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Protein

Adenomatous polyposis coli protein

Gene

APC

Organism
Homo sapiens (Human)
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. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<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>

<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

Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.5 Publications

Miscellaneous

APC mutations have led to some interesting observations. (1) the great majority of the mutations found to date would result in truncation of the APC product. (2) almost all the mutations have occurred within the first half of the coding sequence, and somatic mutations in colorectal tumors are further clustered in a particular region, called MCR (mutation cluster region). (3) most identified point mutations in the APC gene are transitions from cytosine to other nucleotides. (4) the location of germline mutations tends to correlate with the number of colorectal polyps in FAP patients. Inactivation of both alleles of the APC gene seems to be required as an early event to develop most adenomas and carcinomas in the colon and rectum as well as some of those in the stomach.

<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

  • beta-catenin binding Source: BHF-UCL
  • dynein complex binding Source: CAFA
  • gamma-catenin binding Source: BHF-UCL
  • identical protein binding Source: CAFA
  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein kinase regulator activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

<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 processWnt signaling pathway

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:ENSG00000134982-MONOMER

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-111465 Apoptotic cleavage of cellular proteins
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-196299 Beta-catenin phosphorylation cascade
R-HSA-3769402 Deactivation of the beta-catenin transactivating complex
R-HSA-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-HSA-5339716 Misspliced GSK3beta mutants stabilize beta-catenin
R-HSA-5358747 S33 mutants of beta-catenin aren't phosphorylated
R-HSA-5358749 S37 mutants of beta-catenin aren't phosphorylated
R-HSA-5358751 S45 mutants of beta-catenin aren't phosphorylated
R-HSA-5358752 T41 mutants of beta-catenin aren't phosphorylated
R-HSA-5467333 APC truncation mutants are not K63 polyubiquitinated
R-HSA-5467337 APC truncation mutants have impaired AXIN binding
R-HSA-5467340 AXIN missense mutants destabilize the destruction complex
R-HSA-5467348 Truncations of AMER1 destabilize the destruction complex
R-HSA-5689896 Ovarian tumor domain proteases

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P25054

SIGNOR Signaling Network Open Resource

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SIGNORi
P25054

<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:
Adenomatous polyposis coli protein
Short name:
Protein APC
Alternative name(s):
Deleted in polyposis 2.5
<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:APCImported
Synonyms:DP2.5
<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>OrganismiHomo sapiens (Human)
<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 NCBI 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000134982.16

Human Gene Nomenclature Database

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HGNCi
HGNC:583 APC

Online Mendelian Inheritance in Man (OMIM)

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MIMi
611731 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P25054

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Familial adenomatous polyposis (FAP)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA cancer predisposition syndrome characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.
See also OMIM:175100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00961399R → W in FAP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139196838EnsemblClinVar.1
Natural variantiVAR_005032171S → I in FAP. 1 Publication1
Natural variantiVAR_005033414R → C in FAP. Corresponds to variant dbSNP:rs137854567EnsemblClinVar.1
Natural variantiVAR_009614722S → G in FAP. 1 Publication1
Natural variantiVAR_005034784S → T in FAP. 1
Natural variantiVAR_005038911E → G in FAP and colorectal tumor. 1
Natural variantiVAR_0050441176P → L in FAP. 1
Natural variantiVAR_0096161184A → P in FAP. 1 Publication1
Natural variantiVAR_0050471292T → M in FAP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs371113837EnsemblClinVar.1
Natural variantiVAR_0050511313T → A in FAP and colorectal tumor. Corresponds to variant dbSNP:rs863225349EnsemblClinVar.1
Natural variantiVAR_0050531348R → W in FAP. 1 Publication1
Natural variantiVAR_0050562621S → C in FAP. Corresponds to variant dbSNP:rs72541816EnsemblClinVar.1
Natural variantiVAR_0050572839L → F in FAP. Corresponds to variant dbSNP:rs876658156EnsemblClinVar.1
Hereditary desmoid disease (HDD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.
See also OMIM:135290
Medulloblastoma (MDB)1 Publication
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionMalignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.
See also OMIM:155255
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0176531296A → V in MDB; sporadic. 1 PublicationCorresponds to variant dbSNP:rs1291513037Ensembl.1
Natural variantiVAR_0176541472V → I in MDB; sporadic. 1 PublicationCorresponds to variant dbSNP:rs878853445EnsemblClinVar.1
Natural variantiVAR_0176551495S → G in MDB; sporadic. 1 Publication1
Gastric cancer (GASC)
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.
See also OMIM:613659
Hepatocellular carcinoma (HCC)
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes.
See also OMIM:114550

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi516K → E: Impairs interaction with KHDRBS1. 1 Publication1
Mutagenesisi549R → E: Impairs interaction with KHDRBS1. 1 Publication1
Mutagenesisi2841T → L: Loss of interaction with SCRIB. 1 Publication1
Mutagenesisi2843V → Q: Loss of interaction with SCRIB. 1 Publication1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNET

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DisGeNETi
324

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
APC

MalaCards human disease database

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MalaCardsi
APC
MIMi114550 phenotype
135290 phenotype
155255 phenotype
175100 phenotype
613659 phenotype

Open Targets

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OpenTargetsi
ENSG00000134982

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
247806 APC-related attenuated familial adenomatous polyposis
3258 Cenani-Lenz syndrome
873 Desmoid tumor
261584 Familial adenomatous polyposis due to 5q22.2 microdeletion
79665 Gardner syndrome
314022 Gastric adenocarcinoma and proximal polyposis of the stomach
99818 Turcot syndrome with polyposis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24875

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
APC

Domain mapping of disease mutations (DMDM)

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DMDMi
97535708

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000646272 – 2843Adenomatous polyposis coli proteinAdd BLAST2842

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylalanineCombined sources1
Modified residuei107PhosphoserineBy similarity1
Modified residuei111PhosphoserineBy similarity1
Modified residuei744PhosphoserineCombined sources1
Modified residuei748PhosphoserineCombined sources1
Modified residuei780PhosphoserineCombined sources1
Modified residuei908PhosphoserineCombined sources1
Modified residuei987PhosphoserineBy similarity1
Modified residuei1038PhosphoserineBy similarity1
Modified residuei1042PhosphoserineCombined sources1
Modified residuei1360PhosphoserineCombined sources1
Modified residuei1371PhosphoserineCombined sources1
Modified residuei1385PhosphoserineCombined sources1
Modified residuei1392PhosphoserineBy similarity1
Modified residuei1395PhosphoserineBy similarity1
Modified residuei1438PhosphothreonineCombined sources1
Modified residuei1567PhosphoserineBy similarity1
Modified residuei1774PhosphoserineCombined sources1
Modified residuei1861PhosphoserineCombined sources1
Modified residuei1863PhosphoserineCombined sources1
Modified residuei1864PhosphoserineCombined sources1
Modified residuei1971PhosphoserineBy similarity1
Modified residuei1973PhosphoserineBy similarity1
Modified residuei2088PhosphoserineBy similarity1
Modified residuei2093PhosphoserineBy similarity1
Modified residuei2125PhosphoserineBy similarity1
Modified residuei2129PhosphoserineBy similarity1
Modified residuei2130PhosphoserineBy similarity1
Modified residuei2132PhosphoserineBy similarity1
Modified residuei2151PhosphothreonineCombined sources1
Modified residuei2260PhosphoserineCombined sources1
Modified residuei2270PhosphoserineCombined sources1
Modified residuei2283PhosphoserineCombined sources1
Modified residuei2473PhosphoserineCombined sources1
Modified residuei2535PhosphoserineCombined sources1
Modified residuei2569PhosphoserineCombined sources1
Modified residuei2671PhosphoserineCombined sources1
Modified residuei2674PhosphoserineCombined sources1
Modified residuei2679PhosphothreonineCombined sources1
Modified residuei2710PhosphoserineBy similarity1
Modified residuei2724PhosphoserineCombined sources1
Modified residuei2789PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/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 GSK3B.
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P25054

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P25054

MaxQB - The MaxQuant DataBase

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MaxQBi
P25054

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P25054

PeptideAtlas

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PeptideAtlasi
P25054

PRoteomics IDEntifications database

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PRIDEi
P25054

ProteomicsDB human proteome resource

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ProteomicsDBi
54247
54248 [P25054-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P25054

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P25054

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in a variety of tissues: brain, small intestine, colon, thymus, skeletal muscle, heart, prostate, lung, spleen, ovary, testis kidney, placenta, blood and liver (PubMed:21643010, PubMed:27217144). Isoform 1A: Very strongly expressed in brain but has relatively low expression levels in other tissues (PubMed:19527921, PubMed:21643010, PubMed:27217144). Isoform 1B: Predominant form in all tissues except for brain, including gastric mucosa and blood (PubMed:19527921, PubMed:21643010, PubMed:27217144).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000134982 Expressed in 231 organ(s), highest expression level in pigmented layer of retina

CleanEx database of gene expression profiles

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CleanExi
HS_APC

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P25054 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P25054 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA013349

<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

Forms homooligomers and heterooligomers with APC2. Interacts with DIAPH1 and DIAPH2 (By similarity). Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with ARHGEF4 (via N-terminus). Interacts with MAPRE1 (via C-terminus); probably required for APC targeting to the growing microtubule plus ends. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells. Interacts with SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3 domain). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By similarity). Interacts at the cell membrane with AMER1 and AMER2 (via ARM repeats). Interacts with KHDRBS1. The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (PubMed:25169422).By similarity15 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106821, 211 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-107 Beta-catenin destruction core complex, variant 5
CPX-109 Beta-catenin destruction core complex, variant 1
CPX-439 Beta-catenin destruction core complex, variant 3
CPX-441 Beta-catenin destruction core complex, variant 7

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P25054

Database of interacting proteins

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DIPi
DIP-33556N

Protein interaction database and analysis system

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IntActi
P25054, 190 interactors

Molecular INTeraction database

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MINTi
P25054

STRING: functional protein association networks

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STRINGi
9606.ENSP00000257430

<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

Secondary structure

12843
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DEBX-ray2.40A/B2-55[»]
1EMUX-ray1.90B2034-2049[»]
1JPPX-ray3.10C/D1021-1035[»]
1M5IX-ray2.00A126-250[»]
1T08X-ray2.10C1484-1498[»]
1TH1X-ray2.50C/D1362-1540[»]
1V18X-ray2.10B1482-1528[»]
2RQUNMR-B1578-1596[»]
3AU3X-ray2.10A396-732[»]
3NMWX-ray1.60A/B407-751[»]
3NMXX-ray2.30A/B/C407-751[»]
3NMZX-ray3.01A/B303-739[»]
3QHEX-ray2.40A/C396-732[»]
3RL7X-ray2.30G/H/I/J/K/L2833-2843[»]
3RL8X-ray2.20F2833-2843[»]
3T7UX-ray2.90A/B407-775[»]
4G69X-ray2.00B2833-2843[»]
4YJEX-ray1.90A407-751[»]
4YJLX-ray2.10A/B/C/D/E/F407-751[»]
4YK6X-ray1.70A407-751[»]
5B6GX-ray1.99A407-751[»]
5IZ6X-ray2.15A407-751[»]
5IZ8X-ray3.06A/B407-751[»]
5IZ9X-ray2.93A407-751[»]
5IZAX-ray1.50A407-751[»]

Database of protein disorder

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DisProti
DP00519

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P25054

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P25054

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P25054

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Repeati453 – 495ARM 1Add BLAST43
Repeati505 – 547ARM 2Add BLAST43
Repeati548 – 591ARM 3Add BLAST44
Repeati592 – 638ARM 4Add BLAST47
Repeati639 – 683ARM 5Add BLAST45
Repeati684 – 725ARM 6Add BLAST42
Repeati726 – 767ARM 7Add BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni960 – 1337Responsible for down-regulation through a process mediated by direct ubiquitinationAdd BLAST378
Regioni1866 – 1893Highly chargedAdd BLAST28

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 coili2 – 61Sequence analysisAdd BLAST60
Coiled coili127 – 248Sequence analysisAdd BLAST122

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi2803 – 2806Microtubule tip localization signal4
Motifi2841 – 2843PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 730Leu-richAdd BLAST730
Compositional biasi731 – 2832Ser-richAdd BLAST2102
Compositional biasi1131 – 1156Asp/Glu-rich (acidic)Add BLAST26
Compositional biasi1558 – 1577Asp/Glu-rich (acidic)Add BLAST20

<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

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2122 Eukaryota
ENOG410XR2V LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00530000063749

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000033986

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004264

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P25054

KEGG Orthology (KO)

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KOi
K02085

Identification of Orthologs from Complete Genome Data

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OMAi
NRVGSNH

Database of Orthologous Groups

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OrthoDBi
31524at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P25054

TreeFam database of animal gene trees

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TreeFami
TF106496

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR026836 APC
IPR009240 APC_15aa_rpt
IPR009234 APC_basic_dom
IPR026831 APC_dom
IPR026818 Apc_fam
IPR032038 APC_N
IPR036149 APC_N_sf
IPR009223 APC_rpt
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR009232 EB1-bd
IPR009224 SAMP

The PANTHER Classification System

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PANTHERi
PTHR12607 PTHR12607, 1 hit
PTHR12607:SF11 PTHR12607:SF11, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF05972 APC_15aa, 3 hits
PF05956 APC_basic, 1 hit
PF16689 APC_N_CC, 1 hit
PF05923 APC_r, 7 hits
PF00514 Arm, 2 hits
PF05937 EB1_binding, 1 hit
PF05924 SAMP, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00185 ARM, 7 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 1 hit
SSF58050 SSF58050, 1 hit
SSF82931 SSF82931, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50176 ARM_REPEAT, 1 hit

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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 promoter usage and alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1A1 Publication (identifier: P25054-1) [UniParc]FASTAAdd to basket
Also known as: Long1 Publication

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.

« Hide
        10         20         30         40         50
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ
60 70 80 90 100
LQGSIEDEAM ASSGQIDLLE RLKELNLDSS NFPGVKLRSK MSLRSYGSRE
110 120 130 140 150
GSVSSRSGEC SPVPMGSFPR RGFVNGSRES TGYLEELEKE RSLLLADLDK
160 170 180 190 200
EEKEKDWYYA QLQNLTKRID SLPLTENFSL QTDMTRRQLE YEARQIRVAM
210 220 230 240 250
EEQLGTCQDM EKRAQRRIAR IQQIEKDILR IRQLLQSQAT EAERSSQNKH
260 270 280 290 300
ETGSHDAERQ NEGQGVGEIN MATSGNGQGS TTRMDHETAS VLSSSSTHSA
310 320 330 340 350
PRRLTSHLGT KVEMVYSLLS MLGTHDKDDM SRTLLAMSSS QDSCISMRQS
360 370 380 390 400
GCLPLLIQLL HGNDKDSVLL GNSRGSKEAR ARASAALHNI IHSQPDDKRG
410 420 430 440 450
RREIRVLHLL EQIRAYCETC WEWQEAHEPG MDQDKNPMPA PVEHQICPAV
460 470 480 490 500
CVLMKLSFDE EHRHAMNELG GLQAIAELLQ VDCEMYGLTN DHYSITLRRY
510 520 530 540 550
AGMALTNLTF GDVANKATLC SMKGCMRALV AQLKSESEDL QQVIASVLRN
560 570 580 590 600
LSWRADVNSK KTLREVGSVK ALMECALEVK KESTLKSVLS ALWNLSAHCT
610 620 630 640 650
ENKADICAVD GALAFLVGTL TYRSQTNTLA IIESGGGILR NVSSLIATNE
660 670 680 690 700
DHRQILRENN CLQTLLQHLK SHSLTIVSNA CGTLWNLSAR NPKDQEALWD
710 720 730 740 750
MGAVSMLKNL IHSKHKMIAM GSAAALRNLM ANRPAKYKDA NIMSPGSSLP
760 770 780 790 800
SLHVRKQKAL EAELDAQHLS ETFDNIDNLS PKASHRSKQR HKQSLYGDYV
810 820 830 840 850
FDTNRHDDNR SDNFNTGNMT VLSPYLNTTV LPSSSSSRGS LDSSRSEKDR
860 870 880 890 900
SLERERGIGL GNYHPATENP GTSSKRGLQI STTAAQIAKV MEEVSAIHTS
910 920 930 940 950
QEDRSSGSTT ELHCVTDERN ALRRSSAAHT HSNTYNFTKS ENSNRTCSMP
960 970 980 990 1000
YAKLEYKRSS NDSLNSVSSS DGYGKRGQMK PSIESYSEDD ESKFCSYGQY
1010 1020 1030 1040 1050
PADLAHKIHS ANHMDDNDGE LDTPINYSLK YSDEQLNSGR QSPSQNERWA
1060 1070 1080 1090 1100
RPKHIIEDEI KQSEQRQSRN QSTTYPVYTE STDDKHLKFQ PHFGQQECVS
1110 1120 1130 1140 1150
PYRSRGANGS ETNRVGSNHG INQNVSQSLC QEDDYEDDKP TNYSERYSEE
1160 1170 1180 1190 1200
EQHEEEERPT NYSIKYNEEK RHVDQPIDYS LKYATDIPSS QKQSFSFSKS
1210 1220 1230 1240 1250
SSGQSSKTEH MSSSSENTST PSSNAKRQNQ LHPSSAQSRS GQPQKAATCK
1260 1270 1280 1290 1300
VSSINQETIQ TYCVEDTPIC FSRCSSLSSL SSAEDEIGCN QTTQEADSAN
1310 1320 1330 1340 1350
TLQIAEIKEK IGTRSAEDPV SEVPAVSQHP RTKSSRLQGS SLSSESARHK
1360 1370 1380 1390 1400
AVEFSSGAKS PSKSGAQTPK SPPEHYVQET PLMFSRCTSV SSLDSFESRS
1410 1420 1430 1440 1450
IASSVQSEPC SGMVSGIISP SDLPDSPGQT MPPSRSKTPP PPPQTAQTKR
1460 1470 1480 1490 1500
EVPKNKAPTA EKRESGPKQA AVNAAVQRVQ VLPDADTLLH FATESTPDGF
1510 1520 1530 1540 1550
SCSSSLSALS LDEPFIQKDV ELRIMPPVQE NDNGNETESE QPKESNENQE
1560 1570 1580 1590 1600
KEAEKTIDSE KDLLDDSDDD DIEILEECII SAMPTKSSRK AKKPAQTASK
1610 1620 1630 1640 1650
LPPPVARKPS QLPVYKLLPS QNRLQPQKHV SFTPGDDMPR VYCVEGTPIN
1660 1670 1680 1690 1700
FSTATSLSDL TIESPPNELA AGEGVRGGAQ SGEFEKRDTI PTEGRSTDEA
1710 1720 1730 1740 1750
QGGKTSSVTI PELDDNKAEE GDILAECINS AMPKGKSHKP FRVKKIMDQV
1760 1770 1780 1790 1800
QQASASSSAP NKNQLDGKKK KPTSPVKPIP QNTEYRTRVR KNADSKNNLN
1810 1820 1830 1840 1850
AERVFSDNKD SKKQNLKNNS KVFNDKLPNN EDRVRGSFAF DSPHHYTPIE
1860 1870 1880 1890 1900
GTPYCFSRND SLSSLDFDDD DVDLSREKAE LRKAKENKES EAKVTSHTEL
1910 1920 1930 1940 1950
TSNQQSANKT QAIAKQPINR GQPKPILQKQ STFPQSSKDI PDRGAATDEK
1960 1970 1980 1990 2000
LQNFAIENTP VCFSHNSSLS SLSDIDQENN NKENEPIKET EPPDSQGEPS
2010 2020 2030 2040 2050
KPQASGYAPK SFHVEDTPVC FSRNSSLSSL SIDSEDDLLQ ECISSAMPKK
2060 2070 2080 2090 2100
KKPSRLKGDN EKHSPRNMGG ILGEDLTLDL KDIQRPDSEH GLSPDSENFD
2110 2120 2130 2140 2150
WKAIQEGANS IVSSLHQAAA AACLSRQASS DSDSILSLKS GISLGSPFHL
2160 2170 2180 2190 2200
TPDQEEKPFT SNKGPRILKP GEKSTLETKK IESESKGIKG GKKVYKSLIT
2210 2220 2230 2240 2250
GKVRSNSEIS GQMKQPLQAN MPSISRGRTM IHIPGVRNSS SSTSPVSKKG
2260 2270 2280 2290 2300
PPLKTPASKS PSEGQTATTS PRGAKPSVKS ELSPVARQTS QIGGSSKAPS
2310 2320 2330 2340 2350
RSGSRDSTPS RPAQQPLSRP IQSPGRNSIS PGRNGISPPN KLSQLPRTSS
2360 2370 2380 2390 2400
PSTASTKSSG SGKMSYTSPG RQMSQQNLTK QTGLSKNASS IPRSESASKG
2410 2420 2430 2440 2450
LNQMNNGNGA NKKVELSRMS STKSSGSESD RSERPVLVRQ STFIKEAPSP
2460 2470 2480 2490 2500
TLRRKLEESA SFESLSPSSR PASPTRSQAQ TPVLSPSLPD MSLSTHSSVQ
2510 2520 2530 2540 2550
AGGWRKLPPN LSPTIEYNDG RPAKRHDIAR SHSESPSRLP INRSGTWKRE
2560 2570 2580 2590 2600
HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDEK HVNSISGTKQ
2610 2620 2630 2640 2650
SKENQVSAKG TWRKIKENEF SPTNSTSQTV SSGATNGAES KTLIYQMAPA
2660 2670 2680 2690 2700
VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKA NPNIKDSKDN
2710 2720 2730 2740 2750
QAKQNVGNGS VPMRTVGLEN RLNSFIQVDA PDQKGTEIKP GQNNPVPVSE
2760 2770 2780 2790 2800
TNESSIVERT PFSSSSSSKH SSPSGTVAAR VTPFNYNPSP RKSSADSTSA
2810 2820 2830 2840
RPSQIPTPVN NNTKKRDSKT DSTESSGTQS PKRHSGSYLV TSV
Length:2,843
Mass (Da):311,646
Last modified:May 16, 2006 - 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:i77E194AE4A91DC5A
GO
Isoform 2 (identifier: P25054-2) [UniParc]FASTAAdd to basket
Also known as: Short1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     312-412: Missing.

Show »
Length:2,742
Mass (Da):300,439
Checksum:i49CF92BE7A81EBEC
GO
Isoform 1B1 Publication (identifier: P25054-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MAAASYDQLL...KLETEASNMK → MYASLGSGPV...TSGHWASVWQ
     217-244: Missing.

Note: Produced by alternative promoter usage.1 Publication
Show »
Length:2,825
Mass (Da):308,734
Checksum:iB1EC014A9D3D910E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PFT7E9PFT7_HUMAN
Adenomatous polyposis coli protein
APC
1,304Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A2Q2SV78A0A2Q2SV78_HUMAN
Adenomatous polyposis coli protein
APC
1,135Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EMH9E7EMH9_HUMAN
Adenomatous polyposis coli protein
APC
287Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RFL6D6RFL6_HUMAN
Adenomatous polyposis coli protein
APC
118Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087X2F3A0A087X2F3_HUMAN
Adenomatous polyposis coli protein
APC
51Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
R4GMU6R4GMU6_HUMAN
Adenomatous polyposis coli protein
APC
272Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WYF3A0A087WYF3_HUMAN
Adenomatous polyposis coli protein
APC
58Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti184M → L in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti184M → L in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti970S → N in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti970S → N in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti1309E → G in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti1309E → G in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti1325 – 1331AVSQHPR → SSVHSTLE in AAA60353 (PubMed:1678319).Curated7
Sequence conflicti1325 – 1331AVSQHPR → SSVHSTLE in AAA60354 (PubMed:1678319).Curated7
Sequence conflicti1355S → P in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti1355S → P in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti1591A → G in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti1591A → G in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti2723N → T in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti2723N → T in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti2755S → P in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti2755S → P in AAA60354 (PubMed:1678319).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00961399R → W in FAP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139196838EnsemblClinVar.1
Natural variantiVAR_005032171S → I in FAP. 1 Publication1
Natural variantiVAR_005033414R → C in FAP. Corresponds to variant dbSNP:rs137854567EnsemblClinVar.1
Natural variantiVAR_009614722S → G in FAP. 1 Publication1
Natural variantiVAR_005034784S → T in FAP. 1
Natural variantiVAR_005035817G → C in gastric cancer. 1
Natural variantiVAR_053976870P → S. Corresponds to variant dbSNP:rs33974176EnsemblClinVar.1
Natural variantiVAR_005036880I → T in colorectal carcinoma and gastric cancer; from a patient with MMRCS. 1 Publication1
Natural variantiVAR_012975890V → I in colorectal carcinoma; from a patient with MMRCS. 1 PublicationCorresponds to variant dbSNP:rs779998847Ensembl.1
Natural variantiVAR_005037906S → Y in colorectal tumor. 1
Natural variantiVAR_005038911E → G in FAP and colorectal tumor. 1
Natural variantiVAR_005039942N → D in gastric cancer. 1
Natural variantiVAR_0050401027Y → C in colorectal tumor. Corresponds to variant dbSNP:rs869312784EnsemblClinVar.1
Natural variantiVAR_0096151057E → G in non-FAP; unknown pathological significance. 1 Publication1
Natural variantiVAR_0050411118N → D1 PublicationCorresponds to variant dbSNP:rs140493115EnsemblClinVar.1
Natural variantiVAR_0050421120G → E in gastric cancer. Corresponds to variant dbSNP:rs28933379EnsemblClinVar.1
Natural variantiVAR_0089921171R → C1 PublicationCorresponds to variant dbSNP:rs201830995EnsemblClinVar.1
Natural variantiVAR_0050431171R → H in gastric cancer. Corresponds to variant dbSNP:rs372481703EnsemblClinVar.1
Natural variantiVAR_0050441176P → L in FAP. 1
Natural variantiVAR_0096161184A → P in FAP. 1 Publication1
Natural variantiVAR_0050451197F → S in gastric cancer. 1
Natural variantiVAR_0357941254I → F in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0050461259I → T in gastric cancer. 1
Natural variantiVAR_0050471292T → M in FAP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs371113837EnsemblClinVar.1
Natural variantiVAR_0176531296A → V in MDB; sporadic. 1 PublicationCorresponds to variant dbSNP:rs1291513037Ensembl.1
Natural variantiVAR_0050481304I → V1 PublicationCorresponds to variant dbSNP:rs770157475EnsemblClinVar.1
Natural variantiVAR_0050491307I → K in 6% of Ashkenazi Jews; associated with slightly increased risk of colon and breast cancer. 4 PublicationsCorresponds to variant dbSNP:rs1801155EnsemblClinVar.1
Natural variantiVAR_0050501312G → E in gastric cancer. 1
Natural variantiVAR_0050511313T → A in FAP and colorectal tumor. Corresponds to variant dbSNP:rs863225349EnsemblClinVar.1
Natural variantiVAR_0096171317E → Q May contribute to colorectal tumor development. 1 PublicationCorresponds to variant dbSNP:rs1801166EnsemblClinVar.1
Natural variantiVAR_0050521326V → A in gastric cancer. 1
Natural variantiVAR_0050531348R → W in FAP. 1 Publication1
Natural variantiVAR_0651331395S → C in hepatoblastoma. 1 PublicationCorresponds to variant dbSNP:rs137854578EnsemblClinVar.1
Natural variantiVAR_0050541422D → H in colorectal tumor. 1
Natural variantiVAR_0176541472V → I in MDB; sporadic. 1 PublicationCorresponds to variant dbSNP:rs878853445EnsemblClinVar.1
Natural variantiVAR_0176551495S → G in MDB; sporadic. 1 Publication1
Natural variantiVAR_0201411496T → S. Corresponds to variant dbSNP:rs2229996EnsemblClinVar.1
Natural variantiVAR_0129761508A → V in colorectal carcinoma from a patient with MMRCS. 1 Publication1
Natural variantiVAR_0089931822V → D4 PublicationsCorresponds to variant dbSNP:rs459552EnsemblClinVar.1
Natural variantiVAR_0539771882R → T. Corresponds to variant dbSNP:rs34157245EnsemblClinVar.1
Natural variantiVAR_0201421973S → T. Corresponds to variant dbSNP:rs4987109Ensembl.1
Natural variantiVAR_0539782499V → L. Corresponds to variant dbSNP:rs33941929EnsemblClinVar.1
Natural variantiVAR_0050552502G → S1 PublicationCorresponds to variant dbSNP:rs2229995EnsemblClinVar.1
Natural variantiVAR_0050562621S → C in FAP. Corresponds to variant dbSNP:rs72541816EnsemblClinVar.1
Natural variantiVAR_0089942738I → T1 PublicationCorresponds to variant dbSNP:rs863224552EnsemblClinVar.1
Natural variantiVAR_0050572839L → F in FAP. Corresponds to variant dbSNP:rs876658156EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_0590271 – 45MAAAS…ASNMK → MYASLGSGPVAPLPASVPPS VLGSWSTGGSRSCVRQETKS PGGARTSGHWASVWQ in isoform 1B. Add BLAST45
Alternative sequenceiVSP_059028217 – 244Missing in isoform 1B. Add BLAST28
Alternative sequenceiVSP_004115312 – 412Missing in isoform 2. 1 PublicationAdd BLAST101

