APC_HUMAN
ID APC_HUMAN Reviewed; 2843 AA.
AC P25054; B7Z2B6; D3DT03; Q15162; Q15163; Q93042;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 259.
DE RecName: Full=Adenomatous polyposis coli protein;
DE Short=Protein APC;
DE AltName: Full=Deleted in polyposis 2.5;
GN Name=APC {ECO:0000312|HGNC:HGNC:583}; Synonyms=DP2.5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 2), AND VARIANT ASP-1822.
RC TISSUE=Fetal brain;
RX PubMed=1678319; DOI=10.1016/0092-8674(81)90022-2;
RA Joslyn G., Carlson M., Thliveris A., Albertsen H., Gelbert L., Samowitz W.,
RA Groden J., Stevens J., Spirio L., Robertson M., Sargeant L., Krapcho K.,
RA Wolff E., Burt R., Hughes J.P., Warrington J., McPherson J.D.,
RA Wasmuth J.J., le Paslier D., Abderrahim H., Cohen D., Leppert M., White R.;
RT "Identification of deletion mutations and three new genes at the familial
RT polyposis locus.";
RL Cell 66:601-613(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), AND VARIANT ASP-1822.
RX PubMed=1651562; DOI=10.1126/science.1651562;
RA Kinzler K.W., Nilbert M.C., Su L.-K., Vogelstein B., Bryan T.M., Levy D.B.,
RA Smith K.J., Preisinger A.C., Hedge P., McKechnie D., Finniear R.,
RA Markham A., Groffen J., Boguski M.S., Altschul S.F., Horii A.K., Ando H.,
RA Miyoshi Y., Miki Y., Nishisho I., Nakamura Y.;
RT "Identification of FAP locus genes from chromosome 5q21.";
RL Science 253:661-665(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH ARHGEF4, AND IDENTIFICATION IN A COMPLEX WITH ARHGEF4 AND
RP CTNNB1.
RX PubMed=10947987; DOI=10.1126/science.289.5482.1194;
RA Kawasaki Y., Senda T., Ishidate T., Koyama R., Morishita T., Iwayama Y.,
RA Higuchi O., Akiyama T.;
RT "Asef, a link between the tumor suppressor APC and G-protein signaling.";
RL Science 289:1194-1197(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-1822.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1135 (ISOFORM 1B).
RC TISSUE=Amygdala {ECO:0000312|EMBL:BAH11802.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1506-1524.
RX PubMed=1310068;
RA Miki Y., Nishisho I., Horii A., Miyoshi Y., Utsunomiya J., Kinzler K.W.,
RA Vogelstein B., Nakamura Y.;
RT "Disruption of the APC gene by a retrotransposal insertion of L1 sequence
RT in a colon cancer.";
RL Cancer Res. 52:643-645(1992).
RN [8]
RP ASSOCIATION WITH CATENINS.
RX PubMed=8259519; DOI=10.1126/science.8259519;
RA Su L.-K., Vogelstein B., Kinzler K.W.;
RT "Association of the APC tumor suppressor protein with catenins.";
RL Science 262:1734-1737(1993).
RN [9]
RP INTERACTION WITH DLG1.
RX PubMed=8638125; DOI=10.1126/science.272.5264.1020;
RA Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H.,
RA Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T.;
RT "Binding of APC to the human homolog of the Drosophila discs large tumor
RT suppressor protein.";
RL Science 272:1020-1023(1996).
RN [10]
RP INTERACTION WITH DLG3.
RC TISSUE=Fetal brain;
RX PubMed=9188857; DOI=10.1038/sj.onc.1201087;
RA Makino K., Kuwahara H., Masuko N., Nishiyama Y., Morisaki T., Sasaki J.,
RA Nakao M., Kuwano A., Nakata M., Ushio Y., Saya H.;
RT "Cloning and characterization of NE-dlg: a novel human homolog of the
RT Drosophila discs large (dlg) tumor suppressor protein interacts with the
RT APC protein.";
RL Oncogene 14:2425-2433(1997).
RN [11]
RP INTERACTION WITH APC2.
RX PubMed=11691822;
RA Jarrett C.R., Blancato J., Cao T., Bressette D.S., Cepeda M., Young P.E.,
RA King C.R., Byers S.W.;
RT "Human APC2 localization and allelic imbalance.";
RL Cancer Res. 61:7978-7984(2001).
RN [12]
RP INTERACTION WITH MAPRE1; MAPRE2 AND MAPRE3.
RX PubMed=14514668; DOI=10.1074/jbc.m306194200;
RA Bu W., Su L.-K.;
RT "Characterization of functional domains of human EB1 family proteins.";
RL J. Biol. Chem. 278:49721-49731(2003).
RN [13]
RP UBIQUITINATION.
RX PubMed=15355978; DOI=10.1074/jbc.m404655200;
RA Choi J., Park S.Y., Costantini F., Jho E.-H., Joo C.-K.;
RT "Adenomatous polyposis coli is down-regulated by the ubiquitin-proteasome
RT pathway in a process facilitated by Axin.";
RL J. Biol. Chem. 279:49188-49198(2004).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP SUBCELLULAR LOCATION, INTERACTION WITH SCRIB, AND MUTAGENESIS OF THR-2841
RP AND VAL-2843.
RX PubMed=16611247; DOI=10.1111/j.1365-2443.2006.00954.x;
RA Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K., Yasugi T.,
RA Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T., Taketani Y.;
RT "Human scribble, a novel tumor suppressor identified as a target of high-
RT risk HPV E6 for ubiquitin-mediated degradation, interacts with adenomatous
RT polyposis coli.";
RL Genes Cells 11:453-464(2006).
RN [16]
RP FUNCTION, AND INTERACTION WITH SPATA13.
RX PubMed=17599059; DOI=10.1038/sj.onc.1210574;
RA Kawasaki Y., Sagara M., Shibata Y., Shirouzu M., Yokoyama S., Akiyama T.;
RT "Identification and characterization of Asef2, a guanine-nucleotide
RT exchange factor specific for Rac1 and Cdc42.";
RL Oncogene 26:7620-7627(2007).
RN [17]
RP DEUBIQUITINATION.
RX PubMed=18281465; DOI=10.1101/gad.463208;
RA Tran H., Hamada F., Schwarz-Romond T., Bienz M.;
RT "Trabid, a new positive regulator of Wnt-induced transcription with
RT preference for binding and cleaving K63-linked ubiquitin chains.";
RL Genes Dev. 22:528-542(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2671, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780; SER-1042; SER-1360;
RP SER-1861; SER-1863; SER-1864; THR-2151; SER-2260; SER-2270; SER-2283;
RP SER-2473; SER-2535; SER-2671; SER-2674; THR-2679 AND SER-2789, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP ALTERNATIVE PROMOTER USAGE, AND TISSUE SPECIFICITY.
RX PubMed=19527921; DOI=10.1016/j.canlet.2009.05.016;
RA Hosoya K., Yamashita S., Ando T., Nakajima T., Itoh F., Ushijima T.;
RT "Adenomatous polyposis coli 1A is likely to be methylated as a passenger in
RT human gastric carcinogenesis.";
RL Cancer Lett. 285:182-189(2009).
RN [22]
RP INTERACTION WITH MAPRE1, AND SUBCELLULAR LOCATION.
RX PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
RA Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
RA Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
RA Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
RT "An EB1-binding motif acts as a microtubule tip localization signal.";
RL Cell 138:366-376(2009).
RN [23]
RP FUNCTION.
RX PubMed=19893577; DOI=10.1038/embor.2009.233;
RA Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M.,
RA Ohwada S., Akiyama T.;
RT "The adenomatous polyposis coli-associated exchange factors Asef and Asef2
RT are required for adenoma formation in Apc(Min/+)mice.";
RL EMBO Rep. 10:1355-1362(2009).
RN [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19151759; DOI=10.1038/onc.2008.478;
RA Sagara M., Kawasaki Y., Iemura S.I., Natsume T., Takai Y., Akiyama T.;
RT "Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal organization
RT and are involved in HGF-induced cell migration.";
RL Oncogene 28:1357-1365(2009).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [26]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20937854; DOI=10.1073/pnas.1000975107;
RA Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
RT "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
RT plasma membrane of migrating cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744 AND SER-780, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
RP INTERACTION WITH AMER1.
RX PubMed=21498506; DOI=10.1074/jbc.m111.224881;
RA Tanneberger K., Pfister A.S., Kriz V., Bryja V., Schambony A., Behrens J.;
RT "Structural and functional characterization of the Wnt inhibitor APC
RT membrane recruitment 1 (Amer1).";
RL J. Biol. Chem. 286:19204-19214(2011).
RN [29]
RP ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, AND INVOLVEMENT IN FAP1.
RX PubMed=21643010; DOI=10.1038/onc.2011.201;
RA Rohlin A., Engwall Y., Fritzell K., Goeransson K., Bergsten A.,
RA Einbeigi Z., Nilbert M., Karlsson P., Bjoerk J., Nordling M.;
RT "Inactivation of promoter 1B of APC causes partial gene silencing: evidence
RT for a significant role of the promoter in regulation and causative of
RT familial adenomatous polyposis.";
RL Oncogene 30:4977-4989(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861; SER-1863 AND SER-1864,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP INTERACTION WITH AMER2.
RX PubMed=22128170; DOI=10.1074/jbc.m111.308650;
RA Pfister A.S., Tanneberger K., Schambony A., Behrens J.;
RT "Amer2 protein is a novel negative regulator of Wnt/beta-Catenin signaling
RT involved in neuroectodermal patterning.";
RL J. Biol. Chem. 287:1734-1741(2012).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744; SER-748; SER-908;
RP SER-1042; SER-1371; SER-1385; THR-1438; SER-1774; SER-1861; SER-2260;
RP SER-2283; SER-2569; SER-2674; SER-2724 AND SER-2789, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP INTERACTION WITH JPT1.
RX PubMed=25169422; DOI=10.1002/jcb.24956;
RA Varisli L., Ozturk B.E., Akyuz G.K., Korkmaz K.S.;
RT "HN1 negatively influences the beta-catenin/E-cadherin interaction, and
RT contributes to migration in prostate cells.";
RL J. Cell. Biochem. 116:170-178(2015).
RN [36]
RP ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, AND INVOLVEMENT IN FAP1.
RX PubMed=27217144; DOI=10.1038/srep26011;
RA Yamaguchi K., Nagayama S., Shimizu E., Komura M., Yamaguchi R., Shibuya T.,
RA Arai M., Hatakeyama S., Ikenoue T., Ueno M., Miyano S., Imoto S.,
RA Furukawa Y.;
RT "Reduced expression of APC-1B but not APC-1A by the deletion of promoter 1B
RT is responsible for familial adenomatous polyposis.";
RL Sci. Rep. 6:26011-26011(2016).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-55.
RX PubMed=10926498; DOI=10.1006/jmbi.2000.3895;
RA Day C.L., Alber T.;
RT "Crystal structure of the amino-terminal coiled-coil domain of the APC
RT tumor suppressor.";
RL J. Mol. Biol. 301:147-156(2000).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1021-1035 IN COMPLEX WITH CTNNB1.
RX PubMed=11707392; DOI=10.1093/emboj/20.22.6203;
RA Eklof Spink K., Fridman S.G., Weis W.I.;
RT "Molecular mechanisms of beta-catenin recognition by adenomatous polyposis
RT coli revealed by the structure of an APC-beta-catenin complex.";
RL EMBO J. 20:6203-6212(2001).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2034-2049 IN COMPLEX WITH AXIN.
RX PubMed=10811618; DOI=10.1093/emboj/19.10.2270;
RA Spink K.E., Polakis P., Weis W.I.;
RT "Structural basis of the axin-adenomatous polyposis coli interaction.";
RL EMBO J. 19:2270-2279(2000).
RN [40]
RP REVIEW ON VARIANTS.
RX PubMed=8111410; DOI=10.1002/humu.1380020602;
RA Nagase H., Nakamura Y.;
RT "Mutations of the APC (adenomatous polyposis coli) gene.";
RL Hum. Mutat. 2:425-434(1993).
RN [41]
RP STRUCTURE BY NMR OF 1578-1596 IN COMPLEX WITH ASAP1.
RX PubMed=20509626; DOI=10.1021/bi100563z;
RA Kaieda S., Matsui C., Mimori-Kiyosue Y., Ikegami T.;
RT "Structural basis of the recognition of the SAMP motif of adenomatous
RT polyposis coli by the Src-homology 3 domain.";
RL Biochemistry 49:5143-5153(2010).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 407-775, AND DOMAIN ARM REPEATS.
RX PubMed=21871439; DOI=10.1016/j.bbrc.2011.08.044;
RA Zhang Z., Lin K., Gao L., Chen L., Shi X., Wu G.;
RT "Crystal structure of the armadillo repeat domain of adenomatous polyposis
RT coli which reveals its inherent flexibility.";
RL Biochem. Biophys. Res. Commun. 412:732-736(2011).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 396-732 IN COMPLEX WITH KHDRBS1,
RP AND MUTAGENESIS OF LYS-516 AND ARG-549.
RX PubMed=22000517; DOI=10.1016/j.str.2011.07.013;
RA Morishita E.C., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y.,
RA Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T.,
RA Yokoyama S.;
RT "Crystal structures of the armadillo repeat domain of adenomatous polyposis
RT coli and its complex with the tyrosine-rich domain of Sam68.";
RL Structure 19:1496-1508(2011).
RN [44]
RP VARIANTS FAP1.
RX PubMed=1651563; DOI=10.1126/science.1651563;
RA Nishisho I., Nakamura Y., Miyoshi Y., Miki Y., Ando H., Horii A.,
RA Koyama K., Utsunomiya J., Baba S., Hedge P., Markham A., Krush A.J.,
RA Petersen G.M., Hamilton S.R., Nilbert M.C., Levy D.B., Bryan T.M.,
RA Preisinger A.C., Smith K.J., Su L.-K., Kinzler K.W., Vogelstein B.;
RT "Mutations of chromosome 5q21 genes in FAP and colorectal cancer
RT patients.";
RL Science 253:665-669(1991).
RN [45]
RP VARIANTS FAP1.
RX PubMed=1338904; DOI=10.1093/hmg/1.4.229;
RA Miyoshi Y., Nagase H., Ando H., Ichii S., Nakatsuru S., Aoki T., Miki Y.,
RA Mori T., Nakamura Y.;
RT "Somatic mutations of the APC gene in colorectal tumors: mutation cluster
RT region in the APC gene.";
RL Hum. Mol. Genet. 1:229-233(1992).
RN [46]
RP VARIANTS FAP1.
RX PubMed=1338691; DOI=10.1093/hmg/1.8.559;
RA Nakatsuru S., Yanagisawa A., Ichii S., Tahara E., Kato Y., Nakamura Y.,
RA Horii A.;
RT "Somatic mutation of the APC gene in gastric cancer: frequent mutations in
RT very well differentiated adenocarcinoma and signet-ring cell carcinoma.";
RL Hum. Mol. Genet. 1:559-563(1992).
RN [47]
RP VARIANTS FAP1 MET-1292 AND TRP-1348, AND VARIANTS ASP-1118; VAL-1304 AND
RP SER-2502.
RX PubMed=1338764; DOI=10.1002/humu.1380010603;
RA Nagase H., Miyoshi Y., Horii A., Aoki T., Petersen G.M., Vogelstein B.,
RA Maher E., Ogawa M., Maruyama M., Utsunomiya J., Baba S., Nakamura Y.;
RT "Screening for germ-line mutations in familial adenomatous polyposis
RT patients: 61 new patients and a summary of 150 unrelated patients.";
RL Hum. Mutat. 1:467-473(1992).
RN [48]
RP VARIANT FAP1 CYS-2621.
RX PubMed=1316610; DOI=10.1073/pnas.89.10.4452;
RA Miyoshi Y., Ando H., Nagase H., Nishisho I., Horii A., Miki Y., Mori T.,
RA Utsunomiya J., Baba S., Petersen G.;
RT "Germ-line mutations of the APC gene in 53 familial adenomatous polyposis
RT patients.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4452-4456(1992).
RN [49]
RP VARIANT FAP1 TRP-99.
RC TISSUE=Peripheral blood lymphocyte;
RX PubMed=7833149; DOI=10.1016/0959-8049(94)00294-f;
RA Dobbie Z., Spycher M., Huerliman R., Ammann R., Ammann T., Roth J.,
RA Mueller A., Mueller H., Scott R.J.;
RT "Mutational analysis of the first 14 exons of the adenomatous polyposis
RT coli (APC) gene.";
RL Eur. J. Cancer 30A:1709-1713(1994).
RN [50]
RP VARIANT FAP1 GLY-722.
RX PubMed=7833931; DOI=10.1093/hmg/3.9.1687;
RA Stella A., Montera M., Resta N., Marchese C., Susca F., Gentile M.,
RA Romio L., Pilia S., Prete F., Mareni C., Guanti G.;
RT "Four novel mutations of the APC (adenomatous polyposis coli) gene in FAP
RT patients.";
RL Hum. Mol. Genet. 3:1687-1688(1994).
RN [51]
RP ERRATUM OF PUBMED:7833931.
RA Stella A., Montera M., Resta N., Marchese C., Susca F., Gentile M.,
RA Romio L., Pilia S., Prete F., Mareni C., Guanti G.;
RL Hum. Mol. Genet. 3:1918-1918(1994).
RN [52]
RP INVOLVEMENT IN FAP1.
RX PubMed=7661930; DOI=10.1056/nejm199503303321302;
RA Hamilton S.R., Liu B., Parsons R.E., Papadopoulos N., Jen J., Powell S.M.,
RA Krush A.J., Berk T., Cohen Z., Tetu B., Burger P.C., Wood P.A., Taqi F.,
RA Booker S.V., Petersen G.M., Offerhaus G.J.A., Tersmette A.C.,
RA Giardiello F.M., Vogelstein B., Kinzler K.W.;
RT "The molecular basis of Turcot's syndrome.";
RL N. Engl. J. Med. 332:839-847(1995).
RN [53]
RP INVOLVEMENT IN DESMD.
RX PubMed=8940264;
RA Eccles D.M., van der Luijt R.B., Breukel C., Bullman H., Bunyan D.,
RA Fisher A., Barber J., du Boulay C., Primrose J., Burn J., Fodde R.;
RT "Hereditary desmoid disease due to a frameshift mutation at codon 1924 of
RT the APC gene.";
RL Am. J. Hum. Genet. 59:1193-1201(1996).
RN [54]
RP VARIANT HEPATOBLASTOMA CYS-1395.
RX PubMed=8764128;
RA Oda H., Imai Y., Nakatsuru Y., Hata J., Ishikawa T.;
RT "Somatic mutations of the APC gene in sporadic hepatoblastomas.";
RL Cancer Res. 56:3320-3323(1996).
RN [55]
RP VARIANT FAP1 ILE-171.
RX PubMed=8990002;
RX DOI=10.1002/(sici)1098-1004(1997)9:1<7::aid-humu2>3.0.co;2-8;
RA van der Luijt R.B., Meera Khan P., Vasen H.F.A., Tops C.M.J.,
RA van Leeuwen-Cornelisse I.S.J., Wijnen J.T., van der Klift H.M., Plug R.J.,
RA Griffioen G., Fodde R.;
RT "Molecular analysis of the APC gene in 105 Dutch kindreds with familial
RT adenomatous polyposis: 67 germline mutations identified by DGGE, PTT, and
RT southern analysis.";
RL Hum. Mutat. 9:7-16(1997).
RN [56]
RP VARIANTS COLORECTAL CARCINOMA THR-880; ILE-890 AND VAL-1508.
RX PubMed=9419979; DOI=10.1038/sj.onc.1201668;
RA Miyaki M., Nishio J., Konishi M., Kikuchi-Yanoshita R., Tanaka K.,
RA Muraoka M., Nagato M., Chong J.-M., Koike M., Terada T., Kawahara Y.,
RA Fukutome A., Tomiyama J., Chuganji Y., Momoi M., Utsunomiya J.;
RT "Drastic genetic instability of tumors and normal tissues in Turcot
RT syndrome.";
RL Oncogene 15:2877-2881(1997).
RN [57]
RP VARIANT LYS-1307.
RX PubMed=9731522; DOI=10.1038/1666;
RA Redston M., Nathanson K.L., Yuan Z.Q., Neuhausen S.L., Satagopan J.,
RA Wong N., Yang D., Nafa D., Abrahamson J., Ozcelik H., Antin-Ozerkis D.,
RA Andrulis I., Daly M., Pinsky L., Schrag D., Gallinger S., Kaback M.,
RA King M.-C., Woodage T., Brody L.C., Godwin A., Warner E., Weber B.,
RA Foulkes W., Offit K.;
RT "The APC I1307K allele and breast cancer risk.";
RL Nat. Genet. 20:13-14(1998).
RN [58]
RP VARIANTS LYS-1307 AND GLN-1317.
RC TISSUE=Peripheral blood;
RX PubMed=9724771; DOI=10.1073/pnas.95.18.10722;
RA Frayling I.M., Beck N.E., Ilyas M., Dove-Edwin I., Goodman P., Pack K.,
RA Bell J.A., Williams C.B., Hodgson S.V., Thomas H.J.W., Talbot I.C.,
RA Bodmer W.F., Tomlinson I.P.M.;
RT "The APC variants I1307K and E1317Q are associated with colorectal tumors,
RT but not always with a family history.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10722-10727(1998).
RN [59]
RP VARIANT LYS-1307.
RX PubMed=9731533; DOI=10.1038/1722;
RA Woodage T., King S.M., Wacholder S., Hartge P., Struewing J.P., McAdams M.,
RA Laken S.J., Tucker M.A., Brody L.C.;
RT "The APC I1307K allele and cancer risk in a community-based study of
RT Ashkenazi Jews.";
RL Nat. Genet. 20:62-65(1998).
RN [60]
RP VARIANT LYS-1307.
RX PubMed=9973276; DOI=10.1086/302262;
RA Gryfe R., Di Nicola N., Lal G., Gallinger S., Redston M.;
RT "Inherited colorectal polyposis and cancer risk of the APC I1307K
RT polymorphism.";
RL Am. J. Hum. Genet. 64:378-384(1999).
RN [61]
RP VARIANTS GLY-1057; CYS-1171; ASP-1822 AND THR-2738.
RX PubMed=9950360;
RA Wallis Y.L., Morton D.G., McKeown C.M., Macdonald F.;
RT "Molecular analysis of the APC gene in 205 families: extended genotype-
RT phenotype correlations in FAP and evidence for the role of APC amino acid
RT changes in colorectal cancer predisposition.";
RL J. Med. Genet. 36:14-20(1999).
RN [62]
RP VARIANT FAP1 PRO-1184.
RX PubMed=10470088; DOI=10.1038/12511;
RA Lamlum H., Ilyas M., Rowan A., Clark S., Johnson V., Bell J.A.,
RA Frayling I.M., Efstathiou J., Pack K., Payne S., Roylance R., Gorman P.,
RA Sheer D., Neale K., Phillips R., Talbot I.C., Bodmer W.F.,
RA Tomlinson I.P.M.;
RT "The type of somatic mutation at APC in familial adenomatous polyposis is
RT determined by the site of the germline mutation: a new facet to Knudson's
RT 'two-hit' hypothesis.";
RL Nat. Med. 5:1071-1075(1999).
RN [63]
RP VARIANTS MDB VAL-1296; ILE-1472 AND GLY-1495.
RX PubMed=10666372; DOI=10.1016/s0002-9440(10)64747-5;
RA Huang H., Mahler-Araujo B.M., Sankila A., Chimelli L., Yonekawa Y.,
RA Kleihues P., Ohgaki H.;
RT "APC mutations in sporadic medulloblastomas.";
RL Am. J. Pathol. 156:433-437(2000).
RN [64]
RP INVOLVEMENT IN DESMD.
RX PubMed=10782927; DOI=10.1034/j.1399-0004.2000.570306.x;
RA Couture J., Mitri A., Lagace R., Smits R., Berk T., Bouchard H.-L.,
RA Fodde R., Alman B., Bapat B.;
RT "A germline mutation at the extreme 3' end of the APC gene results in a
RT severe desmoid phenotype and is associated with overexpression of beta-
RT catenin in the desmoid tumor.";
RL Clin. Genet. 57:205-212(2000).
RN [65]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-1254.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [66]
RP INVOLVEMENT IN GAPPS.
RX PubMed=27087319; DOI=10.1016/j.ajhg.2016.03.001;
RA Li J., Woods S.L., Healey S., Beesley J., Chen X., Lee J.S.,
RA Sivakumaran H., Wayte N., Nones K., Waterfall J.J., Pearson J., Patch A.M.,
RA Senz J., Ferreira M.A., Kaurah P., Mackenzie R., Heravi-Moussavi A.,
RA Hansford S., Lannagan T.R.M., Spurdle A.B., Simpson P.T., da Silva L.,
RA Lakhani S.R., Clouston A.D., Bettington M., Grimpen F., Busuttil R.A.,
RA Di Costanzo N., Boussioutas A., Jeanjean M., Chong G., Fabre A.,
RA Olschwang S., Faulkner G.J., Bellos E., Coin L., Rioux K., Bathe O.F.,
RA Wen X., Martin H.C., Neklason D.W., Davis S.R., Walker R.L., Calzone K.A.,
RA Avital I., Heller T., Koh C., Pineda M., Rudloff U., Quezado M.,
RA Pichurin P.N., Hulick P.J., Weissman S.M., Newlin A., Rubinstein W.S.,
RA Sampson J.E., Hamman K., Goldgar D., Poplawski N., Phillips K.,
RA Schofield L., Armstrong J., Kiraly-Borri C., Suthers G.K., Huntsman D.G.,
RA Foulkes W.D., Carneiro F., Lindor N.M., Edwards S.L., French J.D.,
RA Waddell N., Meltzer P.S., Worthley D.L., Schrader K.A., Chenevix-Trench G.;
RT "Point Mutations in Exon 1B of APC Reveal Gastric Adenocarcinoma and
RT Proximal Polyposis of the Stomach as a Familial Adenomatous Polyposis
RT Variant.";
RL Am. J. Hum. Genet. 98:830-842(2016).
RN [67]
RP INVOLVEMENT IN GAPPS.
RX PubMed=27343414; DOI=10.1016/j.gie.2016.06.023;
RA Repak R., Kohoutova D., Podhola M., Rejchrt S., Minarik M., Benesova L.,
RA Lesko M., Bures J.;
RT "The first European family with gastric adenocarcinoma and proximal
RT polyposis of the stomach: case report and review of the literature.";
RL Gastrointest. Endosc. 84:718-725(2016).
RN [68]
RP INVOLVEMENT IN GAPPS.
RX PubMed=33242120; DOI=10.1007/s12328-020-01290-6;
RA Kanemitsu K., Iwatsuki M., Yamashita K., Komohara Y., Morinaga T.,
RA Iwagami S., Eto K., Nagai Y., Kurashige J., Baba Y., Yoshida N., Baba H.;
RT "Two Asian families with gastric adenocarcinoma and proximal polyposis of
RT the stomach successfully treated via laparoscopic total gastrectomy.";
RL Clin. J. Gastroenterol. 14:92-97(2021).
CC -!- FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1 and
CC participates in Wnt signaling as a negative regulator. APC activity is
CC correlated with its phosphorylation state. Activates the GEF activity
CC of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-
CC induced cell migration. Required for MMP9 up-regulation via the JNK
CC signaling pathway in colorectal tumor cells. Acts as a mediator of
CC ERBB2-dependent stabilization of microtubules at the cell cortex. It is
CC required for the localization of MACF1 to the cell membrane and this
CC localization of MACF1 is critical for its function in microtubule
CC stabilization. {ECO:0000269|PubMed:10947987,
CC ECO:0000269|PubMed:17599059, ECO:0000269|PubMed:19151759,
CC ECO:0000269|PubMed:19893577, ECO:0000269|PubMed:20937854}.
CC -!- SUBUNIT: Forms homooligomers and heterooligomers with APC2. Interacts
CC with DIAPH1 and DIAPH2 (By similarity). Interacts with PDZ domains of
CC DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with
CC ARHGEF4 (via N-terminus). Interacts with MAPRE1 (via C-terminus);
CC probably required for APC targeting to the growing microtubule plus
CC ends. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a
CC complex consisting of ARHGEF4, APC and CTNNB1. Interacts with SCRIB;
CC may mediate APC targeting to adherens junctions of epithelial cells.
CC Interacts with SPATA13 (via N-terminus and SH3 domain). Interacts with
CC ASAP1 (via SH3 domain). Found in a complex composed of MACF1, APC,
CC AXIN1, CTNNB1 and GSK3B (By similarity). Interacts at the cell membrane
CC with AMER1 and AMER2 (via ARM repeats). Interacts with KHDRBS1. The
CC complex composed, at least, of APC, CTNNB1 and GSK3B interacts with
CC JPT1; the interaction requires the inactive form of GSK3B
CC (phosphorylated at 'Ser-9') (PubMed:25169422).
CC {ECO:0000250|UniProtKB:Q61315, ECO:0000269|PubMed:10811618,
CC ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:11691822,
CC ECO:0000269|PubMed:11707392, ECO:0000269|PubMed:14514668,
CC ECO:0000269|PubMed:16611247, ECO:0000269|PubMed:17599059,
CC ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:20509626,
CC ECO:0000269|PubMed:21498506, ECO:0000269|PubMed:22000517,
CC ECO:0000269|PubMed:22128170, ECO:0000269|PubMed:25169422,
CC ECO:0000269|PubMed:8638125, ECO:0000269|PubMed:9188857}.
CC -!- INTERACTION:
CC P25054; Q5JTC6: AMER1; NbExp=4; IntAct=EBI-727707, EBI-6169747;
CC P25054; Q8N944: AMER3; NbExp=8; IntAct=EBI-727707, EBI-8869590;
CC P25054; Q9NR80-3: ARHGEF4; NbExp=5; IntAct=EBI-727707, EBI-13639160;
CC P25054; O15169: AXIN1; NbExp=17; IntAct=EBI-727707, EBI-710484;
CC P25054; P60953: CDC42; NbExp=9; IntAct=EBI-727707, EBI-81752;
CC P25054; P49674: CSNK1E; NbExp=8; IntAct=EBI-727707, EBI-749343;
CC P25054; P35221: CTNNA1; NbExp=3; IntAct=EBI-727707, EBI-701918;
CC P25054; P35222: CTNNB1; NbExp=19; IntAct=EBI-727707, EBI-491549;
CC P25054; Q12959: DLG1; NbExp=2; IntAct=EBI-727707, EBI-357481;
CC P25054; O14640: DVL1; NbExp=6; IntAct=EBI-727707, EBI-723489;
CC P25054; P54792: DVL1P1; NbExp=2; IntAct=EBI-727707, EBI-7848109;
CC P25054; O14641: DVL2; NbExp=2; IntAct=EBI-727707, EBI-740850;
CC P25054; P14923: JUP; NbExp=3; IntAct=EBI-727707, EBI-702484;
CC P25054; Q07666: KHDRBS1; NbExp=4; IntAct=EBI-727707, EBI-1364;
CC P25054; Q14114: LRP8; NbExp=2; IntAct=EBI-727707, EBI-2681187;
CC P25054; Q15691: MAPRE1; NbExp=5; IntAct=EBI-727707, EBI-1004115;
CC P25054; Q14160: SCRIB; NbExp=5; IntAct=EBI-727707, EBI-357345;
CC P25054; Q96N96: SPATA13; NbExp=5; IntAct=EBI-727707, EBI-13618641;
CC P25054; Q96N96-1: SPATA13; NbExp=5; IntAct=EBI-727707, EBI-13638906;
CC P25054; Q96N96-2: SPATA13; NbExp=2; IntAct=EBI-727707, EBI-13639118;
CC P25054; Q02248: Ctnnb1; Xeno; NbExp=8; IntAct=EBI-727707, EBI-397872;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:16611247}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:20937854}. Cell
CC projection, lamellipodium {ECO:0000269|PubMed:19151759}. Cell
CC projection, ruffle membrane {ECO:0000269|PubMed:19151759}. Cytoplasm
CC {ECO:0000269|PubMed:10947987}. Cell membrane
CC {ECO:0000269|PubMed:10947987, ECO:0000269|PubMed:16611247,
CC ECO:0000269|PubMed:20937854}. Note=Associated with the microtubule
CC network at the growing distal tip of microtubules (PubMed:19632184).
CC Accumulates in the lamellipodium and ruffle membrane in response to
CC hepatocyte growth factor (HGF) treatment (PubMed:19151759). The MEMO1-
CC RHOA-DIAPH1 signaling pathway controls localization of the
CC phosphorylated form to the cell membrane (PubMed:20937854).
CC {ECO:0000269|PubMed:19151759, ECO:0000269|PubMed:19632184,
CC ECO:0000269|PubMed:20937854}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=1A {ECO:0000303|PubMed:19527921}; Synonyms=Long
CC {ECO:0000303|PubMed:1678319};
CC IsoId=P25054-1; Sequence=Displayed;
CC Name=2; Synonyms=Short {ECO:0000303|PubMed:1678319};
CC IsoId=P25054-2; Sequence=VSP_004115;
CC Name=1B {ECO:0000303|PubMed:19527921};
CC IsoId=P25054-3; Sequence=VSP_059027, VSP_059028;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues: brain, small
CC intestine, colon, thymus, skeletal muscle, heart, prostate, lung,
CC spleen, ovary, testis kidney, placenta, blood and liver
CC (PubMed:21643010, PubMed:27217144). Isoform 1A: Very strongly expressed
CC in brain but has relatively low expression levels in other tissues
CC (PubMed:19527921, PubMed:21643010, PubMed:27217144). Isoform 1B:
CC Predominant form in all tissues except for brain, including gastric
CC mucosa and blood (PubMed:19527921, PubMed:21643010, PubMed:27217144).
CC {ECO:0000269|PubMed:19527921, ECO:0000269|PubMed:21643010,
CC ECO:0000269|PubMed:27217144}.
CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates
CC interaction with MAPRE1 and targeting to the growing microtubule plus
CC ends. {ECO:0000250}.
CC -!- PTM: Phosphorylated by GSK3B.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC Ubiquitination is facilitated by Axin. Deubiquitinated by
CC ZRANB1/TRABID. {ECO:0000269|PubMed:15355978,
CC ECO:0000269|PubMed:18281465}.
CC -!- DISEASE: Familial adenomatous polyposis 1 (FAP1) [MIM:175100]: An
CC autosomal dominant cancer predisposition syndrome characterized by
CC adenomatous polyps of the colon and rectum, but also of upper
CC gastrointestinal tract (ampullary, duodenal and gastric adenomas). This
CC is a viciously premalignant disease with one or more polyps progressing
CC through dysplasia to malignancy in untreated gene carriers with a
CC median age at diagnosis of 40 years. {ECO:0000269|PubMed:10470088,
CC ECO:0000269|PubMed:1316610, ECO:0000269|PubMed:1338691,
CC ECO:0000269|PubMed:1338764, ECO:0000269|PubMed:1338904,
CC ECO:0000269|PubMed:1651563, ECO:0000269|PubMed:21643010,
CC ECO:0000269|PubMed:27217144, ECO:0000269|PubMed:7661930,
CC ECO:0000269|PubMed:7833149, ECO:0000269|PubMed:7833931,
CC ECO:0000269|PubMed:8990002}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Desmoid disease, hereditary (DESMD) [MIM:135290]: An autosomal
CC dominant disease characterized by multifocal fibromatosis of the
CC abdominal wall and mesentery. Desmoid tumors can also affect paraspinal
CC muscles, breast, occiput, arms, and lower ribs.
CC {ECO:0000269|PubMed:10782927, ECO:0000269|PubMed:8940264}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive
CC embryonal tumor of the cerebellum with a preferential manifestation in
CC children. {ECO:0000269|PubMed:10666372}. Note=The gene represented in
CC this entry may be involved in disease pathogenesis.
CC -!- DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which
CC starts in the stomach, can spread to the esophagus or the small
CC intestine, and can extend through the stomach wall to nearby lymph
CC nodes and organs. It also can metastasize to other parts of the body.
CC The term gastric cancer or gastric carcinoma refers to adenocarcinoma
CC of the stomach that accounts for most of all gastric malignant tumors.
CC Two main histologic types are recognized, diffuse type and intestinal
CC type carcinomas. Diffuse tumors are poorly differentiated infiltrating
CC lesions, resulting in thickening of the stomach. In contrast,
CC intestinal tumors are usually exophytic, often ulcerating, and
CC associated with intestinal metaplasia of the stomach, most often
CC observed in sporadic disease. Note=The gene represented in this entry
CC may be involved in disease pathogenesis.
CC -!- DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary
CC malignant neoplasm of epithelial liver cells. The major risk factors
CC for HCC are chronic hepatitis B virus (HBV) infection, chronic
CC hepatitis C virus (HCV) infection, prolonged dietary aflatoxin
CC exposure, alcoholic cirrhosis, and cirrhosis due to other causes.
CC Note=The gene represented in this entry may be involved in disease
CC pathogenesis.
CC -!- DISEASE: Gastric adenocarcinoma and proximal polyposis of the stomach
CC (GAPPS) [MIM:619182]: A familial gastric polyposis syndrome
CC characterized by autosomal dominant transmission of fundic gland
CC polyposis with occasional hyperplastic and adenomatous polyps, sparing
CC of the gastric antrum, and a significant risk of intestinal-type
CC gastric adenocarcinoma development. Colorectal polyposis is not
CC observed, and family history does not include colorectal cancer.
CC {ECO:0000269|PubMed:27087319, ECO:0000269|PubMed:27343414,
CC ECO:0000269|PubMed:33242120}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis.
CC -!- MISCELLANEOUS: APC mutations have led to some interesting observations.
CC (1) the great majority of the mutations found to date would result in
CC truncation of the APC product. (2) almost all the mutations have
CC occurred within the first half of the coding sequence, and somatic
CC mutations in colorectal tumors are further clustered in a particular
CC region, called MCR (mutation cluster region). (3) most identified point
CC mutations in the APC gene are transitions from cytosine to other
CC nucleotides. (4) the location of germline mutations tends to correlate
CC with the number of colorectal polyps in FAP1 patients. Inactivation of
CC both alleles of the APC gene seems to be required as an early event to
CC develop most adenomas and carcinomas in the colon and rectum as well as
CC some of those in the stomach.
CC -!- MISCELLANEOUS: [Isoform 1B]: Produced by alternative promoter usage.
CC {ECO:0000269|PubMed:19527921}.
CC -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Colon cancer gene variant databases Adenomatous
CC Polyposis Coli (APC); Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/APC";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/APCID118.html";
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DR EMBL; M73548; AAA60353.1; -; mRNA.
DR EMBL; M73548; AAA60354.1; -; mRNA.
DR EMBL; M74088; AAA03586.1; -; mRNA.
DR EMBL; AC008575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW49002.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW49007.1; -; Genomic_DNA.
DR EMBL; AK294544; BAH11802.1; -; mRNA.
DR EMBL; S78214; AAB21145.2; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS4107.1; -. [P25054-1]
DR PIR; A37261; RBHUAP.
DR RefSeq; NP_000029.2; NM_000038.5. [P25054-1]
DR RefSeq; NP_001120982.1; NM_001127510.2. [P25054-1]
DR RefSeq; NP_001120983.2; NM_001127511.2. [P25054-3]
DR PDB; 1DEB; X-ray; 2.40 A; A/B=2-55.
DR PDB; 1EMU; X-ray; 1.90 A; B=2034-2049.
DR PDB; 1JPP; X-ray; 3.10 A; C/D=1021-1035.
DR PDB; 1M5I; X-ray; 2.00 A; A=126-250.
DR PDB; 1T08; X-ray; 2.10 A; C=1484-1498.
DR PDB; 1TH1; X-ray; 2.50 A; C/D=1362-1540.
DR PDB; 1V18; X-ray; 2.10 A; B=1482-1528.
DR PDB; 2RQU; NMR; -; B=1578-1596.
DR PDB; 3AU3; X-ray; 2.10 A; A=396-732.
DR PDB; 3NMW; X-ray; 1.60 A; A/B=407-751.
DR PDB; 3NMX; X-ray; 2.30 A; A/B/C=407-751.
DR PDB; 3NMZ; X-ray; 3.01 A; A/B=303-739.
DR PDB; 3QHE; X-ray; 2.40 A; A/C=396-732.
DR PDB; 3RL7; X-ray; 2.30 A; G/H/I/J/K/L=2833-2843.
DR PDB; 3RL8; X-ray; 2.20 A; F=2833-2843.
DR PDB; 3T7U; X-ray; 2.90 A; A/B=407-775.
DR PDB; 4G69; X-ray; 2.00 A; B=2833-2843.
DR PDB; 4YJE; X-ray; 1.90 A; A=407-751.
DR PDB; 4YJL; X-ray; 2.10 A; A/B/C/D/E/F=407-751.
DR PDB; 4YK6; X-ray; 1.70 A; A=407-751.
DR PDB; 5B6G; X-ray; 1.99 A; A=407-751.
DR PDB; 5IZ6; X-ray; 2.15 A; A=407-751.
DR PDB; 5IZ8; X-ray; 3.06 A; A/B=407-751.
DR PDB; 5IZ9; X-ray; 2.93 A; A=407-751.
DR PDB; 5IZA; X-ray; 1.50 A; A=407-751.
DR PDB; 5Z8H; X-ray; 1.79 A; A=407-741.
DR PDBsum; 1DEB; -.
DR PDBsum; 1EMU; -.
DR PDBsum; 1JPP; -.
DR PDBsum; 1M5I; -.
DR PDBsum; 1T08; -.
DR PDBsum; 1TH1; -.
DR PDBsum; 1V18; -.
DR PDBsum; 2RQU; -.
DR PDBsum; 3AU3; -.
DR PDBsum; 3NMW; -.
DR PDBsum; 3NMX; -.
DR PDBsum; 3NMZ; -.
DR PDBsum; 3QHE; -.
DR PDBsum; 3RL7; -.
DR PDBsum; 3RL8; -.
DR PDBsum; 3T7U; -.
DR PDBsum; 4G69; -.
DR PDBsum; 4YJE; -.
DR PDBsum; 4YJL; -.
DR PDBsum; 4YK6; -.
DR PDBsum; 5B6G; -.
DR PDBsum; 5IZ6; -.
DR PDBsum; 5IZ8; -.
DR PDBsum; 5IZ9; -.
DR PDBsum; 5IZA; -.
DR PDBsum; 5Z8H; -.
DR BMRB; P25054; -.
DR SMR; P25054; -.
DR BioGRID; 106821; 318.
DR ComplexPortal; CPX-107; Beta-catenin destruction core complex, variant 5.
DR ComplexPortal; CPX-109; Beta-catenin destruction core complex, variant 1.
DR ComplexPortal; CPX-439; Beta-catenin destruction core complex, variant 3.
DR ComplexPortal; CPX-441; Beta-catenin destruction core complex, variant 7.
DR CORUM; P25054; -.
DR DIP; DIP-33556N; -.
DR IntAct; P25054; 207.
DR MINT; P25054; -.
DR STRING; 9606.ENSP00000257430; -.
DR BindingDB; P25054; -.
DR ChEMBL; CHEMBL3233; -.
DR GlyGen; P25054; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; P25054; -.
DR PhosphoSitePlus; P25054; -.
DR BioMuta; APC; -.
DR DMDM; 97535708; -.
DR EPD; P25054; -.
DR jPOST; P25054; -.
DR MassIVE; P25054; -.
DR MaxQB; P25054; -.
DR PaxDb; P25054; -.
DR PeptideAtlas; P25054; -.
DR PRIDE; P25054; -.
DR ProteomicsDB; 54247; -. [P25054-1]
DR ProteomicsDB; 54248; -. [P25054-2]
DR ProteomicsDB; 6428; -.
DR Antibodypedia; 1054; 761 antibodies from 44 providers.
DR DNASU; 324; -.
DR Ensembl; ENST00000257430.9; ENSP00000257430.4; ENSG00000134982.17. [P25054-1]
DR Ensembl; ENST00000508376.6; ENSP00000427089.2; ENSG00000134982.17. [P25054-1]
DR GeneID; 324; -.
DR KEGG; hsa:324; -.
DR MANE-Select; ENST00000257430.9; ENSP00000257430.4; NM_000038.6; NP_000029.2.
DR UCSC; uc003kpy.5; human. [P25054-1]
DR UCSC; uc063gan.1; human.
DR CTD; 324; -.
DR DisGeNET; 324; -.
DR GeneCards; APC; -.
DR GeneReviews; APC; -.
DR HGNC; HGNC:583; APC.
DR HPA; ENSG00000134982; Tissue enhanced (brain).
DR MalaCards; APC; -.
DR MIM; 114550; phenotype.
DR MIM; 135290; phenotype.
DR MIM; 155255; phenotype.
DR MIM; 175100; phenotype.
DR MIM; 611731; gene.
DR MIM; 613659; phenotype.
DR MIM; 619182; phenotype.
DR neXtProt; NX_P25054; -.
DR OpenTargets; ENSG00000134982; -.
DR Orphanet; 247806; APC-related attenuated familial adenomatous polyposis.
DR Orphanet; 3258; Cenani-Lenz syndrome.
DR Orphanet; 873; Desmoid tumor.
DR Orphanet; 261584; Familial adenomatous polyposis due to 5q22.2 microdeletion.
DR Orphanet; 79665; Gardner syndrome.
DR Orphanet; 314022; Gastric adenocarcinoma and proximal polyposis of the stomach.
DR Orphanet; 99818; Turcot syndrome with polyposis.
DR PharmGKB; PA24875; -.
DR VEuPathDB; HostDB:ENSG00000134982; -.
DR eggNOG; KOG2122; Eukaryota.
DR GeneTree; ENSGT00530000063749; -.
DR HOGENOM; CLU_001012_0_0_1; -.
DR InParanoid; P25054; -.
DR OMA; DHEKHSP; -.
DR OrthoDB; 31524at2759; -.
DR PhylomeDB; P25054; -.
DR TreeFam; TF106496; -.
DR BioCyc; MetaCyc:ENSG00000134982-MON; -.
DR PathwayCommons; P25054; -.
DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5339716; Signaling by GSK3beta mutants.
DR Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated.
DR Reactome; R-HSA-5467333; APC truncation mutants are not K63 polyubiquitinated.
DR Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
DR Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
DR Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR SignaLink; P25054; -.
DR SIGNOR; P25054; -.
DR BioGRID-ORCS; 324; 166 hits in 1084 CRISPR screens.
DR ChiTaRS; APC; human.
DR EvolutionaryTrace; P25054; -.
DR GeneWiki; Adenomatous_polyposis_coli; -.
DR GenomeRNAi; 324; -.
DR Pharos; P25054; Tchem.
DR PRO; PR:P25054; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P25054; protein.
DR Bgee; ENSG00000134982; Expressed in substantia nigra pars compacta and 205 other tissues.
DR ExpressionAtlas; P25054; baseline and differential.
DR Genevisible; P25054; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0016342; C:catenin complex; IDA:CACAO.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:1990909; C:Wnt signalosome; NAS:ParkinsonsUK-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR GO; GO:0070840; F:dynein complex binding; IPI:CAFA.
DR GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:CAFA.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:CAFA.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:MGI.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:CAFA.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IMP:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:MGI.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR DisProt; DP00519; -.
DR Gene3D; 1.25.10.10; -; 1.
DR IDEAL; IID00035; -.
DR InterPro; IPR026836; APC.
DR InterPro; IPR009240; APC_15aa_rpt.
DR InterPro; IPR009234; APC_basic_dom.
DR InterPro; IPR026831; APC_dom.
DR InterPro; IPR026818; Apc_fam.
DR InterPro; IPR032038; APC_N.
DR InterPro; IPR036149; APC_N_sf.
DR InterPro; IPR041257; APC_rep.
DR InterPro; IPR009223; APC_rpt.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR009232; EB1-bd.
DR InterPro; IPR009224; SAMP.
DR PANTHER; PTHR12607; PTHR12607; 1.
DR PANTHER; PTHR12607:SF11; PTHR12607:SF11; 1.
DR Pfam; PF05972; APC_15aa; 3.
DR Pfam; PF05956; APC_basic; 1.
DR Pfam; PF16689; APC_N_CC; 1.
DR Pfam; PF05923; APC_r; 7.
DR Pfam; PF18797; APC_rep; 1.
DR Pfam; PF00514; Arm; 2.
DR Pfam; PF05937; EB1_binding; 1.
DR Pfam; PF05924; SAMP; 3.
DR SMART; SM00185; ARM; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF58050; SSF58050; 1.
DR SUPFAM; SSF82931; SSF82931; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative promoter usage;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Membrane;
KW Microtubule; Phosphoprotein; Reference proteome; Repeat; Tumor suppressor;
KW Ubl conjugation; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..2843
FT /note="Adenomatous polyposis coli protein"
FT /id="PRO_0000064627"
FT REPEAT 453..495
FT /note="ARM 1"
FT REPEAT 505..547
FT /note="ARM 2"
FT REPEAT 548..591
FT /note="ARM 3"
FT REPEAT 592..638
FT /note="ARM 4"
FT REPEAT 639..683
FT /note="ARM 5"
FT REPEAT 684..725
FT /note="ARM 6"
FT REPEAT 726..767
FT /note="ARM 7"
FT REGION 239..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1337
FT /note="Responsible for down-regulation through a process
FT mediated by direct ubiquitination"
FT REGION 1099..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1893
FT /note="Highly charged"
FT REGION 1881..1950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1965..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2043..2072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2147..2635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2667..2714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2729..2843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..61
FT /evidence="ECO:0000255"
FT COILED 127..248
FT /evidence="ECO:0000255"
FT MOTIF 2803..2806
FT /note="Microtubule tip localization signal"
FT MOTIF 2841..2843
FT /note="PDZ-binding"
FT COMPBIAS 244..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1881..1895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1896..1938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1978..1995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2170..2191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2200..2225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2234..2249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2258..2426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2461..2501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2519..2533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2557..2580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2581..2596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2617..2635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2669..2686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2697..2711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2737..2813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2823..2843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 1038
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 1395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 1438
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 1774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1971
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 1973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 2088
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2093
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 2129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2151
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 2674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2679
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70478"
FT MOD_RES 2724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..45
FT /note="MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMK -> MYA
FT SLGSGPVAPLPASVPPSVLGSWSTGGSRSCVRQETKSPGGARTSGHWASVWQ (in
FT isoform 1B)"
FT /id="VSP_059027"
FT VAR_SEQ 217..244
FT /note="Missing (in isoform 1B)"
FT /id="VSP_059028"
FT VAR_SEQ 312..412
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1678319"
FT /id="VSP_004115"
FT VARIANT 99
FT /note="R -> W (in FAP1; unknown pathological significance;
FT dbSNP:rs139196838)"
FT /evidence="ECO:0000269|PubMed:7833149"
FT /id="VAR_009613"
FT VARIANT 171
FT /note="S -> I (in FAP1)"
FT /evidence="ECO:0000269|PubMed:8990002"
FT /id="VAR_005032"
FT VARIANT 414
FT /note="R -> C (in FAP1; dbSNP:rs137854567)"
FT /id="VAR_005033"
FT VARIANT 722
FT /note="S -> G (in FAP1)"
FT /evidence="ECO:0000269|PubMed:7833931"
FT /id="VAR_009614"
FT VARIANT 784
FT /note="S -> T (in FAP1)"
FT /id="VAR_005034"
FT VARIANT 817
FT /note="G -> C (in gastric cancer)"
FT /id="VAR_005035"
FT VARIANT 870
FT /note="P -> S (in dbSNP:rs33974176)"
FT /id="VAR_053976"
FT VARIANT 880
FT /note="I -> T (in colorectal carcinoma and gastric cancer;
FT from a patient with MMRCS; dbSNP:rs1400295986)"
FT /evidence="ECO:0000269|PubMed:9419979"
FT /id="VAR_005036"
FT VARIANT 890
FT /note="V -> I (in colorectal carcinoma; from a patient with
FT MMRCS; dbSNP:rs779998847)"
FT /evidence="ECO:0000269|PubMed:9419979"
FT /id="VAR_012975"
FT VARIANT 906
FT /note="S -> Y (in colorectal tumor)"
FT /id="VAR_005037"
FT VARIANT 911
FT /note="E -> G (in FAP1 and colorectal tumor)"
FT /id="VAR_005038"
FT VARIANT 942
FT /note="N -> D (in gastric cancer)"
FT /id="VAR_005039"
FT VARIANT 1027
FT /note="Y -> C (in colorectal tumor; dbSNP:rs869312784)"
FT /id="VAR_005040"
FT VARIANT 1057
FT /note="E -> G (found in a family whose members exhibit
FT gastrointestinal cancers and multiple pigmented cutaneous
FT lesions; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:9950360"
FT /id="VAR_009615"
FT VARIANT 1118
FT /note="N -> D (in dbSNP:rs140493115)"
FT /evidence="ECO:0000269|PubMed:1338764"
FT /id="VAR_005041"
FT VARIANT 1120
FT /note="G -> E (in gastric cancer; dbSNP:rs28933379)"
FT /id="VAR_005042"
FT VARIANT 1171
FT /note="R -> C (in dbSNP:rs201830995)"
FT /evidence="ECO:0000269|PubMed:9950360"
FT /id="VAR_008992"
FT VARIANT 1171
FT /note="R -> H (in gastric cancer; dbSNP:rs372481703)"
FT /id="VAR_005043"
FT VARIANT 1176
FT /note="P -> L (in FAP1)"
FT /id="VAR_005044"
FT VARIANT 1184
FT /note="A -> P (in FAP1)"
FT /evidence="ECO:0000269|PubMed:10470088"
FT /id="VAR_009616"
FT VARIANT 1197
FT /note="F -> S (in gastric cancer)"
FT /id="VAR_005045"
FT VARIANT 1254
FT /note="I -> F (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035794"
FT VARIANT 1259
FT /note="I -> T (in gastric cancer)"
FT /id="VAR_005046"
FT VARIANT 1292
FT /note="T -> M (in FAP1; unknown pathological significance;
FT dbSNP:rs371113837)"
FT /evidence="ECO:0000269|PubMed:1338764"
FT /id="VAR_005047"
FT VARIANT 1296
FT /note="A -> V (in MDB; sporadic; dbSNP:rs1291513037)"
FT /evidence="ECO:0000269|PubMed:10666372"
FT /id="VAR_017653"
FT VARIANT 1304
FT /note="I -> V (in dbSNP:rs770157475)"
FT /evidence="ECO:0000269|PubMed:1338764"
FT /id="VAR_005048"
FT VARIANT 1307
FT /note="I -> K (may be associated with increased risk of
FT colon and breast cancer; dbSNP:rs1801155)"
FT /evidence="ECO:0000269|PubMed:9724771,
FT ECO:0000269|PubMed:9731522, ECO:0000269|PubMed:9731533,
FT ECO:0000269|PubMed:9973276"
FT /id="VAR_005049"
FT VARIANT 1312
FT /note="G -> E (in gastric cancer)"
FT /id="VAR_005050"
FT VARIANT 1313
FT /note="T -> A (in FAP1 and colorectal tumor;
FT dbSNP:rs863225349)"
FT /id="VAR_005051"
FT VARIANT 1317
FT /note="E -> Q (may contribute to colorectal tumor
FT development; dbSNP:rs1801166)"
FT /evidence="ECO:0000269|PubMed:9724771"
FT /id="VAR_009617"
FT VARIANT 1326
FT /note="V -> A (in gastric cancer)"
FT /id="VAR_005052"
FT VARIANT 1348
FT /note="R -> W (in FAP1)"
FT /evidence="ECO:0000269|PubMed:1338764"
FT /id="VAR_005053"
FT VARIANT 1395
FT /note="S -> C (in hepatoblastoma; dbSNP:rs137854578)"
FT /evidence="ECO:0000269|PubMed:8764128"
FT /id="VAR_065133"
FT VARIANT 1422
FT /note="D -> H (in colorectal tumor)"
FT /id="VAR_005054"
FT VARIANT 1472
FT /note="V -> I (in MDB; sporadic; dbSNP:rs878853445)"
FT /evidence="ECO:0000269|PubMed:10666372"
FT /id="VAR_017654"
FT VARIANT 1495
FT /note="S -> G (in MDB; sporadic)"
FT /evidence="ECO:0000269|PubMed:10666372"
FT /id="VAR_017655"
FT VARIANT 1496
FT /note="T -> S (in dbSNP:rs2229996)"
FT /id="VAR_020141"
FT VARIANT 1508
FT /note="A -> V (in colorectal carcinoma from a patient with
FT MMRCS)"
FT /evidence="ECO:0000269|PubMed:9419979"
FT /id="VAR_012976"
FT VARIANT 1822
FT /note="V -> D (in dbSNP:rs459552)"
FT /evidence="ECO:0000269|PubMed:1651562,
FT ECO:0000269|PubMed:1678319, ECO:0000269|PubMed:9950360,
FT ECO:0000269|Ref.5"
FT /id="VAR_008993"
FT VARIANT 1882
FT /note="R -> T (in dbSNP:rs34157245)"
FT /id="VAR_053977"
FT VARIANT 1973
FT /note="S -> T (in dbSNP:rs4987109)"
FT /id="VAR_020142"
FT VARIANT 2499
FT /note="V -> L (in dbSNP:rs33941929)"
FT /id="VAR_053978"
FT VARIANT 2502
FT /note="G -> S (in dbSNP:rs2229995)"
FT /evidence="ECO:0000269|PubMed:1338764"
FT /id="VAR_005055"
FT VARIANT 2621
FT /note="S -> C (in FAP1; unknown pathological significance;
FT dbSNP:rs72541816)"
FT /evidence="ECO:0000269|PubMed:1316610"
FT /id="VAR_005056"
FT VARIANT 2738
FT /note="I -> T (in dbSNP:rs863224552)"
FT /evidence="ECO:0000269|PubMed:9950360"
FT /id="VAR_008994"
FT VARIANT 2839
FT /note="L -> F (in FAP1; dbSNP:rs876658156)"
FT /id="VAR_005057"
FT MUTAGEN 516
FT /note="K->E: Impairs interaction with KHDRBS1."
FT /evidence="ECO:0000269|PubMed:22000517"
FT MUTAGEN 549
FT /note="R->E: Impairs interaction with KHDRBS1."
FT /evidence="ECO:0000269|PubMed:22000517"
FT MUTAGEN 2841
FT /note="T->L: Loss of interaction with SCRIB."
FT /evidence="ECO:0000269|PubMed:16611247"
FT MUTAGEN 2843
FT /note="V->Q: Loss of interaction with SCRIB."
FT /evidence="ECO:0000269|PubMed:16611247"
FT CONFLICT 184
FT /note="M -> L (in Ref. 1; AAA60353/AAA60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="S -> N (in Ref. 1; AAA60353/AAA60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 1309
FT /note="E -> G (in Ref. 1; AAA60353/AAA60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 1325..1331
FT /note="AVSQHPR -> SSVHSTLE (in Ref. 1; AAA60353/AAA60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 1355
FT /note="S -> P (in Ref. 1; AAA60353/AAA60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 1591
FT /note="A -> G (in Ref. 1; AAA60353/AAA60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 2723
FT /note="N -> T (in Ref. 1; AAA60353/AAA60354)"
FT /evidence="ECO:0000305"
FT CONFLICT 2755
FT /note="S -> P (in Ref. 1; AAA60353/AAA60354)"
FT /evidence="ECO:0000305"
FT HELIX 6..53
FT /evidence="ECO:0007829|PDB:1DEB"
FT HELIX 132..169
FT /evidence="ECO:0007829|PDB:1M5I"
FT HELIX 180..204
FT /evidence="ECO:0007829|PDB:1M5I"
FT HELIX 208..238
FT /evidence="ECO:0007829|PDB:1M5I"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:3NMZ"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:3NMZ"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:3NMZ"
FT HELIX 377..393
FT /evidence="ECO:0007829|PDB:3NMZ"
FT HELIX 407..426
FT /evidence="ECO:0007829|PDB:5IZA"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:3AU3"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 460..468
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 471..486
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 492..509
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 513..521
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 523..531
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 538..552
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 557..565
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 568..578
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 582..596
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 600..607
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 612..619
FT /evidence="ECO:0007829|PDB:5IZA"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:3NMW"
FT HELIX 629..646
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 650..658
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 661..668
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 674..687
FT /evidence="ECO:0007829|PDB:5IZA"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:5IZ8"
FT HELIX 692..700
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 703..708
FT /evidence="ECO:0007829|PDB:5IZA"
FT TURN 709..712
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 716..731
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:5IZA"
FT HELIX 739..742
FT /evidence="ECO:0007829|PDB:5IZA"
FT TURN 1027..1030
FT /evidence="ECO:0007829|PDB:1JPP"
FT HELIX 1470..1479
FT /evidence="ECO:0007829|PDB:1TH1"
FT HELIX 1520..1524
FT /evidence="ECO:0007829|PDB:1V18"
FT HELIX 2036..2045
FT /evidence="ECO:0007829|PDB:1EMU"
FT STRAND 2840..2842
FT /evidence="ECO:0007829|PDB:3RL7"
SQ 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
