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P25054 (APC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 186. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenomatous polyposis coli protein

Short name=Protein APC
Alternative name(s):
Deleted in polyposis 2.5
Gene names
Name:APC
Synonyms:DP2.5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2843 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization. Ref.3 Ref.16 Ref.22 Ref.23 Ref.25

Subunit structure

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). Ref.3 Ref.8 Ref.9 Ref.11 Ref.12 Ref.15 Ref.16 Ref.21 Ref.27 Ref.29

Subcellular location

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. Ref.3 Ref.15 Ref.21 Ref.23 Ref.25

Tissue specificity

Expressed in a variety of tissues.

Domain

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends By similarity. Ref.36

Post-translational modification

Phosphorylated by GSK3B.

Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID. Ref.13 Ref.17

Involvement in disease

Familial adenomatous polyposis (FAP) [MIM:175100]: A cancer predisposition syndrome characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.10 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.46 Ref.53

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.10

Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.
Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.7 Ref.10 Ref.54

Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: Autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.10 Ref.44

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. Ref.7 Ref.10

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. Ref.7 Ref.10

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.

Sequence similarities

Belongs to the adenomatous polyposis coli (APC) family.

Contains 7 ARM repeats.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Tumor suppressor
   DomainCoiled coil
Repeat
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

axis specification

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Non-traceable author statement PubMed 11035805. Source: UniProtKB

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Non-traceable author statement PubMed 8259518. Source: UniProtKB

cell cycle arrest

Inferred from direct assay PubMed 8521819. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.23. Source: UniProtKB

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 14728717. Source: UniProtKB

chromosome organization

Inferred from electronic annotation. Source: Ensembl

cytoplasmic microtubule organization

Inferred from electronic annotation. Source: Ensembl

dorsal/ventral pattern formation

Inferred from electronic annotation. Source: Ensembl

hair follicle development

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

metaphase/anaphase transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

mitotic cytokinesis

Inferred from mutant phenotype PubMed 17570218. Source: MGI

mitotic spindle assembly checkpoint

Inferred from mutant phenotype PubMed 17227893. Source: MGI

muscle cell cellular homeostasis

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of canonical Wnt signaling pathway

Inferred from genetic interaction PubMed 12952940. Source: MGI

negative regulation of cell proliferation

Inferred from direct assay PubMed 8521819. Source: UniProtKB

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay PubMed 8521819. Source: UniProtKB

negative regulation of epithelial cell proliferation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

negative regulation of microtubule depolymerization

Inferred from direct assay PubMed 11166179. Source: UniProtKB

negative regulation of odontogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17227893. Source: MGI

positive regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from mutant phenotype PubMed 17192415. Source: MGI

positive regulation of epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of microtubule polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein catabolic process

Inferred by curator PubMed 16188939. Source: BHF-UCL

positive regulation of pseudopodium assembly

Inferred from mutant phenotype PubMed 17192415. Source: MGI

protein complex assembly

Inferred from direct assay PubMed 16188939. Source: UniProtKB

proximal/distal pattern formation

Inferred from electronic annotation. Source: Ensembl

regulation of attachment of spindle microtubules to kinetochore

Non-traceable author statement PubMed 11283619. Source: UniProtKB

regulation of microtubule-based process

Inferred from mutant phenotype Ref.25. Source: UniProtKB

regulation of nitrogen compound metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

thymus development

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Non-traceable author statement PubMed 18502210. Source: UniProtKB

