DEPOD - human DEPhOsphorylation Database

Basic Information
Phosphatases
Pathway
Interacting Proteins
Phosphorylating Kinases

Gene Name	CDH1 (QuickGO)	Interactive visualization of CDH1 structures (A quick tutorial to explore the interctive visulaization) Representative structure: 2OMY
Synonyms	CDH1, CDHE, UVO
Protein Name	CDH1
Alternative Name(s)	Cadherin-1;CAM 120/80;Epithelial cadherin;E-cadherin;Uvomorulin;CD324;E-Cad/CTF1;E-Cad/CTF2;E-Cad/CTF3;
Protein Family	noSimilarity_annotations
EntrezGene ID	999 (Comparitive Toxicogenomics)
UniProt AC (Human)	P12830 (protein sequence)
Enzyme Class	N/A
Molecular Weight	97456 Dalton
Protein Length	882 amino acids (AA)
Genome Browsers	NCBI \| ENSG00000039068 (Ensembl) \| UCSC
Crosslinking annotations	Query our ID-mapping table
Orthologues	Quest For Orthologues (QFO) \| GeneTree \| eggNOG - KOG3594 \| eggNOG - ENOG410XQHI
Phosphorylation Network	Visualize

Domain organization, Expression, Diseases

(show / hide)

Localization, Function, Catalytic activity and Sequence

(show / hide)

Localization (UniProt annotation)
Cell junction Cell membrane ; Single-pass type Imembrane protein Endosome Golgi apparatus, trans-Golgi networkNote=Colocalizes with DLGAP5 at sites of cell-cell contact inintestinal epithelial cells Anchored to actin microfilamentsthrough association with alpha-, beta- and gamma-cateninSequential proteolysis induced by apoptosis or calcium influx,results in translocation from sites of cell-cell contact to thecytoplasm Colocalizes with RAB11A endosomes during its transportfrom the Golgi apparatus to the plasma membrane
Function (UniProt annotation)
Cadherins are calcium-dependent cell adhesion proteins(PubMed:11976333) They preferentially interact with themselves ina homophilic manner in connecting cells; cadherins may thuscontribute to the sorting of heterogeneous cell types CDH1 isinvolved in mechanisms regulating cell-cell adhesions, mobilityand proliferation of epithelial cells (PubMed:11976333) Has apotent invasive suppressor role It is a ligand for integrinalpha-E/beta-7 E-Cad/CTF2 promotes non-amyloidogenic degradation ofAbeta precursors Has a strong inhibitory effect on APP C99 andC83 production
Catalytic Activity (UniProt annotation)
N/A
Protein Sequence
MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTD GVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPP ISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGN AVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTIN RNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTD ADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDV NEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNST YTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTI QYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILAL LILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPR PANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGE DD

Motif information from Eukaryotic Linear Motif atlas (ELM)

(show / hide)

Gene Ontology (P: Process; F: Function and C: Component terms)

(show / hide)

KEGG Pathway
Reactome Pathway

Pathway ID	Pathway Name	Pathway Description (KEGG)
hsa04015	Rap1 signaling pathway	Rap1 is a small GTPase that controls diverse processes, such as cell adhesion, cell-cell junction formation and cell polarity. Like all G proteins, Rap1 cycles between an inactive GDP-bound and an active GTP-bound conformation. A variety of extracellular signals control this cycle through the regulation of several unique guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs). Rap1 plays a dominant role in the control of cell-cell and cell-matrix interactions by regulating the function of integrins and other adhesion molecules in various cell types. Rap1 also regulates MAP kinase (MAPK) activity in a manner highly dependent on the context of cell types.
hsa04371	Apelin signaling pathway	Apelin is an endogenous peptide capable of binding the apelin receptor (APJ), which was originally described as an orphan G-protein-coupled receptor. Apelin and APJ are widely expressed in various tissues and organ systems. They are implicated in different key physiological processes such as angiogenesis, cardiovascular functions, cell proliferation and energy metabolism regulation. On the other hand, this ligand receptor couple is also involved in several pathologies including diabetes, obesity, cardiovascular disease and cancer.
hsa04390	Hippo signaling pathway	Hippo signaling is an evolutionarily conserved signaling pathway that controls organ size from flies to humans. In humans and mice, the pathway consists of the MST1 and MST2 kinases, their cofactor Salvador and LATS1 and LATS2. In response to high cell densities, activated LATS1/2 phosphorylates the transcriptional coactivators YAP and TAZ, promoting its cytoplasmic localization, leading to cell apoptosis and restricting organ size overgrowth. When the Hippo pathway is inactivated at low cell density, YAP/TAZ translocates into the nucleus to bind to the transcription enhancer factor (TEAD/TEF) family of transcriptional factors to promote cell growth and proliferation. YAP/TAZ also interacts with other transcriptional factors or signaling molecules, by which Hippo pathway-mediated processes are interconnected with those of other key signaling cascades, such as those mediated by TGF-beta and Wnt growth factors.
hsa04514	Cell adhesion molecules (CAMs)	Cell adhesion molecules are (glyco)proteins expressed on the cell surface and play a critical role in a wide array of biologic processes that include hemostasis, the immune response, inflammation, embryogenesis, and development of neuronal tissue. There are four main groups: the integrin family, the immunoglobulin superfamily, selectins, and cadherins. Membrane proteins that mediate immune cell–cell interactions fall into different categories, namely those involved in antigen recognition, costimulation and cellular adhesion. Furthermore cell-cell adhesions are important for brain morphology and highly coordinated brain functions such as memory and learning. During early development of the nervous system, neurons elongate their axons towards their targets and establish and maintain synapses through formation of cell-cell adhesions. Cell-cell adhesions also underpin axon-axon contacts and link neurons with supporting schwann cells and oligodendrocytes.
hsa04520	Adherens junction	Cell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation. At AJs, E-cadherin serves as an essential cell adhesion molecules (CAMs). The cytoplasmic tail binds beta-catenin, which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of the cadherin-catenin complex is negatively regulated by phosphorylation of beta-catenin by receptor tyrosine kinases (RTKs) and cytoplasmic tyrosine kinases (Fer, Fyn, Yes, and Src), which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin phosphorylation by casein kinase II, and dephosphorylation by protein tyrosine phosphatases. Changes in the phosphorylation state of beta-catenin affect cell-cell adhesion, cell migration and the level of signaling beta-catenin. Wnt signaling acts as a positive regulator of beta-catenin by inhibiting beta-catenin degradation, which stabilizes beta-catenin, and causes its accumulation. Cadherin may acts as a negative regulator of signaling beta-catenin as it binds beta-catenin at the cell surface and thereby sequesters it from the nucleus. Nectins also function as CAMs at AJs, but are more highly concentrated at AJs than E-cadherin. Nectins transduce signals through Cdc42 and Rac, which reorganize the actin cytoskeleton, regulate the formation of AJs, and strengthen cell-cell adhesion.
hsa05100	Bacterial invasion of epithelial cells	Many pathogenic bacteria can invade phagocytic and non-phagocytic cells and colonize them intracellularly, then become disseminated to other cells. Invasive bacteria induce their own uptake by non-phagocytic host cells (e.g. epithelial cells) using two mechanisms referred to as zipper model and trigger model. Listeria, Staphylococcus, Streptococcus, and Yersinia are examples of bacteria that enter using the zipper model. These bacteria express proteins on their surfaces that interact with cellular receptors, initiating signalling cascades that result in close apposition of the cellular membrane around the entering bacteria. Shigella and Salmonella are the examples of bacteria entering cells using the trigger model. These bacteria use type III secretion systems to inject protein effectors that interact with the actin cytoskeleton.
hsa05130	Pathogenic Escherichia coli infection	Enteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction of attaching and effacing (A/E) lesions that damage intestinal epithelial cells. The capacity to form A/E lesions is encoded mainly by the locus of enterocyte effacement (LEE) pathogenicity island. Tir, Map, EspF, EspG are known LEE-encoded effector proteins secreted via the type III secretion system, which is also LEE-encoded, into the host cell. EPEC and EHEC Tir's link the extracellular bacterium to the cell cytoskeleton. Map and EspF are involved in mitochondrion membrane permeabilization. EspG interacts with tubulins and stimulates microtubule destabilization. LEE-encoded adhesin or intimin (Eae) is exported via the general secretory pathway to the periplasm, where it is inserted into the outer membrane. In addition to Tir, two potential host cell-carried intimin receptors, beta1 integrin (ITGB1) and nucleolin (NCL), have so far been identified. The distinguishing feature of EHEC is the elaboration of Shiga-like toxin (Stx). Stx cleaves ribosomal RNA, thereby disrupting protein synthesis and killing the intoxicated epithelial or endothelial cells.
hsa05200	Pathways in cancer
hsa05213	Endometrial cancer	Endometrial cancer (EC) is the most common gynaecological malignancy and the fourth most common malignancy in women in the developed world after breast, colorectal and lung cancer. Two types of endometrial carcinoma are distinguished with respect to biology and clinical course. Type-I carcinoma is related to hyperestrogenism by association with endometrial hyperplasia, frequent expression of estrogen and progesterone receptors and younger age, whereas type-II carcinoma is unrelated to estrogen, associated with atrophic endometrium, frequent lack of estrogen and progesterone receptors and older age. The morphologic differences in these cancers are mirrored in their molecular genetic profile with type I showing defects in DNA-mismatch repair and mutations in PTEN, K-ras, and beta-catenin, and type II showing aneuploidy, p53 mutations, and her2/neu amplification.
hsa05216	Thyroid cancer	Thyroid cancer is the most common endocrine malignancy and accounts for the majority of endocrine cancer- related deaths each year. More than 95% of thyroid carcinomas are derived from follicular cells. Their behavior varies from the indolent growing, well-differentiated papillary and follicular carcinomas (PTC and FTC, respectively) to the extremely aggressive undifferentiated carcinoma (UC). Somatic rearrangements of RET and TRK are almost exclusively found in PTC and may be found in early stages. The most distinctive molecular features of FTC are the prominence of aneuploidy and the high prevalence of RAS mutations and PAX8-PPAR{gamma} rearrangements. p53 seems to play a crucial role in the dedifferentiation process of thyroid carcinoma.
hsa05218	Melanoma	Melanoma is a form of skin cancer that has a poor prognosis and which is on the rise in Western populations. Melanoma arises from the malignant transformation of pigment-producing cells, melanocytes. The only known environmental risk factor is exposure to ultraviolet (UV) light and in people with fair skin the risk is greatly increased. Melanoma pathogenesis is also driven by genetic factors. Oncogenic NRAS mutations activate both effector pathways Raf-MEK-ERK and PI3K-Akt. The Raf-MEK-ERK pathway may also be activated via mutations in the BRAF gene. The PI3K-Akt pathway may be activated through loss or mutation of the inhibitory tumor suppressor gene PTEN. These mutations arise early during melanoma pathogenesis and are preserved throughout tumor progression. Melanoma development has been shown to be strongly associated with inactivation of the p16INK4a/cyclin dependent kinases 4 and 6/retinoblastoma protein (p16INK4a/CDK4,6/pRb) and p14ARF/human double minute 2/p53 (p14ARF/HMD2/p53) tumor suppressor pathways. MITF and TP53 are implicated in further melanoma progression.
hsa05219	Bladder cancer	The urothelium covers the luminal surface of almost the entire urinary tract, extending from the renal pelvis, through the ureter and bladder, to the proximal urethra. The majority of urothelial carcinoma are bladder carcinomas, and urothelial carcinomas of the renal pelvis and ureter account for only approximately 7% of the total. Urothelial tumours arise and evolve through divergent phenotypic pathways. Some tumours progress from urothelial hyperplasia to low-grade non-invasive superficial papillary tumours. More aggressive variants arise either from flat, high-grade carcinoma in situ (CIS) and progress to invasive tumours, or they arise de novo as invasive tumours. Low-grade papillary tumors frequently show a constitutive activation of the receptor tyrosine kinase-Ras pathway, exhibiting activating mutations in the HRAS and fibroblast growth factor receptor 3 (FGFR3) genes. In contrast, CIS and invasive tumors frequently show alterations in the TP53 and RB genes and pathways. Invasion and metastases are promoted by several factors that alter the tumour microenvironment, including the aberrant expression of E-cadherins (E-cad), matrix metalloproteinases (MMPs), angiogenic factors such as vascular endothelial growth factor (VEGF).
hsa05226	Gastric cancer	Gastric cancer (GC) is one of the world's most common cancers. According to Lauren's histological classification gastric cancer is divided into two distinct histological groups - the intestinal and diffuse types. Several genetic changes have been identified in intestinal-type GC. The intestinal metaplasia is characterized by mutations in p53 gene, reduced expression of retinoic acid receptor beta (RAR-beta) and hTERT expression. Gastric adenomas furthermore display mutations in the APC gene, reduced p27 expression and cyclin E amplification. In addition, amplification and overexpression of c-ErbB2, reduced TGF-beta receptor type I (TGFBRI) expression and complete loss of p27 expression are commonly observed in more advanced GC. The main molecular changes observed in diffuse-type GCs include loss of E-cadherin function by mutations in CDH1 and amplification of MET and FGFR2F.

Pathway ID	Pathway Name	Pathway Description (KEGG)
R-HSA-1474228	Degradation of the extracellular matrix.	Matrix metalloproteinases (MMPs), previously referred to as matrixins because of their role in degradation of the extracellular matrix (ECM), are zinc and calcium dependent proteases belonging to the metzincin family. They contain a characteristic zinc-binding motif HEXXHXXGXXH (Stocker & Bode 1995) and a conserved Methionine which forms a Met-turn. Humans have 24 MMP genes giving rise to 23 MMP proteins, as MMP23 is encoded by two identical genes. All MMPs contain an N-terminal secretory signal peptide and a prodomain with a conserved PRCGXPD motif that in the inactive enzyme is localized with the catalytic site, the cysteine acting as a fourth unpaired ligand for the catalytic zinc atom. Activation involves delocalization of the domain containing this cysteine by a conformational change or proteolytic cleavage, a mechanism referred to as the cysteine-switch (Van Wart & Birkedal-Hansen 1990). Most MMPs are secreted but the membrane type MT-MMPs are membrane anchored and some MMPs may act on intracellular proteins. Various domains determine substrate specificity, cell localization and activation (Hadler-Olsen et al. 2011). MMPs are regulated by transcription, cellular location (most are not activated until secreted), activating proteinases that can be other MMPs, and by metalloproteinase inhibitors such as the tissue inhibitors of metalloproteinases (TIMPs). MMPs are best known for their role in the degradation and removal of ECM molecules. In addition, cleavage of the ECM and other cell surface molecules can release ECM-bound growth factors, and a number of non-ECM proteins are substrates of MMPs (Nagase et al. 2006). MMPs can be divided into subgroups based on domain structure and substrate specificity but it is clear that these are somewhat artificial, many MMPs belong to more than one functional group (Vise & Nagase 2003, Somerville et al. 2003)
R-HSA-198933	Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.	A number of receptors and cell adhesion molecules play a key role in modifying the response of cells of lymphoid origin (such as B-, T- and NK cells) to self and tumor antigens, as well as to pathogenic organisms. Molecules such as KIRs and LILRs form part of a crucial surveillance system that looks out for any derangement, usually caused by cancer or viral infection, in MHC Class I presentation. Somatic cells are also able to report internal functional impairment by displaying surface stress markers such as MICA. The presence of these molecules on somatic cells is picked up by C-lectin NK immune receptors. Lymphoid cells are able to regulate their location and movement in accordance to their state of activation, and home in on tissues expressing the appropriate complementary ligands. For example, lymphoid cells may fine tune the presence and concentration of adhesion molecules belonging to the IgSF, Selectin and Integrin class that interact with a number of vascular markers of inflammation. Furthermore, there are a number of avenues through which lymphoid cells may interact with antigen. This may be presented directly to a specific T-cell receptor in the context of an MHC molecule. Antigen-antibody complexes may anchor to the cell via a small number of lymphoid-specific Fc receptors that may, in turn, influence cell function further. Activated complement factor C3d binds to both antigen and to cell surface receptor CD21. In such cases, the far-reaching influence of CD19 on B-lymphocyte function is tempered by its interaction with CD21
R-HSA-216083	Integrin cell surface interactions.	The extracellular matrix (ECM) is a network of macro-molecules that underlies all epithelia and endothelia and that surrounds all connective tissue cells. This matrix provides the mechanical strength and also influences the behavior and differentiation state of cells in contact with it. The ECM are diverse in composition, but they generally comprise a mixture of fibrillar proteins, polysaccharides synthesized, secreted and organized by neighboring cells. Collagens, fibronectin, and laminins are the principal components involved in cell matrix interactions; other components, such as vitronectin, thrombospondin, and osteopontin, although less abundant, are also important adhesive molecules.Integrins are the receptors that mediate cell adhesion to ECM. Integrins consists of one alpha and one beta subunit forming a noncovalently bound heterodimer. 18 alpha and 8 beta subunits have been identified in humans that combine to form 24 different receptors. The integrin dimers can be broadly divided into three families consisting of the beta1, beta2/beta7, and beta3/alphaV integrins. beta1 associates with 12 alpha-subunits and can be further divided into RGD-, collagen-, or laminin binding and the related alpha4/alpha9 integrins that recognise both matrix and vascular ligands. beta2/beta7 integrins are restricted to leukocytes and mediate cell-cell rather than cell-matrix interactions, although some recognize fibrinogen. The beta3/alphaV family members are all RGD receptors and comprise aIIbb3, an important receptor on platelets, and the remaining b-subunits, which all associate with alphaV. It is the collagen receptors and leukocyte-specific integrins that contain alpha A-domains
R-HSA-351906	Apoptotic cleavage of cell adhesion proteins.	Apoptotic cells show dramatic rearrangements of tight junctions, adherens junctions, and desmosomes (Abreu et al., 2000). Desmosome-specific members of the cadherin superfamily of cell adhesion molecules including desmoglein-3, plakophilin-1 and desmoplakin are cleaved by caspases after onset of apoptosis (Weiske et al., 2001). Cleavage results in the disruption of the desmosome structure and thus contributes to cell rounding and disintegration of the intermediate filament system (Weiske et al., 2001)
R-HSA-418990	Adherens junctions interactions.	The adherens junctions (AJ) are multiprotein complexes that promote homotypic cell adhesion in nearly all types of tissue by linking membrane and cytoskeletal components at discrete contact regions (reviewed in Hartsock & Nelson 2008; Gumbiner 2005; Ebnet, 2008). The molecular constituents of adherens junctions form adhesive units which are organized into higher order junctional adhesions that create a zipper-like seal between adjacent cells. Junctional adhesions function in epithelial cell polarization and in the coupling of cytoskeletons in adjacent cells that allow coordinated movements. During embryonic development, AJs function in specifying adhesion between cells and contribute in the sorting of different cell types. AJs also regulate cell polarity and shape, promote cell-cell communication and help mediate contact inhibition of cell growth. This module covers transdimerization events involving AJ transmembrane proteins (cadherins and nectins) (Gumbiner 2005; Ebnet 2008; Hartsock & Nelson 2008)
R-HSA-5626467	RHO GTPases activate IQGAPs.	IQGAPs constitute a family of scaffolding proteins characterized by a calponin homology (CH) domain, a polyproline binding region (WW domain), a tandem of four IQ (isoleucine and glutamine-rich) repeats and a RAS GTPase-activating protein-related domain (GRD). Three IQGAPs have been identified in human, IQGAP1, IQGAP2 and IQGAP3. The best characterized is IQGAP1 and over 90 proteins have been reported to bind to it. IQGAPs integrate multiple signaling pathways and coordinate a large variety of cellular activities (White et al. 2012). IQGAP proteins IQGAP1, IQGAP2 and IQGAP3, bind activated RHO GTPases RAC1 and CDC42 via their GRD and stabilize them in their GTP-bound state (Kuroda et al. 1996, Swart-Mataraza et al. 2002, Wang et al. 2007). IQGAPs bind F-actin filaments via the CH domain and modulate cell shape and motility through regulation of G-actin/F-actin equilibrium (Brill et al. 1996, Fukata et al. 1997, Bashour et al. 1997, Wang et al. 2007, Pelikan-Conchaudron et al. 2011). Binding of IQGAPs to F-actin is inhibited by calmodulin binding to the IQ repeats (Bashour et al. 1997, Pelikan-Conchaudron et al. 2011). Based on IQGAP1 studies, IQGAPs presumably function as homodimers (Bashour et al. 1997). IQGAP1 is involved in the regulation of adherens junctions through its interaction with E-cadherin (CDH1) and catenins (CTTNB1 and CTTNA1) (Kuroda et al. 1998, Hage et al. 2009). IQGAP1 contributes to cell polarity and lamellipodia formation through its interaction with microtubules (Fukata et al. 2002, Suzuki and Takahashi 2008)
R-HSA-8876493	InlA-mediated entry of Listeria monocytogenes into host cells.	The pathogenic bacteria Listeria monocytogenes can enter host cells through endocytosis triggered by binding of the bacterial cell wall protein internalin (InlA) to the E-cadherin (CDH1) complex at the host cell plasma membrane (Mengaud et al. 1996, Lecuit et al. 1999). Binding of InlA to CDH1, similar to CDH1 engagement during normal cell-to-cell adhesion, triggers activation of the SRC protein tyrosine kinase and phosphorylation of CDH1 and CDH1-bound beta-catenin (CTNNB1) (Fujita et al. 2002, McLachlan et al. 2007, Sousa et al. 2007, Bonazzi et al. 2008). Integrins likely contribute to CDH1-triggered SRC activation, and ERKs (MAPK1 and MAPK3), ROCKs and MLCK may also be involved (Avizienyte et al. 2002, Avizienyte et al. 2004, Martinez-Rico et al. 2010). FAK1 (PTK2), a SRC-regulated protein tyrosine kinase, may contribute to SRC-mediated regulation of CDH1 (Avizienyte et al. 2002).Phosphorylation of CDH1 and CTNNB1 by SRC creates docking sites for a CBL-like ubiquitin protein ligase Hakai (CBLL1). CBLL1 ubiquitinates SRC-phosphorylated CDH1 and CTNNB1 upon InlA binding, as well as in the context of CDH1-mediated cell-to-cell adhesion, thus triggering CDH1 endocytosis (Fujita et al. 2002, Bonazzi et al. 2008, Mukherjee et al. 2012).CBLL1 may also undergo SRC-mediated phosphorylation and subsequent autoubiquitination (Fujita et al. 2002).Both clathrin-mediated and caveolin-mediated endocytosis are implicated in the InlA-mediated entry of Listeria monocytogenes to host cells (Veiga et al. 2007). SRC-mediated phosphorylation of cortactin and the ARP2/3 complex involved in actin polymerization is implicated in CDH1 endocytosis and Listeria monocytogenes internalization (Sousa et al. 2007, Ren et al. 2009)

BioGRID
IntAct
MINT
ALL

Visualize Download

Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ACTN4	pull down, surface plasmon resonance	association, physical association	16212417, (Europe PMC)	0.50	IntAct
AKT1	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
ANP32B	Affinity Capture-MS, pull down	association, physical	16212417, (Europe PMC)	0.35	BioGRID, IntAct
AOPEP	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
AP2M1	Affinity Capture-MS, tandem affinity purification	association, physical	24189400, (Europe PMC)	0.35	BioGRID, IntAct
BEX1	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
BLID	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
C1QBP	Affinity Capture-MS, pull down	association, physical	16212417, (Europe PMC)	0.35	BioGRID, IntAct
CASP3	Co-localization, proximity ligation assay	physical, physical association	25241761, (Europe PMC)	0.40	BioGRID, IntAct
CBLL1	Affinity Capture-Western, Co-localization, FRET, Two-hybrid, anti bait coimmunoprecipitation	physical, physical association	11836526, 16336960, 18057010, 19711372, 21685945, 22252131, 22715382, 22850631, 28069439, (Europe PMC)	0.40	BioGRID, IntAct
CCL5	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
CCND1	anti bait coimmunoprecipitation	physical association	20439707, (Europe PMC)	0.40	IntAct
CCT6A	surface plasmon resonance	physical association	16212417, (Europe PMC)	0.40	IntAct
CDC27	Affinity Capture-Western, anti bait coimmunoprecipitation, immunodepleted coimmunoprecipitation	physical, physical association	20686030, 20802534, 20951947, 22539978, (Europe PMC)	0.59	BioGRID, IntAct
CDH1	Affinity Capture-Western, Co-purification, Reconstituted Complex, atomic force microscopy, bead aggregation assay, cross-linking study, fluorescent resonance energy transfer, intermolecular force, tandem affinity purification	direct interaction, physical, physical association	10202138, 10910767, 19114658, 19646884, 21300292, 23112161, 24725409, (Europe PMC)	0.88	BioGRID, IntAct
CDK8	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
CFTR	Affinity Capture-MS, anti bait coimmunoprecipitation	association, physical	17110338, 26618866, (Europe PMC)	0.35	BioGRID, IntAct
CRYAB	Affinity Capture-Western, anti bait coimmunoprecipitation, pull down	physical, physical association	22158051, (Europe PMC)	0.52	BioGRID, IntAct
CTNNA1	Affinity Capture-MS, Affinity Capture-Western, Proximity Label-MS, anti bait coimmunoprecipitation, pull down, surface plasmon resonance	association, physical, physical association	10381631, 11960376, 16212417, 19016843, 22750944, 25468996, 7542250, 8227214, 9233779, (Europe PMC)	0.75	BioGRID, IntAct, MINT
CTNNB1	Affinity Capture-MS, Affinity Capture-Western, Co-crystal Structure, Co-localization, FRET, Proximity Label-MS, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, fluorescence microscopy, proximity ligation assay, pull down, surface plasmon resonance	association, colocalization, physical, physical association	10381631, 10772923, 11113628, 11245482, 11254878, 11348595, 11401320, 11712088, 11960376, 12061792, 12169098, 12640114, 12830000, 15023525, 16125672, 16212417, 16574648, 16983094, 17220478, 17909039, 18593713, 18593907, 19016843, 22056988, 22158051, 22375065, 22715382, 22752307, 22850631, 23180380, 24424122, 24798214, 25344754, 25468996, 7542250, 7876318, 7954478, 8227214, 9233779, 9405455, 9535896, 9819408, (Europe PMC)	0.95	BioGRID, IntAct, MINT
CTNND1	Affinity Capture-Western, Co-crystal Structure, Co-localization, FRET, Proximity Label-MS, Reconstituted Complex, Two-hybrid, fluorescence microscopy, proximity ligation assay, x-ray crystallography	colocalization, direct interaction, physical, physical association	10409703, 12427869, 12640114, 12707304, 19711372, 20371349, 21670201, 22715382, 22752307, 22850631, 23180380, 24424122, 25468996, 7542250, 7651399, 7876318, 9535896, (Europe PMC)	0.27, 0.40, 0.44	BioGRID, IntAct
CYP17A1	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
DKK3	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
ECT2	Affinity Capture-Western, anti bait coimmunoprecipitation	association, physical, physical association	21886810, 22750944, (Europe PMC)	0.50	BioGRID, IntAct
EGFR	Affinity Capture-MS, Affinity Capture-Western, Co-localization, PCA, Proximity Label-MS, Two-hybrid, proximity ligation assay, tandem affinity purification, ubiquitin reconstruction	association, physical, physical association	10969083, 24189400, 24658140, 25241761, 25402006, 25468996, (Europe PMC)	0.68	BioGRID, IntAct
EPSTI1	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
FGFR1	Co-localization, anti bait coimmunoprecipitation, proximity ligation assay	physical, physical association	11401320, 25241761, (Europe PMC)	0.59	BioGRID, IntAct
FRMD5	anti bait coimmunoprecipitation	association	22846708, (Europe PMC)	0.35	IntAct, MINT
GALNT12	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
GSK3B	Co-localization, proximity ligation assay	physical, physical association	25241761, (Europe PMC)	0.40	BioGRID, IntAct
HDAC2	Affinity Capture-Western, Co-localization, Co-purification, proximity ligation assay	physical, physical association	15388328, 25241761, (Europe PMC)	0.40	BioGRID, IntAct
HEMGN	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
HRAS	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
HSD17B3	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
HSP90AA1	Affinity Capture-MS, pull down, surface plasmon resonance	association, physical, physical association	16212417, (Europe PMC)	0.50	BioGRID, IntAct
HSPD1	Affinity Capture-MS, surface plasmon resonance	physical, physical association	16212417, (Europe PMC)	0.40	BioGRID, IntAct
IGHA1	surface plasmon resonance	physical association	16212417, (Europe PMC)	0.40	IntAct
ILK	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	25852190, (Europe PMC)	0.35	BioGRID, IntAct
KIFC3	confocal microscopy	colocalization	19041755, (Europe PMC)	0.27	IntAct
KRT1	Affinity Capture-MS, surface plasmon resonance	physical, physical association	16212417, (Europe PMC)	0.40	BioGRID, IntAct
KRT9	Affinity Capture-MS, surface plasmon resonance	physical, physical association	16212417, (Europe PMC)	0.40	BioGRID, IntAct
LIMA1	Proximity Label-MS, anti bait coimmunoprecipitation	physical, physical association	18093941, 25468996, (Europe PMC)	0.40	BioGRID, IntAct
LMNA	Affinity Capture-MS, surface plasmon resonance	physical, physical association	16212417, (Europe PMC)	0.40	BioGRID, IntAct
MAP2K1	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
MAPKAPK3	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
MSANTD3	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
MTA3	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
NANS	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
NAT2	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
NDRG1	Affinity Capture-Western, Proximity Label-MS, anti bait coimmunoprecipitation	association, physical	17220478, 25468996, (Europe PMC)	0.35	BioGRID, IntAct
NIPSNAP1	Affinity Capture-MS, pull down	association, physical	16212417, (Europe PMC)	0.35	BioGRID, IntAct
NIPSNAP2	pull down	association	16212417, (Europe PMC)	0.35	IntAct
PHLPP1	fluorescence microscopy	colocalization	21701506, (Europe PMC)	0.27	IntAct, MINT
PLEKHA7	Proximity Label-MS, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, confocal microscopy	association, colocalization, physical, physical association	19041755, 25468996, 28877994, (Europe PMC)	0.60	BioGRID, IntAct
POLR2E	Affinity Capture-MS, surface plasmon resonance	physical, physical association	16212417, (Europe PMC)	0.40	BioGRID, IntAct
PPP1CA	Affinity Capture-Western, Proximity Label-MS, anti bait coimmunoprecipitation, antibody array	physical, physical association	17274640, 25468996, (Europe PMC)	0.52	BioGRID, IntAct
PRKD1	anti bait coimmunoprecipitation, confocal microscopy, protein kinase assay	colocalization, phosphorylation reaction, physical association	15695390, (Europe PMC)	0.57	IntAct
PSEN1	Affinity Capture-Western, coimmunoprecipitation	physical, physical association	10635315, 11953314, 16126725, (Europe PMC)	0.40	BioGRID, IntAct, MINT
PSMC3IP	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
PVR	fluorescence microscopy	colocalization	17717529, (Europe PMC)	0.27	IntAct, MINT
RACGAP1	anti bait coimmunoprecipitation	association	22750944, (Europe PMC)	0.35	IntAct
RACK1	confocal microscopy	colocalization	21685945, (Europe PMC)	0.27	IntAct
RALBP1	anti bait coimmunoprecipitation	association	28851898, (Europe PMC)	0.35	IntAct
SCRIB	Proximity Label-MS, fluorescence microscopy	colocalization, physical	21701506, 25468996, (Europe PMC)	0.27	BioGRID, IntAct, MINT
SET	Affinity Capture-MS, pull down	association, physical	16212417, (Europe PMC)	0.35	BioGRID, IntAct
SFRP2	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
SKP2	Affinity Capture-Western, Biochemical Activity, anti tag coimmunoprecipitation	physical, physical association	20717963, 22770219, 26474281, (Europe PMC)	0.40	BioGRID, IntAct
SRC	Affinity Capture-Western, Proximity Label-MS, anti bait coimmunoprecipitation	association, physical, physical association	10744074, 18057010, 21685945, 25468996, (Europe PMC)	0.50	BioGRID, IntAct
STX17	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
TGM2	Affinity Capture-MS, surface plasmon resonance	physical, physical association	16212417, (Europe PMC)	0.40	BioGRID, IntAct
THRSP	two hybrid array	physical association	25640309, (Europe PMC)	0.37	IntAct, MINT
TMOD1	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT
TNS3	anti bait coimmunoprecipitation	association, physical association	19732724, (Europe PMC)	0.50	IntAct
TP53BP2	Proximity Label-MS, anti bait coimmunoprecipitation	association, physical	25344754, 25468996, (Europe PMC)	0.35	BioGRID, IntAct
XRCC5	Affinity Capture-MS, surface plasmon resonance	physical, physical association	16212417, (Europe PMC)	0.40	BioGRID, IntAct
YAP1	Proximity Label-MS, anti bait coimmunoprecipitation	association, physical	21376238, 25468996, (Europe PMC)	0.35	BioGRID, IntAct
ZNF510	two hybrid array	physical association	24412244, (Europe PMC)	0.37	IntAct, MINT

Top

CDH1