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Search results 301 to 400 out of 447 for Apc2

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Type Details Score
GXD Expression
GXD Expression
 
Probe: MGI:4423063
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4823173
Age: embryonic day 14.5
Image: euxassay_007719_17
Specimen Label: euxassay_007719_17
Detected: true
Specimen Num: 17
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GXD Expression
GXD Expression
 
Probe: MGI:4423063
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4823173
Age: embryonic day 14.5
Image: euxassay_007719_18
Specimen Label: euxassay_007719_18
Detected: true
Specimen Num: 18
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GXD Expression
GXD Expression
 
Probe: MGI:4423063
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4823173
Age: embryonic day 14.5
Image: euxassay_007719_19
Specimen Label: euxassay_007719_19
Detected: true
Specimen Num: 19
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GXD Expression
GXD Expression
 
Probe: MGI:4423063
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4823173
Age: embryonic day 14.5
Image: euxassay_007719_20
Specimen Label: euxassay_007719_20
Detected: true
Specimen Num: 20
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GXD Expression
GXD Expression
 
Probe: MGI:3042987
Assay Type: RNA in situ
Annotation Date: 2004-06-17
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3521728
Pattern: Not Specified
Stage: TS28
Assay Id: MGI:3043016
Age: postnatal adult
Image: 7E
Specimen Label: 7E
Detected: true
Specimen Num: 5
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GXD Expression
GXD Expression
   
Probe: MGI:4423063
Assay Type: RNA in situ
Annotation Date: 2014-02-07
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:2826626
Stage: TS26
Assay Id: MGI:5540603
Age: embryonic day 17.5
Image: GUDMAP:14775
Specimen Label: GUDMAP:14775
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
   
Probe: MGI:4423063
Assay Type: RNA in situ
Annotation Date: 2014-02-07
Strength: Absent
Sex: Male
Emaps: EMAPS:2826628
Stage: TS28
Assay Id: MGI:5540603
Age: postnatal day 84
Image: GUDMAP:14776
Specimen Label: GUDMAP:14776
Detected: false
Specimen Num: 2
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GXD Expression
GXD Expression
   
Probe: MGI:4423063
Assay Type: RNA in situ
Annotation Date: 2014-02-07
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:2772126
Stage: TS26
Assay Id: MGI:5540603
Age: embryonic day 17.5
Image: GUDMAP:14775
Specimen Label: GUDMAP:14775
Detected: false
Specimen Num: 1
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Publication
26516211 | J:227851
First Author: Pataskar A
Year: 2016
Journal: EMBO J
Title: NeuroD1 reprograms chromatin and transcription factor landscapes to induce the neuronal program.
Volume: 35
Issue: 1
Pages: 24-45
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Publication
9601641 | J:319997
First Author: Hart MJ
Year: 1998
Journal: Curr Biol
Title: Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3 beta.
Volume: 8
Issue: 10
Pages: 573-81
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Publication
35915179 | J:335582
First Author: Yuan W
Year: 2022
Journal: Nat Neurosci
Title: Temporally divergent regulatory mechanisms govern neuronal diversification and maturation in the mouse and marmoset neocortex.
Volume: 25
Issue: 8
Pages: 1049-1058
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Publication
25535916 | J:311814
First Author: Eom TY
Year: 2014
Journal: Dev Cell
Title: Differential regulation of microtubule severing by APC underlies distinct patterns of projection neuron and interneuron migration.
Volume: 31
Issue: 6
Pages: 677-89
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Publication
- | J:193309
       
First Author: Mouse Genome Informatics Scientfic Curators
Year: 2013
Title: Curated associations of genes in MGI and UniProt sequence records
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Publication
- | J:73065
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
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Publication
24952961 | J:215487
First Author: Thompson CL
Year: 2014
Journal: Neuron
Title: A high-resolution spatiotemporal atlas of gene expression of the developing mouse brain.
Volume: 83
Issue: 2
Pages: 309-323
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Publication
- | J:204812
     
First Author: International Mouse Strain Resource
Year: 2014
Journal: Database Download
Title: MGI download of germline transmission data for alleles from IMSR strain data
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Publication
- | J:148605
     
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
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Publication
- | J:171409
     
First Author: GUDMAP Consortium
Year: 2004
Journal: www.gudmap.org
Title: GUDMAP: the GenitoUrinary Development Molecular Anatomy Project
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
- | J:155856
       