   Cellular_componentadherens junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

axonal growth cone

Inferred from electronic annotation. Source: Ensembl

beta-catenin destruction complex

Inferred from direct assay PubMed 16188939PubMed 9601641. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 11283619. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11035805PubMed 12955080Ref.25. Source: UniProtKB

cytoplasmic microtubule

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay PubMed 11283619. Source: UniProtKB

lamellipodium

Inferred from direct assay Ref.23. Source: UniProtKB

lateral plasma membrane

Inferred from direct assay PubMed 12072559. Source: MGI

microtubule plus-end

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 11035805PubMed 12955080. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.25. Source: UniProtKB

ruffle membrane

Inferred from direct assay Ref.23. Source: UniProtKB

tight junction

Inferred from direct assay PubMed 18502210. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Inferred from physical interaction PubMed 10773885PubMed 11533658. Source: UniProtKB

gamma-catenin binding

Inferred from physical interaction PubMed 7890674. Source: BHF-UCL

microtubule binding

Inferred from direct assay PubMed 11166179PubMed 16188939. Source: UniProtKB

microtubule plus-end binding

Inferred from direct assay Ref.21. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 8638126. Source: UniProtKB

protein kinase regulator activity

Inferred from direct assay PubMed 11972058. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P25054-1)

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.
Isoform Short (identifier: P25054-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.30
Chain2 – 28432842Adenomatous polyposis coli protein
PRO_0000064627

Regions

Repeat453 – 49543ARM 1
Repeat505 – 54743ARM 2
Repeat548 – 59144ARM 3
Repeat592 – 63847ARM 4
Repeat639 – 68345ARM 5
Repeat684 – 72542ARM 6
Repeat726 – 76742ARM 7
Region960 – 1337378Responsible for down-regulation through a process mediated by direct ubiquitination
Region1866 – 189328Highly charged
Coiled coil2 – 6160 Potential
Coiled coil127 – 248122 Potential
Motif2803 – 28064Microtubule tip localization signal
Motif2841 – 28433PDZ-binding
Compositional bias1 – 730730Leu-rich
Compositional bias731 – 28322102Ser-rich
Compositional bias1131 – 115626Asp/Glu-rich (acidic)
Compositional bias1558 – 157720Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylalanine Ref.30
Modified residue7441Phosphoserine Ref.26
Modified residue7801Phosphoserine Ref.19 Ref.26
Modified residue10421Phosphoserine Ref.19
Modified residue13601Phosphoserine Ref.19
Modified residue18611Phosphoserine Ref.19 Ref.28
Modified residue18631Phosphoserine Ref.19 Ref.28
Modified residue18641Phosphoserine Ref.19 Ref.28
Modified residue21511Phosphothreonine Ref.19
Modified residue22601Phosphoserine Ref.19
Modified residue22701Phosphoserine Ref.19
Modified residue22831Phosphoserine Ref.19
Modified residue24731Phosphoserine Ref.19
Modified residue25351Phosphoserine Ref.19
Modified residue26711Phosphoserine Ref.18 Ref.19
Modified residue26741Phosphoserine Ref.19
Modified residue26791Phosphothreonine Ref.19
Modified residue27891Phosphoserine Ref.19

Natural variations

Alternative sequence312 – 412101Missing in isoform Short.
VSP_004115
Natural variant991R → W in FAP; unknown pathological significance. Ref.41
VAR_009613
Natural variant1711S → I in FAP. Ref.46
VAR_005032
Natural variant4141R → C in FAP.
Corresponds to variant rs137854567 [ dbSNP | Ensembl ].
VAR_005033
Natural variant7221S → G in FAP. Ref.42
VAR_009614
Natural variant7841S → T in FAP.
VAR_005034
Natural variant8171G → C in gastric cancer.
VAR_005035
Natural variant8701P → S.
Corresponds to variant rs33974176 [ dbSNP | Ensembl ].
VAR_053976
Natural variant8801I → T in colorectal carcinoma and gastric cancer; from a patient with MMRCS. Ref.47
VAR_005036
Natural variant8901V → I in colorectal carcinoma; from a patient with MMRCS. Ref.47
VAR_012975
Natural variant9061S → Y in colorectal tumor.
VAR_005037
Natural variant9111E → G in FAP and colorectal tumor.
VAR_005038
Natural variant9421N → D in gastric cancer.
VAR_005039
Natural variant10271Y → C in colorectal tumor.
VAR_005040
Natural variant10571E → G in non-FAP; unknown pathological significance. Ref.52
VAR_009615
Natural variant11181N → D. Ref.40
VAR_005041
Natural variant11201G → E in gastric cancer.
Corresponds to variant rs28933379 [ dbSNP | Ensembl ].
VAR_005042
Natural variant11711R → C. Ref.52
VAR_008992
Natural variant11711R → H in gastric cancer.
VAR_005043
Natural variant11761P → L in FAP.
VAR_005044
Natural variant11841A → P in FAP. Ref.53
VAR_009616
Natural variant11971F → S in gastric cancer.
VAR_005045
Natural variant12541I → F in a colorectal cancer sample; somatic mutation. Ref.55
VAR_035794
Natural variant12591I → T in gastric cancer.
VAR_005046
Natural variant12921T → M. Ref.40
VAR_005047
Natural variant12961A → V in MDB; sporadic. Ref.54
VAR_017653
Natural variant13041I → V. Ref.40
VAR_005048
Natural variant13071I → K in 6% of Ashkenazi Jews; associated with slightly increased risk of colon and breast cancer. Ref.48 Ref.49 Ref.50 Ref.51
Corresponds to variant rs1801155 [ dbSNP | Ensembl ].
VAR_005049
Natural variant13121G → E in gastric cancer.
VAR_005050
Natural variant13131T → A in FAP and colorectal tumor.
VAR_005051
Natural variant13171E → Q May contribute to colorectal tumor development. Ref.49
Corresponds to variant rs1801166 [ dbSNP | Ensembl ].
VAR_009617
Natural variant13261V → A in gastric cancer.
VAR_005052
Natural variant13481R → W in FAP. Ref.40
VAR_005053
Natural variant13951S → C in hepatoblastoma. Ref.45
VAR_065133
Natural variant14221D → H in colorectal tumor.
VAR_005054
Natural variant14721V → I in MDB; sporadic. Ref.54
VAR_017654
Natural variant14951S → G in MDB; sporadic. Ref.54
VAR_017655
Natural variant14961T → S.
Corresponds to variant rs2229996 [ dbSNP | Ensembl ].
VAR_020141
Natural variant15081A → V in colorectal carcinoma from a patient with MMRCS. Ref.47
VAR_012976
Natural variant18221V → D. Ref.1 Ref.2 Ref.4 Ref.52
Corresponds to variant rs459552 [ dbSNP | Ensembl ].
VAR_008993
Natural variant18821R → T.
Corresponds to variant rs34157245 [ dbSNP | Ensembl ].
VAR_053977
Natural variant19731S → T.
Corresponds to variant rs4987109 [ dbSNP | Ensembl ].
VAR_020142
Natural variant24991V → L.
Corresponds to variant rs33941929 [ dbSNP | Ensembl ].
VAR_053978
Natural variant25021G → S. Ref.40
Corresponds to variant rs2229995 [ dbSNP | Ensembl ].
VAR_005055
Natural variant26211S → C in FAP.
Corresponds to variant rs72541816 [ dbSNP | Ensembl ].
VAR_005056
Natural variant27381I → T. Ref.52
VAR_008994
Natural variant28391L → F in FAP.
VAR_005057

Experimental info

Mutagenesis28411T → L: Loss of interaction with SCRIB. Ref.15
Mutagenesis28431V → Q: Loss of interaction with SCRIB. Ref.15
Sequence conflict1841M → L in AAA60353. Ref.1
Sequence conflict1841M → L in AAA60354. Ref.1
Sequence conflict9701S → N in AAA60353. Ref.1
Sequence conflict9701S → N in AAA60354. Ref.1
Sequence conflict13091E → G in AAA60353. Ref.1
Sequence conflict13091E → G in AAA60354. Ref.1
Sequence conflict1325 – 13317AVSQHPR → SSVHSTLE in AAA60353. Ref.1
Sequence conflict1325 – 13317AVSQHPR → SSVHSTLE in AAA60354. Ref.1
Sequence conflict13551S → P in AAA60353. Ref.1
Sequence conflict13551S → P in AAA60354. Ref.1
Sequence conflict15911A → G in AAA60353. Ref.1
Sequence conflict15911A → G in AAA60354. Ref.1
Sequence conflict27231N → T in AAA60353. Ref.1
Sequence conflict27231N → T in AAA60354. Ref.1
Sequence conflict27551S → P in AAA60353. Ref.1
Sequence conflict27551S → P in AAA60354. Ref.1

