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 17-JUN-2020, entry version 165. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 eggNOG; ENOG410XR2V; LUCA. DR InParanoid; P70478; -. DR KO; K02085; -. 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:0005623; C:cell; IEA:GOC. 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; ISO:RGD. DR GO; GO:0005874; C:microtubule; IDA:RGD. DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. 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: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:0007050; P:cell cycle arrest; ISS:UniProtKB. 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; 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: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: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: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:0042493; P:response to drug; 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 1864..1891 FT /note="Highly charged" 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 1..728 FT /note="Leu-rich" FT COMPBIAS 739..2831 FT /note="Ser-rich" FT COMPBIAS 1130..1155 FT /note="Asp/Glu-rich (acidic)" FT COMPBIAS 1556..1575 FT /note="Asp/Glu-rich (acidic)" 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:0000244|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:0000244|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:0000244|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:0000244|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:0000244|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:0000244|PubMed:22673903" FT MOD_RES 1714 FT /note="Phosphoserine" FT /evidence="ECO:0000244|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:0000244|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:0000244|PubMed:22673903" FT MOD_RES 2092 FT /note="Phosphoserine" FT /evidence="ECO:0000244|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:0000244|PubMed:22673903" FT MOD_RES 2130 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:22673903" FT MOD_RES 2132 FT /note="Phosphoserine" FT /evidence="ECO:0000244|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:0000244|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 //