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P25054

- APC_HUMAN

UniProt

P25054 - APC_HUMAN

Protein

Adenomatous polyposis coli protein

Gene

APC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 191 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      Previous versions | rss
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    Functioni

    Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.5 Publications

    GO - Molecular functioni

    1. beta-catenin binding Source: UniProtKB
    2. gamma-catenin binding Source: BHF-UCL
    3. microtubule binding Source: UniProtKB
    4. microtubule plus-end binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. protein kinase regulator activity Source: UniProtKB

    GO - Biological processi

    1. anterior/posterior pattern specification Source: Ensembl
    2. apoptotic process Source: Reactome
    3. axis specification Source: Ensembl
    4. axonogenesis Source: Ensembl
    5. canonical Wnt signaling pathway Source: UniProtKB
    6. canonical Wnt signaling pathway involved in negative regulation of apoptotic process Source: Ensembl
    7. canonical Wnt signaling pathway involved in positive regulation of apoptotic process Source: Ensembl
    8. cell adhesion Source: UniProtKB
    9. cell cycle arrest Source: UniProtKB
    10. cell migration Source: UniProtKB
    11. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    12. cellular response to DNA damage stimulus Source: UniProtKB
    13. chromosome organization Source: Ensembl
    14. cytoplasmic microtubule organization Source: Ensembl
    15. dorsal/ventral pattern formation Source: Ensembl
    16. hair follicle development Source: Ensembl
    17. kidney development Source: Ensembl
    18. metaphase/anaphase transition of mitotic cell cycle Source: Ensembl
    19. mitotic cytokinesis Source: MGI
    20. mitotic spindle assembly checkpoint Source: MGI
    21. muscle cell cellular homeostasis Source: Ensembl
    22. negative regulation of canonical Wnt signaling pathway Source: MGI
    23. negative regulation of cell proliferation Source: UniProtKB
    24. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    25. negative regulation of epithelial cell proliferation involved in prostate gland development Source: Ensembl
    26. negative regulation of MAPK cascade Source: Ensembl
    27. negative regulation of microtubule depolymerization Source: UniProtKB
    28. negative regulation of odontogenesis Source: Ensembl
    29. positive regulation of apoptotic process Source: MGI
    30. positive regulation of cell adhesion Source: Ensembl
    31. positive regulation of cell division Source: Ensembl
    32. positive regulation of cell migration Source: MGI
    33. positive regulation of epithelial cell differentiation Source: Ensembl
    34. positive regulation of microtubule polymerization Source: Ensembl
    35. positive regulation of protein catabolic process Source: BHF-UCL
    36. positive regulation of pseudopodium assembly Source: MGI
    37. protein complex assembly Source: UniProtKB
    38. proximal/distal pattern formation Source: Ensembl
    39. regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
    40. regulation of microtubule-based process Source: UniProtKB
    41. regulation of nitrogen compound metabolic process Source: Ensembl
    42. regulation of osteoblast differentiation Source: Ensembl
    43. regulation of osteoclast differentiation Source: Ensembl
    44. retina development in camera-type eye Source: Ensembl
    45. somatic stem cell maintenance Source: Ensembl
    46. T cell differentiation in thymus Source: Ensembl
    47. thymus development Source: Ensembl
    48. tight junction assembly Source: UniProtKB

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000134982-MONOMER.
    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    SignaLinkiP25054.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenomatous polyposis coli protein
    Short name:
    Protein APC
    Alternative name(s):
    Deleted in polyposis 2.5
    Gene namesi
    Name:APC
    Synonyms:DP2.5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:583. APC.

    Subcellular locationi

    Cell junctionadherens junction. Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle membrane. Cytoplasm. Cell membrane
    Note: Associated with the microtubule network at the growing distal tip of microtubules. Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane.

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB-SubCell
    2. axonal growth cone Source: Ensembl
    3. beta-catenin destruction complex Source: UniProtKB
    4. centrosome Source: UniProtKB
    5. cytoplasm Source: UniProtKB
    6. cytoplasmic microtubule Source: Ensembl
    7. cytosol Source: Reactome
    8. kinetochore Source: UniProtKB
    9. lamellipodium Source: UniProtKB
    10. lateral plasma membrane Source: MGI
    11. microtubule plus-end Source: Ensembl
    12. nucleus Source: UniProtKB
    13. plasma membrane Source: UniProtKB
    14. ruffle membrane Source: UniProtKB
    15. tight junction Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Familial adenomatous polyposis (FAP) [MIM:175100]: A cancer predisposition syndrome characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991R → W in FAP; unknown pathological significance. 1 Publication
    VAR_009613
    Natural varianti171 – 1711S → I in FAP. 1 Publication
    VAR_005032
    Natural varianti414 – 4141R → C in FAP.
    Corresponds to variant rs137854567 [ dbSNP | Ensembl ].
    VAR_005033
    Natural varianti722 – 7221S → G in FAP. 1 Publication
    VAR_009614
    Natural varianti784 – 7841S → T in FAP.
    VAR_005034
    Natural varianti911 – 9111E → G in FAP and colorectal tumor.
    VAR_005038
    Natural varianti1057 – 10571E → G in non-FAP; unknown pathological significance. 1 Publication
    VAR_009615
    Natural varianti1176 – 11761P → L in FAP.
    VAR_005044
    Natural varianti1184 – 11841A → P in FAP. 1 Publication
    VAR_009616
    Natural varianti1313 – 13131T → A in FAP and colorectal tumor.
    VAR_005051
    Natural varianti1348 – 13481R → W in FAP. 1 Publication
    VAR_005053
    Natural varianti2621 – 26211S → C in FAP.
    Corresponds to variant rs72541816 [ dbSNP | Ensembl ].
    VAR_005056
    Natural varianti2839 – 28391L → F in FAP.
    VAR_005057
    Hereditary desmoid disease (HDD) [MIM:135290]: Autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.1 Publication
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1296 – 12961A → V in MDB; sporadic. 1 Publication
    VAR_017653
    Natural varianti1472 – 14721V → I in MDB; sporadic. 1 Publication
    VAR_017654
    Natural varianti1495 – 14951S → G in MDB; sporadic. 1 Publication
    VAR_017655
    Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: An autosomal recessive, rare, childhood cancer predisposition syndrome encompassing a broad tumor spectrum. This includes hematological malignancies, central nervous system tumors, Lynch syndrome-associated malignancies such as colorectal tumors as well as multiple intestinal polyps, embryonic tumors and rhabdomyosarcoma. Multiple cafe-au-lait macules, a feature reminiscent of neurofibromatosis type 1, are often found as first manifestation of the underlying cancer. Areas of skin hypopigmentation have also been reported in MMRCS patients.1 Publication
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti880 – 8801I → T in colorectal carcinoma and gastric cancer; from a patient with MMRCS. 1 Publication
    VAR_005036
    Natural varianti890 – 8901V → I in colorectal carcinoma; from a patient with MMRCS. 1 Publication
    VAR_012975
    Natural varianti1508 – 15081A → V in colorectal carcinoma from a patient with MMRCS. 1 Publication
    VAR_012976
    Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes.
    Note: The gene represented in this entry may be involved in disease pathogenesis.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2841 – 28411T → L: Loss of interaction with SCRIB. 1 Publication
    Mutagenesisi2843 – 28431V → Q: Loss of interaction with SCRIB. 1 Publication

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi114550. phenotype.
    135290. phenotype.
    155255. phenotype.
    175100. phenotype.
    276300. phenotype.
    613659. phenotype.
    Orphaneti247806. APC-related attenuated familial adenomatous polyposis.
    873. Desmoid tumor.
    261584. Familial adenomatous polyposis due to 5q22.2 microdeletion.
    79665. Gardner syndrome.
    99818. Turcot syndrome with polyposis.
    PharmGKBiPA24875.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 28432842Adenomatous polyposis coli proteinPRO_0000064627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei744 – 7441Phosphoserine1 Publication
    Modified residuei780 – 7801Phosphoserine2 Publications
    Modified residuei1042 – 10421Phosphoserine1 Publication
    Modified residuei1360 – 13601Phosphoserine1 Publication
    Modified residuei1861 – 18611Phosphoserine2 Publications
    Modified residuei1863 – 18631Phosphoserine2 Publications
    Modified residuei1864 – 18641Phosphoserine2 Publications
    Modified residuei2151 – 21511Phosphothreonine1 Publication
    Modified residuei2260 – 22601Phosphoserine1 Publication
    Modified residuei2270 – 22701Phosphoserine1 Publication
    Modified residuei2283 – 22831Phosphoserine1 Publication
    Modified residuei2473 – 24731Phosphoserine1 Publication
    Modified residuei2535 – 25351Phosphoserine1 Publication
    Modified residuei2671 – 26711Phosphoserine2 Publications
    Modified residuei2674 – 26741Phosphoserine1 Publication
    Modified residuei2679 – 26791Phosphothreonine1 Publication
    Modified residuei2789 – 27891Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by GSK3B.4 Publications
    Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP25054.
    PaxDbiP25054.
    PRIDEiP25054.

    PTM databases

    PhosphoSiteiP25054.

    Expressioni

    Tissue specificityi

    Expressed in a variety of tissues.

    Gene expression databases

    ArrayExpressiP25054.
    BgeeiP25054.
    CleanExiHS_APC.
    GenevestigatoriP25054.

    Organism-specific databases

    HPAiCAB025994.
    HPA013349.

    Interactioni

    Subunit structurei

    Forms homooligomers and heterooligomers with APC2. Interacts with DIAPH1 and DIAPH2 By similarity. Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with ARHGEF4 (via N-terminus). Interacts with MAPRE1 (via C-terminus); probably required for APC targeting to the growing microtubule plus ends. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells. Interacts with SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3 domain). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Interacts at the cell membrane with AMER1 and AMER2 (via ARM repeats).By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AMER3Q8N9448EBI-727707,EBI-8869590
    CSNK1EP496748EBI-727707,EBI-749343
    CTNNA1P352212EBI-727707,EBI-701918
    CTNNB1P3522210EBI-727707,EBI-491549
    Ctnnb1Q022488EBI-727707,EBI-397872From a different organism.
    DVL1O146406EBI-727707,EBI-723489
    DVL1P1P547922EBI-727707,EBI-7848109
    JUPP149232EBI-727707,EBI-702484
    MAPRE1Q156914EBI-727707,EBI-1004115
    SCRIBQ141604EBI-727707,EBI-357345

    Protein-protein interaction databases

    BioGridi106821. 131 interactions.
    DIPiDIP-33556N.
    IntActiP25054. 122 interactions.
    MINTiMINT-88204.
    STRINGi9606.ENSP00000257430.