Secondary structure

............................................................................... 2843
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 77E194AE4A91DC5A

FASTA2,843311,646
        10         20         30         40         50         60 
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDEAM 

        70         80         90        100        110        120 
ASSGQIDLLE RLKELNLDSS NFPGVKLRSK MSLRSYGSRE GSVSSRSGEC SPVPMGSFPR 

       130        140        150        160        170        180 
RGFVNGSRES TGYLEELEKE RSLLLADLDK EEKEKDWYYA QLQNLTKRID SLPLTENFSL 

       190        200        210        220        230        240 
QTDMTRRQLE YEARQIRVAM EEQLGTCQDM EKRAQRRIAR IQQIEKDILR IRQLLQSQAT 

       250        260        270        280        290        300 
EAERSSQNKH ETGSHDAERQ NEGQGVGEIN MATSGNGQGS TTRMDHETAS VLSSSSTHSA 

       310        320        330        340        350        360 
PRRLTSHLGT KVEMVYSLLS MLGTHDKDDM SRTLLAMSSS QDSCISMRQS GCLPLLIQLL 

       370        380        390        400        410        420 
HGNDKDSVLL GNSRGSKEAR ARASAALHNI IHSQPDDKRG RREIRVLHLL EQIRAYCETC 

       430        440        450        460        470        480 
WEWQEAHEPG MDQDKNPMPA PVEHQICPAV CVLMKLSFDE EHRHAMNELG GLQAIAELLQ 

       490        500        510        520        530        540 
VDCEMYGLTN DHYSITLRRY AGMALTNLTF GDVANKATLC SMKGCMRALV AQLKSESEDL 

       550        560        570        580        590        600 
QQVIASVLRN LSWRADVNSK KTLREVGSVK ALMECALEVK KESTLKSVLS ALWNLSAHCT 

       610        620        630        640        650        660 
ENKADICAVD GALAFLVGTL TYRSQTNTLA IIESGGGILR NVSSLIATNE DHRQILRENN 

       670        680        690        700        710        720 
CLQTLLQHLK SHSLTIVSNA CGTLWNLSAR NPKDQEALWD MGAVSMLKNL IHSKHKMIAM 

       730        740        750        760        770        780 
GSAAALRNLM ANRPAKYKDA NIMSPGSSLP SLHVRKQKAL EAELDAQHLS ETFDNIDNLS 

       790        800        810        820        830        840 
PKASHRSKQR HKQSLYGDYV FDTNRHDDNR SDNFNTGNMT VLSPYLNTTV LPSSSSSRGS 

       850        860        870        880        890        900 
LDSSRSEKDR SLERERGIGL GNYHPATENP GTSSKRGLQI STTAAQIAKV MEEVSAIHTS 

       910        920        930        940        950        960 
QEDRSSGSTT ELHCVTDERN ALRRSSAAHT HSNTYNFTKS ENSNRTCSMP YAKLEYKRSS 

       970        980        990       1000       1010       1020 
NDSLNSVSSS DGYGKRGQMK PSIESYSEDD ESKFCSYGQY PADLAHKIHS ANHMDDNDGE 

      1030       1040       1050       1060       1070       1080 
LDTPINYSLK YSDEQLNSGR QSPSQNERWA RPKHIIEDEI KQSEQRQSRN QSTTYPVYTE 

      1090       1100       1110       1120       1130       1140 
STDDKHLKFQ PHFGQQECVS PYRSRGANGS ETNRVGSNHG INQNVSQSLC QEDDYEDDKP 

      1150       1160       1170       1180       1190       1200 
TNYSERYSEE EQHEEEERPT NYSIKYNEEK RHVDQPIDYS LKYATDIPSS QKQSFSFSKS 

      1210       1220       1230       1240       1250       1260 
SSGQSSKTEH MSSSSENTST PSSNAKRQNQ LHPSSAQSRS GQPQKAATCK VSSINQETIQ 

      1270       1280       1290       1300       1310       1320 
TYCVEDTPIC FSRCSSLSSL SSAEDEIGCN QTTQEADSAN TLQIAEIKEK IGTRSAEDPV 

      1330       1340       1350       1360       1370       1380 
SEVPAVSQHP RTKSSRLQGS SLSSESARHK AVEFSSGAKS PSKSGAQTPK SPPEHYVQET 

      1390       1400       1410       1420       1430       1440 
PLMFSRCTSV SSLDSFESRS IASSVQSEPC SGMVSGIISP SDLPDSPGQT MPPSRSKTPP 

      1450       1460       1470       1480       1490       1500 
PPPQTAQTKR EVPKNKAPTA EKRESGPKQA AVNAAVQRVQ VLPDADTLLH FATESTPDGF 

      1510       1520       1530       1540       1550       1560 
SCSSSLSALS LDEPFIQKDV ELRIMPPVQE NDNGNETESE QPKESNENQE KEAEKTIDSE 

      1570       1580       1590       1600       1610       1620 
KDLLDDSDDD DIEILEECII SAMPTKSSRK AKKPAQTASK LPPPVARKPS QLPVYKLLPS 

      1630       1640       1650       1660       1670       1680 
QNRLQPQKHV SFTPGDDMPR VYCVEGTPIN FSTATSLSDL TIESPPNELA AGEGVRGGAQ 

      1690       1700       1710       1720       1730       1740 
SGEFEKRDTI PTEGRSTDEA QGGKTSSVTI PELDDNKAEE GDILAECINS AMPKGKSHKP 

      1750       1760       1770       1780       1790       1800 
FRVKKIMDQV QQASASSSAP NKNQLDGKKK KPTSPVKPIP QNTEYRTRVR KNADSKNNLN 

      1810       1820       1830       1840       1850       1860 
AERVFSDNKD SKKQNLKNNS KVFNDKLPNN EDRVRGSFAF DSPHHYTPIE GTPYCFSRND 

      1870       1880       1890       1900       1910       1920 
SLSSLDFDDD DVDLSREKAE LRKAKENKES EAKVTSHTEL TSNQQSANKT QAIAKQPINR 

      1930       1940       1950       1960       1970       1980 
GQPKPILQKQ STFPQSSKDI PDRGAATDEK LQNFAIENTP VCFSHNSSLS SLSDIDQENN 

      1990       2000       2010       2020       2030       2040 
NKENEPIKET EPPDSQGEPS KPQASGYAPK SFHVEDTPVC FSRNSSLSSL SIDSEDDLLQ 

      2050       2060       2070       2080       2090       2100 
ECISSAMPKK KKPSRLKGDN EKHSPRNMGG ILGEDLTLDL KDIQRPDSEH GLSPDSENFD 

      2110       2120       2130       2140       2150       2160 
WKAIQEGANS IVSSLHQAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT 

      2170       2180       2190       2200       2210       2220 
SNKGPRILKP GEKSTLETKK IESESKGIKG GKKVYKSLIT GKVRSNSEIS GQMKQPLQAN 

      2230       2240       2250       2260       2270       2280 
MPSISRGRTM IHIPGVRNSS SSTSPVSKKG PPLKTPASKS PSEGQTATTS PRGAKPSVKS 

      2290       2300       2310       2320       2330       2340 
ELSPVARQTS QIGGSSKAPS RSGSRDSTPS RPAQQPLSRP IQSPGRNSIS PGRNGISPPN 

      2350       2360       2370       2380       2390       2400 
KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQMSQQNLTK QTGLSKNASS IPRSESASKG 

      2410       2420       2430       2440       2450       2460 
LNQMNNGNGA NKKVELSRMS STKSSGSESD RSERPVLVRQ STFIKEAPSP TLRRKLEESA 

      2470       2480       2490       2500       2510       2520 
SFESLSPSSR PASPTRSQAQ TPVLSPSLPD MSLSTHSSVQ AGGWRKLPPN LSPTIEYNDG 

      2530       2540       2550       2560       2570       2580 
RPAKRHDIAR SHSESPSRLP INRSGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES 

      2590       2600       2610       2620       2630       2640 
SEKAKSEDEK HVNSISGTKQ SKENQVSAKG TWRKIKENEF SPTNSTSQTV SSGATNGAES 

      2650       2660       2670       2680       2690       2700 
KTLIYQMAPA VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKA NPNIKDSKDN 

      2710       2720       2730       2740       2750       2760 
QAKQNVGNGS VPMRTVGLEN RLNSFIQVDA PDQKGTEIKP GQNNPVPVSE TNESSIVERT 

      2770       2780       2790       2800       2810       2820 
PFSSSSSSKH SSPSGTVAAR VTPFNYNPSP RKSSADSTSA RPSQIPTPVN NNTKKRDSKT 

      2830       2840 
DSTESSGTQS PKRHSGSYLV TSV 

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Isoform Short [UniParc].

Checksum: 49CF92BE7A81EBEC
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FASTA2,742300,439

References

« Hide 'large scale' references
[1]"Identification of deletion mutations and three new genes at the familial polyposis locus."
Joslyn G., Carlson M., Thliveris A., Albertsen H., Gelbert L., Samowitz W., Groden J., Stevens J., Spirio L., Robertson M., Sargeant L., Krapcho K., Wolff E., Burt R., Hughes J.P., Warrington J., McPherson J.D., Wasmuth J.J. expand/collapse author list , le Paslier D., Abderrahim H., Cohen D., Leppert M., White R.
Cell 66:601-613(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), VARIANT ASP-1822.
Tissue: Fetal brain.
[2]"Identification of FAP locus genes from chromosome 5q21."
Kinzler K.W., Nilbert M.C., Su L.-K., Vogelstein B., Bryan T.M., Levy D.B., Smith K.J., Preisinger A.C., Hedge P., McKechnie D., Finniear R., Markham A., Groffen J., Boguski M.S., Altschul S.F., Horii A.K., Ando H., Miyoshi Y. expand/collapse author list , Miki Y., Nishisho I., Nakamura Y.
Science 253:661-665(1991) [PubMed] [Europe PMC] [Abstract]
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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients."
Nishisho I., Nakamura Y., Miyoshi Y., Miki Y., Ando H., Horii A., Koyama K., Utsunomiya J., Baba S., Hedge P., Markham A., Krush A.J., Petersen G.M., Hamilton S.R., Nilbert M.C., Levy D.B., Bryan T.M., Preisinger A.C. expand/collapse author list , Smith K.J., Su L.-K., Kinzler K.W., Vogelstein B.
Science 253:665-669(1991) [PubMed] [Europe PMC] [Abstract]
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]Erratum
Stella A., Montera M., Resta N., Marchese C., Susca F., Gentile M., Romio L., Pilia S., Prete F., Mareni C., Guanti G.
Hum. Mol. Genet. 3:1918-1918(1994)
[44]"The molecular basis of Turcot's syndrome."
Hamilton S.R., Liu B., Parsons R.E., Papadopoulos N., Jen J., Powell S.M., Krush A.J., Berk T., Cohen Z., Tetu B., Burger P.C., Wood P.A., Taqi F., Booker S.V., Petersen G.M., Offerhaus G.J.A., Tersmette A.C., Giardiello F.M., Vogelstein B., Kinzler K.W.
N. Engl. J. Med. 332:839-847(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MMRCS.
[45]"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.
[46]"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.
[47]"Drastic genetic instability of tumors and normal tissues in Turcot syndrome."
Miyaki M., Nishio J., Konishi M., Kikuchi-Yanoshita R., Tanaka K., Muraoka M., Nagato M., Chong J.-M., Koike M., Terada T., Kawahara Y., Fukutome A., Tomiyama J., Chuganji Y., Momoi M., Utsunomiya J.
Oncogene 15:2877-2881(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS COLORECTAL CARCINOMA THR-880; ILE-890 AND VAL-1508.
[48]"The APC I1307K allele and breast cancer risk."
Redston M., Nathanson K.L., Yuan Z.Q., Neuhausen S.L., Satagopan J., Wong N., Yang D., Nafa D., Abrahamson J., Ozcelik H., Antin-Ozerkis D., Andrulis I., Daly M., Pinsky L., Schrag D., Gallinger S., Kaback M., King M.-C. expand/collapse author list , Woodage T., Brody L.C., Godwin A., Warner E., Weber B., Foulkes W., Offit K.
Nat. Genet. 20:13-14(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-1307.
[49]"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.
[50]"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.
[51]"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.
[52]"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.
[53]"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.
[54]"APC mutations in sporadic medulloblastomas."
Huang H., Mahler-Araujo B.M., Sankila A., Chimelli L., Yonekawa Y., Kleihues P., Ohgaki H.
Am. J. Pathol. 156:433-437(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MDB VAL-1296; ILE-1472 AND GLY-1495.
[55]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-1254.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRRBHUAP. A37261.
RefSeqNP_000029.2. NM_000038.5.
NP_001120982.1. NM_001127510.2.
UniGeneHs.158932.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00519.
ProteinModelPortalP25054.
SMRP25054. Positions 2-55, 130-239, 326-736, 1485-1528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106821. 130 interactions.
DIPDIP-33556N.
IntActP25054. 118 interactions.
MINTMINT-88204.
STRING9606.ENSP00000257430.

PTM databases

PhosphoSiteP25054.

Polymorphism databases

DMDM97535708.

Proteomic databases

PaxDbP25054.
PRIDEP25054.

Protocols and materials databases

DNASU324.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257430; ENSP00000257430; ENSG00000134982. [P25054-1]
ENST00000457016; ENSP00000413133; ENSG00000134982. [P25054-1]
ENST00000508376; ENSP00000427089; ENSG00000134982. [P25054-1]
GeneID324.
KEGGhsa:324.
UCSCuc003kpy.4. human. [P25054-1]

Organism-specific databases

CTD324.
GeneCardsGC05P112101.
HGNCHGNC:583. APC.
HPACAB025994.
HPA013349.
MIM114550. phenotype.
135290. phenotype.
155255. phenotype.
175100. phenotype.
276300. phenotype.
611731. gene.
613659. phenotype.
neXtProtNX_P25054.
Orphanet247806. 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.
PharmGKBPA24875.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259696.
HOVERGENHBG004264.
InParanoidP25054.
KOK02085.
OMAIEDCPIN.
PhylomeDBP25054.
TreeFamTF106496.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000134982-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_578. Apoptosis.
SignaLinkP25054.

Gene expression databases

ArrayExpressP25054.
BgeeP25054.
CleanExHS_APC.
GenevestigatorP25054.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR026836. 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]
PANTHERPTHR12607. PTHR12607. 1 hit.
PTHR12607:SF2. PTHR12607:SF2. 1 hit.
PfamPF05972. 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]
SMARTSM00185. ARM. 6 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPC. human.
EvolutionaryTraceP25054.
GeneWikiAdenomatous_polyposis_coli.
GenomeRNAi324.
NextBio1329.
PROP25054.
SOURCESearch...

Entry information

Entry nameAPC_HUMAN
AccessionPrimary (citable) accession number: P25054
Secondary accession number(s): D3DT03 expand/collapse secondary AC list , Q15162, Q15163, Q93042
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 186 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM