Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 APC_HUMAN               Reviewed;        2843 AA.
P25054; B7Z2B6; D3DT03; Q15162; Q15163; Q93042;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
27-SEP-2017, entry version 224.
RecName: Full=Adenomatous polyposis coli protein;
Short=Protein APC;
AltName: Full=Deleted in polyposis 2.5;
Name=APC {ECO:0000312|HGNC:HGNC:583}; Synonyms=DP2.5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 2), AND VARIANT ASP-1822.
TISSUE=Fetal brain;
PubMed=1678319; DOI=10.1016/0092-8674(81)90022-2;
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 1A), AND VARIANT ASP-1822.
PubMed=1651562; DOI=10.1126/science.1651562;
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 1A), FUNCTION, SUBCELLULAR
LOCATION, INTERACTION WITH ARHGEF4, AND IDENTIFICATION IN A COMPLEX
WITH ARHGEF4 AND CTNNB1.
PubMed=10947987; DOI=10.1126/science.289.5482.1194;
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 [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-1822.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1135 (ISOFORM 1B).
TISSUE=Amygdala {ECO:0000312|EMBL:BAH11802.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1506-1524.
PubMed=1310068;
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).
[8]
ASSOCIATION WITH CATENINS.
PubMed=8259519; DOI=10.1126/science.8259519;
Su L.-K., Vogelstein B., Kinzler K.W.;
"Association of the APC tumor suppressor protein with catenins.";
Science 262:1734-1737(1993).
[9]
INVOLVEMENT IN HEREDITARY DESMOID DISEASE.
PubMed=8940264;
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).
[10]
INTERACTION WITH DLG1.
PubMed=8638125; DOI=10.1126/science.272.5264.1020;
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).
[11]
INTERACTION WITH DLG3.
TISSUE=Fetal brain;
PubMed=9188857; DOI=10.1038/sj.onc.1201087;
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).
[12]
INVOLVEMENT IN HEREDITARY DESMOID DISEASE.
PubMed=10782927; DOI=10.1034/j.1399-0004.2000.570306.x;
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).
[13]
INTERACTION WITH APC2.
PubMed=11691822;
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).
[14]
INTERACTION WITH MAPRE1; MAPRE2 AND MAPRE3.
PubMed=14514668; DOI=10.1074/jbc.M306194200;
Bu W., Su L.-K.;
"Characterization of functional domains of human EB1 family
proteins.";
J. Biol. Chem. 278:49721-49731(2003).
[15]
UBIQUITINATION.
PubMed=15355978; DOI=10.1074/jbc.M404655200;
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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[17]
SUBCELLULAR LOCATION, INTERACTION WITH SCRIB, AND MUTAGENESIS OF
THR-2841 AND VAL-2843.
PubMed=16611247; DOI=10.1111/j.1365-2443.2006.00954.x;
Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K.,
Yasugi T., Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T.,
Taketani Y.;
"Human scribble, a novel tumor suppressor identified as a target of
high-risk HPV E6 for ubiquitin-mediated degradation, interacts with
adenomatous polyposis coli.";
Genes Cells 11:453-464(2006).
[18]
FUNCTION, AND INTERACTION WITH SPATA13.
PubMed=17599059; DOI=10.1038/sj.onc.1210574;
Kawasaki Y., Sagara M., Shibata Y., Shirouzu M., Yokoyama S.,
Akiyama T.;
"Identification and characterization of Asef2, a guanine-nucleotide
exchange factor specific for Rac1 and Cdc42.";
Oncogene 26:7620-7627(2007).
[19]
DEUBIQUITINATION.
PubMed=18281465; DOI=10.1101/gad.463208;
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2671, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780; SER-1042; SER-1360;
SER-1861; SER-1863; SER-1864; THR-2151; SER-2260; SER-2270; SER-2283;
SER-2473; SER-2535; SER-2671; SER-2674; THR-2679 AND SER-2789, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
ALTERNATIVE PROMOTER USAGE, AND TISSUE SPECIFICITY.
PubMed=19527921; DOI=10.1016/j.canlet.2009.05.016;
Hosoya K., Yamashita S., Ando T., Nakajima T., Itoh F., Ushijima T.;
"Adenomatous polyposis coli 1A is likely to be methylated as a
passenger in human gastric carcinogenesis.";
Cancer Lett. 285:182-189(2009).
[24]
INTERACTION WITH MAPRE1, AND SUBCELLULAR LOCATION.
PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
"An EB1-binding motif acts as a microtubule tip localization signal.";
Cell 138:366-376(2009).
[25]
FUNCTION.
PubMed=19893577; DOI=10.1038/embor.2009.233;
Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M.,
Ohwada S., Akiyama T.;
"The adenomatous polyposis coli-associated exchange factors Asef and
Asef2 are required for adenoma formation in Apc(Min/+)mice.";
EMBO Rep. 10:1355-1362(2009).
[26]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19151759; DOI=10.1038/onc.2008.478;
Sagara M., Kawasaki Y., Iemura S.I., Natsume T., Takai Y., Akiyama T.;
"Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal
organization and are involved in HGF-induced cell migration.";
Oncogene 28:1357-1365(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[28]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20937854; DOI=10.1073/pnas.1000975107;
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
plasma membrane of migrating cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744 AND SER-780, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
INTERACTION WITH AMER1.
PubMed=21498506; DOI=10.1074/jbc.M111.224881;
Tanneberger K., Pfister A.S., Kriz V., Bryja V., Schambony A.,
Behrens J.;
"Structural and functional characterization of the Wnt inhibitor APC
membrane recruitment 1 (Amer1).";
J. Biol. Chem. 286:19204-19214(2011).
[31]
ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, AND INVOLVEMENT IN
FAP.
PubMed=21643010; DOI=10.1038/onc.2011.201;
Rohlin A., Engwall Y., Fritzell K., Goeransson K., Bergsten A.,
Einbeigi Z., Nilbert M., Karlsson P., Bjoerk J., Nordling M.;
"Inactivation of promoter 1B of APC causes partial gene silencing:
evidence for a significant role of the promoter in regulation and
causative of familial adenomatous polyposis.";
Oncogene 30:4977-4989(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861; SER-1863 AND
SER-1864, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
INTERACTION WITH AMER2.
PubMed=22128170; DOI=10.1074/jbc.M111.308650;
Pfister A.S., Tanneberger K., Schambony A., Behrens J.;
"Amer2 protein is a novel negative regulator of Wnt/beta-Catenin
signaling involved in neuroectodermal patterning.";
J. Biol. Chem. 287:1734-1741(2012).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744; SER-748; SER-908;
SER-1042; SER-1371; SER-1385; THR-1438; SER-1774; SER-1861; SER-2260;
SER-2283; SER-2569; SER-2674; SER-2724 AND SER-2789, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[37]
INTERACTION WITH JPT1.
PubMed=25169422; DOI=10.1002/jcb.24956;
Varisli L., Ozturk B.E., Akyuz G.K., Korkmaz K.S.;
"HN1 negatively influences the beta-catenin/E-cadherin interaction,
and contributes to migration in prostate cells.";
J. Cell. Biochem. 116:170-178(2015).
[38]
ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, AND INVOLVEMENT IN
FAP.
PubMed=27217144; DOI=10.1038/srep26011;
Yamaguchi K., Nagayama S., Shimizu E., Komura M., Yamaguchi R.,
Shibuya T., Arai M., Hatakeyama S., Ikenoue T., Ueno M., Miyano S.,
Imoto S., Furukawa Y.;
"Reduced expression of APC-1B but not APC-1A by the deletion of
promoter 1B is responsible for familial adenomatous polyposis.";
Sci. Rep. 6:26011-26011(2016).
[39]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-55.
PubMed=10926498; DOI=10.1006/jmbi.2000.3895;
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).
[40]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1021-1035 IN COMPLEX WITH
CTNNB1.
PubMed=11707392; DOI=10.1093/emboj/20.22.6203;
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).
[41]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2034-2049 IN COMPLEX WITH
AXIN.
PubMed=10811618; DOI=10.1093/emboj/19.10.2270;
Spink K.E., Polakis P., Weis W.I.;
"Structural basis of the axin-adenomatous polyposis coli
interaction.";
EMBO J. 19:2270-2279(2000).
[42]
REVIEW ON VARIANTS.
PubMed=8111410; DOI=10.1002/humu.1380020602;
Nagase H., Nakamura Y.;
"Mutations of the APC (adenomatous polyposis coli) gene.";
Hum. Mutat. 2:425-434(1993).
[43]
STRUCTURE BY NMR OF 1578-1596 IN COMPLEX WITH ASAP1.
PubMed=20509626; DOI=10.1021/bi100563z;
Kaieda S., Matsui C., Mimori-Kiyosue Y., Ikegami T.;
"Structural basis of the recognition of the SAMP motif of adenomatous
polyposis coli by the Src-homology 3 domain.";
Biochemistry 49:5143-5153(2010).
[44]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 407-775, AND DOMAIN ARM
REPEATS.
PubMed=21871439; DOI=10.1016/j.bbrc.2011.08.044;
Zhang Z., Lin K., Gao L., Chen L., Shi X., Wu G.;
"Crystal structure of the armadillo repeat domain of adenomatous
polyposis coli which reveals its inherent flexibility.";
Biochem. Biophys. Res. Commun. 412:732-736(2011).
[45]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 396-732 IN COMPLEX WITH
KHDRBS1, AND MUTAGENESIS OF LYS-516 AND ARG-549.
PubMed=22000517; DOI=10.1016/j.str.2011.07.013;
Morishita E.C., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y.,
Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M.,
Akiyama T., Yokoyama S.;
"Crystal structures of the armadillo repeat domain of adenomatous
polyposis coli and its complex with the tyrosine-rich domain of
Sam68.";
Structure 19:1496-1508(2011).
[46]
VARIANTS FAP.
PubMed=1651563; DOI=10.1126/science.1651563;
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).
[47]
VARIANTS FAP.
PubMed=1338904; DOI=10.1093/hmg/1.4.229;
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).
[48]
VARIANTS FAP.
PubMed=1338691; DOI=10.1093/hmg/1.8.559;
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).
[49]
VARIANT FAP TRP-1348, AND VARIANTS ASP-1118; MET-1292; VAL-1304 AND
SER-2502.
PubMed=1338764; DOI=10.1002/humu.1380010603;
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).
[50]
VARIANT FAP TRP-99.
TISSUE=Peripheral blood lymphocyte;
PubMed=7833149; DOI=10.1016/0959-8049(94)00294-F;
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).
[51]
VARIANT FAP GLY-722.
PubMed=7833931; DOI=10.1093/hmg/3.9.1687;
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).
[52]
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).
[53]
INVOLVEMENT IN FAP.
PubMed=7661930; DOI=10.1056/NEJM199503303321302;
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).
[54]
VARIANT HEPATOBLASTOMA CYS-1395.
PubMed=8764128;
Oda H., Imai Y., Nakatsuru Y., Hata J., Ishikawa T.;
"Somatic mutations of the APC gene in sporadic hepatoblastomas.";
Cancer Res. 56:3320-3323(1996).
[55]
VARIANT FAP ILE-171.
PubMed=8990002;
DOI=10.1002/(SICI)1098-1004(1997)9:1<7::AID-HUMU2>3.0.CO;2-8;
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).
[56]
VARIANTS COLORECTAL CARCINOMA THR-880; ILE-890 AND VAL-1508.
PubMed=9419979; DOI=10.1038/sj.onc.1201668;
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).
[57]
VARIANT LYS-1307.
PubMed=9731522; DOI=10.1038/1666;
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).
[58]
VARIANTS LYS-1307 AND GLN-1317.
TISSUE=Peripheral blood;
PubMed=9724771; DOI=10.1073/pnas.95.18.10722;
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).
[59]
VARIANT LYS-1307.
PubMed=9731533; DOI=10.1038/1722;
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).
[60]
VARIANT LYS-1307.
PubMed=9973276; DOI=10.1086/302262;
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).
[61]
VARIANTS GLY-1057; CYS-1171; ASP-1822 AND THR-2738.
PubMed=9950360;
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).
[62]
VARIANT FAP PRO-1184.
PubMed=10470088; DOI=10.1038/12511;
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).
[63]
VARIANTS MDB VAL-1296; ILE-1472 AND GLY-1495.
PubMed=10666372; DOI=10.1016/S0002-9440(10)64747-5;
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).
[64]
VARIANT [LARGE SCALE ANALYSIS] PHE-1254.
PubMed=16959974; DOI=10.1126/science.1133427;
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).
-!- 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. 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:0000269|PubMed:10947987,
ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19151759,
ECO:0000269|PubMed:19893577, ECO:0000269|PubMed:20937854}.
-!- SUBUNIT: Forms homooligomers and heterooligomers with APC2.
Interacts with DIAPH1 and DIAPH2 (By similarity). Interacts with
PDZ domains of DLG1 and DLG3. Associates with catenins. Binds
axin. Interacts with ARHGEF4 (via N-terminus). Interacts with
MAPRE1 (via C-terminus); probably required for APC targeting to
the growing microtubule plus ends. Interacts with MAPRE2 and
MAPRE3 (via C-terminus). Found in a complex consisting of ARHGEF4,
APC and CTNNB1. Interacts with SCRIB; may mediate APC targeting to
adherens junctions of epithelial cells. Interacts with SPATA13
(via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3
domain). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1
and GSK3B (By similarity). Interacts at the cell membrane with
AMER1 and AMER2 (via ARM repeats). Interacts with KHDRBS1. The
complex composed, at least, of APC, CTNNB1 and GSK3B interacts
with JPT1; the interaction requires the inactive form of GSK3B
(phosphorylated at 'Ser-9') (PubMed:25169422).
{ECO:0000250|UniProtKB:Q61315, ECO:0000269|PubMed:10811618,
ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:11691822,
ECO:0000269|PubMed:11707392, ECO:0000269|PubMed:14514668,
ECO:0000269|PubMed:16611247, ECO:0000269|PubMed:17599059,
ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:20509626,
ECO:0000269|PubMed:21498506, ECO:0000269|PubMed:22000517,
ECO:0000269|PubMed:22128170, ECO:0000269|PubMed:25169422,
ECO:0000269|PubMed:8638125, ECO:0000269|PubMed:9188857}.
-!- INTERACTION:
Q5JTC6:AMER1; NbExp=4; IntAct=EBI-727707, EBI-6169747;
Q8N944:AMER3; NbExp=8; IntAct=EBI-727707, EBI-8869590;
Q9NR80-3:ARHGEF4; NbExp=5; IntAct=EBI-727707, EBI-13639160;
P49674:CSNK1E; NbExp=8; IntAct=EBI-727707, EBI-749343;
P35221:CTNNA1; NbExp=3; IntAct=EBI-727707, EBI-701918;
P35222:CTNNB1; NbExp=16; IntAct=EBI-727707, EBI-491549;
Q02248:Ctnnb1 (xeno); NbExp=8; IntAct=EBI-727707, EBI-397872;
O14640:DVL1; NbExp=6; IntAct=EBI-727707, EBI-723489;
P54792:DVL1P1; NbExp=2; IntAct=EBI-727707, EBI-7848109;
O14641:DVL2; NbExp=2; IntAct=EBI-727707, EBI-740850;
P14923:JUP; NbExp=3; IntAct=EBI-727707, EBI-702484;
Q15691:MAPRE1; NbExp=5; IntAct=EBI-727707, EBI-1004115;
Q14160:SCRIB; NbExp=4; IntAct=EBI-727707, EBI-357345;
Q96N96:SPATA13; NbExp=5; IntAct=EBI-727707, EBI-13618641;
Q96N96-1:SPATA13; NbExp=5; IntAct=EBI-727707, EBI-13638906;
Q96N96-2:SPATA13; NbExp=2; IntAct=EBI-727707, EBI-13639118;
-!- 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). 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
Name=1A {ECO:0000303|PubMed:19527921}; Synonyms=Long
{ECO:0000303|PubMed:1678319};
IsoId=P25054-1; Sequence=Displayed;
Name=2; Synonyms=Short {ECO:0000303|PubMed:1678319};
IsoId=P25054-2; Sequence=VSP_004115;
Name=1B {ECO:0000303|PubMed:19527921};
IsoId=P25054-3; Sequence=VSP_059027, VSP_059028;
Note=Produced by alternative promoter usage.
{ECO:0000269|PubMed:19527921};
-!- TISSUE SPECIFICITY: Expressed in a variety of tissues: brain,
small intestine, colon, thymus, skeletal muscle, heart, prostate,
lung, spleen, ovary, testis kidney, placenta, blood and liver
(PubMed:21643010, PubMed:27217144). Isoform 1A: Very strongly
expressed in brain but has relatively low expression levels in
other tissues (PubMed:19527921, PubMed:21643010, PubMed:27217144).
Isoform 1B: Predominant form in all tissues except for brain,
including gastric mucosa and blood (PubMed:19527921,
PubMed:21643010, PubMed:27217144). {ECO:0000269|PubMed:19527921,
ECO:0000269|PubMed:21643010, ECO:0000269|PubMed:27217144}.
-!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
mediates interaction with MAPRE1 and targeting to the growing
microtubule plus ends. {ECO:0000250}.
-!- PTM: Phosphorylated by GSK3B.
-!- 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}.
-!- DISEASE: Familial adenomatous polyposis (FAP) [MIM:175100]: A
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: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:8990002}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Hereditary desmoid disease (HDD) [MIM:135290]: 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.
{ECO:0000269|PubMed:10782927, ECO:0000269|PubMed:8940264}.
Note=The disease is caused by mutations 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}. 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. 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.
-!- MISCELLANEOUS: 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.
-!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC)
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Colon cancer gene variant databases Adenomatous
Polyposis Coli (APC); Note=Leiden Open Variation Database (LOVD);
URL="http://chromium.lovd.nl/LOVD2/colon_cancer/home.php?select_db=APC";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/APCID118.html";
-!- 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";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M73548; AAA60353.1; -; mRNA.
EMBL; M73548; AAA60354.1; -; mRNA.
EMBL; M74088; AAA03586.1; -; mRNA.
EMBL; AC008575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC136500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471086; EAW49002.1; -; Genomic_DNA.
EMBL; CH471086; EAW49007.1; -; Genomic_DNA.
EMBL; AK294544; BAH11802.1; -; mRNA.
