P25054 (APC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenomatous polyposis coli protein
Short name=Protein APC

Alternative name(s):
Deleted in polyposis 2.5

Gene names

Name:	APC
Synonyms:	DP2.5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2843 AA.
Sequence status	Complete.
Protein existence	Evidence 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.21 Ref.22 Ref.24
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.20 Ref.26 Ref.28
Subcellular location	Cell junction › adherens junction. Cytoplasm › cytoskeleton. Cell projection › lamellipodium. Cell projection › ruffle 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.20 Ref.22 Ref.24
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.34
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.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.44 Ref.51 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.52 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.42 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 process	Wnt signaling pathway
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Tumor suppressor
Domain	Coiled coil Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell differentiation in thymus Inferred from electronic annotation. Source: Compara anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara axis specification Inferred from electronic annotation. Source: Compara axonogenesis Inferred from electronic annotation. Source: Compara canonical Wnt receptor signaling pathway Non-traceable author statement PubMed 11035805. Source: UniProtKB 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.22. Source: UniProtKB cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome chromosome organization Inferred from electronic annotation. Source: Compara cytokinesis after mitosis Inferred from mutant phenotype PubMed 17570218. Source: MGI cytoplasmic microtubule organization Inferred from electronic annotation. Source: Compara dorsal/ventral pattern formation Inferred from electronic annotation. Source: Compara hair follicle development Inferred from electronic annotation. Source: Compara kidney development Inferred from electronic annotation. Source: Compara metaphase/anaphase transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara mitotic spindle assembly checkpoint Inferred from mutant phenotype PubMed 17227893. Source: MGI muscle cell homeostasis Inferred from electronic annotation. Source: Compara negative regulation of MAPK cascade Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of canonical Wnt receptor 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: Compara negative regulation of microtubule depolymerization Inferred from direct assay PubMed 11166179. Source: UniProtKB negative regulation of odontogenesis Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from mutant phenotype PubMed 17227893. Source: MGI positive regulation of cell adhesion Inferred from electronic annotation. Source: Compara positive regulation of cell division Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from mutant phenotype PubMed 17192415. Source: MGI positive regulation of epithelial cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of microtubule polymerization Inferred from electronic annotation. Source: Compara 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: Compara regulation of attachment of spindle microtubules to kinetochore Non-traceable author statement PubMed 11283619. Source: UniProtKB regulation of nitrogen compound metabolic process Inferred from electronic annotation. Source: Compara regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara regulation of osteoclast differentiation Inferred from electronic annotation. Source: Compara response to DNA damage stimulus Inferred from direct assay PubMed 14728717. Source: UniProtKB retina development in camera-type eye Inferred from electronic annotation. Source: Compara skin development Inferred from electronic annotation. Source: Compara somatic stem cell maintenance Inferred from electronic annotation. Source: Compara thymus development Inferred from electronic annotation. Source: Compara tight junction assembly Non-traceable author statement PubMed 18502210. Source: UniProtKB
Cellular_component	adherens junction Inferred from electronic annotation. Source: UniProtKB-SubCell axonal growth cone Inferred from electronic annotation. Source: Compara beta-catenin destruction complex Inferred from direct assay PubMed 16188939PubMed 9601641. Source: UniProtKB centrosome Inferred from direct assay PubMed 11283619. Source: UniProtKB cytoplasmic microtubule Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome kinetochore Inferred from direct assay PubMed 11283619. Source: UniProtKB lamellipodium Inferred from direct assay Ref.22. Source: UniProtKB lateral plasma membrane Inferred from direct assay PubMed 12072559. Source: MGI microtubule plus end Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 11035805PubMed 12955080. Source: UniProtKB ruffle membrane Inferred from direct assay Ref.22. Source: UniProtKB tight junction Inferred from direct assay PubMed 18502210. Source: UniProtKB
Molecular_function	microtubule plus-end binding Inferred from direct assay Ref.20. Source: UniProtKB protein kinase regulator activity Inferred from direct assay PubMed 11972058. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTNNB1	P35222	7	EBI-727707,EBI-491549
Ctnnb1	Q02248	8	EBI-727707,EBI-397872	From a different organism.
MAPRE1	Q15691	4	EBI-727707,EBI-1004115

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2843

2843

Adenomatous polyposis coli protein

PRO_0000064627

Regions

Repeat

453 – 495

43

ARM 1

Repeat

505 – 547

43

ARM 2

Repeat

548 – 591

44

ARM 3

Repeat

592 – 638

47

ARM 4

Repeat

639 – 683

45

ARM 5

Repeat

684 – 725

42

ARM 6

Repeat

726 – 767

42

ARM 7

Region

960 – 1337

378

Responsible for down-regulation through a process mediated by direct ubiquitination

Region

1866 – 1893

28

Highly charged

Coiled coil

1 – 61

61

Potential

Coiled coil

127 – 248

122

Potential

Motif

2803 – 2806

4

Microtubule tip localization signal

Motif

2841 – 2843

3

PDZ-binding

Compositional bias

1 – 730

730

Leu-rich

Compositional bias

731 – 2832

2102

Ser-rich

Compositional bias

1131 – 1156

26

Asp/Glu-rich (acidic)

Compositional bias

1558 – 1577

20

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

744

1

Phosphoserine Ref.25

Modified residue

780

1

Phosphoserine Ref.19 Ref.25

Modified residue

1038

1

Phosphoserine By similarity

Modified residue

1042

1

Phosphoserine Ref.19

Modified residue

1180

1

Phosphoserine By similarity

Modified residue

1360

1

Phosphoserine Ref.19

Modified residue

1371

1

Phosphoserine By similarity

Modified residue

1559

1

Phosphoserine By similarity

Modified residue

1697

1

Phosphothreonine By similarity

Modified residue

1861

1

Phosphoserine Ref.19 Ref.27

Modified residue

1863

1

Phosphoserine Ref.19 Ref.27

Modified residue

1864

1

Phosphoserine Ref.19 Ref.27

Modified residue

2151

1

Phosphothreonine Ref.19

Modified residue

2260

1

Phosphoserine Ref.19

Modified residue

2270

1

Phosphoserine Ref.19

Modified residue

2283

1

Phosphoserine Ref.19

Modified residue

2473

1

Phosphoserine Ref.19

Modified residue

2535

1

Phosphoserine Ref.19

Modified residue

2671

1

Phosphoserine Ref.18 Ref.19

Modified residue

2674

1

Phosphoserine Ref.19

Modified residue

2679

1

Phosphothreonine Ref.19

Modified residue

2789

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

312 – 412

101

Missing in isoform Short.

VSP_004115

Natural variant

99

1

R → W in FAP; could be a rare polymorphism. Ref.39

VAR_009613

Natural variant

171

1

S → I in FAP. Ref.44

VAR_005032

Natural variant

414

1

R → C in FAP.

VAR_005033

Natural variant

722

1

S → G in FAP. Ref.40

VAR_009614

Natural variant

784

1

S → T in FAP.

VAR_005034

Natural variant

817

1

G → C in gastric cancer.

VAR_005035

Natural variant

870

1

P → S.
Corresponds to variant rs33974176 [ dbSNP | Ensembl ].

VAR_053976

Natural variant

880

1

I → T in colorectal carcinoma and gastric cancer; from a patient with MMRCS. Ref.45

VAR_005036

Natural variant

890

1

V → I in colorectal carcinoma; from a patient with MMRCS. Ref.45

VAR_012975

Natural variant

906

1

S → Y in colorectal tumor.

VAR_005037

Natural variant

911

1

E → G in FAP and colorectal tumor.

VAR_005038

Natural variant

942

1

N → D in gastric cancer.

VAR_005039

Natural variant

1027

1

Y → C in colorectal tumor.

VAR_005040

Natural variant

1057

1

E → G in non-FAP; unknown pathological significance. Ref.50

VAR_009615

Natural variant

1118

1

N → D. Ref.38

VAR_005041

Natural variant

1120

1

G → E in gastric cancer.
Corresponds to variant rs28933379 [ dbSNP | Ensembl ].

VAR_005042

Natural variant

1171

1

R → C. Ref.50

VAR_008992

Natural variant

1171

1

R → H in gastric cancer.

