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P25054

- APC_HUMAN

UniProt

P25054 - APC_HUMAN

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Protein
Adenomatous polyposis coli protein
Gene
APC, DP2.5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:583. APC.

Subcellular locationi

Cell junctionadherens junction. Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle membrane. Cytoplasm. Cell membrane
Note: Associated with the microtubule network at the growing distal tip of microtubules. Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane.5 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Familial adenomatous polyposis (FAP) [MIM:175100]: A cancer predisposition syndrome characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.
Note: The disease is caused by mutations affecting the gene represented in this entry.10 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti99 – 991R → W in FAP; unknown pathological significance. 1 Publication
VAR_009613
Natural varianti171 – 1711S → I in FAP. 1 Publication
VAR_005032
Natural varianti414 – 4141R → C in FAP.
Corresponds to variant rs137854567 [ dbSNP | Ensembl ].
VAR_005033
Natural varianti722 – 7221S → G in FAP. 1 Publication
VAR_009614
Natural varianti784 – 7841S → T in FAP.
VAR_005034
Natural varianti911 – 9111E → G in FAP and colorectal tumor.
VAR_005038
Natural varianti1057 – 10571E → G in non-FAP; unknown pathological significance. 1 Publication
VAR_009615
Natural varianti1176 – 11761P → L in FAP.
VAR_005044
Natural varianti1184 – 11841A → P in FAP. 1 Publication
VAR_009616
Natural varianti1313 – 13131T → A in FAP and colorectal tumor.
VAR_005051
Natural varianti1348 – 13481R → W in FAP. 1 Publication
VAR_005053
Natural varianti2621 – 26211S → C in FAP.
Corresponds to variant rs72541816 [ dbSNP | Ensembl ].
VAR_005056
Natural varianti2839 – 28391L → F in FAP.
VAR_005057
Hereditary desmoid disease (HDD) [MIM:135290]: Autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1296 – 12961A → V in MDB; sporadic. 1 Publication
VAR_017653
Natural varianti1472 – 14721V → I in MDB; sporadic. 1 Publication
VAR_017654
Natural varianti1495 – 14951S → G in MDB; sporadic. 1 Publication
VAR_017655
Mismatch repair cancer syndrome (MMRCS) [MIM:276300]: 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.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti880 – 8801I → T in colorectal carcinoma and gastric cancer; from a patient with MMRCS. 1 Publication
VAR_005036
Natural varianti890 – 8901V → I in colorectal carcinoma; from a patient with MMRCS. 1 Publication
VAR_012975
Natural varianti1508 – 15081A → V in colorectal carcinoma from a patient with MMRCS. 1 Publication
VAR_012976
Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.
Note: The gene represented in this entry may be involved in disease pathogenesis.2 Publications
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.2 Publications

Mutagenesis

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

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 28432842Adenomatous polyposis coli protein
PRO_0000064627Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25054.
PaxDbiP25054.
PRIDEiP25054.

PTM databases

PhosphoSiteiP25054.

Expressioni

Tissue specificityi

Expressed in a variety of tissues.

Gene expression databases

ArrayExpressiP25054.
BgeeiP25054.
CleanExiHS_APC.
GenevestigatoriP25054.

Organism-specific databases

HPAiCAB025994.
HPA013349.

Interactioni

Subunit structurei

Forms homooligomers and heterooligomers with APC2. Interacts with DIAPH1 and DIAPH2 By similarity. Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with ARHGEF4 (via N-terminus). Interacts with MAPRE1 (via C-terminus); probably required for APC targeting to the growing microtubule plus ends. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells. Interacts with SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3 domain). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Interacts at the cell membrane with AMER1 and AMER2 (via ARM repeats).10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMER3Q8N9448EBI-727707,EBI-8869590
CSNK1EP496747EBI-727707,EBI-749343
CTNNB1P352229EBI-727707,EBI-491549
Ctnnb1Q022488EBI-727707,EBI-397872From a different organism.
DVL1O146406EBI-727707,EBI-723489
DVL1P1P547922EBI-727707,EBI-7848109
MAPRE1Q156914EBI-727707,EBI-1004115
SCRIBQ141604EBI-727707,EBI-357345

Protein-protein interaction databases

BioGridi106821. 131 interactions.
DIPiDIP-33556N.
IntActiP25054. 118 interactions.
MINTiMINT-88204.
STRINGi9606.ENSP00000257430.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP25054.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 6160 Reviewed prediction
Add
BLAST
Coiled coili127 – 248122 Reviewed prediction
Add
BLAST

Motif

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

Compositional bias

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

Domaini

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends By similarity.1 Publication

Sequence similaritiesi

Contains 7 ARM repeats.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

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

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

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

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

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

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

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

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei312 – 412101Missing in isoform Short.
VSP_004115Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841M → L in AAA60353. 1 Publication
Sequence conflicti184 – 1841M → L in AAA60354. 1 Publication
Sequence conflicti970 – 9701S → N in AAA60353. 1 Publication
Sequence conflicti970 – 9701S → N in AAA60354. 1 Publication
Sequence conflicti1309 – 13091E → G in AAA60353. 1 Publication
Sequence conflicti1309 – 13091E → G in AAA60354. 1 Publication
Sequence conflicti1325 – 13317AVSQHPR → SSVHSTLE in AAA60353. 1 Publication
Sequence conflicti1325 – 13317AVSQHPR → SSVHSTLE in AAA60354. 1 Publication
Sequence conflicti1355 – 13551S → P in AAA60353. 1 Publication
Sequence conflicti1355 – 13551S → P in AAA60354. 1 Publication
Sequence conflicti1591 – 15911A → G in AAA60353. 1 Publication
Sequence conflicti1591 – 15911A → G in AAA60354. 1 Publication
Sequence conflicti2723 – 27231N → T in AAA60353. 1 Publication
Sequence conflicti2723 – 27231N → T in AAA60354. 1 Publication
Sequence conflicti2755 – 27551S → P in AAA60353. 1 Publication
Sequence conflicti2755 – 27551S → P in AAA60354. 1 Publication

Sequence databases

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

Genome annotation databases

EnsembliENST00000257430; ENSP00000257430; ENSG00000134982. [P25054-1]
ENST00000457016; ENSP00000413133; ENSG00000134982. [P25054-1]
ENST00000508376; ENSP00000427089; ENSG00000134982. [P25054-1]
GeneIDi324.
KEGGihsa:324.
UCSCiuc003kpy.4. human. [P25054-1]

Polymorphism databases

DMDMi97535708.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Colon cancer gene variant databases Adenomatous Polyposis Coli (APC)

Leiden Open Variation Database (LOVD)

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

APC entry

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi 106821. 131 interactions.
DIPi DIP-33556N.
IntActi P25054. 118 interactions.
MINTi MINT-88204.
STRINGi 9606.ENSP00000257430.

PTM databases

PhosphoSitei P25054.

Polymorphism databases

DMDMi 97535708.

Proteomic databases

MaxQBi P25054.
PaxDbi P25054.
PRIDEi P25054.

Protocols and materials databases

DNASUi 324.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257430 ; ENSP00000257430 ; ENSG00000134982 . [P25054-1 ]
ENST00000457016 ; ENSP00000413133 ; ENSG00000134982 . [P25054-1 ]
ENST00000508376 ; ENSP00000427089 ; ENSG00000134982 . [P25054-1 ]
GeneIDi 324.
KEGGi hsa:324.
UCSCi uc003kpy.4. human. [P25054-1 ]

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

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

Publicationsi

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

Entry informationi

Entry nameiAPC_HUMAN
AccessioniPrimary (citable) accession number: P25054
Secondary accession number(s): D3DT03
, Q15162, Q15163, Q93042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 16, 2006
Last modified: September 3, 2014
This is version 190 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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