UniProtKB - P30999 (CTND1_MOUSE)
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- BLAST>sp|P30999|CTND1_MOUSE Catenin delta-1 OS=Mus musculus OX=10090 GN=Ctnnd1 PE=1 SV=2 MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANSLMANGTL TRRHQNGRFVGDADLERQKFSDLKLNGPQDHNHLLYSTIPRMQEPGQIVETYTEEDPEGA MSVVSVETTDDGTTRRTETTVKKVVKTMTTRTVQPVPMGPDGLPVDASAVSNNYIQTLGR DFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYGRHYEDGYPGGSDNYGSLSRVTRIEER YRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMS DYGTARRTGTPSDPRRRLRSYEDMIGEEVPPDQYYWAPLAQHERGSLASLDSLRKGMPPP SNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPILVGLLDHP KKEVHLGACGALKNISFGRDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLS SHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSE RSEARRKLRECDGLVDALIFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERY QEALPTVANSTGPHAASCFGAKKGKDEWFSRGKKPTEDPANDTVDFPKRTSPARGYELLF QPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAIAELLT SEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVVSILN TINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKELRKPLE KEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIPMSNMGSNTKSL DNNYSTLNERGDHNRTLDRSGDLGDMEPLKGAPLMQKI
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Protein
Catenin delta-1
Gene
Ctnnd1
Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). Associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage.By similarity3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression."
Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
J. Cell Sci. 117:2675-2686(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 622-LYS-LYS-623. - Ref.10"The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of the beta-catenin/TCF target gene matrilysin."
Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C., Daniel J.M.
Exp. Cell Res. 305:253-265(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.13"The transcriptional repressor Glis2 is a novel binding partner for p120 catenin."
Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., Birchmeier W., Briscoe J., Fujita Y.
Mol. Biol. Cell 18:1918-1927(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 401 | Essential for interaction with cadherinsBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 478 | Essential for interaction with cadherinsBy similarity | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- cadherin binding Source: MGI
- protein domain specific binding Source: MGI <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein phosphatase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- receptor binding Source: MGI
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cell adhesion Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cell-cell adhesion Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- epithelial cell differentiation involved in salivary gland development Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- glomerulus morphogenesis Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- keratinocyte differentiation Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- kidney development Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- morphogenesis of a polarized epithelium Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of canonical Wnt signaling pathway Source: MGI
- positive regulation of peptidyl-tyrosine autophosphorylation Source: MGI <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactioni
- positive regulation of protein processing Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of transcription, DNA-templated Source: UniProtKB-KW
- salivary gland morphogenesis Source: MGI <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- transcription, DNA-templated Source: UniProtKB-KW
- Wnt signaling pathway Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Biological process | Cell adhesion, Transcription, Transcription regulation, Wnt signaling pathway |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-MMU-418990. Adherens junctions interactions. R-MMU-5218920. VEGFR2 mediated vascular permeability. |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Catenin delta-1Alternative name(s): Cadherin-associated Src substrate Short name: CAS p120 catenin Short name: p120(ctn) p120(cas) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:Ctnnd1 Synonyms:Catns, Kiaa0384 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Mus musculus (Mouse) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 10090 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Mouse genome database (MGD) from Mouse Genome Informatics (MGI) More...MGIi | MGI:105100. Ctnnd1. |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression."
Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
J. Cell Sci. 117:2675-2686(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 622-LYS-LYS-623. - Ref.13"The transcriptional repressor Glis2 is a novel binding partner for p120 catenin."
Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., Birchmeier W., Briscoe J., Fujita Y.
Mol. Biol. Cell 18:1918-1927(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
- Nucleus 2 Publications
Plasma membrane
- Cell membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.13"The transcriptional repressor Glis2 is a novel binding partner for p120 catenin."
Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., Birchmeier W., Briscoe J., Fujita Y.
Mol. Biol. Cell 18:1918-1927(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
- Cell membrane 1 Publication
Other locations
- Cytoplasm 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression."
Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
J. Cell Sci. 117:2675-2686(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 622-LYS-LYS-623. - Ref.13"The transcriptional repressor Glis2 is a novel binding partner for p120 catenin."
Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., Birchmeier W., Briscoe J., Fujita Y.
Mol. Biol. Cell 18:1918-1927(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
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).By similarity- Cytoplasm 2 Publications
- Ref.13"The transcriptional repressor Glis2 is a novel binding partner for p120 catenin."
Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., Birchmeier W., Briscoe J., Fujita Y.
Mol. Biol. Cell 18:1918-1927(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi
1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Isoform 2 :
Nucleus
- Nucleus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression."
Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
J. Cell Sci. 117:2675-2686(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 622-LYS-LYS-623.
- Nucleus 1 Publication
Cytosol
- cytosol Source: MGI
Nucleus
- nucleus Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Plasma Membrane
- flotillin complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- bicellular tight junction Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cell-cell adherens junction Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cell-cell junction Source: MGI
- cytoplasm Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- lamellipodium Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- membrane Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- midbody Source: UniProtKB
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell membrane, Cytoplasm, Membrane, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 622 – 623 | KK → AA: Abolishes nuclear localization. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 2 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000064297 | 1 – 938 | Catenin delta-1Add BLAST | 938 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1 | N-acetylmethionineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 4 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 47 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 59 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 112 | Phosphotyrosine; by FYNBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 125 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 217 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 221 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 225 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 228 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 230 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 252 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 257 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 268 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 269 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 280 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 288 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 291 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 300 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 304 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 320 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 346 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 349 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 352 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 421 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 517 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 617 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 713 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 811 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 847 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 857 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 859 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 861 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 864 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 865 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 868 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 869 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 879 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 882 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 899 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 904 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 906 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 916 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 920 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK5. Dephosphorylated by PTPRJ (By similarity).By similarity
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | P30999. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P30999. |
PeptideAtlas More...PeptideAtlasi | P30999. |
PRoteomics IDEntifications database More...PRIDEi | P30999. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P30999. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P30999. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P30999. |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSMUSG00000034101. |
CleanEx database of gene expression profiles More...CleanExi | MM_CTNND1. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P30999. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P30999. MM. |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
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).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toi
4 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.6"The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor."
Daniel J.M., Reynolds A.B.
Mol. Cell. Biol. 19:3614-3623(1999) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZBTB33. - Ref.7"The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein that recognizes both a sequence-specific consensus and methylated CpG dinucleotides."
Daniel J.M., Spring C.M., Crawford H.C., Reynolds A.B., Baig A.
Nucleic Acids Res. 30:2911-2919(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZBTB33. - Ref.9"A role for Galpha12/Galpha13 in p120ctn regulation."
Krakstad B.F., Ardawatia V.V., Aragay A.M.
Proc. Natl. Acad. Sci. U.S.A. 101:10314-10319(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GNA12 AND GNA13. - Ref.13"The transcriptional repressor Glis2 is a novel binding partner for p120 catenin."
Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., Birchmeier W., Briscoe J., Fujita Y.
Mol. Biol. Cell 18:1918-1927(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
<p>This subsection of the ‘<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>’ section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Cttn | Q60598 | 4 | EBI-529924,EBI-397955 | |
| PLEKHA7 | Q6IQ23 | 3 | EBI-529924,EBI-2125301 | From Homo sapiens. |
| Ptpn11 | P35235 | 3 | EBI-529924,EBI-397236 | |
| Zbtb33 | Q8BN78 | 3 | EBI-529924,EBI-1216314 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- cadherin binding Source: MGI
- protein domain specific binding Source: MGI <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein phosphatase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- receptor binding Source: MGI
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 198513. 24 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P30999. |
Database of interacting proteins More...DIPi | DIP-31972N. |
Protein interaction database and analysis system More...IntActi | P30999. 24 interactors. |
Molecular INTeraction database More...MINTi | P30999. |
STRING: functional protein association networks More...STRINGi | 10090.ENSMUSP00000064518. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P30999. |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P30999. |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 358 – 395 | ARM 1Add BLAST | 38 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 398 – 437 | ARM 2Add BLAST | 40 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 441 – 475 | ARM 3Add BLAST | 35 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 476 – 516 | ARM 4Add BLAST | 41 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 534 – 573 | ARM 5Add BLAST | 40 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 583 – 624 | ARM 6Add BLAST | 42 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 653 – 693 | ARM 7Add BLAST | 41 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 700 – 739 | ARM 8Add BLAST | 40 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 740 – 780 | ARM 9Add BLAST | 41 | |
| <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 781 – 826 | ARM 10Add BLAST | 46 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 10 – 46 | Sequence analysisAdd BLAST | 37 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
ARM repeats 1 to 5 mediate interaction with cadherins.By similarity
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the beta-catenin family.Curated
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Coiled coil, RepeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1048. Eukaryota. ENOG410Y21Q. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119167. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231862. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004284. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P30999. |
KEGG Orthology (KO) More...KOi | K05690. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P30999. |
TreeFam database of animal gene trees More...TreeFami | TF321877. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.25.10.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000225. Armadillo. IPR028439. Catenin_d1. IPR028435. Plakophilin/d_Catenin. |
The PANTHER Classification System More...PANTHERi | PTHR10372. PTHR10372. 1 hit. PTHR10372:SF6. PTHR10372:SF6. 1 hit. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00514. Arm. 3 hits. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00185. ARM. 7 hits. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48371. SSF48371. 2 hits. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50176. ARM_REPEAT. 3 hits. |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Isoform 1 (identifier: P30999-1) [UniParc]FASTAAdd to basketAdded to basketShow »
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.
10 20 30 40 50
MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD
60 70 80 90 100
ANSLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP
110 120 130 140 150
RMQEPGQIVE TYTEEDPEGA MSVVSVETTD DGTTRRTETT VKKVVKTMTT
160 170 180 190 200
RTVQPVPMGP DGLPVDASAV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA
210 220 230 240 250
TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA
260 270 280 290 300
PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS
310 320 330 340 350
DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL
360 370 380 390 400
DSLRKGMPPP SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV
410 420 430 440 450
KTDVRKLKGI PILVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC
460 470 480 490 500
DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE
510 520 530 540 550
VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE
560 570 580 590 600
CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY
610 620 630 640 650
QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT
660 670 680 690 700
SPARGYELLF QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR
710 720 730 740 750
YIRSALRQEK ALSAIAELLT SEHERVVKAA SGALRNLAVD ARNKELIGKH
760 770 780 790 800
AIPNLVKNLP GGQQNSSWNF SEDTVVSILN TINEVIAENL EAAKKLRETQ
810 820 830 840 850
GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE KEGWKKSDFQ
860 870 880 890 900
VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIPM SNMGSNTKSL
910 920 930
DNNYSTLNER GDHNRTLDRS GDLGDMEPLK GAPLMQKI
Length:938
Mass (Da):104,925
Last modified:January 15, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i2F13DB7350355832
Isoform 2 (identifier: P30999-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
626-631: Missing.
880-900: Missing.
10 20 30 40 50
MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD
60 70 80 90 100
ANSLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP
110 120 130 140 150
RMQEPGQIVE TYTEEDPEGA MSVVSVETTD DGTTRRTETT VKKVVKTMTT
160 170 180 190 200
RTVQPVPMGP DGLPVDASAV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA
210 220 230 240 250
TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA
260 270 280 290 300
PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS
310 320 330 340 350
DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL
360 370 380 390 400
DSLRKGMPPP SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV
410 420 430 440 450
KTDVRKLKGI PILVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC
460 470 480 490 500
DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE
510 520 530 540 550
VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE
560 570 580 590 600
CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY
610 620 630 640 650
QEALPTVANS TGPHAASCFG AKKGKGKKPT EDPANDTVDF PKRTSPARGY
660 670 680 690 700
ELLFQPEVVR IYISLLKESK TPAILEASAG AIQNLCAGRW TYGRYIRSAL
710 720 730 740 750
RQEKALSAIA ELLTSEHERV VKAASGALRN LAVDARNKEL IGKHAIPNLV
760 770 780 790 800
KNLPGGQQNS SWNFSEDTVV SILNTINEVI AENLEAAKKL RETQGIEKLV
810 820 830 840 850
LINKSGNRSE KEVRAAALVL QTIWGYKELR KPLEKEGWKK SDFQVNLNNA
860 870 880 890 900
SRSQSSHSYD DSTLPLIDRN QKSDNNYSTL NERGDHNRTL DRSGDLGDME
910
PLKGAPLMQK I
Note: Contains a nuclear localization signal (NLS) domain at positions 622-629.1 Publication
Show »<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression."
Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
J. Cell Sci. 117:2675-2686(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 622-LYS-LYS-623.
Length:911
Mass (Da):101,744
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i8EBEA0D3FA88C843
Isoform 3 (identifier: P30999-3) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
880-900: Missing.
10 20 30 40 50
MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD
60 70 80 90 100
ANSLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP
110 120 130 140 150
RMQEPGQIVE TYTEEDPEGA MSVVSVETTD DGTTRRTETT VKKVVKTMTT
160 170 180 190 200
RTVQPVPMGP DGLPVDASAV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA
210 220 230 240 250
TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA
260 270 280 290 300
PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS
310 320 330 340 350
DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL
360 370 380 390 400
DSLRKGMPPP SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV
410 420 430 440 450
KTDVRKLKGI PILVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC
460 470 480 490 500
DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE
510 520 530 540 550
VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE
560 570 580 590 600
CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY
610 620 630 640 650
QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT
660 670 680 690 700
SPARGYELLF QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR
710 720 730 740 750
YIRSALRQEK ALSAIAELLT SEHERVVKAA SGALRNLAVD ARNKELIGKH
760 770 780 790 800
AIPNLVKNLP GGQQNSSWNF SEDTVVSILN TINEVIAENL EAAKKLRETQ
810 820 830 840 850
GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE KEGWKKSDFQ
860 870 880 890 900
VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD NNYSTLNERG DHNRTLDRSG
910
DLGDMEPLKG APLMQKI
Length:917
Mass (Da):102,565
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i8FA40C72176733E8
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence BAC41421 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 405 | R → A in CAA79078 (PubMed:1334250).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 676 | K → N in CAA79078 (PubMed:1334250).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 715 | I → R in CAA79078 (PubMed:1334250).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 752 | I → R in CAA79078 (PubMed:1334250).Curated | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_030567 | 626 – 631 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 6 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_030568 | 880 – 900 | Missing in isoform 2 and isoform 3. 3 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
| 21 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | Z17804 mRNA. Translation: CAA79078.1. AB093237 mRNA. Translation: BAC41421.1. Different initiation. AK133193 mRNA. Translation: BAE21551.1. AK161790 mRNA. Translation: BAE36576.1. BC043108 mRNA. Translation: AAH43108.1. BC054544 mRNA. Translation: AAH54544.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS16186.1. [P30999-1] CCDS50622.1. [P30999-2] CCDS50623.1. [P30999-3] |
Protein sequence database of the Protein Information Resource More...PIRi | I48701. S28498. |
NCBI Reference Sequences More...RefSeqi | NP_001078917.1. NM_001085448.1. [P30999-3] NP_001078918.1. NM_001085449.1. NP_001078919.1. NM_001085450.1. [P30999-1] NP_001078922.1. NM_001085453.1. [P30999-2] NP_031641.2. NM_007615.4. [P30999-1] XP_006498698.1. XM_006498635.1. XP_017170690.1. XM_017315201.1. [P30999-1] XP_017170697.1. XM_017315208.1. [P30999-3] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Mm.35738. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENSMUST00000036811; ENSMUSP00000042543; ENSMUSG00000034101. [P30999-3] ENSMUST00000066177; ENSMUSP00000065252; ENSMUSG00000034101. [P30999-2] ENSMUST00000067232; ENSMUSP00000064518; ENSMUSG00000034101. [P30999-1] ENSMUST00000111691; ENSMUSP00000107320; ENSMUSG00000034101. [P30999-1] ENSMUST00000111697; ENSMUSP00000107326; ENSMUSG00000034101. [P30999-3] ENSMUST00000189772; ENSMUSP00000141166; ENSMUSG00000101645. [P30999-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 12388. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | mmu:12388. |
UCSC genome browser More...UCSCi | uc008kio.1. mouse. [P30999-3] uc008kip.1. mouse. [P30999-1] uc008kit.1. mouse. [P30999-2] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Organisms | Length | Cluster ID | Cluster name | Size | |
|---|---|---|---|---|---|---|---|
| P30999 | D3Z2H2 D3Z7H6 | Mus musculus (Mouse) | 938 | UniRef100_P30999 | Cluster: Catenin delta-1 | 3 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | Z17804 mRNA. Translation: CAA79078.1. AB093237 mRNA. Translation: BAC41421.1. Different initiation. AK133193 mRNA. Translation: BAE21551.1. AK161790 mRNA. Translation: BAE36576.1. BC043108 mRNA. Translation: AAH43108.1. BC054544 mRNA. Translation: AAH54544.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS16186.1. [P30999-1] CCDS50622.1. [P30999-2] CCDS50623.1. [P30999-3] |
Protein sequence database of the Protein Information Resource More...PIRi | I48701. S28498. |
NCBI Reference Sequences More...RefSeqi | NP_001078917.1. NM_001085448.1. [P30999-3] NP_001078918.1. NM_001085449.1. NP_001078919.1. NM_001085450.1. [P30999-1] NP_001078922.1. NM_001085453.1. [P30999-2] NP_031641.2. NM_007615.4. [P30999-1] XP_006498698.1. XM_006498635.1. XP_017170690.1. XM_017315201.1. [P30999-1] XP_017170697.1. XM_017315208.1. [P30999-3] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Mm.35738. |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P30999. |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P30999. |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 198513. 24 interactors. |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P30999. |
Database of interacting proteins More...DIPi | DIP-31972N. |
Protein interaction database and analysis system More...IntActi | P30999. 24 interactors. |
Molecular INTeraction database More...MINTi | P30999. |
STRING: functional protein association networks More...STRINGi | 10090.ENSMUSP00000064518. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P30999. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P30999. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P30999. |
Proteomic databases
MaxQB - The MaxQuant DataBase More...MaxQBi | P30999. |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P30999. |
PeptideAtlas More...PeptideAtlasi | P30999. |
PRoteomics IDEntifications database More...PRIDEi | P30999. |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENSMUST00000036811; ENSMUSP00000042543; ENSMUSG00000034101. [P30999-3] ENSMUST00000066177; ENSMUSP00000065252; ENSMUSG00000034101. [P30999-2] ENSMUST00000067232; ENSMUSP00000064518; ENSMUSG00000034101. [P30999-1] ENSMUST00000111691; ENSMUSP00000107320; ENSMUSG00000034101. [P30999-1] ENSMUST00000111697; ENSMUSP00000107326; ENSMUSG00000034101. [P30999-3] ENSMUST00000189772; ENSMUSP00000141166; ENSMUSG00000101645. [P30999-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 12388. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | mmu:12388. |
UCSC genome browser More...UCSCi | uc008kio.1. mouse. [P30999-3] uc008kip.1. mouse. [P30999-1] uc008kit.1. mouse. [P30999-2] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 1500. |
Mouse genome database (MGD) from Mouse Genome Informatics (MGI) More...MGIi | MGI:105100. Ctnnd1. |
Rodent Unidentified Gene-Encoded large proteins database More...Rougei | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1048. Eukaryota. ENOG410Y21Q. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119167. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000231862. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG004284. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P30999. |
KEGG Orthology (KO) More...KOi | K05690. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P30999. |
TreeFam database of animal gene trees More...TreeFami | TF321877. |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-MMU-418990. Adherens junctions interactions. R-MMU-5218920. VEGFR2 mediated vascular permeability. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | Ctnnd1. mouse. |
Protein Ontology More...PROi | PR:P30999. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSMUSG00000034101. |
CleanEx database of gene expression profiles More...CleanExi | MM_CTNND1. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P30999. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P30999. MM. |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.25.10.10. 1 hit. |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000225. Armadillo. IPR028439. Catenin_d1. IPR028435. Plakophilin/d_Catenin. |
The PANTHER Classification System More...PANTHERi | PTHR10372. PTHR10372. 1 hit. PTHR10372:SF6. PTHR10372:SF6. 1 hit. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00514. Arm. 3 hits. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00185. ARM. 7 hits. |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF48371. SSF48371. 2 hits. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50176. ARM_REPEAT. 3 hits. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | CTND1_MOUSE | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P30999Primary (citable) accession number: P30999 Secondary accession number(s): Q3TSU9, Q80XQ4, Q8CHF8 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
| Last sequence update: | January 15, 2008 | |
| Last modified: | March 28, 2018 | |
| This is version 162 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |