Protein detail
APC
Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)
Entry name APC | UniProt ID | EVMP confidence score 0.50 |
Supporting publications (n) 1 | Transmembrane count | Protein classification Cancer-related genesDisease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information11
Protein Names
Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)
Protein Class (5)
Cancer-related genesDisease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins
Protein Function (8)
- Cancer-related genes:Mutational cancer driver genes
- Human disease related genes:Cancers:Cancers of the digestive system
- Human disease related genes:Cancers:Cancers of eye, brain, and central nervous system
- Predicted intracellular proteins
- Cancer-related genes:Mutated cancer genes
- Disease related genes
- Human disease related genes:Digestive system diseases:Gastrointestinal diseases
- Human disease related genes:Endocrine and metabolic diseases:Adrenal gland diseases
Ensembl
Entrez Gene Symbol
Gene Synonym (4)
DP2DP2.5DP3PPP1R46
Gene Description
APC regulator of WNT signaling pathway
Chromosome
5
Position
112707498-112846239
Supporting publications (n)
1
EVMP confidence score
0.50
Fluorescence & Localization6
Tissue SpecificbrainCell SpecificAstrocytesSingle-Nuclei Brain SpecificBergmann gliaSecretome LocationSecreted in brainSecretome FunctionEnzyme
Function & Pathway7
Protein Function (8)
- Cancer-related genes:Mutational cancer driver genes
- Human disease related genes:Cancers:Cancers of the digestive system
- Human disease related genes:Cancers:Cancers of eye, brain, and central nervous system
- Predicted intracellular proteins
- Cancer-related genes:Mutated cancer genes
- Disease related genes
- Human disease related genes:Digestive system diseases:Gastrointestinal diseases
- Human disease related genes:Endocrine and metabolic diseases:Adrenal gland diseases
Cellular Component (19)
- GO:0000776 kinetochore
- GO:0005634 nucleus
- GO:0005654 nucleoplasm
- GO:0005737 cytoplasm
- GO:0005794 Golgi apparatus
- GO:0005813 centrosome
- GO:0005829 cytosol
- GO:0005874 microtubule
- GO:0005881 cytoplasmic microtubule
- GO:0005886 plasma membrane
Page 1 of 2
Molecular Function (9)
- GO:0005515 protein binding
- GO:0008013 beta-catenin binding
- GO:0008017 microtubule binding
- GO:0019887 protein kinase regulator activity
- GO:0019901 protein kinase binding
- GO:0031625 ubiquitin protein ligase binding
- GO:0045295 gamma-catenin binding
- GO:0051010 microtubule plus-end binding
- GO:0070840 dynein complex binding
Biological Process (3)
KEGG (17)
- hsa04310 Wnt signaling pathway
- KEGG:hsa04390 Hippo signaling pathway
- KEGG:hsa04519 Cadherin signaling
- KEGG:hsa04550 Signaling pathways regulating pluripotency of stem cells
- KEGG:hsa04810 Regulation of actin cytoskeleton
- KEGG:hsa04934 Cushing syndrome
- KEGG:hsa05010 Alzheimer disease
- KEGG:hsa05022 Pathways of neurodegeneration - multiple diseases
- KEGG:hsa05165 Human papillomavirus infection
- KEGG:hsa05200 Pathways in cancer
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Reactome (16)
- R-hsa-109581 apoptosis
- R-hsa-111465 apoptotic cleavage of cellular proteins
- R-hsa-75153 apoptotic execution phase
- R-hsa-196299 beta catenin phosphorylation cascade
- R-hsa-3769402 deactivation of the beta catenin transactivating complex
- R-hsa-195253 degradation of beta catenin by the destruction complex
- R-hsa-5688426 deubiquitination
- R-hsa-4641262 disassembly of the destruction complex and recruitment of axin to the membrane
- R-hsa-5663202 diseases of signal transduction by growth factor receptors and second messengers
- R-hsa-5689896 ovarian tumor domain proteases
Page 1 of 2
Mediation Categories (4)
Clinical-translation mediationFusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence181
Enzyme-Mediated Modification (53)
53 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| APC | CSNK1D | P48730 | S | 1,504 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper | |
| APC | CSNK1D | P48730 | S | 1,505 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper | |
| APC | CSNK1D | P48730 | S | 1,279 | phosphorylation | KEA | KEA:11487578 |
| APC | CSNK1D | P48730 | S | 1,392 | phosphorylation | KEA | KEA:11487578 |
| APC | GSK3B | P49841 | S | 1,501 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPProtMapperKEAPhosphoSitePhosphoSite_ProtMapper | KEA:15327768 |
| APC | GSK3B | P49841 | S | 1,503 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPProtMapperKEAPhosphoSitePhosphoSite_ProtMapper | KEA:15327768 |
| APC | CDK2 | P24941 | S | 1,360 | phosphorylation | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper | |
| APC | CSNK1A1 | P48729 | S | 1,507 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper | |
| APC | CSNK1A1 | P48729 | S | 1,510 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper | |
| APC | CSNK1A1 | P48729 | S | 1,504 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper |
Ligand-Receptor Signaling (15)
15 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | LOCATE | No | No | No | No | No |
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| cell_adhesion | cell_adhesion | Cellinker | Yes | Yes | No | No | No |
| adhesion | adhesion | OmniPath | Yes | Yes | No | No | No |
| cell_adhesion | cell_adhesion | OmniPath | Yes | Yes | No | No | No |
| tight_junction | tight_junction | GO_Intercell | Yes | Yes | No | No | No |
| tight_junction | tight_junction | OmniPath | Yes | Yes | No | No | No |
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Regulatory Interaction Network (15)
15 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| K2C1 | P04264 | APC | P25054 | Yes | Yes | No | SPIKE_LCSIGNOR | SPIKE_LC:17145710SIGNOR:18359618 |
| KAPCA | P17612 | APC | P25054 | Yes | No | Yes | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDPhosphoSite_KEAKEAACSNHPRD_KEASIGNOR_ProtMapperHPRD-phos | SIGNOR:11050185HPRD-phos:11050185ACSN:11689703HPRD:11050185HPRD:11166179ProtMapper:11050185ACSN:15649893KEA:11050185 |
| AMER1 | Q5JTC6 | APC | P25054 | Yes | Yes | No | HINTSIGNORIntAct | IntAct:24251807SIGNOR:23151663IntAct:17510365HINT:27462415HINT:24251807HINT:26496610 |
| KC1A | P48729 | APC | P25054 | Yes | Yes | No | PhosphoSite_MIMPMIMPHPRD_MIMPPhosphoSite_norefPhosphoPointiPTMnetProtMapperELMPhosphoSite_KEAKEAWangPhosphoSitePhosphoSite_ProtMapper | KEA:11487578ELM:17910481PhosphoSite:12628243 |
| CDK2 | P24941 | APC | P25054 | Yes | No | No | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetProtMapperELMPhosphoSitePhosphoSite_ProtMapper | PhosphoSite:19703905ELM:19703905 |
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Protein Complex Composition (97)
97 records.
Sequence, Structure & Domains17
Sequences
Length
2,843
Mass
311,646
Sequence
MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRIRQLLQSQATEAERSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKRHVDQPIDYSLKYATDIPSSQKQSFSFSKSSSGQSSKTEHMSSSSENTSTPSSNAKRQNQLHPSSAQSRSGQPQKAATCKVSSINQETIQTYCVEDTPICFSRCSSLSSLSSAEDEIGCNQTTQEADSANTLQIAEIKEKIGTRSAEDPVSEVPAVSQHPRTKSSRLQGSSLSSESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLMFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTAQTKREVPKNKAPTAEKRESGPKQAAVNAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPKESNENQEKEAEKTIDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKPAQTASKLPPPVARKPSQLPVYKLLPSQNRLQPQKHVSFTPGDDMPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGEGVRGGAQSGEFEKRDTIPTEGRSTDEAQGGKTSSVTIPELDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASASSSAPNKNQLDGKKKKPTSPVKPIPQNTEYRTRVRKNADSKNNLNAERVFSDNKDSKKQNLKNNSKVFNDKLPNNEDRVRGSFAFDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKAKENKESEAKVTSHTELTSNQQSANKTQAIAKQPINRGQPKPILQKQSTFPQSSKDIPDRGAATDEKLQNFAIENTPVCFSHNSSLSSLSDIDQENNNKENEPIKETEPPDSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKKPSRLKGDNEKHSPRNMGGILGEDLTLDLKDIQRPDSEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLETKKIESESKGIKGGKKVYKSLITGKVRSNSEISGQMKQPLQANMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGQTATTSPRGAKPSVKSELSPVARQTSQIGGSSKAPSRSGSRDSTPSRPAQQPLSRPIQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQMSQQNLTKQTGLSKNASSIPRSESASKGLNQMNNGNGANKKVELSRMSSTKSSGSESDRSERPVLVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPASPTRSQAQTPVLSPSLPDMSLSTHSSVQAGGWRKLPPNLSPTIEYNDGRPAKRHDIARSHSESPSRLPINRSGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSISGTKQSKENQVSAKGTWRKIKENEFSPTNSTSQTVSSGATNGAESKTLIYQMAPAVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKANPNIKDSKDNQAKQNVGNGSVPMRTVGLENRLNSFIQVDAPDQKGTEIKPGQNNPVPVSETNESSIVERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVNNNTKKRDSKTDSTESSGTQSPKRHSGSYLVTSV
Alternative Products
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3; Name=1A; Synonyms=Long; IsoId=P25054-1; Sequence=Displayed; Name=2; Synonyms=Short; IsoId=P25054-2; Sequence=VSP_004115; Name=1B; IsoId=P25054-3; Sequence=VSP_059027, VSP_059028
Alternative Sequence
1..45; MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMK -> MYASLGSGPVAPLPASVPPSVLGSWSTGGSRSCVRQETKSPGGARTSGHWASVWQ (in isoform 1B); 217..244; Missing (in isoform 1B); 312..412; Missing (in isoform 2)
3D Structural Models
Turn
433..435; 709..712; 1027..1030
Helix
6..53; 132..169; 176..178; 180..204; 208..238; 328..338; 343..350; 353..360; 377..393; 407..426; 441..444; 446..456; 460..468; 471..486; 492..509; 513..521; 523..531; 532..534; 538..552; 557..565; 568..578; 582..596; 600..607; 612..619; 629..646; 650..658; 661..668; 674..687; 692..700; 703..708; 716..731; 735..737; 739..742; 1470..1479; 1520..1524; 2036..2045
Beta Strand
429..431; 625..627; 688..690; 2841..2843
3D Structure
NMR spectroscopy (1); X-ray crystallography (30)
Domain & Motif Annotations
Compositional Bias
241..261; Basic and acidic residues; 271..282; Polar residues; 290..299; Low complexity; 833..843; Low complexity; 844..857; Basic and acidic residues; 869..878; Polar residues; 927..943; Polar residues; 961..971; Low complexity; 1107..1130; Polar residues; 1146..1159; Basic and acidic residues; 1190..1224; Low complexity; 1225..1244; Polar residues; 1335..1345; Low complexity; 1355..1366; Low complexity; 1448..1466; Basic and acidic residues; 1540..1564; Basic and acidic residues; 1683..1698; Basic and acidic residues; 1735..1744; Basic residues; 1785..1794; Basic and acidic residues; 1804..1813; Basic and acidic residues; 1881..1896; Basic and acidic residues; 1897..1913; Polar residues; 1928..1938; Polar residues; 1939..1950; Basic and acidic residues; 1979..1991; Basic and acidic residues; 2169..2187; Basic and acidic residues; 2203..2223; Polar residues; 2257..2271; Polar residues; 2286..2331; Polar residues; 2348..2369; Low complexity; 2370..2409; Polar residues; 2418..2427; Polar residues; 2459..2477; Low complexity; 2518..2535; Basic and acidic residues; 2555..2568; Polar residues; 2569..2579; Low complexity; 2580..2592; Basic and acidic residues; 2593..2608; Polar residues; 2620..2635; Polar residues; 2668..2679; Polar residues; 2741..2757; Polar residues; 2763..2774; Low complexity; 2784..2812; Polar residues
Repeat
453..495; ARM 1; 505..547; ARM 2; 548..591; ARM 3; 592..638; ARM 4; 639..683; ARM 5; 684..725; ARM 6; 726..767; ARM 7
Motif
2803..2806; Microtubule tip localization signal; 2841..2843; PDZ-binding
Coiled Coil
2..61; 127..248
Domain (CC)
The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.; DOMAIN: The basic region (residues 2167-2674) mediates the association with both microtubule and actin proteins and promotes the bundling of F-actin.
Region
239..305; Disordered; 828..878; Disordered; 923..943; Disordered; 958..987; Disordered; 960..1337; Responsible for down-regulation through a process mediated by direct ubiquitination; 1020..1169; Interaction with catenins; 1099..1169; Disordered; 1190..1244; Disordered; 1311..1376; Disordered; 1403..1475; Disordered; 1526..1569; Disordered; 1583..1611; Disordered; 1664..1717; Disordered; 1729..1836; Disordered; 1866..1893; Highly charged; 1881..1950; Disordered; 1965..2011; Disordered; 2035..2059; Interaction with AXIN1; 2043..2072; Disordered; 2147..2635; Disordered; 2167..2674; Basic region; 2475..2843; Interaction with DLG1; 2667..2714; Disordered; 2674..2843; Interaction with MAPRE1; 2729..2843; Disordered
Protein Families
Adenomatous polyposis coli (APC) family
Sequence Similarities
Belongs to the adenomatous polyposis coli (APC) family.
Clinical Relevance6
Disease Involvement (3)
Cancer-related genesDisease variantTumor suppressor
Drugs (46)
SURAMINNULLOSUGACESTATDACTOLISIBABIRATERONE ACETATEMRS2768ERLOTINIBPYRVINIUMICG-001DIQUAFOSOLLIOTHYRONINETETMYB DNA VACCINEENZALUTAMIDEADENOSINE TRIPHOSPHATEDASATINIB ANHYDROUSPSB-416URIDINE 5'-TRIPHOSPHATEAP4ANICLOSAMIDETRAMETINIB DIMETHYL SULFOXIDECELECOXIBDENUFOSOLNIROGACESTATUTP&GAMMASBUPARLISIBIBUPROFEN, SODIUM SALTDECITABINEMRS2698NONSTEROIDAL ANTIINFLAMMATORY DRUG4-THIO-UTP2-THIOUTPVINORELBINEVANDETANIBBINIMETINIBREACTIVE BLUE-2AR-C118925XX5BRUTPVANTICTUMABHISTONE DEACETYLASE INHIBITORSULINDACEFLORNITHINEPSB1114AR-C126313SIROLIMUSBASROPARIB
Interaction Protein (12)
ENSG00000044115ENSG00000082701ENSG00000101367ENSG00000103126ENSG00000150477ENSG00000164924ENSG00000166913ENSG00000168036ENSG00000173801ENSG00000175793ENSG00000176771ENSG00000213923
Interaction Count
12
Interaction Dataset (3)
intact_biogridintact_biogrid_opencellbiogrid_opencell
Supporting Publications1
| PMID | Title | Abstract |
|---|---|---|
| 35611462 | Extracellular vesicles expressing CEACAM proteins in the urine of bladder cancer patients. | No abstract available |