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Publication
16602821 | J:162220
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein
Q8BZQ7
Organism: Mus musculus/domesticus
Length: 837  
Fragment?: false
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DO Term
DOID:0112104 | Sotos syndrome 3
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Interaction Experiment
Morgan D (2002)
Description: Expression analyses and interaction with the anaphase promoting complex protein Apc2 suggest a role for inversin in primary cilia and involvement in the cell cycle.
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Publication
12471060 | -
First Author: Morgan D
Year: 2002
Journal: Hum Mol Genet
Title: Expression analyses and interaction with the anaphase promoting complex protein Apc2 suggest a role for inversin in primary cilia and involvement in the cell cycle.
Volume: 11
Issue: 26
Pages: 3345-50
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DO Term
DOID:0081218 | autosomal recessive intellectual developmental disorder 74
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Protein Coding Gene
MGI:2139135 | Anapc2
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
11514192 | -
First Author: Dikovskaya D
Year: 2001
Journal: Trends Cell Biol
Title: The adenomatous polyposis coli protein: in the limelight out at the edge.
Volume: 11
Issue: 9
Pages: 378-84
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Protein Domain
IPR009232 | EB1-bd
Type: Domain
Description: This region at the C terminus of the APC proteins binds the microtubule-associating protein EB-1 []. At the C terminus of the alignment is also a PDZ-binding domain. A short motif in the middle of the region appears to be found in the APC2 proteins (e.g. ).
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Publication
14724179 | J:87782
First Author: Wirth KG
Year: 2004
Journal: Genes Dev
Title: Loss of the anaphase-promoting complex in quiescent cells causes unscheduled hepatocyte proliferation.
Volume: 18
Issue: 1
Pages: 88-98
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Publication
29533772 | J:347406
First Author: Saito-Diaz K
Year: 2018
Journal: Dev Cell
Title: APC Inhibits Ligand-Independent Wnt Signaling by the Clathrin Endocytic Pathway.
Volume: 44
Issue: 5
Pages: 566-581.e8
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Protein
E0CYT5
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: true
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Protein
Q3TLY0
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: false
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Protein
A0A3Q4EBZ1
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: false
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Protein
F6ZZK0
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: true
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Protein
Q05CY9
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Protein
D3Z2H3
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
Q3UD60
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: true
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Protein
F6UV36
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
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Protein
E9PXT5
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: false
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Protein
Q78GU9
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: false
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Publication
8681378 | -
First Author: Kipreos ET
Year: 1996
Journal: Cell
Title: cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family.
Volume: 85
Issue: 6
Pages: 829-39
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Publication
11961546 | J:76096
First Author: Zheng N
Year: 2002
Journal: Nature
Title: Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.
Volume: 416
Issue: 6882
Pages: 703-9
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Publication
15537541 | -
First Author: Goldenberg SJ
Year: 2004
Journal: Cell
Title: Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases.
Volume: 119
Issue: 4
Pages: 517-28
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Publication
15688063 | -
First Author: Petroski MD
Year: 2005
Journal: Nat Rev Mol Cell Biol
Title: Function and regulation of cullin-RING ubiquitin ligases.
Volume: 6
Issue: 1
Pages: 9-20
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Protein
H7BX52
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: false
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Protein
A0A0N4SUW1
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: false
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Protein Domain
IPR016157 | Cullin_CS
Type: Conserved_site
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].This entry represents a conserved site found in various cullin proteins.
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Protein Domain
IPR016159 | Cullin_repeat-like_dom_sf
Type: Homologous_superfamily
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].This superfamily represents the N-terminal cullin repeat-containing domain; these repeats form a domain with a multi-helical 2-layered alpha/alpha structure, which in turn is folded into a right-handed superhelix. A similar structural domain is found in exocyst complex components such as EXO70 and EXO84.
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Protein Domain
IPR016158 | Cullin_homology
Type: Domain
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].
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Protein Domain
IPR036317 | Cullin_homology_sf
Type: Homologous_superfamily