VAR_005043

Natural variant

1176

1

P → L in FAP.

VAR_005044

Natural variant

1184

1

A → P in FAP. Ref.51

VAR_009616

Natural variant

1197

1

F → S in gastric cancer.

VAR_005045

Natural variant

1254

1

I → F in a colorectal cancer sample; somatic mutation. Ref.53

VAR_035794

Natural variant

1259

1

I → T in gastric cancer.

VAR_005046

Natural variant

1292

1

T → M. Ref.38

VAR_005047

Natural variant

1296

1

A → V in MDB; sporadic. Ref.52

VAR_017653

Natural variant

1304

1

I → V. Ref.38

VAR_005048

Natural variant

1307

1

I → K in 6% of Ashkenazi Jews; associated with slightly increased risk of colon and breast cancer. Ref.46 Ref.47 Ref.48 Ref.49
Corresponds to variant rs1801155 [ dbSNP | Ensembl ].

VAR_005049

Natural variant

1312

1

G → E in gastric cancer.

VAR_005050

Natural variant

1313

1

T → A in FAP and colorectal tumor.

VAR_005051

Natural variant

1317

1

E → Q May contribute to colorectal tumor development. Ref.47
Corresponds to variant rs1801166 [ dbSNP | Ensembl ].

VAR_009617

Natural variant

1326

1

V → A in gastric cancer.

VAR_005052

Natural variant

1348

1

R → W in FAP. Ref.38

VAR_005053

Natural variant

1395

1

S → C in hepatoblastoma. Ref.43

VAR_065133

Natural variant

1422

1

D → H in colorectal tumor.

VAR_005054

Natural variant

1472

1

V → I in MDB; sporadic. Ref.52

VAR_017654

Natural variant

1495

1

S → G in MDB; sporadic. Ref.52

VAR_017655

Natural variant

1496

1

T → S.
Corresponds to variant rs2229996 [ dbSNP | Ensembl ].

VAR_020141

Natural variant

1508

1

A → V in colorectal carcinoma from a patient with MMRCS. Ref.45

VAR_012976

Natural variant

1822

1

V → D. Ref.1 Ref.2 Ref.4 Ref.50
Corresponds to variant rs459552 [ dbSNP | Ensembl ].

VAR_008993

Natural variant

1882

1

R → T.
Corresponds to variant rs34157245 [ dbSNP | Ensembl ].

VAR_053977

Natural variant

1973

1

S → T.
Corresponds to variant rs4987109 [ dbSNP | Ensembl ].

VAR_020142

Natural variant

2499

1

V → L.
Corresponds to variant rs33941929 [ dbSNP | Ensembl ].

VAR_053978

Natural variant

2502

1

G → S. Ref.38
Corresponds to variant rs2229995 [ dbSNP | Ensembl ].

VAR_005055

Natural variant

2621

1

S → C in FAP.

VAR_005056

Natural variant

2738

1

I → T. Ref.50

VAR_008994

Natural variant

2839

1

L → F in FAP.

VAR_005057

Experimental info

Mutagenesis

2841

1

T → L: Loss of interaction with SCRIB. Ref.15

Mutagenesis

2843

1

V → Q: Loss of interaction with SCRIB. Ref.15

Sequence conflict

184

1

M → L in AAA60353. Ref.1

Sequence conflict

184

1

M → L in AAA60354. Ref.1

Sequence conflict

970

1

S → N in AAA60353. Ref.1

Sequence conflict

970

1

S → N in AAA60354. Ref.1

Sequence conflict

1309

1

E → G in AAA60353. Ref.1

Sequence conflict

1309

1

E → G in AAA60354. Ref.1

Sequence conflict

1325 – 1331

7

AVSQHPR → SSVHSTLE in AAA60353. Ref.1

Sequence conflict

1325 – 1331

7

AVSQHPR → SSVHSTLE in AAA60354. Ref.1

Sequence conflict

1355

1

S → P in AAA60353. Ref.1

Sequence conflict

1355

1

S → P in AAA60354. Ref.1

Sequence conflict

1591

1

A → G in AAA60353. Ref.1

Sequence conflict

1591

1

A → G in AAA60354. Ref.1

Sequence conflict

2723

1

N → T in AAA60353. Ref.1

Sequence conflict

2723

1

N → T in AAA60354. Ref.1

Sequence conflict

2755

1

S → P in AAA60353. Ref.1

Sequence conflict

2755

1

S → P in AAA60354. Ref.1

Secondary structure

1

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2843

Helix Strand Turn

Details...

