APC_RAT
ID APC_RAT Reviewed; 2842 AA.
AC P70478;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 23-FEB-2022, entry version 172.
DE RecName: Full=Adenomatous polyposis coli protein;
DE Short=Protein APC;
GN Name=Apc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344/N; TISSUE=Brain;
RX PubMed=8563176; DOI=10.1007/bf00354300;
RA Toyota M., Ushijima T., Kakiuchi H., Watanabe M., Imai K., Yachi A.,
RA Sugimura T., Nagao M.;
RT "cDNA cloning of the rat APC gene and assignment to chromosome 18.";
RL Mamm. Genome 6:746-748(1995).
RN [2]
RP MUTAGENESIS.
RC STRAIN=Fischer 344/N, and Sprague-Dawley;
RX PubMed=7846077; DOI=10.1073/pnas.92.3.910;
RA Kakiuchi H., Watanabe M., Ushijima T., Toyota M., Imai K., Weisburger J.H.,
RA Sugimura T., Nagao M.;
RT "Specific 5'-GGGA-3'-->5'-GGA-3' mutation of the Apc gene in rat colon
RT tumors induced by 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:910-914(1995).
RN [3]
RP IDENTIFICATION IN A COMPLEX WITH MACF1; CTNNB1; AXIN1 AND GSK3B.
RX PubMed=16815997; DOI=10.1101/gad.1411206;
RA Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
RT "The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt
RT signaling pathway.";
RL Genes Dev. 20:1933-1945(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742; SER-778; SER-985;
RP SER-1040; SER-1368; SER-1565; SER-1859; SER-2087; SER-2092; SER-2129;
RP SER-2130; SER-2132 AND SER-2710, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250|UniProtKB:P25054,
CC ECO:0000250|UniProtKB:Q61315}.
CC -!- SUBUNIT: Forms homooligomers and heterooligomers with APC2. Interacts
CC with DIAPH1 and DIAPH2. Interacts with PDZ domains of DLG1 and DLG3.
CC Associates with catenins. Binds axin. Interacts with ARHGEF4 (via N-
CC terminus). Interacts with MAPRE1 (via C-terminus); probably required
CC for APC targeting to the growing microtubule plus ends. Interacts with
CC MAPRE2 and MAPRE3 (via C-terminus). Found in a complex consisting of
CC ARHGEF4, APC and CTNNB1. Interacts with SCRIB; may mediate APC
CC targeting to adherens junctions of epithelial cells. Interacts with
CC SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3
CC domain). Interacts at the cell membrane with AMER1 and AMER2 (via ARM
CC repeats) (By similarity). Found in a complex composed of MACF1, APC,
CC AXIN1, CTNNB1 and GSK3B. Interacts with KHDRBS1 (By similarity). 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') (By similarity).
CC {ECO:0000250|UniProtKB:P25054, ECO:0000250|UniProtKB:Q61315,
CC ECO:0000269|PubMed:16815997}.
CC -!- INTERACTION:
CC P70478; P31016: Dlg4; NbExp=2; IntAct=EBI-631663, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P25054}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P25054}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P25054}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P25054}. Cytoplasm
CC {ECO:0000250|UniProtKB:P25054}. Cell membrane
CC {ECO:0000250|UniProtKB:P25054}. Note=Associated with the microtubule
CC network at the growing distal tip of microtubules. Accumulates in the
CC lamellipodium and ruffle membrane in response to hepatocyte growth
CC factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway
CC controls localization of the phosphorylated form to the cell membrane.
CC {ECO:0000250|UniProtKB:P25054}.
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. {ECO:0000250}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC) family.
CC {ECO:0000305}.
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DR EMBL; D38629; BAA07609.1; -; mRNA.
DR RefSeq; NP_036631.1; NM_012499.1.
DR SMR; P70478; -.
DR BioGRID; 246393; 6.
DR CORUM; P70478; -.
DR IntAct; P70478; 3.
DR STRING; 10116.ENSRNOP00000027691; -.
DR iPTMnet; P70478; -.
DR PhosphoSitePlus; P70478; -.
DR PaxDb; P70478; -.
DR PRIDE; P70478; -.
DR GeneID; 24205; -.
DR KEGG; rno:24205; -.
DR UCSC; RGD:2123; rat.
DR CTD; 324; -.
DR RGD; 2123; Apc.
DR eggNOG; KOG2122; Eukaryota.
DR InParanoid; P70478; -.
DR OrthoDB; 31524at2759; -.
DR PhylomeDB; P70478; -.
DR Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-RNO-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-RNO-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
DR PRO; PR:P70478; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0016342; C:catenin complex; ISO:RGD.
DR GO; GO:0070852; C:cell body fiber; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; IDA:RGD.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0031253; C:cell projection membrane; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0034750; C:Scrib-APC-beta-catenin complex; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:RGD.
DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0019887; F:protein kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR GO; GO:0009798; P:axis specification; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:RGD.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IDA:RGD.
DR GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISO:RGD.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; ISO:RGD.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0042483; P:negative regulation of odontogenesis; ISO:RGD.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IMP:RGD.
DR GO; GO:0031016; P:pancreas development; IEP:RGD.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR GO; GO:0051781; P:positive regulation of cell division; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; ISO:RGD.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0009954; P:proximal/distal pattern formation; ISO:RGD.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:2000211; P:regulation of glutamate metabolic process; IDA:RGD.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; ISO:RGD.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0097305; P:response to alcohol; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR Gene3D; 1.25.10.10; -; 1.
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 Acetylation; Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat; Tumor suppressor; Ubl conjugation;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT CHAIN 2..2842
FT /note="Adenomatous polyposis coli protein"
FT /id="PRO_0000064629"
FT REPEAT 451..493
FT /note="ARM 1"
FT REPEAT 503..545
FT /note="ARM 2"
FT REPEAT 546..589
FT /note="ARM 3"
FT REPEAT 590..636
FT /note="ARM 4"
FT REPEAT 637..681
FT /note="ARM 5"
FT REPEAT 682..723
FT /note="ARM 6"
FT REPEAT 724..765
FT /note="ARM 7"
FT REGION 238..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1398..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1584..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1864..1891
FT /note="Highly charged"
FT REGION 1963..2010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2043..2067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2148..2173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2234..2641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2664..2842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..62
FT /evidence="ECO:0000255"
FT COILED 125..260
FT /evidence="ECO:0000255"
FT MOTIF 2802..2805
FT /note="Microtubule tip localization signal"
FT MOTIF 2840..2842
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 242..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1894..1916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..1984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2043..2061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2155..2173
FT /note="Basic and acidic 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 2261..2426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2461..2499
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..2639
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..2730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2756..2812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2822..2842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 1435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 1772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1862
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 1969
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 1971
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 2087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61315"
FT MOD_RES 2129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2679
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MOD_RES 2788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25054"
FT MUTAGEN 523
FT /note="C->R: In an IQ-induced colon tumor."
FT /evidence="ECO:0000269|PubMed:7846077"
SQ SEQUENCE 2842 AA; 310533 MW; 3CBB2EA8A34E8F47 CRC64;
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTELETE ASNMKEVLKQ LQGSIEDETM
TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRA
FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT
DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA
ERSSQSKHET ASHEAERQLE GQGVAESNLA TSGSGQSSAA RVDHETAGVL SSSGTHSAPR
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG
NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE
WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD
CEMHGLTDDH YSVTLRRYAG MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ
VIASVLRNLS WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH RQILRENNCL
QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG AVSMLKNLIH SKHKMIAMGS
AAALRNLMAN RPAKYKDANI MSPGSSLPSL HVRKQKALEA ELDAQHLSET FDNIDNLSPK
ASHRSKQRHK QNLYGDYVFD ASRHDDNRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD
SSRSEKDRSL ERERGIGLST YHSATENPGT SSKRGLQLSA TAAQIAKVME EVSALHTSQD
DRSPASAAEL HCVAEERTAA RRSSASHTHP NTHNFAKSES SNRTCSMPYA KVEYKRSSND
SLNSVTSSDG YGKRGQMKPS VESYSEDDEG KFCSYGQYPA DLAHKIHSAN HMDDNGGELD
TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQSRSQN TNFPVYSENT
DDKHLKFQQH FGQQECVSPY RSRGTNGSET NRMGSSHAVN QNVNQSLCQE DDYEDDKPTN
YSERYSEEEQ HEEEERPTNY SIKYNEEKHH VDQPIDYSLK YATDISSSQK PSFSFSKTPS
VQGTKTEHNS PSSEAASAPS SNAKRQSQLH PSSAQRNGQT PKGTACKVPS INQETMQTYC
VEDTPICFSR CSSLSSLSSA EDEIGCDQTT QEADSANTLQ IAEIKENDVT RSAQDPASDV
PAVSQSTRTK PSRLQASGLA SESARHKAVE FSSGAKSPSK SGAQTPKSPP EHYVQETPLV
FSRCTSVSSL DSFESRSIAS SVQSEPCSGM VSGIVSPSDL PDSPGQTMPP SRSKTPPPPP
PPQPVQTKRE VPKTKVPAAE QREGGPKQTA VSAAVQRVQV LPDADTLLHF ATESTPDGFS
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETEPEQ PEESNENQDK EVEKPDSEKD
LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPSQS
RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELAAG DGVRASVQSG
EFEKRDTIPT EGRSTDEAQR GKVSSIAIPD LDGSKAEEGD ILAECINSAL PKGRSHKPFR
VKKIMDQVQQ ASMTSSGTNK NQIDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
ETFSDNKDSK KQSLKNNPKD LNDKLPDNED RVRGGFTFDS PHHYAPIEGT PYCFSRNDSL
SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCHTEPSS SQQSARKAQA STKHPVNRGP
SKPLLQEQPT FPQSSKDVPD RGAATDEKLQ NFAIENTPVC FSRNSSLSSL SDVDQENNNN
EETGPVRDAE PANAQGQPGK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLRE
CISSAMPKKR RPSRLKGEGE WQSPRKVGSV LAEDLTLDLK DIQRPESEHG LSPDSENFDW
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GVSLGSPFHL TPDQEEKPFT
SHKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLQTN
MPSISRGRTM IHIPGVRNSS SSTSPVSKKG PPLKTPASKS PSEGPVATTS PRGTKPAVKS
ELSPITRQTS HISGSNKGPS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISTPN
KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLSK QTGLSKNASS IPRSESASKG
LNQMNNSNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP TLRRKLEESA
SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYSDG
RPSKRHDIAR SHSESPSRLP VNRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES
SEKAKSEDEK HVNSVPGPRQ MKENQVPTKG TWRKIKESEI SPTNTVSQTT SSGAASGAES
KTLIYQMAPA VSRTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSISEKG NPSIKDSKDT
QGKQSVGSGS PVQTVGLENR LNSFIQVEAP EQKGTETKAG QGSPAPVAET GETCMAERTP
FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR PSQIPTPVGS STKKRDSKTD
STESSGAQSP KRHSGSYLVT SV