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M73548 mRNA Translation: AAA60353.1
M73548 mRNA Translation: AAA60354.1
M74088 mRNA Translation: AAA03586.1
AC008575 Genomic DNA No translation available.
AC136500 Genomic DNA No translation available.
CH471086 Genomic DNA Translation: EAW49002.1
CH471086 Genomic DNA Translation: EAW49007.1
AK294544 mRNA Translation: BAH11802.1
S78214 Genomic DNA Translation: AAB21145.2 Sequence problems.

The Consensus CDS (CCDS) project

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CCDSi
CCDS4107.1 [P25054-1]

Protein sequence database of the Protein Information Resource

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PIRi
A37261 RBHUAP

NCBI Reference Sequences

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RefSeqi
NP_000029.2, NM_000038.5 [P25054-1]
NP_001120982.1, NM_001127510.2 [P25054-1]
NP_001120983.2, NM_001127511.2 [P25054-3]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.158932

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000257430; ENSP00000257430; ENSG00000134982 [P25054-1]
ENST00000508376; ENSP00000427089; ENSG00000134982 [P25054-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
324

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:324

UCSC genome browser

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UCSCi
uc003kpy.5 human [P25054-1]
uc063gan.1 human

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

<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

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Colon cancer gene variant databases Adenomatous Polyposis Coli (APC)

Leiden Open Variation Database (LOVD)

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73548 mRNA Translation: AAA60353.1
M73548 mRNA Translation: AAA60354.1
M74088 mRNA Translation: AAA03586.1
AC008575 Genomic DNA No translation available.
AC136500 Genomic DNA No translation available.
CH471086 Genomic DNA Translation: EAW49002.1
CH471086 Genomic DNA Translation: EAW49007.1
AK294544 mRNA Translation: BAH11802.1
S78214 Genomic DNA Translation: AAB21145.2 Sequence problems.
CCDSiCCDS4107.1 [P25054-1]
PIRiA37261 RBHUAP
RefSeqiNP_000029.2, NM_000038.5 [P25054-1]
NP_001120982.1, NM_001127510.2 [P25054-1]
NP_001120983.2, NM_001127511.2 [P25054-3]
UniGeneiHs.158932

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DEBX-ray2.40A/B2-55[»]
1EMUX-ray1.90B2034-2049[»]
1JPPX-ray3.10C/D1021-1035[»]
1M5IX-ray2.00A126-250[»]
1T08X-ray2.10C1484-1498[»]
1TH1X-ray2.50C/D1362-1540[»]
1V18X-ray2.10B1482-1528[»]
2RQUNMR-B1578-1596[»]
3AU3X-ray2.10A396-732[»]
3NMWX-ray1.60A/B407-751[»]
3NMXX-ray2.30A/B/C407-751[»]
3NMZX-ray3.01A/B303-739[»]
3QHEX-ray2.40A/C396-732[»]
3RL7X-ray2.30G/H/I/J/K/L2833-2843[»]
3RL8X-ray2.20F2833-2843[»]
3T7UX-ray2.90A/B407-775[»]
4G69X-ray2.00B2833-2843[»]
4YJEX-ray1.90A407-751[»]
4YJLX-ray2.10A/B/C/D/E/F407-751[»]
4YK6X-ray1.70A407-751[»]
5B6GX-ray1.99A407-751[»]
5IZ6X-ray2.15A407-751[»]
5IZ8X-ray3.06A/B407-751[»]
5IZ9X-ray2.93A407-751[»]
5IZAX-ray1.50A407-751[»]
DisProtiDP00519
ProteinModelPortaliP25054
SMRiP25054
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106821, 211 interactors
ComplexPortaliCPX-107 Beta-catenin destruction core complex, variant 5
CPX-109 Beta-catenin destruction core complex, variant 1
CPX-439 Beta-catenin destruction core complex, variant 3
CPX-441 Beta-catenin destruction core complex, variant 7
CORUMiP25054
DIPiDIP-33556N
IntActiP25054, 190 interactors
MINTiP25054
STRINGi9606.ENSP00000257430

PTM databases

iPTMnetiP25054
PhosphoSitePlusiP25054

Polymorphism and mutation databases

BioMutaiAPC
DMDMi97535708

Proteomic databases

EPDiP25054
jPOSTiP25054
MaxQBiP25054
PaxDbiP25054
PeptideAtlasiP25054
PRIDEiP25054
ProteomicsDBi54247
54248 [P25054-2]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
324
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257430; ENSP00000257430; ENSG00000134982 [P25054-1]
ENST00000508376; ENSP00000427089; ENSG00000134982 [P25054-1]
GeneIDi324
KEGGihsa:324
UCSCiuc003kpy.5 human [P25054-1]
uc063gan.1 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
324
DisGeNETi324
EuPathDBiHostDB:ENSG00000134982.16

GeneCards: human genes, protein and diseases

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GeneCardsi
APC
GeneReviewsiAPC
HGNCiHGNC:583 APC
HPAiHPA013349
MalaCardsiAPC
MIMi114550 phenotype
135290 phenotype
155255 phenotype
175100 phenotype
611731 gene
613659 phenotype
neXtProtiNX_P25054
OpenTargetsiENSG00000134982
Orphaneti247806 APC-related attenuated familial adenomatous polyposis
3258 Cenani-Lenz syndrome
873 Desmoid tumor
261584 Familial adenomatous polyposis due to 5q22.2 microdeletion
79665 Gardner syndrome
314022 Gastric adenocarcinoma and proximal polyposis of the stomach
99818 Turcot syndrome with polyposis
PharmGKBiPA24875

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2122 Eukaryota
ENOG410XR2V LUCA
GeneTreeiENSGT00530000063749
HOGENOMiHOG000033986
HOVERGENiHBG004264
InParanoidiP25054
KOiK02085
OMAiNRVGSNH
OrthoDBi31524at2759
PhylomeDBiP25054
TreeFamiTF106496

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000134982-MONOMER
ReactomeiR-HSA-111465 Apoptotic cleavage of cellular proteins
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-196299 Beta-catenin phosphorylation cascade
R-HSA-3769402 Deactivation of the beta-catenin transactivating complex
R-HSA-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-HSA-5339716 Misspliced GSK3beta mutants stabilize beta-catenin
R-HSA-5358747 S33 mutants of beta-catenin aren't phosphorylated
R-HSA-5358749 S37 mutants of beta-catenin aren't phosphorylated
R-HSA-5358751 S45 mutants of beta-catenin aren't phosphorylated
R-HSA-5358752 T41 mutants of beta-catenin aren't phosphorylated
R-HSA-5467333 APC truncation mutants are not K63 polyubiquitinated
R-HSA-5467337 APC truncation mutants have impaired AXIN binding
R-HSA-5467340 AXIN missense mutants destabilize the destruction complex
R-HSA-5467348 Truncations of AMER1 destabilize the destruction complex
R-HSA-5689896 Ovarian tumor domain proteases
SignaLinkiP25054
SIGNORiP25054

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
APC human
EvolutionaryTraceiP25054

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Adenomatous_polyposis_coli

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
324

Protein Ontology

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PROi
PR:P25054

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000134982 Expressed in 231 organ(s), highest expression level in pigmented layer of retina
CleanExiHS_APC
ExpressionAtlasiP25054 baseline and differential
GenevisibleiP25054 HS

Family and domain databases

Gene3Di1.25.10.10, 1 hit
InterProiView protein in InterPro
IPR026836 APC
IPR009240 APC_15aa_rpt
IPR009234 APC_basic_dom
IPR026831 APC_dom
IPR026818 Apc_fam
IPR032038 APC_N
IPR036149 APC_N_sf
IPR009223 APC_rpt
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000225 Armadillo
IPR009232 EB1-bd
IPR009224 SAMP
PANTHERiPTHR12607 PTHR12607, 1 hit
PTHR12607:SF11 PTHR12607:SF11, 1 hit
PfamiView protein in Pfam
PF05972 APC_15aa, 3 hits
PF05956 APC_basic, 1 hit
PF16689 APC_N_CC, 1 hit
PF05923 APC_r, 7 hits
PF00514 Arm, 2 hits
PF05937 EB1_binding, 1 hit
PF05924 SAMP, 3 hits
SMARTiView protein in SMART
SM00185 ARM, 7 hits
SUPFAMiSSF48371 SSF48371, 1 hit
SSF58050 SSF58050, 1 hit
SSF82931 SSF82931, 1 hit
PROSITEiView protein in PROSITE
PS50176 ARM_REPEAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiAPC_HUMAN
<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>AccessioniPrimary (citable) accession number: P25054
Secondary accession number(s): B7Z2B6
, D3DT03, Q15162, Q15163, Q93042
<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 historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 16, 2006
Last modified: January 16, 2019
This is version 238 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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