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UniProtKB - P25054 (APC_HUMAN)

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Protein

Adenomatous polyposis coli protein

Gene

APC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

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.

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • dynein complex binding Source: CAFA
  • gamma-catenin binding Source: BHF-UCL
  • identical protein binding Source: CAFA
  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein kinase regulator activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI
Complete GO annotation...

GO - Biological processi

  • beta-catenin destruction complex assembly Source: Reactome
  • beta-catenin destruction complex disassembly Source: Reactome
  • bicellular tight junction assembly Source: UniProtKB
  • canonical Wnt signaling pathway Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • cell migration Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • execution phase of apoptosis Source: Reactome
  • insulin receptor signaling pathway Source: CAFA
  • mitotic cytokinesis Source: MGI
  • mitotic spindle assembly checkpoint Source: MGI
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  • negative regulation of microtubule depolymerization Source: UniProtKB
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of cell death Source: CAFA
  • positive regulation of cell migration Source: MGI
  • positive regulation of protein catabolic process Source: MGI
  • positive regulation of protein localization to centrosome Source: CAFA
  • positive regulation of pseudopodium assembly Source: MGI
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: Reactome
  • protein complex assembly Source: UniProtKB
  • protein deubiquitination Source: Reactome
  • protein homooligomerization Source: CAFA
  • regulation of attachment of spindle microtubules to kinetochore Source: MGI
  • regulation of microtubule-based process Source: UniProtKB
  • Wnt signaling pathway Source: Reactome
Complete GO annotation...

Keywordsi

Biological processWnt signaling pathway

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000134982-MONOMER.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467333. APC truncation mutants are not K63 polyubiquitinated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5689896. Ovarian tumor domain proteases.
SignaLinkiP25054.
SIGNORiP25054.

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:APCImported
Synonyms:DP2.5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:583. APC.

Subcellular locationi

GO - Cellular componenti

  • adherens junction Source: UniProtKB-SubCell
  • beta-catenin destruction complex Source: UniProtKB
  • bicellular tight junction Source: UniProtKB
  • catenin complex Source: CACAO
  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • lateral plasma membrane Source: MGI
  • microtubule Source: UniProtKB-KW
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: UniProtKB
  • ruffle membrane Source: UniProtKB
  • Wnt signalosome Source: ParkinsonsUK-UCL
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)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:175100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00961399R → W in FAP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139196838Ensembl.1
Natural variantiVAR_005032171S → I in FAP. 1 Publication1
Natural variantiVAR_005033414R → C in FAP. Corresponds to variant dbSNP:rs137854567Ensembl.1
Natural variantiVAR_009614722S → G in FAP. 1 Publication1
Natural variantiVAR_005034784S → T in FAP. 1
Natural variantiVAR_005038911E → G in FAP and colorectal tumor. 1
Natural variantiVAR_0096151057E → G in non-FAP; unknown pathological significance. 1 Publication1
Natural variantiVAR_0050441176P → L in FAP. 1
Natural variantiVAR_0096161184A → P in FAP. 1 Publication1
Natural variantiVAR_0050511313T → A in FAP and colorectal tumor. Corresponds to variant dbSNP:rs863225349Ensembl.1
Natural variantiVAR_0050531348R → W in FAP. 1 Publication1
Natural variantiVAR_0050562621S → C in FAP. Corresponds to variant dbSNP:rs72541816Ensembl.1
Natural variantiVAR_0050572839L → F in FAP. Corresponds to variant dbSNP:rs876658156Ensembl.1
Hereditary desmoid disease (HDD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal 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.
See also OMIM:135290
Medulloblastoma (MDB)1 Publication
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionMalignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.
See also OMIM:155255
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0176531296A → V in MDB; sporadic. 1 Publication1
Natural variantiVAR_0176541472V → I in MDB; sporadic. 1 PublicationCorresponds to variant dbSNP:rs878853445Ensembl.1
Natural variantiVAR_0176551495S → G in MDB; sporadic. 1 Publication1
Gastric cancer (GASC)
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA 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.
See also OMIM:613659
Hepatocellular carcinoma (HCC)
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA 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.
See also OMIM:114550

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi516K → E: Impairs interaction with KHDRBS1. 1 Publication1
Mutagenesisi549R → E: Impairs interaction with KHDRBS1. 1 Publication1
Mutagenesisi2841T → L: Loss of interaction with SCRIB. 1 Publication1
Mutagenesisi2843V → Q: Loss of interaction with SCRIB. 1 Publication1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNETi324.
MalaCardsiAPC.
MIMi114550. phenotype.
135290. phenotype.
155255. phenotype.
175100. phenotype.
613659. phenotype.
OpenTargetsiENSG00000134982.
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.

