APC
entrez
324
canonical
uniprot
P25054
canonical
ensembl
ENSG00000134982
resolver
ensp
ENSP00000257430
resolver
ensp
ENSP00000423224
resolver
ensp
ENSP00000426541
resolver
ensp
ENSP00000427089
resolver
ensp
ENSP00000473355
resolver
ensp
ENSP00000518940
resolver
ensp
ENSP00000587993
resolver
ensp
ENSP00000587994
resolver
ensp
ENSP00000621226
resolver
ensp
ENSP00000696284
resolver
ensp
ENSP00000750891
resolver
ensp
ENSP00000750892
resolver
enst
ENST00000504915
resolver
enst
ENST00000951167
resolver
genesymbol
APC
resolver
genesymbol_syn
DP2.5
resolver
hgnc
HGNC:583
resolver
uniprot
B7Z2B6
resolver
uniprot
D3DT03
resolver
uniprot
Q15162
resolver
uniprot
Q15163
resolver
uniprot
Q93042
resolver
uniprot
R4GMU6
resolver
uniprot_entry
APC_HUMAN
resolver
uniprot_entry
R4GMU6_HUMAN
resolver
uniprot_sec
B7Z2B6
resolver
uniprot_sec
D3DT03
resolver
uniprot_sec
Q15162
resolver
uniprot_sec
Q15163
resolver
uniprot_sec
Q93042
resolver
amino_acid_sequence
MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRIRQLLQSQATEAERSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKRHVDQPIDYSLKYATDIPSSQKQSFSFSKSSSGQSSKTEHMSSSSENTSTPSSNAKRQNQLHPSSAQSRSGQPQKAATCKVSSINQETIQTYCVEDTPICFSRCSSLSSLSSAEDEIGCNQTTQEADSANTLQIAEIKEKIGTRSAEDPVSEVPAVSQHPRTKSSRLQGSSLSSESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLMFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTAQTKREVPKNKAPTAEKRESGPKQAAVNAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPKESNENQEKEAEKTIDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKPAQTASKLPPPVARKPSQLPVYKLLPSQNRLQPQKHVSFTPGDDMPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGEGVRGGAQSGEFEKRDTIPTEGRSTDEAQGGKTSSVTIPELDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASASSSAPNKNQLDGKKKKPTSPVKPIPQNTEYRTRVRKNADSKNNLNAERVFSDNKDSKKQNLKNNSKVFNDKLPNNEDRVRGSFAFDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKAKENKESEAKVTSHTELTSNQQSANKTQAIAKQPINRGQPKPILQKQSTFPQSSKDIPDRGAATDEKLQNFAIENTPVCFSHNSSLSSLSDIDQENNNKENEPIKETEPPDSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKKPSRLKGDNEKHSPRNMGGILGEDLTLDLKDIQRPDSEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLETKKIESESKGIKGGKKVYKSLITGKVRSNSEISGQMKQPLQANMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGQTATTSPRGAKPSVKSELSPVARQTSQIGGSSKAPSRSGSRDSTPSRPAQQPLSRPIQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQMSQQNLTKQTGLSKNASSIPRSESASKGLNQMNNGNGANKKVELSRMSSTKSSGSESDRSERPVLVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPASPTRSQAQTPVLSPSLPDMSLSTHSSVQAGGWRKLPPNLSPTIEYNDGRPAKRHDIARSHSESPSRLPINRSGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSISGTKQSKENQVSAKGTWRKIKENEFSPTNSTSQTVSSGATNGAESKTLIYQMAPAVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKANPNIKDSKDNQAKQNVGNGSVPMRTVGLENRLNSFIQVDAPDQKGTEIKPGQNNPVPVSETNESSIVERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVNNNTKKRDSKTDSTESSGTQSPKRHSGSYLVTSV
uniprot
proteins
disease_involvement
DISEASE: Familial adenomatous polyposis 1 (FAP1) [MIM:175100]: An autosomal dominant 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. {ECO:0000269|PubMed:10470088, ECO:0000269|PubMed:1316610, ECO:0000269|PubMed:1338691, ECO:0000269|PubMed:1338764, ECO:0000269|PubMed:1338904, ECO:0000269|PubMed:1651563, ECO:0000269|PubMed:21643010, ECO:0000269|PubMed:27217144, ECO:0000269|PubMed:7661930, ECO:0000269|PubMed:7833149, ECO:0000269|PubMed:7833931, ECO:0000269|PubMed:8111410, ECO:0000269|PubMed:8990002}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Desmoid disease, hereditary (DESMD) [MIM:135290]: An autosomal dominant disease characterized by multifocal fibromatosis of the abdominal wall and mesentery. Desmoid tumors can also affect paraspinal muscles, breast, occiput, arms, and lower ribs. {ECO:0000269|PubMed:10782927, ECO:0000269|PubMed:8940264}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. {ECO:0000269|PubMed:10666372, ECO:0000269|PubMed:29753700}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A 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. {ECO:0000269|PubMed:1338691}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A 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. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Gastric adenocarcinoma and proximal polyposis of the stomach (GAPPS) [MIM:619182]: A familial gastric polyposis syndrome characterized by autosomal dominant transmission of fundic gland polyposis with occasional hyperplastic and adenomatous polyps, sparing of the gastric antrum, and a significant risk of intestinal-type gastric adenocarcinoma development. Colorectal polyposis is not observed, and family history does not include colorectal cancer. {ECO:0000269|PubMed:27087319, ECO:0000269|PubMed:27343414, ECO:0000269|PubMed:33242120}. Note=The gene represented in this entry may be involved in disease pathogenesis.
uniprot
proteins
function
FUNCTION: 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. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). 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. {ECO:0000250|UniProtKB:Q61315, ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:17293347, ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19151759, ECO:0000269|PubMed:19893577, ECO:0000269|PubMed:20937854}.
uniprot
proteins
mass_dalton
311646
uniprot
proteins
mutagenesis
MUTAGEN 516; /note="K->E: Impairs interaction with KHDRBS1."; /evidence="ECO:0000269|PubMed:22000517"; MUTAGEN 549; /note="R->E: Impairs interaction with KHDRBS1."; /evidence="ECO:0000269|PubMed:22000517"; MUTAGEN 2841; /note="T->L: Loss of interaction with SCRIB."; /evidence="ECO:0000269|PubMed:16611247"; MUTAGEN 2843; /note="V->Q: Loss of interaction with SCRIB."; /evidence="ECO:0000269|PubMed:16611247
uniprot
proteins
post_translational_modification
PTM: Phosphorylated; phosphorylation enhances the F-actin bundling activity (PubMed:17293347). Phosphorylated by GSK3B. {ECO:0000269|PubMed:17293347}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID. {ECO:0000269|PubMed:15355978, ECO:0000269|PubMed:18281465}.
uniprot
proteins
protein_family
Adenomatous polyposis coli (APC) family
uniprot
proteins
pubmed
10470088
uniprot
proteins
pubmed
10666372
uniprot
proteins
pubmed
10782927
uniprot
proteins
pubmed
10811618
uniprot
proteins
pubmed
10926498
uniprot
proteins
pubmed
10947987
uniprot
proteins
pubmed
11691822
uniprot
proteins
pubmed
11707392
uniprot
proteins
pubmed
1310068
uniprot
proteins
pubmed
1316610
uniprot
proteins
pubmed
1338691
uniprot
proteins
pubmed
1338764
uniprot
proteins
pubmed
1338904
uniprot
proteins
pubmed
14514668
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15355978
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
1651562
uniprot
proteins
pubmed
1651563
uniprot
proteins
pubmed
16611247
uniprot
proteins
pubmed
1678319
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17293347
uniprot
proteins
pubmed
17599059
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18281465
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19151759
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19527921
uniprot
proteins
pubmed
19632184
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19893577
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20509626
uniprot
proteins
pubmed
20937854
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21498506
uniprot
proteins
pubmed
21643010
uniprot
proteins
pubmed
21871439
uniprot
proteins
pubmed
22000517
uniprot
proteins
pubmed
22128170
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25169422
uniprot
proteins
pubmed
27087319
uniprot
proteins
pubmed
27217144
uniprot
proteins
pubmed
27343414
uniprot
proteins
pubmed
29753700
uniprot
proteins
pubmed
33242120
uniprot
proteins
pubmed
7661930
uniprot
proteins
pubmed
7833149
uniprot
proteins
pubmed
7833931
uniprot
proteins
pubmed
8111410
uniprot
proteins
pubmed
8259519
uniprot
proteins
pubmed
8638125
uniprot
proteins
pubmed
8764128
uniprot
proteins
pubmed
8940264
uniprot
proteins
pubmed
8990002
uniprot
proteins
pubmed
9188857
uniprot
proteins
pubmed
9419979
uniprot
proteins
pubmed
9724771
uniprot
proteins
pubmed
9731522
uniprot
proteins
pubmed
9731533
uniprot
proteins
pubmed
9950360
uniprot
proteins
pubmed
9973276
uniprot
proteins
sequence_length
2843
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:16611247}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:20937854}. Cell projection, lamellipodium {ECO:0000269|PubMed:19151759}. Cell projection, ruffle membrane {ECO:0000269|PubMed:19151759}. Cytoplasm {ECO:0000269|PubMed:10947987}. Cell membrane {ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:16611247, ECO:0000269|PubMed:20937854}. Note=Associated with the microtubule network at the growing distal tip of microtubules (PubMed:19632184). MAPRE1 may be required for targeting to the growing microtubule plus ends (PubMed:19632184). Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment (PubMed:19151759). The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane (PubMed:20937854). {ECO:0000269|PubMed:19151759, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:20937854}.
uniprot
proteins