EMBL; S78214; AAB21145.2; ALT_SEQ; Genomic_DNA.
CCDS; CCDS4107.1; -. [P25054-1]
PIR; A37261; RBHUAP.
RefSeq; NP_000029.2; NM_000038.5. [P25054-1]
RefSeq; NP_001120982.1; NM_001127510.2. [P25054-1]
RefSeq; NP_001120983.2; NM_001127511.2.
UniGene; Hs.158932; -.
PDB; 1DEB; X-ray; 2.40 A; A/B=2-55.
PDB; 1EMU; X-ray; 1.90 A; B=2034-2049.
PDB; 1JPP; X-ray; 3.10 A; C/D=1021-1035.
PDB; 1M5I; X-ray; 2.00 A; A=126-250.
PDB; 1T08; X-ray; 2.10 A; C=1484-1498.
PDB; 1TH1; X-ray; 2.50 A; C/D=1362-1540.
PDB; 1V18; X-ray; 2.10 A; B=1482-1528.
PDB; 2RQU; NMR; -; B=1578-1596.
PDB; 3AU3; X-ray; 2.10 A; A=396-732.
PDB; 3NMW; X-ray; 1.60 A; A/B=407-751.
PDB; 3NMX; X-ray; 2.30 A; A/B/C=407-751.
PDB; 3NMZ; X-ray; 3.01 A; A/B=303-739.
PDB; 3QHE; X-ray; 2.40 A; A/C=396-732.
PDB; 3RL7; X-ray; 2.30 A; G/H/I/J/K/L=2833-2843.
PDB; 3RL8; X-ray; 2.20 A; F=2833-2843.
PDB; 3T7U; X-ray; 2.90 A; A/B=407-775.
PDB; 4G69; X-ray; 2.00 A; B=2833-2843.
PDB; 4YJE; X-ray; 1.90 A; A=407-751.
PDB; 4YJL; X-ray; 2.10 A; A/B/C/D/E/F=407-751.
PDB; 4YK6; X-ray; 1.70 A; A=407-751.
PDB; 5B6G; X-ray; 1.99 A; A=407-751.
PDBsum; 1DEB; -.
PDBsum; 1EMU; -.
PDBsum; 1JPP; -.
PDBsum; 1M5I; -.
PDBsum; 1T08; -.
PDBsum; 1TH1; -.
PDBsum; 1V18; -.
PDBsum; 2RQU; -.
PDBsum; 3AU3; -.
PDBsum; 3NMW; -.
PDBsum; 3NMX; -.
PDBsum; 3NMZ; -.
PDBsum; 3QHE; -.
PDBsum; 3RL7; -.
PDBsum; 3RL8; -.
PDBsum; 3T7U; -.
PDBsum; 4G69; -.
PDBsum; 4YJE; -.
PDBsum; 4YJL; -.
PDBsum; 4YK6; -.
PDBsum; 5B6G; -.
DisProt; DP00519; -.
ProteinModelPortal; P25054; -.
SMR; P25054; -.
BioGrid; 106821; 197.
CORUM; P25054; -.
DIP; DIP-33556N; -.
IntAct; P25054; 184.
MINT; MINT-88204; -.
STRING; 9606.ENSP00000257430; -.
iPTMnet; P25054; -.
PhosphoSitePlus; P25054; -.
BioMuta; APC; -.
DMDM; 97535708; -.
EPD; P25054; -.
MaxQB; P25054; -.
PaxDb; P25054; -.
PeptideAtlas; P25054; -.
PRIDE; P25054; -.
DNASU; 324; -.
Ensembl; ENST00000257430; ENSP00000257430; ENSG00000134982. [P25054-1]
Ensembl; ENST00000508376; ENSP00000427089; ENSG00000134982. [P25054-1]
GeneID; 324; -.
KEGG; hsa:324; -.
UCSC; uc003kpy.5; human. [P25054-1]
CTD; 324; -.
DisGeNET; 324; -.
EuPathDB; HostDB:ENSG00000134982.16; -.
GeneCards; APC; -.
GeneReviews; APC; -.
HGNC; HGNC:583; APC.
HPA; CAB025994; -.
HPA; HPA013349; -.
MalaCards; APC; -.
MIM; 114550; phenotype.
MIM; 135290; phenotype.
MIM; 155255; phenotype.
MIM; 175100; phenotype.
MIM; 611731; gene.
MIM; 613659; phenotype.
neXtProt; NX_P25054; -.
OpenTargets; ENSG00000134982; -.
Orphanet; 247806; APC-related attenuated familial adenomatous polyposis.
Orphanet; 873; Desmoid tumor.
Orphanet; 261584; Familial adenomatous polyposis due to 5q22.2 microdeletion.
Orphanet; 79665; Gardner syndrome.
Orphanet; 99818; Turcot syndrome with polyposis.
PharmGKB; PA24875; -.
eggNOG; KOG2122; Eukaryota.
eggNOG; ENOG410XR2V; LUCA.
GeneTree; ENSGT00530000063749; -.
HOVERGEN; HBG004264; -.
InParanoid; P25054; -.
KO; K02085; -.
OMA; PRVYCVE; -.
OrthoDB; EOG091G00D4; -.
PhylomeDB; P25054; -.
TreeFam; TF106496; -.
BioCyc; MetaCyc:ENSG00000134982-MONOMER; -.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-5339716; Misspliced GSK3beta mutants stabilize beta-catenin.
Reactome; R-HSA-5358747; S33 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358749; S37 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358751; S45 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358752; T41 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5467333; APC truncation mutants are not K63 polyubiquitinated.
Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
SignaLink; P25054; -.
SIGNOR; P25054; -.
ChiTaRS; APC; human.
EvolutionaryTrace; P25054; -.
GeneWiki; Adenomatous_polyposis_coli; -.
GenomeRNAi; 324; -.
PRO; PR:P25054; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000134982; -.
CleanEx; HS_APC; -.
ExpressionAtlas; P25054; baseline and differential.
Genevisible; P25054; HS.
GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
GO; GO:0030877; C:beta-catenin destruction complex; IDA:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0016342; C:catenin complex; IDA:CACAO.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:1990909; C:Wnt signalosome; NAS:ParkinsonsUK-UCL.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0070840; F:dynein complex binding; IPI:CAFA.
GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019887; F:protein kinase regulator activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI.
GO; GO:1904885; P:beta-catenin destruction complex assembly; TAS:Reactome.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
GO; GO:0070830; P:bicellular tight junction assembly; NAS:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; NAS:UniProtKB.
GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; TAS:Reactome.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:CAFA.
GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0010942; P:positive regulation of cell death; IMP:CAFA.
GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:MGI.
GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:CAFA.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; IMP:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0006461; P:protein complex assembly; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051260; P:protein homooligomerization; IMP:CAFA.
GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:MGI.
GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
Gene3D; 1.25.10.10; -; 2.
InterPro; IPR026836; APC.
InterPro; IPR009240; APC_15aa_rpt.
InterPro; IPR009234; APC_basic_dom.
InterPro; IPR026831; APC_dom.
InterPro; IPR026818; Apc_fam.
InterPro; IPR032038; APC_N.
InterPro; IPR009223; APC_rpt.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR009232; EB1-bd.
InterPro; IPR009224; SAMP.
PANTHER; PTHR12607; PTHR12607; 1.
PANTHER; PTHR12607:SF13; PTHR12607:SF13; 1.
Pfam; PF05972; APC_15aa; 3.
Pfam; PF05956; APC_basic; 1.
Pfam; PF16689; APC_N_CC; 1.
Pfam; PF05923; APC_r; 7.
Pfam; PF00514; Arm; 2.
Pfam; PF05937; EB1_binding; 1.
Pfam; PF05924; SAMP; 3.
SMART; SM00185; ARM; 7.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF58050; SSF58050; 1.
SUPFAM; SSF82931; SSF82931; 1.
PROSITE; PS50176; ARM_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative promoter usage;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Membrane; Microtubule; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Tumor suppressor; Ubl conjugation;
Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 2843 Adenomatous polyposis coli protein.
/FTId=PRO_0000064627.
REPEAT 453 495 ARM 1.
REPEAT 505 547 ARM 2.
REPEAT 548 591 ARM 3.
REPEAT 592 638 ARM 4.
REPEAT 639 683 ARM 5.
REPEAT 684 725 ARM 6.
REPEAT 726 767 ARM 7.
REGION 960 1337 Responsible for down-regulation through a
process mediated by direct
ubiquitination.
REGION 1866 1893 Highly charged.
COILED 2 61 {ECO:0000255}.
COILED 127 248 {ECO:0000255}.
MOTIF 2803 2806 Microtubule tip localization signal.
MOTIF 2841 2843 PDZ-binding.
COMPBIAS 1 730 Leu-rich.
COMPBIAS 731 2832 Ser-rich.
COMPBIAS 1131 1156 Asp/Glu-rich (acidic).
COMPBIAS 1558 1577 Asp/Glu-rich (acidic).
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000250|UniProtKB:Q61315}.
MOD_RES 111 111 Phosphoserine.
{ECO:0000250|UniProtKB:Q61315}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 908 908 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 987 987 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 1038 1038 Phosphoserine.
{ECO:0000250|UniProtKB:Q61315}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1360 1360 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1371 1371 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1385 1385 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1392 1392 Phosphoserine.
{ECO:0000250|UniProtKB:Q61315}.
MOD_RES 1395 1395 Phosphoserine.
{ECO:0000250|UniProtKB:Q61315}.
MOD_RES 1438 1438 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1567 1567 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 1774 1774 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1861 1861 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1863 1863 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1864 1864 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1971 1971 Phosphoserine.
{ECO:0000250|UniProtKB:Q61315}.
MOD_RES 1973 1973 Phosphoserine.
{ECO:0000250|UniProtKB:Q61315}.
MOD_RES 2088 2088 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2093 2093 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2125 2125 Phosphoserine.
{ECO:0000250|UniProtKB:Q61315}.
MOD_RES 2129 2129 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2130 2130 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2132 2132 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2151 2151 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2260 2260 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2270 2270 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2283 2283 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2473 2473 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2535 2535 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2569 2569 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2671 2671 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648}.
MOD_RES 2674 2674 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2679 2679 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2710 2710 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2724 2724 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2789 2789 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 45 MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEA
SNMK -> MYASLGSGPVAPLPASVPPSVLGSWSTGGSRSC
VRQETKSPGGARTSGHWASVWQ (in isoform 1B).
/FTId=VSP_059027.
VAR_SEQ 217 244 Missing (in isoform 1B).
/FTId=VSP_059028.
VAR_SEQ 312 412 Missing (in isoform 2).
{ECO:0000303|PubMed:1678319}.
/FTId=VSP_004115.
VARIANT 99 99 R -> W (in FAP; unknown pathological
significance; dbSNP:rs139196838).
{ECO:0000269|PubMed:7833149}.
/FTId=VAR_009613.
VARIANT 171 171 S -> I (in FAP).
{ECO:0000269|PubMed:8990002}.
/FTId=VAR_005032.
VARIANT 414 414 R -> C (in FAP; dbSNP:rs137854567).
/FTId=VAR_005033.
VARIANT 722 722 S -> G (in FAP).
{ECO:0000269|PubMed:7833931}.
/FTId=VAR_009614.
VARIANT 784 784 S -> T (in FAP).
/FTId=VAR_005034.
VARIANT 817 817 G -> C (in gastric cancer).
/FTId=VAR_005035.
VARIANT 870 870 P -> S (in dbSNP:rs33974176).
/FTId=VAR_053976.
VARIANT 880 880 I -> T (in colorectal carcinoma and
gastric cancer; from a patient with
MMRCS). {ECO:0000269|PubMed:9419979}.
/FTId=VAR_005036.
VARIANT 890 890 V -> I (in colorectal carcinoma; from a
patient with MMRCS; dbSNP:rs779998847).
{ECO:0000269|PubMed:9419979}.
/FTId=VAR_012975.
VARIANT 906 906 S -> Y (in colorectal tumor).
/FTId=VAR_005037.
VARIANT 911 911 E -> G (in FAP and colorectal tumor).
/FTId=VAR_005038.
VARIANT 942 942 N -> D (in gastric cancer).
/FTId=VAR_005039.
VARIANT 1027 1027 Y -> C (in colorectal tumor;
dbSNP:rs869312784).
/FTId=VAR_005040.
VARIANT 1057 1057 E -> G (in non-FAP; unknown pathological
significance).
{ECO:0000269|PubMed:9950360}.
/FTId=VAR_009615.
VARIANT 1118 1118 N -> D (in dbSNP:rs140493115).
{ECO:0000269|PubMed:1338764}.
/FTId=VAR_005041.
VARIANT 1120 1120 G -> E (in gastric cancer;
dbSNP:rs28933379).
/FTId=VAR_005042.
VARIANT 1171 1171 R -> C (in dbSNP:rs201830995).
{ECO:0000269|PubMed:9950360}.
/FTId=VAR_008992.
VARIANT 1171 1171 R -> H (in gastric cancer;
dbSNP:rs372481703).
/FTId=VAR_005043.
VARIANT 1176 1176 P -> L (in FAP).
/FTId=VAR_005044.
VARIANT 1184 1184 A -> P (in FAP).
{ECO:0000269|PubMed:10470088}.
/FTId=VAR_009616.
VARIANT 1197 1197 F -> S (in gastric cancer).
/FTId=VAR_005045.
VARIANT 1254 1254 I -> F (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035794.
VARIANT 1259 1259 I -> T (in gastric cancer).
/FTId=VAR_005046.
VARIANT 1292 1292 T -> M (in dbSNP:rs371113837).
{ECO:0000269|PubMed:1338764}.
/FTId=VAR_005047.
VARIANT 1296 1296 A -> V (in MDB; sporadic).
{ECO:0000269|PubMed:10666372}.
/FTId=VAR_017653.
VARIANT 1304 1304 I -> V (in dbSNP:rs770157475).
{ECO:0000269|PubMed:1338764}.
/FTId=VAR_005048.
VARIANT 1307 1307 I -> K (in 6% of Ashkenazi Jews;
associated with slightly increased risk
of colon and breast cancer;
dbSNP:rs1801155).
{ECO:0000269|PubMed:9724771,
ECO:0000269|PubMed:9731522,
ECO:0000269|PubMed:9731533,
ECO:0000269|PubMed:9973276}.
/FTId=VAR_005049.
VARIANT 1312 1312 G -> E (in gastric cancer).
/FTId=VAR_005050.
VARIANT 1313 1313 T -> A (in FAP and colorectal tumor;
dbSNP:rs863225349).
/FTId=VAR_005051.
VARIANT 1317 1317 E -> Q (may contribute to colorectal
tumor development; dbSNP:rs1801166).
{ECO:0000269|PubMed:9724771}.
/FTId=VAR_009617.
VARIANT 1326 1326 V -> A (in gastric cancer).
/FTId=VAR_005052.
VARIANT 1348 1348 R -> W (in FAP).
{ECO:0000269|PubMed:1338764}.
/FTId=VAR_005053.
VARIANT 1395 1395 S -> C (in hepatoblastoma;
dbSNP:rs137854578).
{ECO:0000269|PubMed:8764128}.
/FTId=VAR_065133.
VARIANT 1422 1422 D -> H (in colorectal tumor).
/FTId=VAR_005054.
VARIANT 1472 1472 V -> I (in MDB; sporadic;
dbSNP:rs878853445).
{ECO:0000269|PubMed:10666372}.
/FTId=VAR_017654.
VARIANT 1495 1495 S -> G (in MDB; sporadic).
{ECO:0000269|PubMed:10666372}.
/FTId=VAR_017655.
VARIANT 1496 1496 T -> S (in dbSNP:rs2229996).
/FTId=VAR_020141.
VARIANT 1508 1508 A -> V (in colorectal carcinoma from a
patient with MMRCS).
{ECO:0000269|PubMed:9419979}.
/FTId=VAR_012976.
VARIANT 1822 1822 V -> D (in dbSNP:rs459552).
{ECO:0000269|PubMed:1651562,
ECO:0000269|PubMed:1678319,
ECO:0000269|PubMed:9950360,
ECO:0000269|Ref.5}.
/FTId=VAR_008993.
VARIANT 1882 1882 R -> T (in dbSNP:rs34157245).
/FTId=VAR_053977.
VARIANT 1973 1973 S -> T (in dbSNP:rs4987109).
/FTId=VAR_020142.
VARIANT 2499 2499 V -> L (in dbSNP:rs33941929).
/FTId=VAR_053978.
VARIANT 2502 2502 G -> S (in dbSNP:rs2229995).
{ECO:0000269|PubMed:1338764}.
/FTId=VAR_005055.
VARIANT 2621 2621 S -> C (in FAP; dbSNP:rs72541816).
/FTId=VAR_005056.
VARIANT 2738 2738 I -> T (in dbSNP:rs863224552).
{ECO:0000269|PubMed:9950360}.
/FTId=VAR_008994.
VARIANT 2839 2839 L -> F (in FAP; dbSNP:rs876658156).
/FTId=VAR_005057.
MUTAGEN 516 516 K->E: Impairs interaction with KHDRBS1.
{ECO:0000269|PubMed:22000517}.
MUTAGEN 549 549 R->E: Impairs interaction with KHDRBS1.
{ECO:0000269|PubMed:22000517}.
MUTAGEN 2841 2841 T->L: Loss of interaction with SCRIB.
{ECO:0000269|PubMed:16611247}.
MUTAGEN 2843 2843 V->Q: Loss of interaction with SCRIB.
{ECO:0000269|PubMed:16611247}.
CONFLICT 184 184 M -> L (in Ref. 1; AAA60353/AAA60354).
{ECO:0000305}.
CONFLICT 970 970 S -> N (in Ref. 1; AAA60353/AAA60354).
{ECO:0000305}.
CONFLICT 1309 1309 E -> G (in Ref. 1; AAA60353/AAA60354).
{ECO:0000305}.
CONFLICT 1325 1331 AVSQHPR -> SSVHSTLE (in Ref. 1; AAA60353/
AAA60354). {ECO:0000305}.
CONFLICT 1355 1355 S -> P (in Ref. 1; AAA60353/AAA60354).
{ECO:0000305}.
CONFLICT 1591 1591 A -> G (in Ref. 1; AAA60353/AAA60354).
{ECO:0000305}.
CONFLICT 2723 2723 N -> T (in Ref. 1; AAA60353/AAA60354).
{ECO:0000305}.
CONFLICT 2755 2755 S -> P (in Ref. 1; AAA60353/AAA60354).
{ECO:0000305}.
HELIX 6 53 {ECO:0000244|PDB:1DEB}.
HELIX 132 169 {ECO:0000244|PDB:1M5I}.
HELIX 180 204 {ECO:0000244|PDB:1M5I}.
HELIX 208 238 {ECO:0000244|PDB:1M5I}.
HELIX 328 338 {ECO:0000244|PDB:3NMZ}.
HELIX 343 350 {ECO:0000244|PDB:3NMZ}.
HELIX 353 360 {ECO:0000244|PDB:3NMZ}.
HELIX 377 393 {ECO:0000244|PDB:3NMZ}.
HELIX 407 425 {ECO:0000244|PDB:3NMW}.
STRAND 429 431 {ECO:0000244|PDB:3AU3}.
HELIX 433 435 {ECO:0000244|PDB:3AU3}.
HELIX 441 444 {ECO:0000244|PDB:3NMW}.
HELIX 446 457 {ECO:0000244|PDB:3NMW}.
HELIX 460 468 {ECO:0000244|PDB:3NMW}.
HELIX 471 486 {ECO:0000244|PDB:3NMW}.
HELIX 492 508 {ECO:0000244|PDB:3NMW}.
HELIX 513 521 {ECO:0000244|PDB:3NMW}.
HELIX 523 531 {ECO:0000244|PDB:3NMW}.
HELIX 532 534 {ECO:0000244|PDB:3NMW}.
HELIX 538 552 {ECO:0000244|PDB:3NMW}.
HELIX 557 565 {ECO:0000244|PDB:3NMW}.
HELIX 568 578 {ECO:0000244|PDB:3NMW}.
HELIX 582 596 {ECO:0000244|PDB:3NMW}.
HELIX 600 608 {ECO:0000244|PDB:3NMW}.
HELIX 612 619 {ECO:0000244|PDB:3NMW}.
STRAND 625 627 {ECO:0000244|PDB:3NMW}.
HELIX 630 646 {ECO:0000244|PDB:3NMW}.
HELIX 650 657 {ECO:0000244|PDB:3NMW}.
TURN 658 660 {ECO:0000244|PDB:3NMW}.
HELIX 661 668 {ECO:0000244|PDB:3NMW}.
HELIX 674 687 {ECO:0000244|PDB:3NMW}.
HELIX 692 700 {ECO:0000244|PDB:3NMW}.
HELIX 703 708 {ECO:0000244|PDB:3NMW}.
TURN 709 712 {ECO:0000244|PDB:3NMW}.
HELIX 716 730 {ECO:0000244|PDB:3NMW}.
HELIX 735 737 {ECO:0000244|PDB:3NMW}.
TURN 1027 1030 {ECO:0000244|PDB:1JPP}.
HELIX 1470 1479 {ECO:0000244|PDB:1TH1}.
HELIX 1520 1524 {ECO:0000244|PDB:1V18}.
HELIX 2036 2045 {ECO:0000244|PDB:1EMU}.
STRAND 2840 2842 {ECO:0000244|PDB:3RL7}.
SEQUENCE 2843 AA; 311646 MW; 77E194AE4A91DC5A CRC64;
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDEAM
ASSGQIDLLE RLKELNLDSS NFPGVKLRSK MSLRSYGSRE GSVSSRSGEC SPVPMGSFPR
RGFVNGSRES TGYLEELEKE RSLLLADLDK EEKEKDWYYA QLQNLTKRID SLPLTENFSL
QTDMTRRQLE YEARQIRVAM EEQLGTCQDM EKRAQRRIAR IQQIEKDILR IRQLLQSQAT
EAERSSQNKH ETGSHDAERQ NEGQGVGEIN MATSGNGQGS TTRMDHETAS VLSSSSTHSA
PRRLTSHLGT KVEMVYSLLS MLGTHDKDDM SRTLLAMSSS QDSCISMRQS GCLPLLIQLL
HGNDKDSVLL GNSRGSKEAR ARASAALHNI IHSQPDDKRG RREIRVLHLL EQIRAYCETC
WEWQEAHEPG MDQDKNPMPA PVEHQICPAV CVLMKLSFDE EHRHAMNELG GLQAIAELLQ
VDCEMYGLTN DHYSITLRRY AGMALTNLTF GDVANKATLC SMKGCMRALV AQLKSESEDL
QQVIASVLRN LSWRADVNSK KTLREVGSVK ALMECALEVK KESTLKSVLS ALWNLSAHCT
ENKADICAVD GALAFLVGTL TYRSQTNTLA IIESGGGILR NVSSLIATNE DHRQILRENN
CLQTLLQHLK SHSLTIVSNA CGTLWNLSAR NPKDQEALWD MGAVSMLKNL IHSKHKMIAM
GSAAALRNLM ANRPAKYKDA NIMSPGSSLP SLHVRKQKAL EAELDAQHLS ETFDNIDNLS
PKASHRSKQR HKQSLYGDYV FDTNRHDDNR SDNFNTGNMT VLSPYLNTTV LPSSSSSRGS
LDSSRSEKDR SLERERGIGL GNYHPATENP GTSSKRGLQI STTAAQIAKV MEEVSAIHTS
QEDRSSGSTT ELHCVTDERN ALRRSSAAHT HSNTYNFTKS ENSNRTCSMP YAKLEYKRSS
NDSLNSVSSS DGYGKRGQMK PSIESYSEDD ESKFCSYGQY PADLAHKIHS ANHMDDNDGE
LDTPINYSLK YSDEQLNSGR QSPSQNERWA RPKHIIEDEI KQSEQRQSRN QSTTYPVYTE
STDDKHLKFQ PHFGQQECVS PYRSRGANGS ETNRVGSNHG INQNVSQSLC QEDDYEDDKP
TNYSERYSEE EQHEEEERPT NYSIKYNEEK RHVDQPIDYS LKYATDIPSS QKQSFSFSKS
SSGQSSKTEH MSSSSENTST PSSNAKRQNQ LHPSSAQSRS GQPQKAATCK VSSINQETIQ
TYCVEDTPIC FSRCSSLSSL SSAEDEIGCN QTTQEADSAN TLQIAEIKEK IGTRSAEDPV
SEVPAVSQHP RTKSSRLQGS SLSSESARHK AVEFSSGAKS PSKSGAQTPK SPPEHYVQET
PLMFSRCTSV SSLDSFESRS IASSVQSEPC SGMVSGIISP SDLPDSPGQT MPPSRSKTPP
PPPQTAQTKR EVPKNKAPTA EKRESGPKQA AVNAAVQRVQ VLPDADTLLH FATESTPDGF
SCSSSLSALS LDEPFIQKDV ELRIMPPVQE NDNGNETESE QPKESNENQE KEAEKTIDSE
KDLLDDSDDD DIEILEECII SAMPTKSSRK AKKPAQTASK LPPPVARKPS QLPVYKLLPS
QNRLQPQKHV SFTPGDDMPR VYCVEGTPIN FSTATSLSDL TIESPPNELA AGEGVRGGAQ
SGEFEKRDTI PTEGRSTDEA QGGKTSSVTI PELDDNKAEE GDILAECINS AMPKGKSHKP
FRVKKIMDQV QQASASSSAP NKNQLDGKKK KPTSPVKPIP QNTEYRTRVR KNADSKNNLN
AERVFSDNKD SKKQNLKNNS KVFNDKLPNN EDRVRGSFAF DSPHHYTPIE GTPYCFSRND
SLSSLDFDDD DVDLSREKAE LRKAKENKES EAKVTSHTEL TSNQQSANKT QAIAKQPINR
GQPKPILQKQ STFPQSSKDI PDRGAATDEK LQNFAIENTP VCFSHNSSLS SLSDIDQENN
NKENEPIKET EPPDSQGEPS KPQASGYAPK SFHVEDTPVC FSRNSSLSSL SIDSEDDLLQ
ECISSAMPKK KKPSRLKGDN EKHSPRNMGG ILGEDLTLDL KDIQRPDSEH GLSPDSENFD
WKAIQEGANS IVSSLHQAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT
SNKGPRILKP GEKSTLETKK IESESKGIKG GKKVYKSLIT GKVRSNSEIS GQMKQPLQAN
MPSISRGRTM IHIPGVRNSS SSTSPVSKKG PPLKTPASKS PSEGQTATTS PRGAKPSVKS
ELSPVARQTS QIGGSSKAPS RSGSRDSTPS RPAQQPLSRP IQSPGRNSIS PGRNGISPPN
KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQMSQQNLTK QTGLSKNASS IPRSESASKG
LNQMNNGNGA NKKVELSRMS STKSSGSESD RSERPVLVRQ STFIKEAPSP TLRRKLEESA
SFESLSPSSR PASPTRSQAQ TPVLSPSLPD MSLSTHSSVQ AGGWRKLPPN LSPTIEYNDG
RPAKRHDIAR SHSESPSRLP INRSGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES
SEKAKSEDEK HVNSISGTKQ SKENQVSAKG TWRKIKENEF SPTNSTSQTV SSGATNGAES
KTLIYQMAPA VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKA NPNIKDSKDN
QAKQNVGNGS VPMRTVGLEN RLNSFIQVDA PDQKGTEIKP GQNNPVPVSE TNESSIVERT
PFSSSSSSKH SSPSGTVAAR VTPFNYNPSP RKSSADSTSA RPSQIPTPVN NNTKKRDSKT
DSTESSGTQS PKRHSGSYLV TSV


Related products :

Catalog number Product name Quantity
G197 Anti_mouse adenomatous polyposis coli protein (APC) 100ug
EH1239 Adenomatous polyposis coli protein Elisa Kit 96T
Y059020 Anti_mouse adenomatous polyposis coli protein (APC) 100ug
CSB-EL001894MO Mouse Adenomatous polyposis coli protein(APC) ELISA kit 96T
E1490h Mouse ELISA Kit FOR Adenomatous polyposis coli protein 2 96T
CSB-EL001894HU Human Adenomatous polyposis coli protein(APC) ELISA kit 96T
G197 Anti-mouse adenomatous polyposis coli protein APC antibody 250ug
Y059020 Anti-mouse adenomatous polyposis coli protein APC antibody 250ug
G197 Anti-mouse adenomatous polyposis coli protein (APC) Antibody 100ug
CSB-EL001895HU Human Adenomatous polyposis coli protein 2(APC2) ELISA kit 96T
Y059020 Anti-mouse adenomatous polyposis coli protein (APC) Antibody 100ug
CSB-EL001894HU Human Adenomatous polyposis coli protein(APC) ELISA kit SpeciesHuman 96T
CSB-EL001894MO Mouse Adenomatous polyposis coli protein(APC) ELISA kit SpeciesMouse 96T
CSB-EL001895HU Human Adenomatous polyposis coli protein 2(APC2) ELISA kit SpeciesHuman 96T
MEDCLA821 Adenomatous Polyposis Coli Protein (APCP), Clone EMM43, Mab anti_; paraffin, IH 1 ml.
GWB-45D888 Adenomatous Polyposis Coli Protein (APC) Rabbit anti-Human Polyclonal (C-Terminus) Antibody
GWB-1B5EEC Adenomatous Polyposis Coli Protein (APC) Rabbit anti-Human Polyclonal (C-Terminus) Antibody
APCDD1 APC Gene adenomatous polyposis coli
AE56121RA Rat Adenomatous polyposis coli (APC) ELISA Kit 48T
CSB-EL001894RA Rat adenomatous polyposis coli (APC) ELISA kit 96T
201-20-0366 APC{adenomatous polyposis coli}rabbit.pAb 0.1ml
CSB-EL001894RA Rat adenomatous polyposis coli (APC) ELISA kit SpeciesRat 96T
17-4084 Polyclonal antibody Anti-Adenomatous Polyposis Coli (APC) 200 μl
bs-3680R Rabbit Anti-Adenomatous Polyposis Coli Polyclonal Antibody 100ul
bs-3680R-Cy7 Rabbit Anti-Adenomatous Polyposis Coli Polyclonal Antibody, Cy7 Conjugated 100ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur