Reviewed, UniProtKB/Swiss-Prot P25054 (APC_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2843 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Ref.3
Subunit structure	Forms homooligomers. Interacts with DIAPH1 and DIAPH2 By similarity. Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with the N-terminus of ARHGEF4, and the C-terminus of MAPRE1, MAPRE2 and MAPRE3. Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with APC2. Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells.
Subcellular location	Cell junction › adherens junction. Ref.3 Ref.14
Tissue specificity	Expressed in a variety of tissues.
Post-translational modification	Phosphorylated by GSK3B. Ref.13 Ref.15 Ref.17 Ref.18 Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID. Ref.12 Ref.16
Involvement in disease	Defects in APC are a cause of familial adenomatous polyposis (FAP) [MIM:175100]; which includes also Gardner syndrome (GS). FAP and GS contribute to tumor development in patients with uninherited forms of colorectal cancer. FAP is 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. Ref.6 Ref.9 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.31 Ref.37 Ref.38 Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:135290]; also known as familial infiltrative fibromatosis (FIF). HDD is an 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. Ref.6 Ref.9 Defects in APC are a cause of medulloblastoma (MDB) [MIM:155255]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome). Ref.6 Ref.9 Ref.39 Defects in APC are a cause of mismatch repair cancer syndrome (MMRCS) [MIM:276300]; also known as Turcot syndrome or brain tumor-polyposis syndrome 1 (BTPS1). MMRCS is an 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. Ref.6 Ref.9 Ref.30
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
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
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway through beta-catenin Non-traceable author statement. Source: UniProtKB cell adhesion Non-traceable author statement. Source: UniProtKB cell cycle arrest Inferred from direct assay. Source: UniProtKB cytokinesis after mitosis Inferred from mutant phenotype. Source: MGI mitotic cell cycle spindle assembly checkpoint Inferred from mutant phenotype. Source: MGI negative regulation of cyclin-dependent protein kinase activity Inferred from direct assay. Source: UniProtKB negative regulation of microtubule depolymerization Inferred from direct assay. Source: UniProtKB positive regulation of apoptosis Inferred from mutant phenotype. Source: MGI positive regulation of cell migration Inferred from mutant phenotype. Source: MGI positive regulation of pseudopodium assembly Inferred from mutant phenotype. Source: MGI protein complex assembly Inferred from direct assay. Source: UniProtKB regulation of attachment of spindle microtubules to kinetochore Non-traceable author statement. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay. Source: UniProtKB tight junction assembly Non-traceable author statement. Source: UniProtKB
Cellular component	Axin-APC-beta-catenin-GSK3B complex Inferred from direct assay. Source: UniProtKB beta-catenin destruction complex Inferred from direct assay. Source: UniProtKB centrosome Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome kinetochore Inferred from direct assay. Source: UniProtKB lateral plasma membrane Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: UniProtKB tight junction Inferred from direct assay. Source: UniProtKB
Molecular function	beta-catenin binding Inferred from physical interaction. Source: UniProtKB microtubule binding Inferred from direct assay. Source: UniProtKB protein kinase binding Inferred from physical interaction. Source: UniProtKB protein kinase regulator activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSNK1E	P49674	1	EBI-727707,EBI-749343
Ctnnb1	Q02248	3	EBI-727707,EBI-397872	From a different organism.
MAPRE1	Q15691	3	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

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

780

1

Phosphoserine Ref.18

Modified residue

1038

1

Phosphoserine By similarity

Modified residue

1042

1

Phosphoserine Ref.18

Modified residue

1180

1

Phosphoserine By similarity

Modified residue

1360

1

Phosphoserine Ref.18

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.13 Ref.18

Modified residue

1863

1

Phosphoserine Ref.13 Ref.18

Modified residue

1864

1

Phosphoserine Ref.13 Ref.18

Modified residue

2088

1

Phosphoserine Ref.18

Modified residue

2093

1

Phosphoserine Ref.18

Modified residue

2096

1

Phosphoserine Ref.18

Modified residue

2125

1

Phosphoserine Ref.17

Modified residue

2143

1

Phosphoserine Ref.18

Modified residue

2151

1

Phosphothreonine Ref.18

Modified residue

2260

1

Phosphoserine Ref.18

Modified residue

2270

1

Phosphoserine Ref.18

Modified residue

2283

1

Phosphoserine Ref.15 Ref.18

Modified residue

2398

1

Phosphoserine Ref.13

Modified residue

2464

1

Phosphoserine Ref.18

Modified residue

2469

1

Phosphoserine Ref.18

Modified residue

2473

1

Phosphoserine Ref.18

Modified residue

2533

1

Phosphoserine Ref.18

Modified residue

2535

1

Phosphoserine Ref.18

Modified residue

2671

1

Phosphoserine Ref.17 Ref.18

Modified residue

2674

1

Phosphoserine Ref.17 Ref.18

Modified residue

2676

1

Phosphothreonine Ref.17

Modified residue

2679

1

Phosphothreonine Ref.18

Modified residue

2710

1

Phosphoserine By similarity

Modified residue

2789

1

Phosphoserine Ref.17 Ref.18

Modified residue

2835

1

Phosphoserine Ref.17

Modified residue

2837

1

Phosphoserine Ref.17

Modified residue

2838

1

Phosphotyrosine Ref.17

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.27

VAR_009613

Natural variant

171

1

S → I in FAP. Ref.31

VAR_005032

Natural variant

414

1

R → C in FAP.

VAR_005033

Natural variant

722

1

S → G in FAP. Ref.28

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: dbSNP rs33974176.

VAR_053976

Natural variant

880

1

I → T in colorectal carcinoma and gastric cancer; from a patient with MMRCS. Ref.32

VAR_005036

Natural variant

890

1

V → I in colorectal carcinoma; from a patient with MMRCS. Ref.32

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. Ref.37

VAR_009615

Natural variant

1118

1

N → D

VAR_005041

Natural variant

1120

1

G → E in gastric cancer.

VAR_005042

Natural variant

1171

1

R → C in FAP; could be a polymorphism. Ref.37

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.38

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.40

VAR_035794

Natural variant

1259

1

I → T in gastric cancer.

VAR_005046

Natural variant

1292

1

T → M

VAR_005047

Natural variant

1296

1

A → V in MDB; sporadic. Ref.39

VAR_017653

Natural variant

1304

1

I → V

VAR_005048

Natural variant

1307

1

I → K in 6% of Ashkenazi Jews; associated with slightly increased risk of colon and breast cancer. dbSNP rs1801155. Ref.33 Ref.34 Ref.35 Ref.36

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. dbSNP rs1801166. Ref.34

VAR_009617

Natural variant

1326

1

V → A in gastric cancer.

VAR_005052

Natural variant

1348

1

R → W in FAP. Ref.26

VAR_005053

Natural variant

1422

1

D → H in colorectal tumor.

VAR_005054

Natural variant

1472

1

V → I in MDB; sporadic. Ref.39

VAR_017654

Natural variant

1495

1

S → G in MDB; sporadic. Ref.39

VAR_017655

Natural variant

1496

1

T → S: dbSNP rs2229996.

VAR_020141

Natural variant

1508

1

A → V in colorectal carcinoma from a patient with MMRCS. Ref.32

VAR_012976

Natural variant

1822

1

V → D: dbSNP rs459552. Ref.37 Ref.1 Ref.2

VAR_008993

Natural variant

1882

1

R → T: dbSNP rs34157245.

VAR_053977

Natural variant

1973

1

S → T: dbSNP rs4987109.

VAR_020142

Natural variant

2499

1

V → L: dbSNP rs33941929.

VAR_053978

Natural variant

2502

1

G → S: dbSNP rs2229995. Ref.26

VAR_005055

Natural variant

2621

1

S → C in FAP.

VAR_005056

Natural variant

2738

1

I → T in FAP. Ref.37

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.14

Mutagenesis

2843

1

V → Q: Loss of interaction with SCRIB. Ref.14

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

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2843

Helix Strand Turn

Details...

Helix

6 – 53

48

Helix

132 – 169

38

Helix

180 – 204

25

Helix

208 – 238

31

Turn

1027 – 1030

4

Helix

1470 – 1479

10

Helix

1520 – 1524

5

Helix

2036 – 2045

10

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. 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: 1678319] [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: 1651562] [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: 10947987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARHGEF4, IDENTIFICATION IN A COMPLEX WITH ARHGEF4 AND CTNNB1.
[4]	"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: 1310068] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1506-1524.
[5]	"Association of the APC tumor suppressor protein with catenins." Su L.-K., Vogelstein B., Kinzler K.W. Science 262:1734-1737(1993) [PubMed: 8259519] [Abstract] Cited for: ASSOCIATION WITH CATENINS.
[6]	"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: 8940264] [Abstract] Cited for: INVOLVEMENT IN HEREDITARY DESMOID DISEASE.
[7]	"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: 8638125] [Abstract] Cited for: INTERACTION WITH DLG1.
[8]	"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: 9188857] [Abstract] Cited for: INTERACTION WITH DLG3. Tissue: Fetal brain.
[9]	"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: 10782927] [Abstract] Cited for: INVOLVEMENT IN HEREDITARY DESMOID DISEASE.
[10]	"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: 11691822] [Abstract] Cited for: INTERACTION WITH APC2.
[11]	"Characterization of functional domains of human EB1 family proteins." Bu W., Su L.-K. J. Biol. Chem. 278:49721-49731(2003) [PubMed: 14514668] [Abstract] Cited for: INTERACTION WITH MAPRE1; MAPRE2 AND MAPRE3.
[12]	"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: 15355978] [Abstract] Cited for: UBIQUITINATION.
[13]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1861; SER-1863; SER-1864 AND SER-2398, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"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: 16611247] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SCRIB, MUTAGENESIS OF THR-2841 AND VAL-2843.
[15]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2283, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"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: 18281465] [Abstract] Cited for: DEUBIQUITINATION.
[17]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2125; SER-2671; SER-2674; THR-2676; SER-2789; SER-2835; SER-2837 AND TYR-2838, MASS SPECTROMETRY.
[18]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780; SER-1042; SER-1360; SER-1861; SER-1863; SER-1864; SER-2088; SER-2093; SER-2096; SER-2143; THR-2151; SER-2260; SER-2270; SER-2283; SER-2464; SER-2469; SER-2473; SER-2533; SER-2535; SER-2671; SER-2674; THR-2679 AND SER-2789, MASS SPECTROMETRY.
[19]	"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: 10926498] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-55.
[20]	"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: 11707392] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1021-1035 IN COMPLEX WITH CTNNB1.
[21]	"Structural basis of the axin-adenomatous polyposis coli interaction." Spink K.E., Polakis P., Weis W.I. EMBO J. 19:2270-2279(2000) [PubMed: 10811618] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2034-2049 IN COMPLEX WITH AXIN.
[22]	"Mutations of the APC (adenomatous polyposis coli) gene." Nagase H., Nakamura Y. Hum. Mutat. 2:425-434(1993) [PubMed: 8111410] [Abstract] Cited for: REVIEW ON VARIANTS.
[23]	"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: 1651563] [Abstract] Cited for: VARIANTS FAP.
[24]	"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: 1338904] [Abstract] Cited for: VARIANTS FAP.
[25]	"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: 1338691] [Abstract] Cited for: VARIANTS FAP.
[26]	"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: 1338764] [Abstract] Cited for: VARIANT FAP TRP-1348, VARIANTS ASP-1118; MET-1292; VAL-1304 AND SER-2502.
[27]	"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: 7833149] [Abstract] Cited for: VARIANT FAP TRP-99. Tissue: Peripheral blood lymphocyte.
[28]	"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: 7833931] [Abstract] Cited for: VARIANT FAP GLY-722.
[29]	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)
[30]	"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: 7661930] [Abstract] Cited for: INVOLVEMENT IN MMRCS.
[31]	"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: 8990002] [Abstract] Cited for: VARIANT FAP ILE-171.
[32]	"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: 9419979] [Abstract] Cited for: VARIANTS COLORECTAL CARCINOMA THR-880; ILE-890 AND VAL-1508.
[33]	"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: 9731522] [Abstract] Cited for: VARIANT LYS-1307.
[34]	"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: 9724771] [Abstract] Cited for: VARIANTS LYS-1307 AND GLN-1317. Tissue: Peripheral blood.
[35]	"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: 9731533] [Abstract] Cited for: VARIANT LYS-1307.
[36]	"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: 9973276] [Abstract] Cited for: VARIANT LYS-1307.
[37]	"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: 9950360] [Abstract] Cited for: VARIANTS FAP CYS-1171 AND THR-2738, VARIANTS GLY-1057 AND ASP-1822.
[38]	"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: 10470088] [Abstract] Cited for: VARIANT FAP PRO-1184.
[39]	"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: 10666372] [Abstract] Cited for: VARIANTS MDB VAL-1296; ILE-1472 AND GLY-1495.
[40]	"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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-1254.
+	Additional computationally mapped references.

Web resources

APC

Information about APC mutations

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneDis

Familial adenomatous polyposis (FAP) website

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

APC entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

M73548 mRNA. Translation: AAA60353.1.
M73548 mRNA. Translation: AAA60354.1.
M74088 mRNA. Translation: AAA03586.1.
S78214 Genomic DNA. Translation: AAB21145.2. Sequence problems.

IPI

IPI00012391.
IPI00215877.

PIR

RBHUAP. A37261.

RefSeq

NP_000029.2.
NP_001120982.1.
NP_001120983.1.

UniGene

Hs.158932

3D structure databases

PDBPDBe

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	[»]

DisProt

DP00519.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25054. 14 interactions.

STRING

P25054.

PTM databases

PhosphoSite

P25054.

Proteomic databases

PRIDE

P25054.

Genome annotation databases

Ensembl

ENST00000257430; ENSP00000257430; ENSG00000134982; Homo sapiens. [Genome view]
ENST00000395617; ENSP00000378979; ENSG00000134982; Homo sapiens. [Genome view]
ENST00000457016; ENSP00000413133; ENSG00000134982; Homo sapiens. [Genome view]

GeneID

324.

KEGG

hsa:324.

UCSC

uc003kpy.2. human.

Organism-specific databases

CTD

324.

GeneCards

GC05P112101.

H-InvDB

HIX0031955.

HGNC

HGNC:583. APC.

HPA

CAB025994.
HPA013349.

MIM

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

Orphanet

873. Desmoid disease.
733. Familial adenomatous polyposis.
79665. Gardner syndrome.
616. Medulloblastoma.
99818. Turcot syndrome with polyposis.

PharmGKB

PA24875.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P25054.

OMA

FATESTP.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_11045. Signaling by Wnt.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P25054.

Bgee

P25054.

CleanEx

HS_APC.

Genevestigator

P25054.

GermOnline

ENSG00000134982. Homo sapiens.

Family and domain databases

InterPro

IPR009240. APC_15aa.
IPR009234. APC_basic.
IPR009223. APC_crr.
IPR011989. ARM-like.
IPR000225. Armadillo.
IPR009232. EB1_bd.
IPR009224. SAMP.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

Pfam

PF05972. APC_15aa. 4 hits.
PF05956. APC_basic. 1 hit.
PF05923. APC_crr. 7 hits.
PF00514. Arm. 4 hits.
PF05937. EB1_binding. 1 hit.
PF05924. SAMP. 3 hits.
[Graphical view]

SMART

SM00185. ARM. 6 hits.
[Graphical view]

PROSITE

PS50176. ARM_REPEAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

1329.

SOURCE

Search...

Entry information

Entry name

APC_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 16, 2006
Last modified:	November 3, 2009
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.