[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND VARIANT ASP-1822. TISSUE=Fetal brain; DOI=10.1016/0092-8674(81)90022-2; PubMed=1678319 [NCBI, ExPASy, EBI, Israel, Japan] Joslyn G., Carlson M., Thliveris A., Albertsen H., Gelbert L., Samowitz W., Groden J., Stevens J., Spirio L., Robertson M., Sargeant L., Krapcho K., Wolff E., Burt R., Hughes J.P., Warrington J., McPherson J.D., Wasmuth J.J., le Paslier D., Abderrahim H., Cohen D., Leppert M., White R.; "Identification of deletion mutations and three new genes at the familial polyposis locus."; Cell 66:601-613(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT ASP-1822. PubMed=1651562 [NCBI, ExPASy, EBI, Israel, Japan] Kinzler K.W., Nilbert M.C., Su L.-K., Vogelstein B., Bryan T.M., Levy D.B., Smith K.J., Preisinger A.C., Hedge P., McKechnie D., Finniear R., Markham A., Groffen J., Boguski M.S., Altschul S.F., Horii A.K., Ando H., Miyoshi Y., Miki Y., Nishisho I., Nakamura Y.; "Identification of FAP locus genes from chromosome 5q21."; Science 253:661-665(1991).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARHGEF4, AND IDENTIFICATION IN A COMPLEX WITH ARHGEF4 AND CTNNB1. DOI=10.1126/science.289.5482.1194; PubMed=10947987 [NCBI, ExPASy, EBI, Israel, Japan] Kawasaki Y., Senda T., Ishidate T., Koyama R., Morishita T., Iwayama Y., Higuchi O., Akiyama T.; "Asef, a link between the tumor suppressor APC and G-protein signaling."; Science 289:1194-1197(2000).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1506-1524. PubMed=1310068 [NCBI, ExPASy, EBI, Israel, Japan] Miki Y., Nishisho I., Horii A., Miyoshi Y., Utsunomiya J., Kinzler K.W., Vogelstein B., Nakamura Y.; "Disruption of the APC gene by a retrotransposal insertion of L1 sequence in a colon cancer."; Cancer Res. 52:643-645(1992).
[5]	ASSOCIATION WITH CATENINS. PubMed=8259519 [NCBI, ExPASy, EBI, Israel, Japan] Su L.-K., Vogelstein B., Kinzler K.W.; "Association of the APC tumor suppressor protein with catenins."; Science 262:1734-1737(1993).
[6]	INTERACTION WITH DLG1. PubMed=8638125 [NCBI, ExPASy, EBI, Israel, Japan] Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H., Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T.; "Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein."; Science 272:1020-1023(1996).
[7]	INTERACTION WITH DLG3. TISSUE=Fetal brain; DOI=10.1038/sj.onc.1201087; PubMed=9188857 [NCBI, ExPASy, EBI, Israel, Japan] Makino K., Kuwahara H., Masuko N., Nishiyama Y., Morisaki T., Sasaki J., Nakao M., Kuwano A., Nakata M., Ushio Y., Saya H.; "Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein."; Oncogene 14:2425-2433(1997).
[8]	INTERACTION WITH APC2. PubMed=11691822 [NCBI, ExPASy, EBI, Israel, Japan] Jarrett C.R., Blancato J., Cao T., Bressette D.S., Cepeda M., Young P.E., King C.R., Byers S.W.; "Human APC2 localization and allelic imbalance."; Cancer Res. 61:7978-7984(2001).
[9]	INTERACTION WITH MAPRE1; MAPRE2 AND MAPRE3. DOI=10.1074/jbc.M306194200; PubMed=14514668 [NCBI, ExPASy, EBI, Israel, Japan] Bu W., Su L.-K.; "Characterization of functional domains of human EB1 family proteins."; J. Biol. Chem. 278:49721-49731(2003).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861; SER-1863; SER-1864 AND SER-2398, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2283, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."; Nat. Biotechnol. 24:1285-1292(2006).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2125; SER-2671; SER-2674; THR-2676; SER-2789; SER-2835; SER-2837 AND TYR-2838, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).
[13]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-55. DOI=10.1006/jmbi.2000.3895; PubMed=10926498 [NCBI, ExPASy, EBI, Israel, Japan] Day C.L., Alber T.; "Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor."; J. Mol. Biol. 301:147-156(2000).
[14]	X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1021-1035 IN COMPLEX WITH CTNNB1. DOI=10.1093/emboj/20.22.6203; PubMed=11707392 [NCBI, ExPASy, EBI, Israel, Japan] Eklof Spink K., Fridman S.G., Weis W.I.; "Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex."; EMBO J. 20:6203-6212(2001).
[15]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2034-2049 IN COMPLEX WITH AXIN. DOI=10.1093/emboj/19.10.2270; PubMed=10811618 [NCBI, ExPASy, EBI, Israel, Japan] Spink K.E., Polakis P., Weis W.I.; "Structural basis of the axin-adenomatous polyposis coli interaction."; EMBO J. 19:2270-2279(2000).
[16]	REVIEW ON VARIANTS. PubMed=8111410 [NCBI, ExPASy, EBI, Israel, Japan] Nagase H., Nakamura Y.; "Mutations of the APC (adenomatous polyposis coli) gene."; Hum. Mutat. 2:425-434(1993).
[17]	VARIANTS FAP. PubMed=1651563 [NCBI, ExPASy, EBI, Israel, Japan] Nishisho I., Nakamura Y., Miyoshi Y., Miki Y., Ando H., Horii A., Koyama K., Utsunomiya J., Baba S., Hedge P., Markham A., Krush A.J., Petersen G.M., Hamilton S.R., Nilbert M.C., Levy D.B., Bryan T.M., Preisinger A.C., Smith K.J., Su L.-K., Kinzler K.W., Vogelstein B.; "Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients."; Science 253:665-669(1991).
[18]	VARIANTS FAP. DOI=10.1093/hmg/1.4.229; PubMed=1338904 [NCBI, ExPASy, EBI, Israel, Japan] Miyoshi Y., Nagase H., Ando H., Ichii S., Nakatsuru S., Aoki T., Miki Y., Mori T., Nakamura Y.; "Somatic mutations of the APC gene in colorectal tumors: mutation cluster region in the APC gene."; Hum. Mol. Genet. 1:229-233(1992).
[19]	VARIANTS FAP. DOI=10.1093/hmg/1.8.559; PubMed=1338691 [NCBI, ExPASy, EBI, Israel, Japan] Nakatsuru S., Yanagisawa A., Ichii S., Tahara E., Kato Y., Nakamura Y., Horii A.; "Somatic mutation of the APC gene in gastric cancer: frequent mutations in very well differentiated adenocarcinoma and signet-ring cell carcinoma."; Hum. Mol. Genet. 1:559-563(1992).
[20]	VARIANT FAP TRP-1348, AND VARIANTS ASP-1118; MET-1292; VAL-1304 AND SER-2502. PubMed=1338764 [NCBI, ExPASy, EBI, Israel, Japan] Nagase H., Miyoshi Y., Horii A., Aoki T., Petersen G.M., Vogelstein B., Maher E., Ogawa M., Maruyama M., Utsunomiya J., Baba S., Nakamura Y.; "Screening for germ-line mutations in familial adenomatous polyposis patients: 61 new patients and a summary of 150 unrelated patients."; Hum. Mutat. 1:467-473(1992).
[21]	VARIANT FAP TRP-99. TISSUE=Peripheral blood lymphocyte; DOI=10.1016/0959-8049(94)00294-F; PubMed=7833149 [NCBI, ExPASy, EBI, Israel, Japan] Dobbie Z., Spycher M., Huerliman R., Ammann R., Ammann T., Roth J., Mueller A., Mueller H., Scott R.J.; "Mutational analysis of the first 14 exons of the adenomatous polyposis coli (APC) gene."; Eur. J. Cancer 30A:1709-1713(1994).
[22]	VARIANT FAP GLY-722. DOI=10.1093/hmg/3.9.1687; PubMed=7833931 [NCBI, ExPASy, EBI, Israel, Japan] Stella A., Montera M., Resta N., Marchese C., Susca F., Gentile M., Romio L., Pilia S., Prete F., Mareni C., Guanti G.; "Four novel mutations of the APC (adenomatous polyposis coli) gene in FAP patients."; Hum. Mol. Genet. 3:1687-1688(1994).
[23]	ERRATUM. Stella A., Montera M., Resta N., Marchese C., Susca F., Gentile M., Romio L., Pilia S., Prete F., Mareni C., Guanti G.; Hum. Mol. Genet. 3:1918-1918(1994).
[24]	INVOLVEMENT IN TURCOT SYNDROME. DOI=10.1056/NEJM199503303321302; PubMed=7661930 [NCBI, ExPASy, EBI, Israel, Japan] Hamilton S.R., Liu B., Parsons R.E., Papadopoulos N., Jen J., Powell S.M., Krush A.J., Berk T., Cohen Z., Tetu B., Burger P.C., Wood P.A., Taqi F., Booker S.V., Petersen G.M., Offerhaus G.J.A., Tersmette A.C., Giardiello F.M., Vogelstein B., Kinzler K.W.; "The molecular basis of Turcot's syndrome."; N. Engl. J. Med. 332:839-847(1995).
[25]	INVOLVEMENT IN HEREDITARY DESMOID DISEASE. PubMed=8940264 [NCBI, ExPASy, EBI, Israel, Japan] Eccles D.M., van der Luijt R.B., Breukel C., Bullman H., Bunyan D., Fisher A., Barber J., du Boulay C., Primrose J., Burn J., Fodde R.; "Hereditary desmoid disease due to a frameshift mutation at codon 1924 of the APC gene."; Am. J. Hum. Genet. 59:1193-1201(1996).
[26]	VARIANT FAP ILE-171. DOI=10.1002/(SICI)1098-1004(1997)9:1<7::AID-HUMU2>3.3.CO;2-7; PubMed=8990002 [NCBI, ExPASy, EBI, Israel, Japan] van der Luijt R.B., Meera Khan P., Vasen H.F.A., Tops C.M.J., van Leeuwen-Cornelisse I.S.J., Wijnen J.T., van der Klift H.M., Plug R.J., Griffioen G., Fodde R.; "Molecular analysis of the APC gene in 105 Dutch kindreds with familial adenomatous polyposis: 67 germline mutations identified by DGGE, PTT, and southern analysis."; Hum. Mutat. 9:7-16(1997).
[27]	VARIANTS COLORECTAL CARCINOMA THR-880; ILE-890 AND VAL-1508. DOI=10.1038/sj.onc.1201668; PubMed=9419979 [NCBI, ExPASy, EBI, Israel, Japan] Miyaki M., Nishio J., Konishi M., Kikuchi-Yanoshita R., Tanaka K., Muraoka M., Nagato M., Chong J.-M., Koike M., Terada T., Kawahara Y., Fukutome A., Tomiyama J., Chuganji Y., Momoi M., Utsunomiya J.; "Drastic genetic instability of tumors and normal tissues in Turcot syndrome."; Oncogene 15:2877-2881(1997).
[28]	VARIANT LYS-1307. DOI=10.1038/1666; PubMed=9731522 [NCBI, ExPASy, EBI, Israel, Japan] Redston M., Nathanson K.L., Yuan Z.Q., Neuhausen S.L., Satagopan J., Wong N., Yang D., Nafa D., Abrahamson J., Ozcelik H., Antin-Ozerkis D., Andrulis I., Daly M., Pinsky L., Schrag D., Gallinger S., Kaback M., King M.-C., Woodage T., Brody L.C., Godwin A., Warner E., Weber B., Foulkes W., Offit K.; "The APC I1307K allele and breast cancer risk."; Nat. Genet. 20:13-14(1998).
[29]	VARIANTS LYS-1307 AND GLN-1317. TISSUE=Peripheral blood; DOI=10.1073/pnas.95.18.10722; PubMed=9724771 [NCBI, ExPASy, EBI, Israel, Japan] Frayling I.M., Beck N.E., Ilyas M., Dove-Edwin I., Goodman P., Pack K., Bell J.A., Williams C.B., Hodgson S.V., Thomas H.J.W., Talbot I.C., Bodmer W.F., Tomlinson I.P.M.; "The APC variants I1307K and E1317Q are associated with colorectal tumors, but not always with a family history."; Proc. Natl. Acad. Sci. U.S.A. 95:10722-10727(1998).
[30]	VARIANT LYS-1307. DOI=10.1038/1722; PubMed=9731533 [NCBI, ExPASy, EBI, Israel, Japan] Woodage T., King S.M., Wacholder S., Hartge P., Struewing J.P., McAdams M., Laken S.J., Tucker M.A., Brody L.C.; "The APC I1307K allele and cancer risk in a community-based study of Ashkenazi Jews."; Nat. Genet. 20:62-65(1998).
[31]	VARIANT LYS-1307. DOI=10.1086/302262; PubMed=9973276 [NCBI, ExPASy, EBI, Israel, Japan] Gryfe R., Di Nicola N., Lal G., Gallinger S., Redston M.; "Inherited colorectal polyposis and cancer risk of the APC I1307K polymorphism."; Am. J. Hum. Genet. 64:378-384(1999).
[32]	VARIANTS FAP CYS-1171 AND THR-2738, AND VARIANTS GLY-1057 AND ASP-1822. PubMed=9950360 [NCBI, ExPASy, EBI, Israel, Japan] Wallis Y.L., Morton D.G., McKeown C.M., Macdonald F.; "Molecular analysis of the APC gene in 205 families: extended genotype-phenotype correlations in FAP and evidence for the role of APC amino acid changes in colorectal cancer predisposition."; J. Med. Genet. 36:14-20(1999).
[33]	VARIANT FAP PRO-1184. DOI=10.1038/12511; PubMed=10470088 [NCBI, ExPASy, EBI, Israel, Japan] Lamlum H., Ilyas M., Rowan A., Clark S., Johnson V., Bell J.A., Frayling I.M., Efstathiou J., Pack K., Payne S., Roylance R., Gorman P., Sheer D., Neale K., Phillips R., Talbot I.C., Bodmer W.F., Tomlinson I.P.M.; "The type of somatic mutation at APC in familial adenomatous polyposis is determined by the site of the germline mutation: a new facet to Knudson's 'two-hit' hypothesis."; Nat. Med. 5:1071-1075(1999).
[34]	VARIANTS MDB VAL-1296; ILE-1472 AND GLY-1495. PubMed=10666372 [NCBI, ExPASy, EBI, Israel, Japan] Huang H., Mahler-Araujo B.M., Sankila A., Chimelli L., Yonekawa Y., Kleihues P., Ohgaki H.; "APC mutations in sporadic medulloblastomas."; Am. J. Pathol. 156:433-437(2000).
[35]	INVOLVEMENT IN HEREDITARY DESMOID DISEASE. PubMed=10782927 [NCBI, ExPASy, EBI, Israel, Japan] Couture J., Mitri A., Lagace R., Smits R., Berk T., Bouchard H.-L., Fodde R., Alman B., Bapat B.; "A germline mutation at the extreme 3' end of the APC gene results in a severe desmoid phenotype and is associated with overexpression of beta-catenin in the desmoid tumor."; Clin. Genet. 57:205-212(2000).
[36]	VARIANT [LARGE SCALE ANALYSIS] PHE-1254. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).

Comments

FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling. APC activity is correlated with its phosphorylation state.
SUBUNIT: Forms homooligomers. Interacts with DIAPH1 and DIAPH2 (By similarity). Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with the N-terminus of ARHGEF4, and the C-terminus of MAPRE1, MAPRE2 and MAPRE3. Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with APC2.
INTERACTION:
P49674:CSNK1E; NbExp=1; IntAct=EBI-727707, EBI-749343;
Q02248:Ctnnb1 (xeno); NbExp=3; IntAct=EBI-727707, EBI-397872;
Q15691:MAPRE1; NbExp=1; IntAct=EBI-727707, EBI-1004115;
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name Long

Isoform ID P25054-1

This is the isoform sequence displayed in this entry.

Name Short

Isoform ID P25054-2

Features which should be applied to build the isoform sequence: VSP_004115.
TISSUE SPECIFICITY: Expressed in a variety of tissues.
PTM: Phosphorylated by GSK3B.
DISEASE: Defects in APC are a cause of familial adenomatous polyposis (FAP) [MIM:175100]; which includes also Gardner syndrome (GS). FAP and GS contribute to tumor development in patients with uninherited forms of colorectal cancer. FAP is 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.
DISEASE: 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.
DISEASE: Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:135290]; also called familial infiltrative fibromatosis (FIF). It is an autosomal 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.
DISEASE: Defects in APC are a cause of medulloblastoma (MDB) [MIM:155255]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome).
DISEASE: Defects in APC are a cause of Turcot syndrome [MIM:276300]. Turcot syndrome is an autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.
SIMILARITY: Belongs to the adenomatous polyposis coli (APC) family.
SIMILARITY: Contains 7 ARM repeats.
WEB RESOURCE: Name=APC; Note=Information about APC mutations; URL="http://p53.curie.fr/p53%20site%20version%202.0/APCdatabase.html#Anchor-47857";.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/APC118.html";.
WEB RESOURCE: Name=GeneDis; Note=Familial adenomatous polyposis (FAP) website; URL="http://life2.tau.ac.il/GeneDis/Tables/APC/apc.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=APC";.
WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APC";.
WEB RESOURCE: Name=Wikipedia; Note=APC entry; URL="http://en.wikipedia.org/wiki/APC_%28gene%29";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M73548; AAA60353.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M73548; AAA60354.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M74088; AAA03586.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S78214; AAB21145.2; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A37261; RBHUAP.

RefSeq

NP_000029.2; -.
NP_001120982.1; -.
NP_001120983.1; -.

UniGene

Hs.158932

3D structure databases

PDB

1DEB; X-ray; 2.40 A; A/B=2-55.	[ExPASy / RCSB / EBI]
1EMU; X-ray; 1.90 A; B=2034-2049.	[ExPASy / RCSB / EBI]
1JPP; X-ray; 3.10 A; C/D=1021-1035.	[ExPASy / RCSB / EBI]
1M5I; X-ray; 2.00 A; A=126-250.	[ExPASy / RCSB / EBI]
1T08; X-ray; 2.10 A; C=1484-1498.	[ExPASy / RCSB / EBI]
1TH1; X-ray; 2.50 A; C/D=1362-1540.	[ExPASy / RCSB / EBI]
1V18; X-ray; 2.10 A; B=1482-1528.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DEB; -.
1EMU; -.
1JPP; -.
1M5I; -.
1T08; -.
1TH1; -.
1V18; -.

DisProt

DP00519; -.

ModBase

P25054.

Protein-protein interaction databases

IntAct

P25054; -.

PTM databases

PhosphoSite

P25054; -.

Enzyme and pathway databases

Reactome

REACT_11045; Signaling by Wnt.

Organism-specific databases

HIX0031955; -.

HGNC:583; APC.

APC.

CAB002211; -.

135290; phenotype. [NCBI / EBI]
155255; phenotype. [NCBI / EBI]
175100; phenotype. [NCBI / EBI]
276300; phenotype. [NCBI / EBI]
611731; gene. [NCBI / EBI]

Orphanet

873; Desmoid disease.
733; Familial adenomatous polyposis.
616; Medulloblastoma.

PharmGKB

PA24875; -.

GeneCards

P25054.

Gene expression databases

ArrayExpress

P25054; -.

CleanEx

HS_APC; -.

GermOnline

ENSG00000134982; Homo sapiens.

Ontologies

GO:0030877;	Cellular component: beta-catenin destruction complex (inferred from direct assay from UniProtKB).
GO:0005813;	Cellular component: centrosome (inferred from direct assay from UniProtKB).
GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0000776;	Cellular component: kinetochore (inferred from direct assay from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0008013;	Molecular function: beta-catenin binding (inferred from physical interaction from UniProtKB).
GO:0008017;	Molecular function: microtubule binding (inferred from direct assay from UniProtKB).
GO:0019901;	Molecular function: protein kinase binding (inferred from direct assay from UniProtKB).
GO:0008605;	Molecular function: protein kinase CK2 regulator activity (inferred from direct assay from UniProtKB).
GO:0007155;	Biological process: cell adhesion (non-traceable author statement from UniProtKB).
GO:0007050;	Biological process: cell cycle arrest (inferred from direct assay from UniProtKB).
GO:0008285;	Biological process: negative regulation of cell proliferation (inferred from direct assay from UniProtKB).
GO:0045736;	Biological process: negative regulation of cyclin-dependent protein kinase activity (inferred from direct assay from UniProtKB).
GO:0007026;	Biological process: negative regulation of microtubule depolymerization (inferred from direct assay from UniProtKB).
GO:0006461;	Biological process: protein complex assembly (inferred from direct assay from UniProtKB).
GO:0051988;	Biological process: regulation of attachment of spindle microtubules to kinetochore (non-traceable author statement from UniProtKB).
GO:0006974;	Biological process: response to DNA damage stimulus (inferred from direct assay from UniProtKB).
GO:0060070;	Biological process: Wnt receptor signaling pathway through beta-catenin (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR009240; APC_15aa.
IPR009234; APC_basic.
IPR009223; APC_crr.
IPR011989; ARM-like.
IPR000225; Armadillo.
IPR009232; EB1_bd.
IPR009224; SAMP.
Graphical view of domain structure.

Gene3D

G3DSA:1.25.10.10; ARM-like; 1.

Pfam

PF05972; APC_15aa; 4.
PF05956; APC_basic; 1.
PF05923; APC_crr; 7.
PF00514; Arm; 4.
PF05937; EB1_binding; 1.
PF05924; SAMP; 3.
Pfam graphical view of domain structure.

SMART

SM00185; ARM; 6.
SMART graphical view of domain structure.

PROSITE

PS50176; ARM_REPEAT; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P25054.

Genome annotation databases

Ensembl

ENSG00000134982; Homo sapiens. [Contig view]

GeneID

324; -.

KEGG

hsa:324; -.

Phylogenomic databases

HOVERGEN

P25054; -.

Other

APC; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Anti-oncogene; Cell cycle; Coiled coil; Disease mutation; Phosphoprotein; Polymorphism; Repeat; Wnt signaling pathway.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 2843`	`2843`	`Adenomatous polyposis coli protein.`	`PRO_0000064627`
`REPEAT`	`453 495`	`43`	`ARM 1.`
`REPEAT`	`505 547`	`43`	`ARM 2.`
`REPEAT`	`548 591`	`44`	`ARM 3.`
`REPEAT`	`592 638`	`47`	`ARM 4.`
`REPEAT`	`639 683`	`45`	`ARM 5.`
`REPEAT`	`684 725`	`42`	`ARM 6.`
`REPEAT`	`726 767`	`42`	`ARM 7.`
`REGION`	`1866 1893`	`28`	`Highly charged.`
`COILED`	`1 61`	`61`	`Potential.`
`COILED`	`127 248`	`122`	`Potential.`
`MOTIF`	`2841 2843`	`3`	`PDZ-binding.`
`COMPBIAS`	`1 730`	`730`	`Leu-rich.`
`COMPBIAS`	`731 2832`	`2102`	`Ser-rich.`
`COMPBIAS`	`1131 1156`	`26`	`Asp/Glu-rich (acidic).`
`COMPBIAS`	`1558 1577`	`20`	`Asp/Glu-rich (acidic).`
`MOD_RES`	`1038 1038`		`Phosphoserine (By similarity).`
`MOD_RES`	`1180 1180`		`Phosphoserine (By similarity).`
`MOD_RES`	`1371 1371`		`Phosphoserine (By similarity).`
`MOD_RES`	`1697 1697`		`Phosphothreonine (By similarity).`
`MOD_RES`	`1861 1861`		`Phosphoserine.`
`MOD_RES`	`1863 1863`		`Phosphoserine.`
`MOD_RES`	`1864 1864`		`Phosphoserine.`
`MOD_RES`