P30999 · CTND1_MOUSE
- ProteinCatenin delta-1
- GeneCtnnd1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids938 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 401 | Essential for interaction with cadherins | ||||
Sequence: K | ||||||
Site | 478 | Essential for interaction with cadherins | ||||
Sequence: N |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCatenin delta-1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP30999
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Interaction with GLIS2 promotes nuclear translocation (PubMed:17344476).
Detected at cell-cell contacts (By similarity).
NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm (By similarity).
CDH1 enhances cell membrane localization (By similarity).
Detected at cell-cell contacts (By similarity).
NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm (By similarity).
CDH1 enhances cell membrane localization (By similarity).
Isoform 2
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 622-623 | Abolishes nuclear localization. | ||||
Sequence: KK → AA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 37 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000064297 | 1-938 | Catenin delta-1 | |||
Sequence: MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANSLMANGTLTRRHQNGRFVGDADLERQKFSDLKLNGPQDHNHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETTDDGTTRRTETTVKKVVKTMTTRTVQPVPMGPDGLPVDASAVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYGRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRSYEDMIGEEVPPDQYYWAPLAQHERGSLASLDSLRKGMPPPSNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPILVGLLDHPKKEVHLGACGALKNISFGRDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDALIFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEALPTVANSTGPHAASCFGAKKGKDEWFSRGKKPTEDPANDTVDFPKRTSPARGYELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAIAELLTSEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVVSILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKELRKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIPMSNMGSNTKSLDNNYSTLNERGDHNRTLDRSGDLGDMEPLKGAPLMQKI | ||||||
Modified residue | 4 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 47 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 59 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 112 | Phosphotyrosine; by FYN | ||||
Sequence: Y | ||||||
Modified residue | 125 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 217 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 221 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 225 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 228 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 230 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 252 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 257 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 268 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 269 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 280 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 288 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 291 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 300 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 304 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 320 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 346 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 349 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 352 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 421 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 517 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 617 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 713 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 811 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 847 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 857 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 859 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 861 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 864 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 865 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 868 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 869 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 879 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 882 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 899 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 904 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 906 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 916 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 920 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK5. Dephosphorylated by PTPRJ (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in basal keratinocytes (at protein level).
Developmental stage
Expressed at the outer limiting membrane of the retina at 18.5 dpc.
Gene expression databases
Interaction
Subunit
Belongs to a multiprotein cell-cell adhesion complex that also contains E-cadherin/CDH1, alpha-catenin/CTNNA1, beta-catenin/CTNNB1, and gamma-catenin/JUP. Binds to the C-terminal fragment of PSEN1 and mutually competes for CDH1 (By similarity).
Interacts with ZBTB33 (PubMed:10207085, PubMed:12087177).
Interacts with GLIS2 (PubMed:17344476).
Interacts with FER (By similarity).
Interacts with NANOS1 (via N-terminal region) (By similarity).
Interacts (via N-terminus) with GNA12; the interaction regulates CDH1-mediated cell-cell adhesion (PubMed:15240885).
Interacts with GNA13 (PubMed:15240885).
Component of a cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity).
Interacts with CCDC85B (By similarity).
Interacts with PLPP3; negatively regulates the PLPP3-mediated stabilization of CTNNB1 (By similarity).
Interacts with ZBTB33 (PubMed:10207085, PubMed:12087177).
Interacts with GLIS2 (PubMed:17344476).
Interacts with FER (By similarity).
Interacts with NANOS1 (via N-terminal region) (By similarity).
Interacts (via N-terminus) with GNA12; the interaction regulates CDH1-mediated cell-cell adhesion (PubMed:15240885).
Interacts with GNA13 (PubMed:15240885).
Component of a cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By similarity).
Interacts with CCDC85B (By similarity).
Interacts with PLPP3; negatively regulates the PLPP3-mediated stabilization of CTNNB1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P30999 | Cttn Q60598 | 4 | EBI-529924, EBI-397955 | |
BINARY | P30999 | Ptpn11 P35235 | 3 | EBI-529924, EBI-397236 | |
BINARY | P30999 | Zbtb33 Q8BN78 | 3 | EBI-529924, EBI-1216314 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil, repeat, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-357 | Necessary and sufficient for interaction with CCDC85B | ||||
Sequence: MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANSLMANGTLTRRHQNGRFVGDADLERQKFSDLKLNGPQDHNHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETTDDGTTRRTETTVKKVVKTMTTRTVQPVPMGPDGLPVDASAVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYGRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRSYEDMIGEEVPPDQYYWAPLAQHERGSLASLDSLRKGM | ||||||
Coiled coil | 10-46 | |||||
Sequence: ASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRV | ||||||
Repeat | 358-395 | ARM 1 | ||||
Sequence: PPPSNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCY | ||||||
Repeat | 398-437 | ARM 2 | ||||
Sequence: DKVKTDVRKLKGIPILVGLLDHPKKEVHLGACGALKNISF | ||||||
Repeat | 441-475 | ARM 3 | ||||
Sequence: QDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGT | ||||||
Repeat | 476-516 | ARM 4 | ||||
Sequence: LWNLSSHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDC | ||||||
Repeat | 534-573 | ARM 5 | ||||
Sequence: LRNVSSERSEARRKLRECDGLVDALIFIVQAEIGQKDSDS | ||||||
Repeat | 583-624 | ARM 6 | ||||
Sequence: LRNLSYQVHREIPQAERYQEALPTVANSTGPHAASCFGAKKG | ||||||
Motif | 622-629 | In isoform P30999-2; Nuclear localization signal (NLS) | ||||
Sequence: KKGKDEWF | ||||||
Repeat | 653-693 | ARM 7 | ||||
Sequence: ARGYELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCA | ||||||
Repeat | 700-739 | ARM 8 | ||||
Sequence: RYIRSALRQEKALSAIAELLTSEHERVVKAASGALRNLAV | ||||||
Repeat | 740-780 | ARM 9 | ||||
Sequence: DARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVVSILN | ||||||
Repeat | 781-826 | ARM 10 | ||||
Sequence: TINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVL | ||||||
Compositional bias | 855-872 | Polar residues | ||||
Sequence: NASRSQSSHSYDDSTLPL | ||||||
Region | 855-938 | Disordered | ||||
Sequence: NASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIPMSNMGSNTKSLDNNYSTLNERGDHNRTLDRSGDLGDMEPLKGAPLMQKI | ||||||
Compositional bias | 873-888 | Basic and acidic residues | ||||
Sequence: IDRNQKSDKKPDREEI | ||||||
Compositional bias | 890-910 | Polar residues | ||||
Sequence: MSNMGSNTKSLDNNYSTLNER | ||||||
Compositional bias | 911-925 | Basic and acidic residues | ||||
Sequence: GDHNRTLDRSGDLGD |
Domain
ARM repeats 1 to 5 mediate interaction with cadherins.
Sequence similarities
Belongs to the beta-catenin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P30999-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length938
- Mass (Da)104,925
- Last updated2008-01-15 v2
- Checksum2F13DB7350355832
P30999-2
- Name2
P30999-3
- Name3
- Differences from canonical
- 880-900: Missing
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9Q986 | E9Q986_MOUSE | Ctnnd1 | 830 | ||
E9Q8Z4 | E9Q8Z4_MOUSE | Ctnnd1 | 868 | ||
E9Q8Z5 | E9Q8Z5_MOUSE | Ctnnd1 | 940 | ||
E9Q8Z6 | E9Q8Z6_MOUSE | Ctnnd1 | 961 | ||
E9Q8Z8 | E9Q8Z8_MOUSE | Ctnnd1 | 967 | ||
E9Q8Z9 | E9Q8Z9_MOUSE | Ctnnd1 | 878 | ||
E9Q901 | E9Q901_MOUSE | Ctnnd1 | 907 | ||
E9Q903 | E9Q903_MOUSE | Ctnnd1 | 892 | ||
E9Q904 | E9Q904_MOUSE | Ctnnd1 | 913 | ||
E9Q905 | E9Q905_MOUSE | Ctnnd1 | 866 | ||
E9Q906 | E9Q906_MOUSE | Ctnnd1 | 839 | ||
E9Q907 | E9Q907_MOUSE | Ctnnd1 | 860 | ||
D3Z7H6 | D3Z7H6_MOUSE | Ctnnd1 | 837 | ||
D3Z2H2 | D3Z2H2_MOUSE | Ctnnd1 | 884 | ||
D3Z2H7 | D3Z2H7_MOUSE | Ctnnd1 | 609 | ||
G3X9V2 | G3X9V2_MOUSE | Ctnnd1 | 932 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 405 | in Ref. 1; CAA79078 | ||||
Sequence: R → A | ||||||
Alternative sequence | VSP_030567 | 626-631 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 676 | in Ref. 1; CAA79078 | ||||
Sequence: K → N | ||||||
Sequence conflict | 715 | in Ref. 1; CAA79078 | ||||
Sequence: I → R | ||||||
Sequence conflict | 752 | in Ref. 1; CAA79078 | ||||
Sequence: I → R | ||||||
Compositional bias | 855-872 | Polar residues | ||||
Sequence: NASRSQSSHSYDDSTLPL | ||||||
Compositional bias | 873-888 | Basic and acidic residues | ||||
Sequence: IDRNQKSDKKPDREEI | ||||||
Alternative sequence | VSP_030568 | 880-900 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 890-910 | Polar residues | ||||
Sequence: MSNMGSNTKSLDNNYSTLNER | ||||||
Compositional bias | 911-925 | Basic and acidic residues | ||||
Sequence: GDHNRTLDRSGDLGD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z17804 EMBL· GenBank· DDBJ | CAA79078.1 EMBL· GenBank· DDBJ | mRNA | ||
AB093237 EMBL· GenBank· DDBJ | BAC41421.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK133193 EMBL· GenBank· DDBJ | BAE21551.1 EMBL· GenBank· DDBJ | mRNA | ||
AK161790 EMBL· GenBank· DDBJ | BAE36576.1 EMBL· GenBank· DDBJ | mRNA | ||
BC043108 EMBL· GenBank· DDBJ | AAH43108.1 EMBL· GenBank· DDBJ | mRNA | ||
BC054544 EMBL· GenBank· DDBJ | AAH54544.1 EMBL· GenBank· DDBJ | mRNA |