Protein detail

APC

Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)

Entry name
APC
UniProt ID
EVMP score
0.50
Frequency
1
Transmembrane count
Protein classification
Cancer-related genesDisease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)
Protein Class
Cancer-related genesDisease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins
Protein Function
  • 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
Entrez Gene Symbol
Gene Synonym
DP2DP2.5DP3PPP1R46
Gene Description
APC regulator of WNT signaling pathway
Chromosome
5
Position
112707498-112846239
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
APC fluorescence
Tissue SpecificbrainCell SpecificAstrocytesSingle-Nuclei Brain SpecificBergmann gliaSecretome LocationSecreted in brainSecretome FunctionEnzyme
Function & Pathway
Protein Function
  • 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
Mediation Categories
Clinical-translation mediationFusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

53 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
APCCSNK1DP48730S1,504phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
APCCSNK1DP48730S1,505phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
APCCSNK1DP48730S1,279phosphorylationKEAKEA:11487578
APCCSNK1DP48730S1,392phosphorylationKEAKEA:11487578
APCGSK3BP49841S1,501phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperKEAPhosphoSitePhosphoSite_ProtMapperKEA:15327768
APCGSK3BP49841S1,503phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperKEAPhosphoSitePhosphoSite_ProtMapperKEA:15327768
APCCDK2P24941S1,360phosphorylationphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
APCCSNK1A1P48729S1,507phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
APCCSNK1A1P48729S1,510phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
APCCSNK1A1P48729S1,504phosphorylationPhosphoSite_MIMPMIMPHPRD_MIMPProtMapperPhosphoSitePhosphoSite_ProtMapper
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Ligand-Receptor Signaling

15 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
cell_adhesioncell_adhesionCellinkerYesYesNoNoNo
adhesionadhesionOmniPathYesYesNoNoNo
cell_adhesioncell_adhesionOmniPathYesYesNoNoNo
tight_junctiontight_junctionGO_IntercellYesYesNoNoNo
tight_junctiontight_junctionOmniPathYesYesNoNoNo
Page 1 of 2Next

Regulatory Interaction Network

15 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
K2C1P04264APCP25054YesYesNoSPIKE_LCSIGNORSPIKE_LC:17145710SIGNOR:18359618
KAPCAP17612APCP25054YesNoYesphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDPhosphoSite_KEAKEAACSNHPRD_KEASIGNOR_ProtMapperHPRD-phosSIGNOR:11050185HPRD-phos:11050185ACSN:11689703HPRD:11050185HPRD:11166179ProtMapper:11050185ACSN:15649893KEA:11050185
AMER1Q5JTC6APCP25054YesYesNoHINTSIGNORIntActIntAct:24251807SIGNOR:23151663IntAct:17510365HINT:27462415HINT:24251807HINT:26496610
KC1AP48729APCP25054YesYesNoPhosphoSite_MIMPMIMPHPRD_MIMPPhosphoSite_norefPhosphoPointiPTMnetProtMapperELMPhosphoSite_KEAKEAWangPhosphoSitePhosphoSite_ProtMapperKEA:11487578ELM:17910481PhosphoSite:12628243
CDK2P24941APCP25054YesNoNophosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetProtMapperELMPhosphoSitePhosphoSite_ProtMapperPhosphoSite:19703905ELM:19703905
Page 2 of 2Previous

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyMass spectrometry3387318684003316337922300
Sequence, Structure & Domains

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 Relevance