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].This entry represents the cullin-homology domain superfamily. This domain is composed of three subdomains: a 4-helical bundle domain, an alpha+beta domain, and a winged helix-like domain.
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Protein Domain
IPR001373 | Cullin_N
Type: Domain
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact withspecific adaptor proteins [, , ].This entry represents the N-terminal region of cullin proteins, which consists of several domains, including cullin repeat domain, a 4-helical bundle domain, an alpha+beta domain, and a winged helix-like domain.
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Protein Domain
IPR045093 | Cullin
Type: Family
Description: Cullins are a family of hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3). Cullins are found throughout eukaryotes. Humans express seven cullins (Cul1, 2, 3, 4A, 4B, 5 and 7), each forming part of a multi-subunit ubiquitin complex. Cullin-RING ubiquitin ligases (CRLs), such as Cul1 (SCF) [], play an essential role in targeting proteins for ubiquitin-mediated destruction; as such, they are diverse in terms of composition and function, regulating many different processes from glucose sensing and DNA replication to limb patterning and circadian rhythms. The catalytic core of CRLs consists of a RING protein and a cullin family member. For Cul1, the C-terminal cullin-homology domain binds the RING protein. The RING protein appears to function as a docking site for ubiquitin-conjugating enzymes (E2s). Other proteins contain a cullin-homology domain, such as the APC2 subunit of the anaphase-promoting complex/cyclosome and the p53 cytoplasmic anchor PARC; both APC2 and PARC have ubiquitin ligase activity. The N-terminal region of cullins is more variable, and is used to interact with specific adaptor proteins [, , ].
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Protein
Q3TPM3
Organism: Mus musculus/domesticus
Length: 699  
Fragment?: true
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Protein
Q05DR6
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: true
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Publication
19249208 | J:148959
First Author: McGuinness BE
Year: 2009
Journal: Curr Biol
Title: Regulation of APC/C activity in oocytes by a Bub1-dependent spindle assembly checkpoint.
Volume: 19
Issue: 5
Pages: 369-80
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Protein
Q9D4H8
Organism: Mus musculus/domesticus
Length: 745  
Fragment?: false
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Protein
Q9WTX6
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: false
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Protein
A2A432
Organism: Mus musculus/domesticus
Length: 970  
Fragment?: false
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Protein
Q9D5V5
Organism: Mus musculus/domesticus
Length: 780  
Fragment?: false
•
•
•
•
•
Protein
Q9JLV5
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: false
•
•
•
•
•
Protein
Q3TCH7
Organism: Mus musculus/domesticus
Length: 759  
Fragment?: false
•
•
•
•
•
Protein
Q2M4H5
Organism: Mus musculus/domesticus
Length: 780  
Fragment?: false
•
•
•
•
•
Protein
Q8R1T2
Organism: Mus musculus/domesticus
Length: 594  
Fragment?: false
•
•
•
•
•
Protein
Q6ZQ84
Organism: Mus musculus/domesticus
Length: 792  
Fragment?: true
•
•
•
•
•
Protein
Q571A2
Organism: Mus musculus/domesticus
Length: 748  
Fragment?: true
•
•
•
•
•
Protein
E9Q6Z0
Organism: Mus musculus/domesticus
Length: 651  
Fragment?: false
•
•
•
•
•
Protein
E9PXY1
Organism: Mus musculus/domesticus
Length: 896  
Fragment?: false
•
•
•
•
•
Protein
E9Q4T8
Organism: Mus musculus/domesticus
Length: 702  
Fragment?: false
•
•
•
•
•
Protein
Q3UIA5
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: false
•
•
•
•
•
Protein
G3X914
Organism: Mus musculus/domesticus
Length: 855  
Fragment?: false
•
•
•
•
•
Protein
E9PV12
Organism: Mus musculus/domesticus
Length: 828  
Fragment?: false
•
•
•
•
•
Protein
Q8R0X2
Organism: Mus musculus/domesticus
Length: 377  
Fragment?: false
•
•
•
•
•
Protein
Q3TAW5
Organism: Mus musculus/domesticus
Length: 246  
Fragment?: false
•
•
•
•
•
Protein
Q921D1
Organism: Mus musculus/domesticus
Length: 327  
Fragment?: true
•
•
•
•
•
Protein
E9PV69
Organism: Mus musculus/domesticus
Length: 347  
Fragment?: false
•
•
•
•
•
Publication
10766743 | -
First Author: Hoier EF
Year: 2000
Journal: Genes Dev
Title: The Caenorhabditis elegans APC-related gene apr-1 is required for epithelial cell migration and Hox gene expression.
Volume: 14
Issue: 7
Pages: 874-86
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•
•
•
•
Protein Domain
IPR026818 | Apc_fam
Type: Family
Description: Adenomatous polyposis coli (APC) is a tumor suppressor protein that induces thedegradation of oncogenic beta-catenin and negatively regulates Wnt signalling []. It has roles in regulating cell migration, DNA replication/repair, mitosis and apoptosis [, ]. APC regulates cell-cell adhesion and cell migration through activating the APC-stimulated guanine nucleotide-exchange factor (GEF; Asef) [, ]. It acts as a mediator of ERBB2-dependent stabilisation of microtubules at the cell cortex []. It is requiredfor the localisation of MACF1/ACF7 to the cell membrane and this localisation of MACF1/ACF7 is critical for its function in microtubule stabilisation []. APC mutations are particularly prevalent in colorectal cancer [].The adenomatous polyposis coli protein family also includes APC2 [, ]and APC-related protein 1 [].
•
•
•
•
•
Protein
Q812A5
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: false
•
•
•
•
•




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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