    Structurei

    Secondary structure

    1
    2843
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 5348
    Helixi132 – 16938
    Helixi180 – 20425
    Helixi208 – 23831
    Helixi328 – 33811
    Helixi343 – 3508
    Helixi353 – 3608
    Helixi377 – 39317
    Helixi407 – 42519
    Beta strandi429 – 4313
    Helixi433 – 4353
    Helixi441 – 4444
    Helixi446 – 45712
    Helixi460 – 4689
    Helixi471 – 48616
    Helixi492 – 50817
    Helixi513 – 5219
    Helixi523 – 5319
    Helixi532 – 5343
    Helixi538 – 55215
    Helixi557 – 5659
    Helixi568 – 57811
    Helixi582 – 59615
    Helixi600 – 6089
    Helixi612 – 6198
    Beta strandi625 – 6273
    Helixi630 – 64617
    Helixi650 – 6578
    Turni658 – 6603
    Helixi661 – 6688
    Helixi674 – 68714
    Helixi692 – 7009
    Helixi703 – 7086
    Turni709 – 7124
    Helixi716 – 73015
    Helixi735 – 7373
    Turni1027 – 10304
    Helixi1470 – 147910
    Helixi1520 – 15245
    Helixi2036 – 204510
    Beta strandi2840 – 28423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DEBX-ray2.40A/B2-55[»]
    1EMUX-ray1.90B2034-2049[»]
    1JPPX-ray3.10C/D1021-1035[»]
    1M5IX-ray2.00A126-250[»]
    1T08X-ray2.10C1484-1498[»]
    1TH1X-ray2.50C/D1362-1540[»]
    1V18X-ray2.10B1482-1528[»]
    2RQUNMR-B1578-1596[»]
    3AU3X-ray2.10A396-732[»]
    3NMWX-ray1.60A/B407-751[»]
    3NMXX-ray2.30A/B/C407-751[»]
    3NMZX-ray3.01A/B303-739[»]
    3QHEX-ray2.40A/C396-732[»]
    3RL7X-ray2.30G/H/I/J/K/L2833-2843[»]
    3RL8X-ray2.20F2833-2843[»]
    3T7UX-ray2.90A/B407-775[»]
    4G69X-ray2.00B2833-2843[»]
    DisProtiDP00519.
    ProteinModelPortaliP25054.
    SMRiP25054. Positions 2-55, 130-239, 326-736, 1485-1528.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25054.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati453 – 49543ARM 1Add
    BLAST
    Repeati505 – 54743ARM 2Add
    BLAST
    Repeati548 – 59144ARM 3Add
    BLAST
    Repeati592 – 63847ARM 4Add
    BLAST
    Repeati639 – 68345ARM 5Add
    BLAST
    Repeati684 – 72542ARM 6Add
    BLAST
    Repeati726 – 76742ARM 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni960 – 1337378Responsible for down-regulation through a process mediated by direct ubiquitinationAdd
    BLAST
    Regioni1866 – 189328Highly chargedAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2 – 6160Sequence AnalysisAdd
    BLAST
    Coiled coili127 – 248122Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2803 – 28064Microtubule tip localization signal
    Motifi2841 – 28433PDZ-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 730730Leu-richAdd
    BLAST
    Compositional biasi731 – 28322102Ser-richAdd
    BLAST
    Compositional biasi1131 – 115626Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi1558 – 157720Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.By similarity

    Sequence similaritiesi

    Contains 7 ARM repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG259696.
    HOVERGENiHBG004264.
    InParanoidiP25054.
    KOiK02085.
    OMAiIEDCPIN.
    PhylomeDBiP25054.
    TreeFamiTF106496.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    InterProiIPR026836. APC.
    IPR009240. APC_15aa_rpt.
    IPR009234. APC_basic_dom.
    IPR009223. APC_Cys-rich_rpt.
    IPR026831. APC_dom.
    IPR026818. Apc_fam.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR009232. EB1-bd.
    IPR009224. SAMP.
    [Graphical view]
    PANTHERiPTHR12607. PTHR12607. 1 hit.
    PTHR12607:SF11. PTHR12607:SF11. 1 hit.
    PfamiPF05972. APC_15aa. 4 hits.
    PF05956. APC_basic. 1 hit.
    PF05923. APC_crr. 7 hits.
    PF00514. Arm. 3 hits.
    PF05937. EB1_binding. 1 hit.
    PF05924. SAMP. 3 hits.
    PF11414. Suppressor_APC. 1 hit.
    [Graphical view]
    SMARTiSM00185. ARM. 6 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50176. ARM_REPEAT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P25054-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ     50
    LQGSIEDEAM ASSGQIDLLE RLKELNLDSS NFPGVKLRSK MSLRSYGSRE 100
    GSVSSRSGEC SPVPMGSFPR RGFVNGSRES TGYLEELEKE RSLLLADLDK 150
    EEKEKDWYYA QLQNLTKRID SLPLTENFSL QTDMTRRQLE YEARQIRVAM 200
    EEQLGTCQDM EKRAQRRIAR IQQIEKDILR IRQLLQSQAT EAERSSQNKH 250
    ETGSHDAERQ NEGQGVGEIN MATSGNGQGS TTRMDHETAS VLSSSSTHSA 300
    PRRLTSHLGT KVEMVYSLLS MLGTHDKDDM SRTLLAMSSS QDSCISMRQS 350
    GCLPLLIQLL HGNDKDSVLL GNSRGSKEAR ARASAALHNI IHSQPDDKRG 400
    RREIRVLHLL EQIRAYCETC WEWQEAHEPG MDQDKNPMPA PVEHQICPAV 450
    CVLMKLSFDE EHRHAMNELG GLQAIAELLQ VDCEMYGLTN DHYSITLRRY 500
    AGMALTNLTF GDVANKATLC SMKGCMRALV AQLKSESEDL QQVIASVLRN 550
    LSWRADVNSK KTLREVGSVK ALMECALEVK KESTLKSVLS ALWNLSAHCT 600
    ENKADICAVD GALAFLVGTL TYRSQTNTLA IIESGGGILR NVSSLIATNE 650
    DHRQILRENN CLQTLLQHLK SHSLTIVSNA CGTLWNLSAR NPKDQEALWD 700
    MGAVSMLKNL IHSKHKMIAM GSAAALRNLM ANRPAKYKDA NIMSPGSSLP 750
    SLHVRKQKAL EAELDAQHLS ETFDNIDNLS PKASHRSKQR HKQSLYGDYV 800
    FDTNRHDDNR SDNFNTGNMT VLSPYLNTTV LPSSSSSRGS LDSSRSEKDR 850
    SLERERGIGL GNYHPATENP GTSSKRGLQI STTAAQIAKV MEEVSAIHTS 900
    QEDRSSGSTT ELHCVTDERN ALRRSSAAHT HSNTYNFTKS ENSNRTCSMP 950
    YAKLEYKRSS NDSLNSVSSS DGYGKRGQMK PSIESYSEDD ESKFCSYGQY 1000
    PADLAHKIHS ANHMDDNDGE LDTPINYSLK YSDEQLNSGR QSPSQNERWA 1050
    RPKHIIEDEI KQSEQRQSRN QSTTYPVYTE STDDKHLKFQ PHFGQQECVS 1100
    PYRSRGANGS ETNRVGSNHG INQNVSQSLC QEDDYEDDKP TNYSERYSEE 1150
    EQHEEEERPT NYSIKYNEEK RHVDQPIDYS LKYATDIPSS QKQSFSFSKS 1200
    SSGQSSKTEH MSSSSENTST PSSNAKRQNQ LHPSSAQSRS GQPQKAATCK 1250
    VSSINQETIQ TYCVEDTPIC FSRCSSLSSL SSAEDEIGCN QTTQEADSAN 1300
    TLQIAEIKEK IGTRSAEDPV SEVPAVSQHP RTKSSRLQGS SLSSESARHK 1350
    AVEFSSGAKS PSKSGAQTPK SPPEHYVQET PLMFSRCTSV SSLDSFESRS 1400
    IASSVQSEPC SGMVSGIISP SDLPDSPGQT MPPSRSKTPP PPPQTAQTKR 1450
    EVPKNKAPTA EKRESGPKQA AVNAAVQRVQ VLPDADTLLH FATESTPDGF 1500
    SCSSSLSALS LDEPFIQKDV ELRIMPPVQE NDNGNETESE QPKESNENQE 1550
    KEAEKTIDSE KDLLDDSDDD DIEILEECII SAMPTKSSRK AKKPAQTASK 1600
    LPPPVARKPS QLPVYKLLPS QNRLQPQKHV SFTPGDDMPR VYCVEGTPIN 1650
    FSTATSLSDL TIESPPNELA AGEGVRGGAQ SGEFEKRDTI PTEGRSTDEA 1700
    QGGKTSSVTI PELDDNKAEE GDILAECINS AMPKGKSHKP FRVKKIMDQV 1750
    QQASASSSAP NKNQLDGKKK KPTSPVKPIP QNTEYRTRVR KNADSKNNLN 1800
    AERVFSDNKD SKKQNLKNNS KVFNDKLPNN EDRVRGSFAF DSPHHYTPIE 1850
    GTPYCFSRND SLSSLDFDDD DVDLSREKAE LRKAKENKES EAKVTSHTEL 1900
    TSNQQSANKT QAIAKQPINR GQPKPILQKQ STFPQSSKDI PDRGAATDEK 1950
    LQNFAIENTP VCFSHNSSLS SLSDIDQENN NKENEPIKET EPPDSQGEPS 2000
    KPQASGYAPK SFHVEDTPVC FSRNSSLSSL SIDSEDDLLQ ECISSAMPKK 2050
    KKPSRLKGDN EKHSPRNMGG ILGEDLTLDL KDIQRPDSEH GLSPDSENFD 2100
    WKAIQEGANS IVSSLHQAAA AACLSRQASS DSDSILSLKS GISLGSPFHL 2150
    TPDQEEKPFT SNKGPRILKP GEKSTLETKK IESESKGIKG GKKVYKSLIT 2200
    GKVRSNSEIS GQMKQPLQAN MPSISRGRTM IHIPGVRNSS SSTSPVSKKG 2250
    PPLKTPASKS PSEGQTATTS PRGAKPSVKS ELSPVARQTS QIGGSSKAPS 2300
    RSGSRDSTPS RPAQQPLSRP IQSPGRNSIS PGRNGISPPN KLSQLPRTSS 2350
    PSTASTKSSG SGKMSYTSPG RQMSQQNLTK QTGLSKNASS IPRSESASKG 2400
    LNQMNNGNGA NKKVELSRMS STKSSGSESD RSERPVLVRQ STFIKEAPSP 2450
    TLRRKLEESA SFESLSPSSR PASPTRSQAQ TPVLSPSLPD MSLSTHSSVQ 2500
    AGGWRKLPPN LSPTIEYNDG RPAKRHDIAR SHSESPSRLP INRSGTWKRE 2550
    HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDEK HVNSISGTKQ 2600
    SKENQVSAKG TWRKIKENEF SPTNSTSQTV SSGATNGAES KTLIYQMAPA 2650
    VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKA NPNIKDSKDN 2700
    QAKQNVGNGS VPMRTVGLEN RLNSFIQVDA PDQKGTEIKP GQNNPVPVSE 2750
    TNESSIVERT PFSSSSSSKH SSPSGTVAAR VTPFNYNPSP RKSSADSTSA 2800
    RPSQIPTPVN NNTKKRDSKT DSTESSGTQS PKRHSGSYLV TSV 2843
    Length:2,843
    Mass (Da):311,646
    Last modified:May 16, 2006 - v2
    Checksum:i77E194AE4A91DC5A
    GO
    Isoform Short (identifier: P25054-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         312-412: Missing.

    Show »
    Length:2,742
    Mass (Da):300,439
    Checksum:i49CF92BE7A81EBEC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841M → L in AAA60353. (PubMed:1678319)Curated
    Sequence conflicti184 – 1841M → L in AAA60354. (PubMed:1678319)Curated
    Sequence conflicti970 – 9701S → N in AAA60353. (PubMed:1678319)Curated
    Sequence conflicti970 – 9701S → N in AAA60354. (PubMed:1678319)Curated
    Sequence conflicti1309 – 13091E → G in AAA60353. (PubMed:1678319)Curated
    Sequence conflicti1309 – 13091E → G in AAA60354. (PubMed:1678319)Curated
    Sequence conflicti1325 – 13317AVSQHPR → SSVHSTLE in AAA60353. (PubMed:1678319)Curated
    Sequence conflicti1325 – 13317AVSQHPR → SSVHSTLE in AAA60354. (PubMed:1678319)Curated
    Sequence conflicti1355 – 13551S → P in AAA60353. (PubMed:1678319)Curated
    Sequence conflicti1355 – 13551S → P in AAA60354. (PubMed:1678319)Curated
    Sequence conflicti1591 – 15911A → G in AAA60353. (PubMed:1678319)Curated
    Sequence conflicti1591 – 15911A → G in AAA60354. (PubMed:1678319)Curated
    Sequence conflicti2723 – 27231N → T in AAA60353. (PubMed:1678319)Curated
    Sequence conflicti2723 – 27231N → T in AAA60354. (PubMed:1678319)Curated
    Sequence conflicti2755 – 27551S → P in AAA60353. (PubMed:1678319)Curated
    Sequence conflicti2755 – 27551S → P in AAA60354. (PubMed:1678319)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991R → W in FAP; unknown pathological significance. 1 Publication
    VAR_009613
    Natural varianti171 – 1711S → I in FAP. 1 Publication
    VAR_005032
    Natural varianti414 – 4141R → C in FAP.
    Corresponds to variant rs137854567 [ dbSNP | Ensembl ].
    VAR_005033
    Natural varianti722 – 7221S → G in FAP. 1 Publication
    VAR_009614
    Natural varianti784 – 7841S → T in FAP.
    VAR_005034
    Natural varianti817 – 8171G → C in gastric cancer.
    VAR_005035
    Natural varianti870 – 8701P → S.
    Corresponds to variant rs33974176 [ dbSNP | Ensembl ].
    VAR_053976
    Natural varianti880 – 8801I → T in colorectal carcinoma and gastric cancer; from a patient with MMRCS. 1 Publication
    VAR_005036
    Natural varianti890 – 8901V → I in colorectal carcinoma; from a patient with MMRCS. 1 Publication
    VAR_012975
    Natural varianti906 – 9061S → Y in colorectal tumor.
    VAR_005037
    Natural varianti911 – 9111E → G in FAP and colorectal tumor.
    VAR_005038
    Natural varianti942 – 9421N → D in gastric cancer.
    VAR_005039
    Natural varianti1027 – 10271Y → C in colorectal tumor.
    VAR_005040
    Natural varianti1057 – 10571E → G in non-FAP; unknown pathological significance. 1 Publication
    VAR_009615
    Natural varianti1118 – 11181N → D.1 Publication
    VAR_005041
    Natural varianti1120 – 11201G → E in gastric cancer.
    Corresponds to variant rs28933379 [ dbSNP | Ensembl ].
    VAR_005042
    Natural varianti1171 – 11711R → C.1 Publication
    VAR_008992
    Natural varianti1171 – 11711R → H in gastric cancer.
    VAR_005043
    Natural varianti1176 – 11761P → L in FAP.
    VAR_005044
    Natural varianti1184 – 11841A → P in FAP. 1 Publication
    VAR_009616
    Natural varianti1197 – 11971F → S in gastric cancer.
    VAR_005045
    Natural varianti1254 – 12541I → F in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035794
    Natural varianti1259 – 12591I → T in gastric cancer.
    VAR_005046
    Natural varianti1292 – 12921T → M.1 Publication
    VAR_005047
    Natural varianti1296 – 12961A → V in MDB; sporadic. 1 Publication
    VAR_017653
    Natural varianti1304 – 13041I → V.1 Publication
    VAR_005048
    Natural varianti1307 – 13071I → K in 6% of Ashkenazi Jews; associated with slightly increased risk of colon and breast cancer. 4 Publications
    Corresponds to variant rs1801155 [ dbSNP | Ensembl ].
    VAR_005049
    Natural varianti1312 – 13121G → E in gastric cancer.
    VAR_005050
    Natural varianti1313 – 13131T → A in FAP and colorectal tumor.
    VAR_005051
    Natural varianti1317 – 13171E → Q May contribute to colorectal tumor development. 1 Publication
    Corresponds to variant rs1801166 [ dbSNP | Ensembl ].
    VAR_009617
    Natural varianti1326 – 13261V → A in gastric cancer.
    VAR_005052
    Natural varianti1348 – 13481R → W in FAP. 1 Publication
    VAR_005053
    Natural varianti1395 – 13951S → C in hepatoblastoma. 1 Publication
    VAR_065133
    Natural varianti1422 – 14221D → H in colorectal tumor.
    VAR_005054
    Natural varianti1472 – 14721V → I in MDB; sporadic. 1 Publication
    VAR_017654
    Natural varianti1495 – 14951S → G in MDB; sporadic. 1 Publication
    VAR_017655
    Natural varianti1496 – 14961T → S.
    Corresponds to variant rs2229996 [ dbSNP | Ensembl ].
    VAR_020141
    Natural varianti1508 – 15081A → V in colorectal carcinoma from a patient with MMRCS. 1 Publication
    VAR_012976
    Natural varianti1822 – 18221V → D.4 Publications
    Corresponds to variant rs459552 [ dbSNP | Ensembl ].
    VAR_008993
    Natural varianti1882 – 18821R → T.
    Corresponds to variant rs34157245 [ dbSNP | Ensembl ].
    VAR_053977
    Natural varianti1973 – 19731S → T.
    Corresponds to variant rs4987109 [ dbSNP | Ensembl ].
    VAR_020142
    Natural varianti2499 – 24991V → L.
    Corresponds to variant rs33941929 [ dbSNP | Ensembl ].
    VAR_053978
    Natural varianti2502 – 25021G → S.1 Publication
    Corresponds to variant rs2229995 [ dbSNP | Ensembl ].
    VAR_005055
    Natural varianti2621 – 26211S → C in FAP.
    Corresponds to variant rs72541816 [ dbSNP | Ensembl ].
    VAR_005056
    Natural varianti2738 – 27381I → T.1 Publication
    VAR_008994
    Natural varianti2839 – 28391L → F in FAP.
    VAR_005057

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei312 – 412101Missing in isoform Short. 1 PublicationVSP_004115Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73548 mRNA. Translation: AAA60353.1.
    M73548 mRNA. Translation: AAA60354.1.
    M74088 mRNA. Translation: AAA03586.1.
    CH471086 Genomic DNA. Translation: EAW49002.1.
    CH471086 Genomic DNA. Translation: EAW49007.1.
    S78214 Genomic DNA. Translation: AAB21145.2. Sequence problems.
    CCDSiCCDS4107.1. [P25054-1]
    PIRiA37261. RBHUAP.
    RefSeqiNP_000029.2. NM_000038.5. [P25054-1]
    NP_001120982.1. NM_001127510.2. [P25054-1]
    UniGeneiHs.158932.

    Genome annotation databases

    EnsembliENST00000257430; ENSP00000257430; ENSG00000134982. [P25054-1]
    ENST00000508376; ENSP00000427089; ENSG00000134982. [P25054-1]
    GeneIDi324.
    KEGGihsa:324.
    UCSCiuc003kpy.4. human. [P25054-1]

    Polymorphism databases

    DMDMi97535708.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Colon cancer gene variant databases Adenomatous Polyposis Coli (APC)

    Leiden Open Variation Database (LOVD)

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    SHMPD

    The Singapore human mutation and polymorphism database

    Wikipedia

    APC entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73548 mRNA. Translation: AAA60353.1 .
    M73548 mRNA. Translation: AAA60354.1 .
    M74088 mRNA. Translation: AAA03586.1 .
    CH471086 Genomic DNA. Translation: EAW49002.1 .
    CH471086 Genomic DNA. Translation: EAW49007.1 .
    S78214 Genomic DNA. Translation: AAB21145.2 . Sequence problems.
    CCDSi CCDS4107.1. [P25054-1 ]
    PIRi A37261. RBHUAP.
    RefSeqi NP_000029.2. NM_000038.5. [P25054-1 ]
    NP_001120982.1. NM_001127510.2. [P25054-1 ]
    UniGenei Hs.158932.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DEB X-ray 2.40 A/B 2-55 [» ]
    1EMU X-ray 1.90 B 2034-2049 [» ]
    1JPP X-ray 3.10 C/D 1021-1035 [» ]
    1M5I X-ray 2.00 A 126-250 [» ]
    1T08 X-ray 2.10 C 1484-1498 [» ]
    1TH1 X-ray 2.50 C/D 1362-1540 [» ]
    1V18 X-ray 2.10 B 1482-1528 [» ]
    2RQU NMR - B 1578-1596 [» ]
    3AU3 X-ray 2.10 A 396-732 [» ]
    3NMW X-ray 1.60 A/B 407-751 [» ]
    3NMX X-ray 2.30 A/B/C 407-751 [» ]
    3NMZ X-ray 3.01 A/B 303-739 [» ]
    3QHE X-ray 2.40 A/C 396-732 [» ]
    3RL7 X-ray 2.30 G/H/I/J/K/L 2833-2843 [» ]
    3RL8 X-ray 2.20 F 2833-2843 [» ]
    3T7U X-ray 2.90 A/B 407-775 [» ]
    4G69 X-ray 2.00 B 2833-2843 [» ]
    DisProti DP00519.
    ProteinModelPortali P25054.
    SMRi P25054. Positions 2-55, 130-239, 326-736, 1485-1528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106821. 131 interactions.
    DIPi DIP-33556N.
    IntActi P25054. 122 interactions.
    MINTi MINT-88204.
    STRINGi 9606.ENSP00000257430.

    PTM databases

    PhosphoSitei P25054.

    Polymorphism databases

    DMDMi 97535708.

    Proteomic databases

    MaxQBi P25054.
    PaxDbi P25054.
    PRIDEi P25054.

    Protocols and materials databases

    DNASUi 324.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257430 ; ENSP00000257430 ; ENSG00000134982 . [P25054-1 ]
    ENST00000508376 ; ENSP00000427089 ; ENSG00000134982 . [P25054-1 ]
    GeneIDi 324.
    KEGGi hsa:324.
    UCSCi uc003kpy.4. human. [P25054-1 ]

    Organism-specific databases

    CTDi 324.
    GeneCardsi GC05P112101.
    GeneReviewsi APC.
    HGNCi HGNC:583. APC.
    HPAi CAB025994.
    HPA013349.
    MIMi 114550. phenotype.
    135290. phenotype.
    155255. phenotype.
    175100. phenotype.
    276300. phenotype.
    611731. gene.
    613659. phenotype.
    neXtProti NX_P25054.
    Orphaneti 247806. APC-related attenuated familial adenomatous polyposis.
    873. Desmoid tumor.
    261584. Familial adenomatous polyposis due to 5q22.2 microdeletion.
    79665. Gardner syndrome.
    99818. Turcot syndrome with polyposis.
    PharmGKBi PA24875.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259696.
    HOVERGENi HBG004264.
    InParanoidi P25054.
    KOi K02085.
    OMAi IEDCPIN.
    PhylomeDBi P25054.
    TreeFami TF106496.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000134982-MONOMER.
    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    SignaLinki P25054.

    Miscellaneous databases

    ChiTaRSi APC. human.
    EvolutionaryTracei P25054.
    GeneWikii Adenomatous_polyposis_coli.
    GenomeRNAii 324.
    NextBioi 1329.
    PROi P25054.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25054.
    Bgeei P25054.
    CleanExi HS_APC.
    Genevestigatori P25054.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    InterProi IPR026836. APC.
    IPR009240. APC_15aa_rpt.
    IPR009234. APC_basic_dom.
    IPR009223. APC_Cys-rich_rpt.
    IPR026831. APC_dom.
    IPR026818. Apc_fam.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR009232. EB1-bd.
    IPR009224. SAMP.
    [Graphical view ]
    PANTHERi PTHR12607. PTHR12607. 1 hit.
    PTHR12607:SF11. PTHR12607:SF11. 1 hit.
    Pfami PF05972. APC_15aa. 4 hits.
    PF05956. APC_basic. 1 hit.
    PF05923. APC_crr. 7 hits.
    PF00514. Arm. 3 hits.
    PF05937. EB1_binding. 1 hit.
    PF05924. SAMP. 3 hits.
    PF11414. Suppressor_APC. 1 hit.
    [Graphical view ]
    SMARTi SM00185. ARM. 6 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50176. ARM_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), VARIANT ASP-1822.
      Tissue: Fetal brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT ASP-1822.
    3. "Asef, a link between the tumor suppressor APC and G-protein signaling."
      Kawasaki Y., Senda T., Ishidate T., Koyama R., Morishita T., Iwayama Y., Higuchi O., Akiyama T.
      Science 289:1194-1197(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARHGEF4, IDENTIFICATION IN A COMPLEX WITH ARHGEF4 AND CTNNB1.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-1822.
    5. "Disruption of the APC gene by a retrotransposal insertion of L1 sequence in a colon cancer."
      Miki Y., Nishisho I., Horii A., Miyoshi Y., Utsunomiya J., Kinzler K.W., Vogelstein B., Nakamura Y.
      Cancer Res. 52:643-645(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1506-1524.
    6. "Association of the APC tumor suppressor protein with catenins."
      Su L.-K., Vogelstein B., Kinzler K.W.
      Science 262:1734-1737(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH CATENINS.
    7. "Hereditary desmoid disease due to a frameshift mutation at codon 1924 of the APC gene."
      Eccles D.M., van der Luijt R.B., Breukel C., Bullman H., Bunyan D., Fisher A., Barber J., du Boulay C., Primrose J., Burn J., Fodde R.
      Am. J. Hum. Genet. 59:1193-1201(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HEREDITARY DESMOID DISEASE.
    8. "Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein."
      Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H., Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T.
      Science 272:1020-1023(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG1.
    9. "Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein."
      Makino K., Kuwahara H., Masuko N., Nishiyama Y., Morisaki T., Sasaki J., Nakao M., Kuwano A., Nakata M., Ushio Y., Saya H.
      Oncogene 14:2425-2433(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG3.
      Tissue: Fetal brain.
    10. "A germline mutation at the extreme 3' end of the APC gene results in a severe desmoid phenotype and is associated with overexpression of beta-catenin in the desmoid tumor."
      Couture J., Mitri A., Lagace R., Smits R., Berk T., Bouchard H.-L., Fodde R., Alman B., Bapat B.
      Clin. Genet. 57:205-212(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HEREDITARY DESMOID DISEASE.
    11. "Human APC2 localization and allelic imbalance."
      Jarrett C.R., Blancato J., Cao T., Bressette D.S., Cepeda M., Young P.E., King C.R., Byers S.W.
      Cancer Res. 61:7978-7984(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APC2.
    12. "Characterization of functional domains of human EB1 family proteins."
      Bu W., Su L.-K.
      J. Biol. Chem. 278:49721-49731(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPRE1; MAPRE2 AND MAPRE3.
    13. "Adenomatous polyposis coli is down-regulated by the ubiquitin-proteasome pathway in a process facilitated by Axin."
      Choi J., Park S.Y., Costantini F., Jho E.-H., Joo C.-K.
      J. Biol. Chem. 279:49188-49198(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Human scribble, a novel tumor suppressor identified as a target of high-risk HPV E6 for ubiquitin-mediated degradation, interacts with adenomatous polyposis coli."
      Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K., Yasugi T., Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T., Taketani Y.
      Genes Cells 11:453-464(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SCRIB, MUTAGENESIS OF THR-2841 AND VAL-2843.
    16. "Identification and characterization of Asef2, a guanine-nucleotide exchange factor specific for Rac1 and Cdc42."
      Kawasaki Y., Sagara M., Shibata Y., Shirouzu M., Yokoyama S., Akiyama T.
      Oncogene 26:7620-7627(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SPATA13.
    17. "Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains."
      Tran H., Hamada F., Schwarz-Romond T., Bienz M.
      Genes Dev. 22:528-542(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEUBIQUITINATION.
    18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780; SER-1042; SER-1360; SER-1861; SER-1863; SER-1864; THR-2151; SER-2260; SER-2270; SER-2283; SER-2473; SER-2535; SER-2671; SER-2674; THR-2679 AND SER-2789, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION.
    22. "The adenomatous polyposis coli-associated exchange factors Asef and Asef2 are required for adenoma formation in Apc(Min/+)mice."
      Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M., Ohwada S., Akiyama T.
      EMBO Rep. 10:1355-1362(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal organization and are involved in HGF-induced cell migration."
      Sagara M., Kawasaki Y., Iemura S.I., Natsume T., Takai Y., Akiyama T.
      Oncogene 28:1357-1365(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
      Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
      Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744 AND SER-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "Structural and functional characterization of the Wnt inhibitor APC membrane recruitment 1 (Amer1)."
      Tanneberger K., Pfister A.S., Kriz V., Bryja V., Schambony A., Behrens J.
      J. Biol. Chem. 286:19204-19214(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AMER1.
    28. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861; SER-1863 AND SER-1864, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Amer2 protein is a novel negative regulator of Wnt/beta-Catenin signaling involved in neuroectodermal patterning."
      Pfister A.S., Tanneberger K., Schambony A., Behrens J.
      J. Biol. Chem. 287:1734-1741(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AMER2.
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    31. "Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor."
      Day C.L., Alber T.
      J. Mol. Biol. 301:147-156(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-55.
    32. "Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex."
      Eklof Spink K., Fridman S.G., Weis W.I.
      EMBO J. 20:6203-6212(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1021-1035 IN COMPLEX WITH CTNNB1.
    33. "Structural basis of the axin-adenomatous polyposis coli interaction."
      Spink K.E., Polakis P., Weis W.I.
      EMBO J. 19:2270-2279(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2034-2049 IN COMPLEX WITH AXIN.
    34. "Mutations of the APC (adenomatous polyposis coli) gene."
      Nagase H., Nakamura Y.
      Hum. Mutat. 2:425-434(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    35. "Structural basis of the recognition of the SAMP motif of adenomatous polyposis coli by the Src-homology 3 domain."
      Kaieda S., Matsui C., Mimori-Kiyosue Y., Ikegami T.
      Biochemistry 49:5143-5153(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1578-1596 IN COMPLEX WITH ASAP1.
    36. "Crystal structure of the armadillo repeat domain of adenomatous polyposis coli which reveals its inherent flexibility."
      Zhang Z., Lin K., Gao L., Chen L., Shi X., Wu G.
      Biochem. Biophys. Res. Commun. 412:732-736(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 407-775, DOMAIN ARM REPEATS.
    37. Cited for: VARIANTS FAP.
    38. "Somatic mutations of the APC gene in colorectal tumors: mutation cluster region in the APC gene."
      Miyoshi Y., Nagase H., Ando H., Ichii S., Nakatsuru S., Aoki T., Miki Y., Mori T., Nakamura Y.
      Hum. Mol. Genet. 1:229-233(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FAP.
    39. "Somatic mutation of the APC gene in gastric cancer: frequent mutations in very well differentiated adenocarcinoma and signet-ring cell carcinoma."
      Nakatsuru S., Yanagisawa A., Ichii S., Tahara E., Kato Y., Nakamura Y., Horii A.
      Hum. Mol. Genet. 1:559-563(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FAP.
    40. "Screening for germ-line mutations in familial adenomatous polyposis patients: 61 new patients and a summary of 150 unrelated patients."
      Nagase H., Miyoshi Y., Horii A., Aoki T., Petersen G.M., Vogelstein B., Maher E., Ogawa M., Maruyama M., Utsunomiya J., Baba S., Nakamura Y.
      Hum. Mutat. 1:467-473(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FAP TRP-1348, VARIANTS ASP-1118; MET-1292; VAL-1304 AND SER-2502.
    41. "Mutational analysis of the first 14 exons of the adenomatous polyposis coli (APC) gene."
      Dobbie Z., Spycher M., Huerliman R., Ammann R., Ammann T., Roth J., Mueller A., Mueller H., Scott R.J.
      Eur. J. Cancer 30A:1709-1713(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FAP TRP-99.
      Tissue: Peripheral blood lymphocyte.
    42. "Four novel mutations of the APC (adenomatous polyposis coli) gene in FAP patients."
      Stella A., Montera M., Resta N., Marchese C., Susca F., Gentile M., Romio L., Pilia S., Prete F., Mareni C., Guanti G.
      Hum. Mol. Genet. 3:1687-1688(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FAP GLY-722.
    43. Cited for: INVOLVEMENT IN MMRCS.
    44. "Somatic mutations of the APC gene in sporadic hepatoblastomas."
      Oda H., Imai Y., Nakatsuru Y., Hata J., Ishikawa T.
      Cancer Res. 56:3320-3323(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HEPATOBLASTOMA CYS-1395.
    45. "Molecular analysis of the APC gene in 105 Dutch kindreds with familial adenomatous polyposis: 67 germline mutations identified by DGGE, PTT, and southern analysis."
      van der Luijt R.B., Meera Khan P., Vasen H.F.A., Tops C.M.J., van Leeuwen-Cornelisse I.S.J., Wijnen J.T., van der Klift H.M., Plug R.J., Griffioen G., Fodde R.
      Hum. Mutat. 9:7-16(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FAP ILE-171.
    46. Cited for: VARIANTS COLORECTAL CARCINOMA THR-880; ILE-890 AND VAL-1508.
    47. Cited for: VARIANT LYS-1307.
    48. "The APC variants I1307K and E1317Q are associated with colorectal tumors, but not always with a family history."
      Frayling I.M., Beck N.E., Ilyas M., Dove-Edwin I., Goodman P., Pack K., Bell J.A., Williams C.B., Hodgson S.V., Thomas H.J.W., Talbot I.C., Bodmer W.F., Tomlinson I.P.M.
      Proc. Natl. Acad. Sci. U.S.A. 95:10722-10727(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LYS-1307 AND GLN-1317.
      Tissue: Peripheral blood.
    49. "The APC I1307K allele and cancer risk in a community-based study of Ashkenazi Jews."
      Woodage T., King S.M., Wacholder S., Hartge P., Struewing J.P., McAdams M., Laken S.J., Tucker M.A., Brody L.C.
      Nat. Genet. 20:62-65(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LYS-1307.
    50. "Inherited colorectal polyposis and cancer risk of the APC I1307K polymorphism."
      Gryfe R., Di Nicola N., Lal G., Gallinger S., Redston M.
      Am. J. Hum. Genet. 64:378-384(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LYS-1307.
    51. "Molecular analysis of the APC gene in 205 families: extended genotype-phenotype correlations in FAP and evidence for the role of APC amino acid changes in colorectal cancer predisposition."
      Wallis Y.L., Morton D.G., McKeown C.M., Macdonald F.
      J. Med. Genet. 36:14-20(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLY-1057; CYS-1171; ASP-1822 AND THR-2738.
    52. "The type of somatic mutation at APC in familial adenomatous polyposis is determined by the site of the germline mutation: a new facet to Knudson's 'two-hit' hypothesis."
      Lamlum H., Ilyas M., Rowan A., Clark S., Johnson V., Bell J.A., Frayling I.M., Efstathiou J., Pack K., Payne S., Roylance R., Gorman P., Sheer D., Neale K., Phillips R., Talbot I.C., Bodmer W.F., Tomlinson I.P.M.
      Nat. Med. 5:1071-1075(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FAP PRO-1184.
    53. Cited for: VARIANTS MDB VAL-1296; ILE-1472 AND GLY-1495.
    54. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-1254.

    Entry informationi

    Entry nameiAPC_HUMAN
    AccessioniPrimary (citable) accession number: P25054
    Secondary accession number(s): D3DT03
    , Q15162, Q15163, Q93042
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 191 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    APC mutations have led to some interesting observations. (1) the great majority of the mutations found to date would result in truncation of the APC product. (2) almost all the mutations have occurred within the first half of the coding sequence, and somatic mutations in colorectal tumors are further clustered in a particular region, called MCR (mutation cluster region). (3) most identified point mutations in the APC gene are transitions from cytosine to other nucleotides. (4) the location of germline mutations tends to correlate with the number of colorectal polyps in FAP patients. Inactivation of both alleles of the APC gene seems to be required as an early event to develop most adenomas and carcinomas in the colon and rectum as well as some of those in the stomach.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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