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 >= 0.40
Basic 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
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
APC fluorescence
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
Mediation Categories (4)
Clinical-translation mediationFusion and delivery mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence181

Enzyme-Mediated Modification (53)

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)

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
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Regulatory Interaction Network (15)

15 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
GSK3BP49841APCP25054YesYesNoHPRD_MIMPSIGNORProtMapperHINTInnateDBHPRDCancerCellMapWangPhosphoSite_ProtMapperPhosphoSite_MIMPMIMPPhosphoSite_norefPhosphoPointiPTMnetKEAHPRD_KEAPhosphoSiteNetPathACSNSPIKE_LCSPIKEACSN:15020233HINT:21118991ACSN:11967263HINT:8638126ACSN:16944320CancerCellMap:10228155ACSN:15327768ProtMapper:15327768ACSN:17318175SIGNOR:10698523NetPath:16799642ACSN:8524413KEA:15327768HINT:35271311ACSN:11487578ACSN:14663202SPIKE:10698523SPIKE_LC:10698523ACSN:12554650CancerCellMap:8638126ACSN:10581160HPRD:8638126PhosphoSite:17910481ACSN:15465828NetPath:8638126HPRD:11166179ACSN:10421629NetPath:10228155InnateDB:8638126ACSN:8638126ACSN:9832503
APCP25054CTNB1P35222YesYesYesWangNetPathSIGNORProtMapperREACH_ProtMapperHPRDCui2007HINTBioGRIDIntActInnateDBCancerCellMapSPIKE_LCLit-BM-17SPIKELit-BM-17:11251183SPIKE_LC:17318191HPRD:15327769HINT:12628243HINT:22682247IntAct:15327769Lit-BM-17:8259519HPRD:9482734Lit-BM-17:12628243SPIKE_LC:17145710IntAct:8638126BioGRID:11533658HINT:8638126ProtMapper:19631635SPIKE:17145710HINT:15525529SPIKE_LC:19061640HINT:8259519HINT:36950384HINT:17318191Lit-BM-17:19576224Lit-BM-17:15327769HPRD:7890674Lit-BM-17:22682247Lit-BM-17:10545404Lit-BM-17:23840886SPIKE:16798748IntAct:9707618SPIKE:19061640IntAct:25241761IntAct:22682247Lit-BM-17:11707392Lit-BM-17:15355978Lit-BM-17:26496610Lit-BM-17:17318191InnateDB:11533658Lit-BM-17:9286858Lit-BM-17:16212417NetPath:8628279Lit-BM-17:27902311HPRD:12628243Lit-BM-17:15327768HINT:35271311InnateDB:15525529SPIKE_LC:15327769HINT:11707392SPIKE_LC:16798748HINT:22056988Lit-BM-17:11972058HINT:16212417HPRD:12000790IntAct:22056988ProtMapper:26910375Lit-BM-17:11533658IntAct:17318191SIGNOR:22083140HINT:15327769HINT:26496610SPIKE:9065401HINT:33961781Lit-BM-17:21664290HINT:9707618HPRD:15327768Lit-BM-17:11712088Lit-BM-17:25241761SPIKE:17318191SPIKE:15327769CancerCellMap:9065403NetPath:8638126HPRD:11166179BioGRID:10545404HINT:15294866HINT:16510874Lit-BM-17:15525529HINT:15327768SPIKE_LC:9065401
AXIN1O15169APCP25054YesYesNoMacrophageNetPathSIGNORHPRDCui2007HINTIntActCancerCellMapWangLit-BM-17HINT:22682247Lit-BM-17:16199882Lit-BM-17:22682247CancerCellMap:10228155Lit-BM-17:26496610Lit-BM-17:23277359HINT:18786926Lit-BM-17:10228155IntAct:10811618HINT:9734785HPRD:11297546Lit-BM-17:19131971HINT:26496610HPRD:9734785HINT:19131971Lit-BM-17:20128690Macrophage:9554852HINT:10811618NetPath:10228155Lit-BM-17:9734785SIGNOR:9734785
CC14BO60729APCP25054YesYesNoSIGNORSIGNOR:18662541
AXIN2Q9Y2T1APCP25054YesYesNoWangHPRDNetPathSIGNORNetPath:9554852SIGNOR:10911903HPRD:10966653
KC1EP49674APCP25054YesYesNoHPRD_MIMPSIGNORProtMapperHINTPhosphoSite_KEAphosphoELM_KEALit-BM-17PhosphoNetworksHPRDIntActWangPhosphoSite_ProtMapperNetworKIN_KEAphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_norefPhosphoPointiPTMnetKEAHPRD_KEAphosphoELMSIGNOR_ProtMapperPhosphoSiteSPIKE_LCHPRD-phosPhosphoSite:11487578SPIKE_LC:17145710SIGNOR:11487578HPRD:11487578ProtMapper:11487578IntAct:25241761ProtMapper:15327768KEA:11487578IntAct:11425858Lit-BM-17:17218255HINT:11425858KEA:15327768IntAct:17218255HINT:17218255PhosphoSite:24722208HPRD:15327768Lit-BM-17:25241761phosphoELM:11487578HPRD-phos:11487578Lit-BM-17:11425858KEA:17570479
ACHB3Q05901APCP25054YesYesNoSIGNORSIGNOR:14502292
BUB1BO60566APCP25054YesYesNoSIGNORSIGNOR:17709426
KPCDQ05655APCP25054YesNoYesSIGNORSIGNOR:23520519
DVL1O14640APCP25054YesNoYesWangHINTSIGNORIntActIntAct:20224554HINT:11425858SIGNOR:10330181HINT:20224554
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Protein Complex Composition (97)

97 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
ANAPC1ANAPC10ANAPC11ANAPC2ANAPC4ANAPC5BUB1BCCNB1CDC16CDC20CDC23CDC27FZR1TP53I3UBR1O60566P14635P30260Q12834Q13042Q53FA7Q8IWV7Q9H1A4Q9NYG5Q9UJX2Q9UJX4Q9UJX5Q9UJX6Q9UM11Q9UM131:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC8087
ANAPC1ANAPC10ANAPC11ANAPC13ANAPC15ANAPC16ANAPC2ANAPC4ANAPC5ANAPC7BUB1BCDC16CDC20CDC23CDC26CDC27MAD2L1O60566P30260P60006Q12834Q13042Q13257Q8NHZ8Q96DE5Q9BS18Q9H1A4Q9NYG5Q9UJX2Q9UJX3Q9UJX4Q9UJX5Q9UJX6Q9UM131:2:1:2:2:1:2:1:1:1:1:2:2:1:1:1:1PDBPDB:6tljPDB:5lcw
ANAPC1ANAPC10ANAPC11ANAPC13ANAPC16ANAPC2ANAPC4ANAPC5ANAPC7BUB1BCDC16CDC20CDC23CDC26CDC27MAD2L1O60566P30260Q12834Q13042Q13257Q8NHZ8Q96DE5Q9BS18Q9H1A4Q9NYG5Q9UJX2Q9UJX3Q9UJX4Q9UJX5Q9UJX6Q9UM131:2:2:2:1:2:1:1:1:1:2:2:1:1:1:1PDBPDB:5khu
ANAPC1ANAPC10ANAPC11ANAPC2ANAPC4ANAPC5CCNB1CDC14BCDC16CDC20CDC23CDC27FZR1NAP1L1TPX2O60729P14635P30260P55209Q12834Q13042Q9H1A4Q9NYG5Q9UJX2Q9UJX4Q9UJX5Q9UJX6Q9ULW0Q9UM11Q9UM131:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC7475
GTF2A1GTF2A2GTF2BSNAPC1SNAPC3SNAPC4SNAPC5TBPO75971P20226P52655P52657Q00403Q16533Q5SXM2Q929661:1:1:1:1:1:1:1PDBPDB:7zwcPDB:7zxe
SNAPC1SNAPC2SNAPC3SNAPC5O75971Q13487Q16533Q929660:0:0:0hu.MAP
APCSEC13SEC23ASEC31AUBCO94979P0CG48P25054P55735Q154361:1:1:1:1CompleatCFinderCompleat:HC5694
ANAPC10CCNA2CCNB1CCNB2CDC16CDC20CDC23CDC27CDK1CDK2CHAF1BCKS1BCKS2FZR1TSPYL2O95067P06493P14635P20248P24941P30260P33552P61024Q12834Q13042Q13112Q9H2G4Q9UJX2Q9UM11Q9UM131:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC7127
APCSP027435PDBPDB:1lgnPDB:1gykPDB:4avvPDB:2a3wPDB:4ayuPDB:3kqrPDB:2w08PDB:4avsPDB:2a3yPDB:2a3xPDB:4avtPDB:1sac
APCDD1CTSGELANEICE2MPOMUC5ACP05164P08246P08311P98088Q659A1Q8J0250:0:0:0:0:0hu.MAP2
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Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyMass spectrometry3387318684003316337922300
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
Supporting Publications1
PMIDTitleAbstract
35611462Extracellular vesicles expressing CEACAM proteins in the urine of bladder cancer patients.No abstract available