Helix

6 – 53

48

Helix

132 – 169

38

Helix

180 – 204

25

Helix

208 – 238

31

Helix

328 – 338

11

Helix

343 – 350

8

Helix

353 – 360

8

Helix

377 – 393

17

Helix

407 – 425

19

Beta strand

429 – 431

3

Helix

433 – 435

3

Helix

441 – 444

4

Helix

446 – 457

12

Helix

460 – 468

9

Helix

471 – 486

16

Helix

492 – 508

17

Helix

513 – 521

9

Helix

523 – 531

9

Helix

532 – 534

3

Helix

538 – 552

15

Helix

557 – 565

9

Helix

568 – 578

11

Helix

582 – 596

15

Helix

600 – 608

9

Helix

612 – 619

8

Beta strand

625 – 627

3

Helix

630 – 646

17

Helix

650 – 657

8

Turn

658 – 660

3

Helix

661 – 668

8

Helix

674 – 687

14

Helix

692 – 700

9

Helix

703 – 708

6

Turn

709 – 712

4

Helix

716 – 730

15

Helix

735 – 737

3

Turn

1027 – 1030

4

Helix

1470 – 1479

10

Helix

1520 – 1524

5

Helix

2036 – 2045

10

Beta strand

2840 – 2842

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified May 16, 2006. Version 2. Checksum: 77E194AE4A91DC5A	FASTA	2,843	311,646
	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
	Isoform Short [UniParc]. Checksum: 49CF92BE7A81EBEC	FASTA	2,742	300,439
	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 KIRAYCETCW EWQEAHEPGM DQDKNPMPAP VEHQICPAVC VLMKLSFDEE 370 380 390 400 410 420 HRHAMNELGG LQAIAELLQV DCEMYGLTND HYSITLRRYA GMALTNLTFG DVANKATLCS 430 440 450 460 470 480 MKGCMRALVA QLKSESEDLQ QVIASVLRNL SWRADVNSKK TLREVGSVKA LMECALEVKK 490 500 510 520 530 540 ESTLKSVLSA LWNLSAHCTE NKADICAVDG ALAFLVGTLT YRSQTNTLAI IESGGGILRN 550 560 570 580 590 600 VSSLIATNED HRQILRENNC LQTLLQHLKS HSLTIVSNAC GTLWNLSARN PKDQEALWDM 610 620 630 640 650 660 GAVSMLKNLI HSKHKMIAMG SAAALRNLMA NRPAKYKDAN IMSPGSSLPS LHVRKQKALE 670 680 690 700 710 720 AELDAQHLSE TFDNIDNLSP KASHRSKQRH KQSLYGDYVF DTNRHDDNRS DNFNTGNMTV 730 740 750 760 770 780 LSPYLNTTVL PSSSSSRGSL DSSRSEKDRS LERERGIGLG NYHPATENPG TSSKRGLQIS 790 800 810 820 830 840 TTAAQIAKVM EEVSAIHTSQ EDRSSGSTTE LHCVTDERNA LRRSSAAHTH SNTYNFTKSE 850 860 870 880 890 900 NSNRTCSMPY AKLEYKRSSN DSLNSVSSSD GYGKRGQMKP SIESYSEDDE SKFCSYGQYP 910 920 930 940 950 960 ADLAHKIHSA NHMDDNDGEL DTPINYSLKY SDEQLNSGRQ SPSQNERWAR PKHIIEDEIK 970 980 990 1000 1010 1020 QSEQRQSRNQ STTYPVYTES TDDKHLKFQP HFGQQECVSP YRSRGANGSE TNRVGSNHGI 1030 1040 1050 1060 1070 1080 NQNVSQSLCQ EDDYEDDKPT NYSERYSEEE QHEEEERPTN YSIKYNEEKR HVDQPIDYSL 1090 1100 1110 1120 1130 1140 KYATDIPSSQ KQSFSFSKSS SGQSSKTEHM SSSSENTSTP SSNAKRQNQL HPSSAQSRSG 1150 1160 1170 1180 1190 1200 QPQKAATCKV SSINQETIQT YCVEDTPICF SRCSSLSSLS SAEDEIGCNQ TTQEADSANT 1210 1220 1230 1240 1250 1260 LQIAEIKEKI GTRSAEDPVS EVPAVSQHPR TKSSRLQGSS LSSESARHKA VEFSSGAKSP 1270 1280 1290 1300 1310 1320 SKSGAQTPKS PPEHYVQETP LMFSRCTSVS SLDSFESRSI ASSVQSEPCS GMVSGIISPS 1330 1340 1350 1360 1370 1380 DLPDSPGQTM PPSRSKTPPP PPQTAQTKRE VPKNKAPTAE KRESGPKQAA VNAAVQRVQV 1390 1400 1410 1420 1430 1440 LPDADTLLHF ATESTPDGFS CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETESEQ 1450 1460 1470 1480 1490 1500 PKESNENQEK EAEKTIDSEK DLLDDSDDDD IEILEECIIS AMPTKSSRKA KKPAQTASKL 1510 1520 1530 1540 1550 1560 PPPVARKPSQ LPVYKLLPSQ NRLQPQKHVS FTPGDDMPRV YCVEGTPINF STATSLSDLT 1570 1580 1590 1600 1610 1620 IESPPNELAA GEGVRGGAQS GEFEKRDTIP TEGRSTDEAQ GGKTSSVTIP ELDDNKAEEG 1630 1640 1650 1660 1670 1680 DILAECINSA MPKGKSHKPF RVKKIMDQVQ QASASSSAPN KNQLDGKKKK PTSPVKPIPQ 1690 1700 1710 1720 1730 1740 NTEYRTRVRK NADSKNNLNA ERVFSDNKDS KKQNLKNNSK VFNDKLPNNE DRVRGSFAFD 1750 1760 1770 1780 1790 1800 SPHHYTPIEG TPYCFSRNDS LSSLDFDDDD VDLSREKAEL RKAKENKESE AKVTSHTELT 1810 1820 1830 1840 1850 1860 SNQQSANKTQ AIAKQPINRG QPKPILQKQS TFPQSSKDIP DRGAATDEKL QNFAIENTPV 1870 1880 1890 1900 1910 1920 CFSHNSSLSS LSDIDQENNN KENEPIKETE PPDSQGEPSK PQASGYAPKS FHVEDTPVCF 1930 1940 1950 1960 1970 1980 SRNSSLSSLS IDSEDDLLQE CISSAMPKKK KPSRLKGDNE KHSPRNMGGI LGEDLTLDLK 1990 2000 2010 2020 2030 2040 DIQRPDSEHG LSPDSENFDW KAIQEGANSI VSSLHQAAAA ACLSRQASSD SDSILSLKSG 2050 2060 2070 2080 2090 2100 ISLGSPFHLT PDQEEKPFTS NKGPRILKPG EKSTLETKKI ESESKGIKGG KKVYKSLITG 2110 2120 2130 2140 2150 2160 KVRSNSEISG QMKQPLQANM PSISRGRTMI HIPGVRNSSS STSPVSKKGP PLKTPASKSP 2170 2180 2190 2200 2210 2220 SEGQTATTSP RGAKPSVKSE LSPVARQTSQ IGGSSKAPSR SGSRDSTPSR PAQQPLSRPI 2230 2240 2250 2260 2270 2280 QSPGRNSISP GRNGISPPNK LSQLPRTSSP STASTKSSGS GKMSYTSPGR QMSQQNLTKQ 2290 2300 2310 2320 2330 2340 TGLSKNASSI PRSESASKGL NQMNNGNGAN KKVELSRMSS TKSSGSESDR SERPVLVRQS 2350 2360 2370 2380 2390 2400 TFIKEAPSPT LRRKLEESAS FESLSPSSRP ASPTRSQAQT PVLSPSLPDM SLSTHSSVQA 2410 2420 2430 2440 2450 2460 GGWRKLPPNL SPTIEYNDGR PAKRHDIARS HSESPSRLPI NRSGTWKREH SKHSSSLPRV 2470 2480 2490 2500 2510 2520 STWRRTGSSS SILSASSESS EKAKSEDEKH VNSISGTKQS KENQVSAKGT WRKIKENEFS 2530 2540 2550 2560 2570 2580 PTNSTSQTVS SGATNGAESK TLIYQMAPAV SKTEDVWVRI EDCPINNPRS GRSPTGNTPP 2590 2600 2610 2620 2630 2640 VIDSVSEKAN PNIKDSKDNQ AKQNVGNGSV PMRTVGLENR LNSFIQVDAP DQKGTEIKPG 2650 2660 2670 2680 2690 2700 QNNPVPVSET NESSIVERTP FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR 2710 2720 2730 2740 PSQIPTPVNN NTKKRDSKTD STESSGTQSP KRHSGSYLVT SV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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.
[27]	"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, MASS SPECTROMETRY.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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. , Smith K.J., Su L.-K., Kinzler K.W., Vogelstein B. Science 253:665-669(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FAP.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	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)
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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. , 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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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. , 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

Colon cancer gene variant databases Adenomatous Polyposis Coli (APC)

Leiden Open Variation Database (LOVD)

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

APC entry

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.

IPI

IPI00012391.
IPI00215877.

PIR

RBHUAP. A37261.

RefSeq

NP_000029.2. NM_000038.5.
NP_001120982.1. NM_001127510.2.

UniGene

Hs.158932.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

DisProt

DP00519.

ProteinModelPortal

P25054.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33556N.

IntAct

P25054. 97 interactions.

MINT

MINT-88204.

STRING

9606.ENSP00000257430.

PTM databases

PhosphoSite

P25054.

Polymorphism databases

DMDM

97535708.

Proteomic databases

PaxDb

P25054.

PRIDE

P25054.

Protocols and materials databases

DNASU

324.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000257430; ENSP00000257430; ENSG00000134982.
ENST00000457016; ENSP00000413133; ENSG00000134982.
ENST00000508376; ENSP00000427089; ENSG00000134982.

GeneID

324.

KEGG

hsa:324.

UCSC

uc003kpy.4. human.

Organism-specific databases

CTD

324.

GeneCards

GC05P112101.

HGNC

HGNC:583. APC.

HPA

CAB025994.
HPA013349.

MIM

114550. phenotype.
135290. phenotype.
155255. phenotype.
175100. phenotype.
276300. phenotype.
611731. gene.
613659. phenotype.

neXtProt

NX_P25054.

Orphanet

247806. APC-related attenuated familial adenomatous polyposis.
873. Desmoid disease.
261584. Familial adenomatous polyposis due to 5q22.2 microdeletion.
79665. Gardner syndrome.
99818. Turcot syndrome with polyposis.

PharmGKB

PA24875.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG259696.

HOVERGEN

HBG004264.

InParanoid

P25054.

KO

K02085.

OMA

IEDCPIN.

PhylomeDB

P25054.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000134982-MONOMER.

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.
ps1pathway. Presenilin action in Notch and Wnt signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_578. Apoptosis.

SignaLink

P25054.

Gene expression databases

ArrayExpress

P25054.

Bgee

P25054.

CleanEx

HS_APC.

Genevestigator

P25054.

GermOnline

ENSG00000134982. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 2 hits.

InterPro

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]

PANTHER

PTHR12607. PTHR12607. 1 hit.
PTHR12607:SF2. PTHR12607:SF2. 1 hit.

Pfam

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]

SMART

SM00185. ARM. 6 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50176. ARM_REPEAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3233.

ChiTaRS

APC. human.

EvolutionaryTrace

P25054.

GenomeRNAi

324.

NextBio

1329.

SOURCE

Search...

Entry information

Entry name

APC_HUMAN

Accession

Primary (citable) accession number: P25054
Secondary accession number(s): D3DT03 , Q15162, Q15163, Q93042

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 16, 2006
Last modified:	May 29, 2013
This is version 176 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.