[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. DOI=10.1126/science.1651562; 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. DOI=10.1126/science.8259519; 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]	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).
[7]	INTERACTION WITH DLG1. DOI=10.1126/science.272.5264.1020; 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).
[8]	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).
[9]	INVOLVEMENT IN HEREDITARY DESMOID DISEASE. DOI=10.1034/j.1399-0004.2000.570306.x; 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).
[10]	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).
[11]	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).
[12]	UBIQUITINATION. DOI=10.1074/jbc.M404655200; PubMed=15355978 [NCBI, ExPASy, EBI, Israel, Japan] Choi J., Park S.Y., Costantini F., Jho E.-H., Joo C.-K.; "Adenomatous polyposis coli is down-regulated by the ubiquitin-proteasome pathway in a process facilitated by Axin."; J. Biol. Chem. 279:49188-49198(2004).
[13]	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).
[14]	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).
[15]	DEUBIQUITINATION. DOI=10.1101/gad.463208; PubMed=18281465 [NCBI, ExPASy, EBI, Israel, Japan] Tran H., Hamada F., Schwarz-Romond T., Bienz M.; "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."; Genes Dev. 22:528-542(2008).
[16]	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).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780; SER-1042; SER-1360; SER-1861; SER-1863; SER-1864; SER-2088; SER-2093; SER-2096; SER-2143; THR-2151; SER-2260; SER-2270; SER-2283; SER-2464; SER-2469; SER-2473; SER-2533; SER-2535; SER-2671; SER-2674; THR-2679 AND SER-2789, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]	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).
[19]	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).
[20]	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).
[21]	REVIEW ON VARIANTS. DOI=10.1002/humu.1380020602; 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).
[22]	VARIANTS FAP. DOI=10.1126/science.1651563; 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).
[23]	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).
[24]	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).
[25]	VARIANT FAP TRP-1348, AND VARIANTS ASP-1118; MET-1292; VAL-1304 AND SER-2502. DOI=10.1002/humu.1380010603; 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).
[26]	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).
[27]	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).
[28]	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).
[29]	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).
[30]	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).
[31]	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).
[32]	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).
[33]	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).
[34]	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).
[35]	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).
[36]	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).
[37]	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).
[38]	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).
[39]	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 as a negative regulator. 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.
PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID.
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://www.tau.ac.il/lifesci/bioinfo/genedis/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]

IPI

IPI00012391; -.
IPI00215877; -.

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; 14.

PTM databases

PhosphoSite

P25054; -.

Enzyme and pathway databases

Pathway_Interaction_DB

wnt_canonical_pathway; Canonical Wnt signaling pathway.
ps1pathway; Presenilin action in Notch and Wnt signaling.

Reactome

REACT_11045; Signaling by Wnt.
REACT_578; Apoptosis.

Organism-specific databases

GC05P112101; -.

HIX0031955; -.

HGNC:583; APC.

APC.

HPA013349; -.

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; -.

Gene expression databases

P25054; -.

P25054; -.

HS_APC; -.

ENSG00000134982; Homo sapiens.

Ontologies

GO:0034747;	Cellular component: Axin-APC-beta-catenin-GSK3B complex (inferred from direct assay from UniProtKB).
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:0016328;	Cellular component: lateral plasma membrane (inferred from direct assay from MGI).
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 physical interaction from UniProtKB).
GO:0019887;	Molecular function: protein kinase 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:0000281;	Biological process: cytokinesis after mitosis (inferred from mutant phenotype from MGI).
GO:0007094;	Biological process: mitotic cell cycle spindle assembly checkpoint (inferred from mutant phenotype from MGI).
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:0043065;	Biological process: positive regulation of apoptosis (inferred from mutant phenotype from MGI).
GO:0030335;	Biological process: positive regulation of cell migration (inferred from mutant phenotype from MGI).
GO:0031274;	Biological process: positive regulation of pseudopodium assembly (inferred from mutant phenotype from MGI).
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).

Proteomic databases

PRIDE

P25054; -.

Genome annotation databases

Ensembl

ENSG00000134982; Homo sapiens. [Contig view]

GeneID

324; -.

KEGG

hsa:324; -.

Phylogenomic databases

HOVERGEN

P25054; -.

OMA

P25054; FATESTP.

Other

1329; -.

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; Ubl conjugation; 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`	`960 1337`	`378`	`Responsible for down-regulation through a process mediated by direct ubiquitination.`
`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`	`780 780`		`Phosphoserine.`
`MOD_RES`	`1038 1038`		`Phosphoserine (By similarity).`
`MOD_RES`	`1042 1042`		`Phosphoserine.`
`MOD_RES`	`1180 1180`		`Phosphoserine (By similarity).`
`MOD_RES`	`1360 1360`		`Phosphoserine.`
`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`	`2088 2088`		`Phosphoserine.`
`MOD_RES`	`2093 2093`		`Phosphoserine.`
`MOD_RES`	`2096 2096`		`Phosphoserine.`
`MOD_RES`	`2125 2125`		`Phosphoserine.`
`MOD_RES`	`2143 2143`		`Phosphoserine.`
`MOD_RES`	`2151 2151`		`Phosphothreonine.`
`MOD_RES`	`2260 2260`		`Phosphoserine.`
`MOD_RES`	`2270 2270`		`Phosphoserine.`
`MOD_RES`	`2283 2283`		`Phosphoserine.`
`MOD_RES`	`2398 2398`		`Phosphoserine.`
`MOD_RES`	`2464 2464`		`Phosphoserine.`
`MOD_RES`	`2469 2469`		`Phosphoserine.`
`MOD_RES`	`2473 2473`		`Phosphoserine.`
`MOD_RES`	`2533 2533`		`Phosphoserine.`
`MOD_RES`	`2535 2535`		`Phosphoserine.`
`MOD_RES`	`2671 2671`		`Phosphoserine.`
`MOD_RES`	`2674 2674`		`Phosphoserine.`
`MOD_RES`	`2676 2676`		`Phosphothreonine.`
`MOD_RES`	`2679 2679`		`Phosphothreonine.`
`MOD_RES`	`2710 2710`		`Phosphoserine (By similarity).`
`MOD_RES`	`2789 2789`		`Phosphoserine.`
`MOD_RES`	`2835 2835`		`Phosphoserine.`
`MOD_RES`	`2837 2837`		`Phosphoserine.`
`MOD_RES`	`2838 2838`		`Phosphotyrosine.`
`VAR_SEQ`	`312 412`		`Missing (in isoform Short).`	`VSP_004115`
`VARIANT`	`99 99`	`1`	`R -> W (in FAP; could be a rare polymorphism).`	`VAR_009613`
`VARIANT`	`171 171`	`1`	`S -> I (in FAP).`	`VAR_005032`
`VARIANT`	`414 414`	`1`	`R -> C (in FAP).`	`VAR_005033`
`VARIANT`	`722 722`	`1`	`S -> G (in FAP).`	`VAR_009614`
`VARIANT`	`784 784`	`1`	`S -> T (in FAP).`	`VAR_005034`
`VARIANT`	`817 817`	`1`	`G -> C (in gastric cancer).`	`VAR_005035`
`VARIANT`	`870 870`	`1`	`P -> S (in dbSNP:rs33974176 [NCBI]).`	`VAR_053976`
`VARIANT`	`880 880`	`1`	`I -> T (in colorectal carcinoma and gastric cancer; from a patient with Turcot syndrome).`	`VAR_005036`
`VARIANT`	`890 890`	`1`	`V -> I (in colorectal carcinoma; from a patient with Turcot syndrome).`	`VAR_012975`
`VARIANT`	`906 906`	`1`	`S -> Y (in colorectal tumor).`	`VAR_005037`
`VARIANT`	`911 911`	`1`	`E -> G (in FAP and colorectal tumor).`	`VAR_005038`
`VARIANT`	`942 942`	`1`	`N -> D (in gastric cancer).`	`VAR_005039`
`VARIANT`	`1027 1027`	`1`	`Y -> C (in colorectal tumor).`	`VAR_005040`
`VARIANT`	`1057 1057`	`1`	`E -> G (in non-FAP).`	`VAR_009615`
`VARIANT`	`1118 1118`	`1`	`N -> D.`	`VAR_005041`
`VARIANT`	`1120 1120`	`1`	`G -> E (in gastric cancer).`	`VAR_005042`
`VARIANT`	`1171 1171`	`1`	`R -> C (in FAP; could be a polymorphism).`	`VAR_008992`
`VARIANT`	`1171 1171`	`1`	`R -> H (in gastric cancer).`	`VAR_005043`
`VARIANT`	`1176 1176`	`1`	`P -> L (in FAP).`	`VAR_005044`
`VARIANT`	`1184 1184`	`1`	`A -> P (in FAP).`	`VAR_009616`
`VARIANT`	`1197 1197`	`1`	`F -> S (in gastric cancer).`	`VAR_005045`
`VARIANT`	`1254 1254`	`1`	`I -> F (in a colorectal cancer sample; somatic mutation).`	`VAR_035794`
`VARIANT`	`1259 1259`	`1`	`I -> T (in gastric cancer).`	`VAR_005046`
`VARIANT`	`1292 1292`	`1`	`T -> M.`	`VAR_005047`
`VARIANT`	`1296 1296`	`1`	`A -> V (in MDB; sporadic).`	`VAR_017653`
`VARIANT`	`1304 1304`	`1`	`I -> V.`	`VAR_005048`
`VARIANT`	`1307 1307`	`1`	`I -> K (in 6% of Ashkenazi Jews; associated with slightly increased risk of colon and breast cancer; dbSNP:rs1801155 [NCBI]).`	`VAR_005049`
`VARIANT`	`1312 1312`	`1`	`G -> E (in gastric cancer).`	`VAR_005050`
`VARIANT`	`1313 1313`	`1`	`T -> A (in FAP and colorectal tumor).`	`VAR_005051`
`VARIANT`	`1317 1317`	`1`	`E -> Q (may contribute to colorectal tumor development; dbSNP:rs1801166 [NCBI]).`	`VAR_009617`
`VARIANT`	`1326 1326`	`1`	`V -> A (in gastric cancer).`	`VAR_005052`
`VARIANT`	`1348 1348`	`1`	`R -> W (in FAP).`	`VAR_005053`
`VARIANT`	`1422 1422`	`1`	`D -> H (in colorectal tumor).`	`VAR_005054`
`VARIANT`	`1472 1472`	`1`	`V -> I (in MDB; sporadic).`	`VAR_017654`
`VARIANT`	`1495 1495`	`1`	`S -> G (in MDB; sporadic).`	`VAR_017655`
`VARIANT`	`1496 1496`	`1`	`T -> S (in dbSNP:rs2229996 [NCBI]).`	`VAR_020141`
`VARIANT`	`1508 1508`	`1`	`A -> V (in colorectal carcinoma from a patient with Turcot syndrome).`	`VAR_012976`
`VARIANT`	`1822 1822`	`1`	`V -> D (in dbSNP:rs459552 [NCBI]).`	`VAR_008993`
`VARIANT`	`1882 1882`	`1`	`R -> T (in dbSNP:rs34157245 [NCBI]).`	`VAR_053977`
`VARIANT`	`1973 1973`	`1`	`S -> T (in dbSNP:rs4987109 [NCBI]).`	`VAR_020142`
`VARIANT`	`2499 2499`	`1`	`V -> L (in dbSNP:rs33941929 [NCBI]).`	`VAR_053978`
`VARIANT`	`2502 2502`	`1`	`G -> S (in dbSNP:rs2229995 [NCBI]).`	`VAR_005055`
`VARIANT`	`2621 2621`	`1`	`S -> C (in FAP).`	`VAR_005056`
`VARIANT`	`2738 2738`	`1`	`I -> T (in FAP).`	`VAR_008994`
`VARIANT`	`2839 2839`	`1`	`L -> F (in FAP).`	`VAR_005057`
`CONFLICT`	`184 184`		`M -> L (in Ref. 1; AAA60353/AAA60354).`
`CONFLICT`	`970 970`		`S -> N (in Ref. 1; AAA60353/AAA60354).`
`CONFLICT`	`1309 1309`		`E -> G (in Ref. 1; AAA60353/AAA60354).`
`CONFLICT`	`1325 1331`		`AVSQHPR -> SSVHSTLE (in Ref. 1; AAA60353/AAA60354).`
`CONFLICT`	`1355 1355`		`S -> P (in Ref. 1; AAA60353/AAA60354).`
`CONFLICT`	`1591 1591`		`A -> G (in Ref. 1; AAA60353/AAA60354).`
`CONFLICT`	`2723 2723`		`N -> T (in Ref. 1; AAA60353/AAA60354).`
`CONFLICT`	`2755 2755`		`S -> P (in Ref. 1; AAA60353/AAA60354).`
`HELIX`	`6 53`	`48`
`HELIX`	`132 169`	`38`
`HELIX`	`180 204`	`25`
`HELIX`	`208 238`	`31`
`TURN`	`1027 1030`	`4`
`HELIX`	`1470 1479`	`10`
`HELIX`	`1520 1524`	`5`
`HELIX`	`2036 2045`	`10`

Sequence information

Length: 2843 AA [This is the length of the unprocessed precursor]

Molecular weight: 311646 Da [This is the MW of the unprocessed precursor]

CRC64: 77E194AE4A91DC5A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDEAM 

        70         80         90        100        110        120 
ASSGQIDLLE RLKELNLDSS NFPGVKLRSK MSLRSYGSRE GSVSSRSGEC SPVPMGSFPR 

       130        140        150        160        170        180 
RGFVNGSRES TGYLEELEKE RSLLLADLDK EEKEKDWYYA QLQNLTKRID SLPLTENFSL 

       190        200        210        220        230        240 
QTDMTRRQLE YEARQIRVAM EEQLGTCQDM EKRAQRRIAR IQQIEKDILR IRQLLQSQAT 

       250        260        270        280        290        300 
EAERSSQNKH ETGSHDAERQ NEGQGVGEIN MATSGNGQGS TTRMDHETAS VLSSSSTHSA 

       310        320        330        340        350        360 
PRRLTSHLGT KVEMVYSLLS MLGTHDKDDM SRTLLAMSSS QDSCISMRQS GCLPLLIQLL 

       370        380        390        400        410        420 
HGNDKDSVLL GNSRGSKEAR ARASAALHNI IHSQPDDKRG RREIRVLHLL EQIRAYCETC 

       430        440        450        460        470        480 
WEWQEAHEPG MDQDKNPMPA PVEHQICPAV CVLMKLSFDE EHRHAMNELG GLQAIAELLQ 

       490        500        510        520        530        540 
VDCEMYGLTN DHYSITLRRY AGMALTNLTF GDVANKATLC SMKGCMRALV AQLKSESEDL 

       550        560        570        580        590        600 
QQVIASVLRN LSWRADVNSK KTLREVGSVK ALMECALEVK KESTLKSVLS ALWNLSAHCT 

       610        620        630        640        650        660 
ENKADICAVD GALAFLVGTL TYRSQTNTLA IIESGGGILR NVSSLIATNE DHRQILRENN 

       670        680        690        700        710        720 
CLQTLLQHLK SHSLTIVSNA CGTLWNLSAR NPKDQEALWD MGAVSMLKNL IHSKHKMIAM 

       730        740        750        760        770        780 
GSAAALRNLM ANRPAKYKDA NIMSPGSSLP SLHVRKQKAL EAELDAQHLS ETFDNIDNLS 

       790        800        810        820        830        840 
PKASHRSKQR HKQSLYGDYV FDTNRHDDNR SDNFNTGNMT VLSPYLNTTV LPSSSSSRGS 

       850        860        870        880        890        900 
LDSSRSEKDR SLERERGIGL GNYHPATENP GTSSKRGLQI STTAAQIAKV MEEVSAIHTS 

       910        920        930        940        950        960 
QEDRSSGSTT ELHCVTDERN ALRRSSAAHT HSNTYNFTKS ENSNRTCSMP YAKLEYKRSS 

       970        980        990       1000       1010       1020 
NDSLNSVSSS DGYGKRGQMK PSIESYSEDD ESKFCSYGQY PADLAHKIHS ANHMDDNDGE 

      1030       1040       1050       1060       1070       1080 
LDTPINYSLK YSDEQLNSGR QSPSQNERWA RPKHIIEDEI KQSEQRQSRN QSTTYPVYTE 

      1090       1100       1110       1120       1130       1140 
STDDKHLKFQ PHFGQQECVS PYRSRGANGS ETNRVGSNHG INQNVSQSLC QEDDYEDDKP 

      1150       1160       1170       1180       1190       1200 
TNYSERYSEE EQHEEEERPT NYSIKYNEEK RHVDQPIDYS LKYATDIPSS QKQSFSFSKS 

      1210       1220       1230       1240       1250       1260 
SSGQSSKTEH MSSSSENTST PSSNAKRQNQ LHPSSAQSRS GQPQKAATCK VSSINQETIQ 

      1270       1280       1290       1300       1310       1320 
TYCVEDTPIC FSRCSSLSSL SSAEDEIGCN QTTQEADSAN TLQIAEIKEK IGTRSAEDPV 

      1330       1340       1350       1360       1370       1380 
SEVPAVSQHP RTKSSRLQGS SLSSESARHK AVEFSSGAKS PSKSGAQTPK SPPEHYVQET 

      1390       1400       1410       1420       1430       1440 
PLMFSRCTSV SSLDSFESRS IASSVQSEPC SGMVSGIISP SDLPDSPGQT MPPSRSKTPP 

      1450       1460       1470       1480       1490       1500 
PPPQTAQTKR EVPKNKAPTA EKRESGPKQA AVNAAVQRVQ VLPDADTLLH FATESTPDGF 

      1510       1520       1530       1540       1550       1560 
SCSSSLSALS LDEPFIQKDV ELRIMPPVQE NDNGNETESE QPKESNENQE KEAEKTIDSE 

      1570       1580       1590       1600       1610       1620 
KDLLDDSDDD DIEILEECII SAMPTKSSRK AKKPAQTASK LPPPVARKPS QLPVYKLLPS 

      1630       1640       1650       1660       1670       1680 
QNRLQPQKHV SFTPGDDMPR VYCVEGTPIN FSTATSLSDL TIESPPNELA AGEGVRGGAQ 

      1690       1700       1710       1720       1730       1740 
SGEFEKRDTI PTEGRSTDEA QGGKTSSVTI PELDDNKAEE GDILAECINS AMPKGKSHKP 

      1750       1760       1770       1780       1790       1800 
FRVKKIMDQV QQASASSSAP NKNQLDGKKK KPTSPVKPIP QNTEYRTRVR KNADSKNNLN 

      1810       1820       1830       1840       1850       1860 
AERVFSDNKD SKKQNLKNNS KVFNDKLPNN EDRVRGSFAF DSPHHYTPIE GTPYCFSRND 

      1870       1880       1890       1900       1910       1920 
SLSSLDFDDD DVDLSREKAE LRKAKENKES EAKVTSHTEL TSNQQSANKT QAIAKQPINR 

      1930       1940       1950       1960       1970       1980 
GQPKPILQKQ STFPQSSKDI PDRGAATDEK LQNFAIENTP VCFSHNSSLS SLSDIDQENN 

      1990       2000       2010       2020       2030       2040 
NKENEPIKET EPPDSQGEPS KPQASGYAPK SFHVEDTPVC FSRNSSLSSL SIDSEDDLLQ 

      2050       2060       2070       2080       2090       2100 
ECISSAMPKK KKPSRLKGDN EKHSPRNMGG ILGEDLTLDL KDIQRPDSEH GLSPDSENFD 

      2110       2120       2130       2140       2150       2160 
WKAIQEGANS IVSSLHQAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT 

      2170       2180       2190       2200       2210       2220 
SNKGPRILKP GEKSTLETKK IESESKGIKG GKKVYKSLIT GKVRSNSEIS GQMKQPLQAN 

      2230       2240       2250       2260       2270       2280 
MPSISRGRTM IHIPGVRNSS SSTSPVSKKG PPLKTPASKS PSEGQTATTS PRGAKPSVKS 

      2290       2300       2310       2320       2330       2340 
ELSPVARQTS QIGGSSKAPS RSGSRDSTPS RPAQQPLSRP IQSPGRNSIS PGRNGISPPN 

      2350       2360       2370       2380       2390       2400 
KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQMSQQNLTK QTGLSKNASS IPRSESASKG 

      2410       2420       2430       2440       2450       2460 
LNQMNNGNGA NKKVELSRMS STKSSGSESD RSERPVLVRQ STFIKEAPSP TLRRKLEESA 

      2470       2480       2490       2500       2510       2520 
SFESLSPSSR PASPTRSQAQ TPVLSPSLPD MSLSTHSSVQ AGGWRKLPPN LSPTIEYNDG 

      2530       2540       2550       2560       2570       2580 
RPAKRHDIAR SHSESPSRLP INRSGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES 

      2590       2600       2610       2620       2630       2640 
SEKAKSEDEK HVNSISGTKQ SKENQVSAKG TWRKIKENEF SPTNSTSQTV SSGATNGAES 

      2650       2660       2670       2680       2690       2700 
KTLIYQMAPA VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKA NPNIKDSKDN 

      2710       2720       2730       2740       2750       2760 
QAKQNVGNGS VPMRTVGLEN RLNSFIQVDA PDQKGTEIKP GQNNPVPVSE TNESSIVERT 

      2770       2780       2790       2800       2810       2820 
PFSSSSSSKH SSPSGTVAAR VTPFNYNPSP RKSSADSTSA RPSQIPTPVN NNTKKRDSKT 

      2830       2840 
DSTESSGTQS PKRHSGSYLV TSV

P25054 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools