfaces between adjacent human embryonic stem cells. Reason: PMID:19785009 Figure 2A shows surface staining concentrated at contacts between cells, with surface flow cytometry in Figure 2B. These observations support the lateral plasma-membrane annotation; they do not alone establish a direct homophilic adhesive bond. Supporting Evidence: |
| GO:0016328 lateral plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Lateral plasma-membrane localization is supported by the ancestral assertion and direct human evidence. Reason: PTN002680918 is an actual ancestor of P16422. The mixed EPCAM/TACSTD2 descendant evidence is appropriate for this ancestral node, and human target evidence is not circular. Independent human intestinal imaging in PMID:23486470 Figure 1 and hESC staining in PMID:19785009 Figure 2 establish the location. |
| GO:0016328 lateral plasma membrane | IDA PMID:16054130 The cell-cell adhesion molecule EpCAM interacts directly wit... | ACCEPT | Summary: Lateral localization is clearly supported for human EPCAM. Reason: The complete cited 2005 article was not recovered, but its reported basolateral association is independently corroborated by the original human intestinal and T84/Caco-2 images in PMID:23486470 Figure 1. Unlike tight-junction residency, this broader lateral location is resolved by accessible direct human evidence. |
| GO:0016328 lateral plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt lateral-cell-membrane mapping accurately describes EPCAM. Reason: Official SL-0153 maps to GO:0016328. Direct human tissue and cell-line microscopy in PMID:23486470 Figure 1 supports this location. This is distinct from assuming that every lateral membrane protein is a tight-junction constituent. |
| GO:0023019 signal transduction involved in regulation of gene expression | IMP PMID:19136966 Nuclear signalling by tumour-associated antigen EpCAM. | KEEP AS NON CORE | Summary: Proteolytically released EpICD participates in signaling linked to gene-expression regulation. Reason: The accessible original figures and supplement of PMID:19136966 show released EpICD, FHL2 association, a nuclear EpICD/FHL2/LEF1/beta-catenin assembly and reporter effects (Figures 1 and 4; Supplementary Figures S5–S7). Independent human experiments in PMID:20064925 support promoter-associated EpICD and expression responses. The role concerns a released EPCAM product; the proteases execute cleavage, and neither promoter ChIP nor complex-associated EMSA establishes direct DNA binding by EPCAM. The main 2009 Methods remain inaccessible. This released-product gene-regulatory role is retained as contextual and non-core, consistent with the non-core nuclear-complex binding annotation and the membrane-claudin scope of the core function. |
| GO:0044877 protein-containing complex binding | IDA PMID:19136966 Nuclear signalling by tumour-associated antigen EpCAM. | KEEP AS NON CORE | Summary: EpICD associates with a nuclear regulatory protein assembly. Reason: PMID:19136966 Figure 4a separates a native nuclear assembly containing EpICD, FHL2, LEF1 and beta-catenin; Supplementary Figure S5 independently supports EpCAM–FHL2 interaction, including endogenous human cells and in-vitro translation. Retain the complex-associated binding claim, but do not infer binary binding to every component, direct DNA recognition, or a specific catalytic activity from co-migration or EMSA. The accessible evidence does not establish a sufficiently precise alternative molecular role for this particular complex-binding annotation. Supporting Evidence: |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:15195135 The carcinoma-associated antigen EpCAM upregulates c-myc and... | KEEP AS NON CORE | Summary: EPCAM signaling can increase transcriptional output in human cell models. Reason: The complete original PMID:15195135 remains unavailable. Independent accessible original Figure 4 of PMID:19136966 shows MYC induction and a LEF/TCF-responsive TOP reporter decreased by EpCAM knockdown; these support positive transcriptional regulation at the gene level. Preserve the old citation without claiming its precise assays were inspected, and distinguish this contextual regulatory output from direct DNA-binding activity. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:15922867 The tumour-associated antigen EpCAM upregulates the fatty ac... | KEEP AS NON CORE | Summary: Positive transcriptional regulation is supported for EPCAM, while the original E-FABP mechanism remains less resolved. Reason: PMID:15922867 is abstract-only and reports E-FABP expression responses. Independent original reporter and MYC-expression experiments in PMID:19136966 Figure 4 support the general positive transcriptional-regulation annotation, without establishing that the same mechanism acts on E-FABP or that EPCAM itself binds its promoter. Retain this context-dependent process rather than inferring a fatty-acid-binding activity from the regulated target. |
| GO:0048863 stem cell differentiation | IMP PMID:19785009 Characterization of epithelial cell adhesion molecule as a s... | MODIFY | Summary: EPCAM influences lineage differentiation of already established human embryonic stem cells. Reason: Current GO:0048863 describes acquisition of stem-cell features, whereas PMID:19785009 studies differentiation from HES2/HES3 cells. Knockdown changes endoderm/mesoderm markers and embryoid-body/teratoma output (Figures 4–6); this is a causal regulatory phenotype, not merely expression correlation. Replace the directionally mismatched process with regulation of cell differentiation. Use the unsigned term because lineage outputs differ and the experiments do not demonstrate a universal inhibition of differentiation or complete loss of stem-cell identity. Proposed replacements: regulation of cell differentiation Supporting Evidence: |
| GO:0070062 extracellular exosome | HDA PMID:11487543 Intestinal epithelial cells secrete exosome-like vesicles. | KEEP AS NON CORE | Summary: EPCAM can occur in extracellular vesicle preparations classified as exosomes. Reason: The complete intestinal-vesicle original PMID:11487543 was not recovered. Independently, the original PMID:19056867 human urinary-exosome study and its author-maintained NHLBI data identify TACSTD1/NP_002345 with one peptide, assigned to that study. This supports the general compartment claim without pretending to verify the older intestinal sample or implying that EPCAM performs vesicle biogenesis. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: Human urinary-exosome proteomics identifies EPCAM. Reason: PMID:19056867 Methods describe pooled healthy-human urine, differential centrifugation and LC-MS/MS with human RefSeq identification. The linked NHLBI Urinary Exosome Protein Database contains TACSTD1/NP_002345, one peptide, reference 2 (this paper). Retain the detected compartment as non-core, recognizing the single-peptide dataset scope. Its historical ancillary GO-function column is not independent evidence of EPCAM enzymatic or ATP-binding activity. Supporting Evidence: |
| GO:0098609 cell-cell adhesion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: EpCAM has context-dependent effects in cell aggregation and attachment assays, distinct from the function of its claudin-7-associated pool. Reason: PTN008351906 is a verified ancestor of human EPCAM. In its rat donor source PMID:19276185, rat EpCAM expressed in HEK/AS cells increased aggregation and attachment when present without associated claudin-7; coexpression with claudin-7 reduced those effects, whereas an association-impaired EpCAM mutant restored them (Results and Figure 3). Thus, this paper does not support an adhesion-promoting EpCAM–CLDN7 complex. Retain the inherited broad adhesion association as contextual, non-core evidence rather than as the process executed by the claudin-binding core. Human biochemical and cell-based experiments in PMID:30185875 Figures 2–5 challenge a direct homophilic trans-adhesion mechanism. The binding/stability evidence in PMID:23486470 is assessed separately and is not used to convert claudin stabilization into positive adhesion. |
| GO:0098641 cadherin binding involved in cell-cell adhesion | IBA GO_REF:0000033 | UNDECIDED | Summary: The inherited cadherin-binding role in trans-cellular adhesion remains unresolved. Reason: PTN000366716 is correctly placed above human EPCAM. Its rat donor assertion points to PMID:19276185, whose operative assays concern EpCAM–CLDN7 association and cell attachment, not binding to cadherin as the adhesive mechanism. GO:0098641 additionally inherits a mediator definition requiring binding to an extracellular component of another cell. The independent human CDH1–EPCAM Y2H pair in PMID:32814053 Table S2 row 3072 establishes a screened construct interaction but does not settle fragment boundaries, native orientation, or this combined ancestral role. The contextual cadherin-regulatory experiments in PMID:9382878 and the T84 co-immunoprecipitation result described in PMID:23486470 do not resolve that gap. Preserve uncertainty independently of the supported screen interaction; no invalid clade or target-specific evolutionary loss is asserted. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000366716 · PTN000366716 UNRESOLVED Verified EPCAM-branch ancestor. The rat donor source assays CLDN7 association and attachment, while the human CDH1 fragment-screen hit does not establish cadherin binding in a native trans-cellular adhesive role. The unresolved question is functional scope, not ancestry, donor count or target-specific loss. |
| GO:2000048 negative regulation of cell-cell adhesion mediated by cadherin | IDA PMID:9382878 Epithelial cell adhesion molecule (Ep-CAM) modulates cell-ce... | KEEP AS NON CORE | Summary: EPCAM expression can attenuate cadherin-mediated cell-cell adhesion. Reason: PMID:9382878 uses human EPCAM in E-cadherin-expressing mouse cells and human HCA cells. Quantitative aggregation, expression controls and cytoskeletal fractionation distinguish reduced cadherin-mediated adhesion from loss of cadherin abundance (Figures 4, 8–9). A surface-expressed tail truncation fails to reproduce the regulatory effect in the human model. Retain this experimentally supported contextual regulatory function without converting it to direct cadherin binding or claiming a universal anti-adhesive role. Supporting Evidence: |
| GO:2000648 positive regulation of stem cell proliferation | IMP PMID:19785009 Characterization of epithelial cell adhesion molecule as a s... | KEEP AS NON CORE | Summary: EPCAM supports proliferation of human embryonic stem cells under the tested culture conditions. Reason: PMID:19785009 Figures 3 and 5 show lower viable-cell counts after transient and stable EPCAM knockdown in human HES cultures. This directly supports positive regulation of stem-cell proliferation, with no requirement that EPCAM itself be a cell-cycle enzyme. The response is context dependent and is not evidence that all EPCAM-positive cells or intestinal epithelia share the same proliferative mechanism. Supporting Evidence: |
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Download this section (compressed HTML)Q: Which tissue, junction-marker controls and spatial resolution distinguish the tight-junction EPCAM pool in PMID:16054130 from the below-junction lateral pool in PMID:23486470?
Q: Does the EPCAM–CDH1 interaction detected in PMID:32814053 occur between full-length endogenous proteins, and is it in cis or in trans across a cell contact?
Q: How does EPCAM–CLDN7 association alter claudin degradation and junction incorporation in primary human epithelia, and why do proliferation/barrier responses differ between cell models?
Q: Which endogenous EpICD cleavage products enter nuclear complexes, and what contacts distinguish its regulatory contribution from direct DNA binding or the activities of FHL2, beta-catenin and LEF1?
Q: What functional evidence beyond developmental expression supports the mouse-to-human ureteric bud development transfer from PMID:16545622?
Q: Which lineage-specific effects explain the differentiation phenotype after EPCAM knockdown in human embryonic stem cells without equating it with acquisition or loss of stem-cell identity?
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