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Search results 801 to 900 out of 928 for Epcam

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Type Details Score
HT Experiment
GSE116272 | Generation of esophageal basal progenitor cells from human pluripotent stem cells
 
Experiment Type: RNA-Seq
Study Type: Baseline
Source: GEO
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Protein
A0A3Q4EI36
Organism: Mus musculus/domesticus
Length: 48  
Fragment?: true
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Publication
25163760 | -
 
First Author: Pavšič M
Year: 2014
Journal: Nat Commun
Title: Crystal structure and its bearing towards an understanding of key biological functions of EpCAM.
Volume: 5
Pages: 4764
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Protein Domain
IPR041630 | EpCAM_N
Type: Domain
Description: EpCAM (epithelial cell adhesion molecule), a stem and carcinoma cell marker, is a cell surface protein involved in homotypic cell-cell adhesion via intercellular oligomerization and proliferative signalling via proteolytic cleavage. Structure analysis indicate that it is composed of three domains: N-terminal domain, Thyroglobulin type-1A (TY) domain and the C-terminal domain. This entry represents the small and compact disulphide-rich N-terminal domain of 39 amino-acid residues [].
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Genotype
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Tg(Epcam-cre/ERT2)#Hmar/?
Background: involves: 129S4/SvJaeSor * C57BL/6
Zygosity: cn
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Tg(Epcam-cre/ERT2)#Hmar/?
Background: involves: 129S6/SvEvTac * C57BL/6
Zygosity: cn
Has Mutant Allele: true
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Protein
Q9D4X6
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
Q8CCR8
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
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Protein
A2BEE3
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
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Protein
A2ARK7
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
A0A571BG29
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
A0A571BDD5
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
Q9CXT3
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
J3QNM1
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
A4IF49
Organism: Mus musculus/domesticus
Length: 41  
Fragment?: true
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Protein
Q9D2K2
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
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Protein
G3UW52
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
A2BED8
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
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Protein
A0A571BDF8
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein
A0A060GU49
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
Q9D9H1
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
Q497M0
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
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Protein
Q9D519
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
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Protein
Q8K193
Organism: Mus musculus/domesticus
Length: 234  
Fragment?: false
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Protein Domain
IPR006187 | Claudin
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].
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HT Experiment
GSE85602 | A YY1-dependent increase in aerobic metabolism is indispensable for intestinal organogenesis
 
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: GEO
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HT Experiment
GSE165063 | A Single Cell Atlas of Alveolar Development
 
Experiment Type: RNA-Seq
Study Type: Baseline
Source: GEO
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Publication
27373157 | J:238584
First Author: Jahchan NS
Year: 2016
Journal: Cell Rep
Title: Identification and Targeting of Long-Term Tumor-Propagating Cells in Small Cell Lung Cancer.
Volume: 16
Issue: 3
Pages: 644-56
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Publication
30889382 | J:273225
First Author: Srivastava S
Year: 2019
Journal: Cancer Cell
Title: Logic-Gated ROR1 Chimeric Antigen Receptor Expression Rescues T Cell-Mediated Toxicity to Normal Tissues and Enables Selective Tumor Targeting.
Volume: 35
Issue: 3
Pages: 489-503.e8
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Publication
38039357 | J:343488
First Author: Li D
Year: 2023
Journal: Sci Adv
Title: EpCAM-targeting CAR-T cell immunotherapy is safe and efficacious for epithelial tumors.
Volume: 9
Issue: 48
Pages: eadg9721
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HT Experiment
GSE148874 | mRNA sequencing of esophageal cells and columnar cells from different tissues
 
Experiment Type: RNA-Seq
Study Type: Baseline
Source: GEO
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Publication
10562289 | J:94758
First Author: Furuse M
Year: 1999
Journal: J Cell Biol
Title: Manner of interaction of heterogeneous claudin species within and between tight junction strands.
Volume: 147
Issue: 4
Pages: 891-903
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Protein
B1AZQ8
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
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Protein
A2ANA3
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
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Protein
J3QQ48
Organism: Mus musculus/domesticus
Length: 107  
Fragment?: true
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Protein
A2AGU5
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
Q9D9N2
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
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Protein
Q80ZS5
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
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Protein
Q3V0X2
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Publication
9931503 | J:52586
First Author: Swisshelm K
Year: 1999
Journal: Gene
Title: SEMP1, a senescence-associated cDNA isolated from human mammary epithelial cells, is a member of an epithelial membrane protein superfamily.
Volume: 226
Issue: 2
Pages: 285-95
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Publication
24665401 | -
First Author: Van Itallie CM
Year: 2013
Journal: Tissue Barriers
Title: Claudin interactions in and out of the tight junction.
Volume: 1
Issue: 3
Pages: e25247
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Publication
20188437 | -
First Author: Inai T
Year: 2010
Journal: Eur J Cell Biol
Title: The protoplasmic or exoplasmic face association of tight junction particles cannot predict paracellular permeability or heterotypic claudin compatibility.
Volume: 89
Issue: 7
Pages: 547-56
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Publication
21372174 | -
First Author: Yamazaki Y
Year: 2011
Journal: Mol Biol Cell
Title: Role of claudin species-specific dynamics in reconstitution and remodeling of the zonula occludens.
Volume: 22
Issue: 9
Pages: 1495-504
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Protein Domain
IPR003554 | Claudin10
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-10 was identified through cDNA database searching, pursuingsequences similar to other claudin family members []. Human and mouseisoforms have been cloned. Claudin-10 shares ~20-45% overall similarity withother claudin family members at the amino acid level, displaying highestsimilarity to claudin-15.
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Protein Domain
IPR003556 | Claudin14
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-14 was identified through cDNA database searching, pursuingsequences similar to other claudin family members []. Human and mouseisoforms have been cloned. Claudin-14 shares ~25-45% overall similarity withother claudin family members at the amino acid level, displaying highestsimilarity to claudin-4.
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Protein Domain
IPR003550 | Claudin4
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-4 was originally termed Clostridium perfringens enterotoxin receptor (CPE-R). It was reclassified as claudin-4 on the basis of cDNA sequence similarity with claudins-1 and -2, and antibody studies thatshowed it to be expressed at tight junctions [].
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Protein Domain
IPR003553 | Claudin9
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-9 was identified through cDNA database searching, pursuing sequencessimilar to other claudin family members []. Human and mouse isoforms havebeen cloned. Claudin-9 shares ~25-70% overall similarity with other claudinfamily members at the amino acid level, displaying highest similarity toclaudin-6.
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Protein Domain
IPR003552 | Claudin7
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-7 was identified through searching expressed sequence tag (EST)databases for sequences similar to claudin-1 and -2. It was subsequently cloned and expressed in cells, where it was shown toconcentrate at tight junctions [].
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Protein Domain
IPR003548 | Claudin1
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-1 was the first member of the claudin family to be identified asa tight junction component []. The human isoform of claudin-1 was originally termed senescence-associated epithelial membrane protein 1 (SEMP1) [], but has since been reclassified.
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Protein Domain
IPR003549 | Claudin3
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B andtheir receptors, EphA and EphB [].Claudin-3 was originally termed rat ventral prostate 1 protein (RVP1), andClostridium perfringens enterotoxin receptor 2 (CPETR2). It was reclassified as claudin-3 on the basis of cDNA similarity with claudins-1 and-2, and antibody studies that showed it to be expressed at tight junctions[].
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Protein Domain
IPR003928 | Claudin18
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Human and mouse isoforms of claudin-18 have been cloned. Claudin-18 shares~22-40% overall similarity with other claudin family members at the aminoacid level, displaying highest similarity to claudin-1.
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Protein Domain
IPR008094 | Claudin15
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Human and mouse isoforms of claudin-15 have been cloned. Claudin-15 shares~25-45% overall similarity with other claudin family members at the aminoacid level, displaying highest similarity to claudin-10.
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Protein
B1AR47
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
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Protein
A0A338P6L6
Organism: Mus musculus/domesticus
Length: 50  
Fragment?: true
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Protein
Q921J6
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Publication
35676935 | J:327705
 
First Author: Liang D
Year: 2022
Journal: Front Cell Dev Biol
Title: Xenotransplantation of Human Spermatogonia Into Various Mouse Recipient Models.
Volume: 10
Pages: 883314
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Publication
29567647 | J:261513
First Author: Zhong L
Year: 2018
Journal: J Lipid Res
Title: Increased liver tumor formation in neutral sphingomyelinase-2-deficient mice.
Volume: 59
Issue: 5
Pages: 795-804
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Publication
22308459 | J:182609
First Author: Meirelles K
Year: 2012
Journal: Proc Natl Acad Sci U S A
Title: Human ovarian cancer stem/progenitor cells are stimulated by doxorubicin but inhibited by Mullerian inhibiting substance.
Volume: 109
Issue: 7
Pages: 2358-63
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Publication
38212454 | J:347103
First Author: Tokumasu R
Year: 2024
Journal: Sci Rep
Title: Transcription factor FoxO1 regulates myoepithelial cell diversity and growth.
Volume: 14
Issue: 1
Pages: 1069
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Publication
29545603 | J:264023
First Author: Wang J
Year: 2018
Journal: Oncogene
Title: Notch2 controls hepatocyte-derived cholangiocarcinoma formation in mice.
Volume: 37
Issue: 24
Pages: 3229-3242
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Publication
31628112 | J:284185
 
First Author: Szabo R
Year: 2019
Journal: Development
Title: Matriptase drives early-onset intestinal failure in a mouse model of congenital tufting enteropathy.
Volume: 146
Issue: 22
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Publication
19188665 | J:148293
First Author: Ziegler A
Year: 2009
Journal: Blood
Title: EpCAM, a human tumor-associated antigen promotes Th2 development and tumor immune evasion.
Volume: 113
Issue: 15
Pages: 3494-502
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Publication
34433637 | J:318716
 
First Author: Belmontes B
Year: 2021
Journal: Sci Transl Med
Title: Immunotherapy combinations overcome resistance to bispecific T cell engager treatment in T cell-cold solid tumors.
Volume: 13
Issue: 608
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Publication
36401092 | J:361472
First Author: Spooner-Harris M
Year: 2023
Journal: Cell Tissue Res
Title: A re-appraisal of mesenchymal-epithelial transition (MET) in endometrial epithelial remodeling.
Volume: 391
Issue: 2
Pages: 393-408
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Publication
17617629 | J:137741
First Author: Kosterink JG
Year: 2007
Journal: J Immunol
Title: Biodistribution studies of epithelial cell adhesion molecule (EpCAM)-directed monoclonal antibodies in the EpCAM-transgenic mouse tumor model.
Volume: 179
Issue: 2
Pages: 1362-8
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Publication
28924038 | J:248567
First Author: He S
Year: 2017
Journal: J Biol Chem
Title: Passive DNA demethylation preferentially up-regulates pluripotency-related genes and facilitates the generation of induced pluripotent stem cells.
Volume: 292
Issue: 45
Pages: 18542-18555
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Publication
21677668 | J:282082
First Author: Eisenwort G
Year: 2011
Journal: J Invest Dermatol
Title: Identification of TROP2 (TACSTD2), an EpCAM-like molecule, as a specific marker for TGF-β1-dependent human epidermal Langerhans cells.
Volume: 131
Issue: 10
Pages: 2049-57
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Publication
26484284 | J:355989
 
First Author: Holik AZ
Year: 2015
Journal: Genom Data
Title: Transcriptome and H3K27 tri-methylation profiling of Ezh2-deficient lung epithelium.
Volume: 5
Pages: 346-51
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Protein
Q99JW5
Organism: Mus musculus/domesticus
Length: 315  
Fragment?: false
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Protein
A0A3Q4EHR5
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
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Publication
25132272 | J:222529
First Author: Morris SM
Year: 2015
Journal: Oncogene
Title: TGF-β signaling alters the pattern of liver tumorigenesis induced by Pten inactivation.
Volume: 34
Issue: 25
Pages: 3273-82
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Publication
36433941 | J:332107
First Author: Sequera C
Year: 2022
Journal: Cell Death Dis
Title: MYC and MET cooperatively drive hepatocellular carcinoma with distinct molecular traits and vulnerabilities.
Volume: 13
Issue: 11
Pages: 994
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Publication
32984356 | J:298971
 
First Author: Tan C
Year: 2020
Journal: Front Cell Dev Biol
Title: Extracellular CIRP Induces Inflammation in Alveolar Type II Cells via TREM-1.
Volume: 8
Pages: 579157
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Publication
37033950 | J:334747
 
First Author: Avlas S
Year: 2023
Journal: Front Immunol
Title: CD300b regulates intestinal inflammation and promotes repair in colitis.
Volume: 14
Pages: 1050245
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Publication
25831548 | J:220813
First Author: Gong Y
Year: 2015
Journal: Proc Natl Acad Sci U S A
Title: KLHL3 regulates paracellular chloride transport in the kidney by ubiquitination of claudin-8.
Volume: 112
Issue: 14
Pages: 4340-5
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Publication
11309411 | -
First Author: Tiwari-Woodruff SK
Year: 2001
Journal: J Cell Biol
Title: OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates proliferation and migration of oligodendrocytes.
Volume: 153
Issue: 2
Pages: 295-305
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Protein
Q8BGV3
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: false
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Publication
20921420 | J:165532
First Author: Hou J
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: Claudin-4 forms paracellular chloride channel in the kidney and requires claudin-8 for tight junction localization.
Volume: 107
Issue: 42
Pages: 18010-5
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Publication
9192844 | J:41222
First Author: Sirotkin H
Year: 1997
Journal: Genomics
Title: Identification, characterization, and precise mapping of a human gene encoding a novel membrane-spanning protein from the 22q11 region deleted in velo-cardio-facial syndrome.
Volume: 42
Issue: 2
Pages: 245-51
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Publication
10810088 | J:62301
First Author: Hirano T
Year: 2000
Journal: Genome Res
Title: Null mutation of PCLN-1/Claudin-16 results in bovine chronic interstitial nephritis.
Volume: 10
Issue: 5
Pages: 659-63
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Publication
10390358 | -
First Author: Simon DB
Year: 1999
Journal: Science
Title: Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption.
Volume: 285
Issue: 5424
Pages: 103-6
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Protein Domain
IPR005411 | Claudin2
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-2 was initially isolated as a peptide fragment from TJ-enriched junctional cell fractions. Following sequencing and similarity searching it was cloned and expressed in cells, where it was shown to concentrate at TJs []. Human and mouse isoforms have been identified. Claudin-2 shares ~22-46% overall similarity with other claudin family members at the aminoacid level, displaying highest similarity to claudin-14.
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Protein Domain
IPR003555 | Claudin11
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-11 was originally termed oligodendrocyte-specific protein (OSP).It was reclassified as claudin-11 due to its sequence similarity to claudins and its ability to form TJ strands in transfected fibroblasts.Claudin-11 expression is highly regulated during development and it has been postulated that it may play an important role in the growth and differentiation of oligodendrocytes and other cells outside the CNS [].
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Protein Domain
IPR003551 | Claudin5
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-5 was originally termed lung-specific membrane protein, brainendothelial cell clone 1 protein (BEC1), and transmembrane protein deletedin velo-cardio-facial syndrome (TMVCF). It was reclassified as claudin-5on the basis of cDNA sequence similarity with claudins-1 and -2, and antibody studies that showed it to be expressed at tight junctions []. Claudin-5 may play an important role in development, since the gene is frequently deleted in velo-cardio-facial/DiGeorge syndrome patients [].
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Protein Domain
IPR003926 | Claudin8
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-8 was identified through searching expressed sequence tag (EST) databases for sequences similar to claudin-1 and -2 []. It was subsequently cloned and expressed in cells, where it was shown to concentrate at tight junctions. Human and mouse isoforms have been identified. Claudin-8 shares ~26-58% overall similarity with other claudin family members at the amino acid level, displaying highest similarity to claudin-17.Claudin-8 interacts with claudin-4 and recruits it to tight junction in the kidney. In the collecting duct, this interaction is required for the anion-selective paracellular pathway in which chloride reabsorption is coupled with sodium reabsorption [, ].
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Protein Domain
IPR003925 | Claudin6
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-6 was identified through searching expressed sequence tag (EST)databases for sequences similar to claudin-1 and -2 []. It was subsequently cloned and expressed in cells, where it was shown to concentrate at tight junctions. Human and mouse isoforms have beenidentified. Claudin-6 shares ~25-70% overall similarity with other claudin family members at the amino acid level, displaying highest similarity to claudin-9.
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Protein Domain
IPR003927 | Claudin16
Type: Family
Description: Claudins form the paracellular tight junction seal in epithelial tissues. In humans, 24 claudins (claudin 1-24) have been identified. Their ability to polymerise and form strands is affected by the cell types [, , ]. They can also form heteropolymers with each other within and between tight junction strands []. Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 []. They also interact with non-tight junction proteins, such as cell adhesion proteins EpCam and tetraspanins and the signaling proteins, ephrin A and B and their receptors, EphA and EphB [].Claudin-16 was originally termed paracellin-1. It was re-classified as claudin-16 on the basis of its sequence similarity to the claudin family[]. Claudin-16 is involved in renal paracellular Mg2+ resorption and is required for selective paracellular conductance []. Defects in the claudin-16 gene are associated with an autosomal recessive chronic interstitial nephritis with diffuse zonal fibrosis (CINF) [, ].
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Publication
9892664 | J:61744
First Author: Morita K
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands.
Volume: 96
Issue: 2
Pages: 511-6
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Protein
Q9Z0S5
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
P56857
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
O88552
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: false
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Protein
O88551
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
Q60771
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
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Protein
Q9Z0S3
Organism: Mus musculus/domesticus
Length: 239  
Fragment?: false
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Protein
Q925N4
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
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Protein
Q9Z0S6
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: false
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Protein
Q9Z0G9
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
O35054
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
Q9Z262
Organism: Mus musculus/domesticus
Length: 219  
Fragment?: false
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Protein
Q9Z261
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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