Polymorphism and mutation databases

BioMutaiAPC.
DMDMi97535708.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000646272 – 2843Adenomatous polyposis coli proteinAdd BLAST2842

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei107PhosphoserineBy similarity1
Modified residuei111PhosphoserineBy similarity1
Modified residuei744PhosphoserineCombined sources1
Modified residuei748PhosphoserineCombined sources1
Modified residuei780PhosphoserineCombined sources1
Modified residuei908PhosphoserineCombined sources1
Modified residuei987PhosphoserineBy similarity1
Modified residuei1038PhosphoserineBy similarity1
Modified residuei1042PhosphoserineCombined sources1
Modified residuei1360PhosphoserineCombined sources1
Modified residuei1371PhosphoserineCombined sources1
Modified residuei1385PhosphoserineCombined sources1
Modified residuei1392PhosphoserineBy similarity1
Modified residuei1395PhosphoserineBy similarity1
Modified residuei1438PhosphothreonineCombined sources1
Modified residuei1567PhosphoserineBy similarity1
Modified residuei1774PhosphoserineCombined sources1
Modified residuei1861PhosphoserineCombined sources1
Modified residuei1863PhosphoserineCombined sources1
Modified residuei1864PhosphoserineCombined sources1
Modified residuei1971PhosphoserineBy similarity1
Modified residuei1973PhosphoserineBy similarity1
Modified residuei2088PhosphoserineBy similarity1
Modified residuei2093PhosphoserineBy similarity1
Modified residuei2125PhosphoserineBy similarity1
Modified residuei2129PhosphoserineBy similarity1
Modified residuei2130PhosphoserineBy similarity1
Modified residuei2132PhosphoserineBy similarity1
Modified residuei2151PhosphothreonineCombined sources1
Modified residuei2260PhosphoserineCombined sources1
Modified residuei2270PhosphoserineCombined sources1
Modified residuei2283PhosphoserineCombined sources1
Modified residuei2473PhosphoserineCombined sources1
Modified residuei2535PhosphoserineCombined sources1
Modified residuei2569PhosphoserineCombined sources1
Modified residuei2671PhosphoserineCombined sources1
Modified residuei2674PhosphoserineCombined sources1
Modified residuei2679PhosphothreonineCombined sources1
Modified residuei2710PhosphoserineBy similarity1
Modified residuei2724PhosphoserineCombined sources1
Modified residuei2789PhosphoserineCombined sources1

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

EPDiP25054.
MaxQBiP25054.
PaxDbiP25054.
PeptideAtlasiP25054.
PRIDEiP25054.

PTM databases

iPTMnetiP25054.
PhosphoSitePlusiP25054.

Expressioni

Tissue specificityi

Expressed in a variety of tissues.

Gene expression databases

BgeeiENSG00000134982.
CleanExiHS_APC.
ExpressionAtlasiP25054. baseline and differential.
GenevisibleiP25054. HS.

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). Interacts with KHDRBS1. The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (PubMed:25169422).By similarity15 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • dynein complex binding Source: CAFA
  • gamma-catenin binding Source: BHF-UCL
  • identical protein binding Source: CAFA
  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI
Complete GO annotation...

Protein-protein interaction databases

BioGridi106821. 192 interactors.
DIPiDIP-33556N.
IntActiP25054. 184 interactors.
MINTiMINT-88204.
STRINGi9606.ENSP00000257430.

Structurei

Secondary structure

12843
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 53Combined sources48
Helixi132 – 169Combined sources38
Helixi180 – 204Combined sources25
Helixi208 – 238Combined sources31
Helixi328 – 338Combined sources11
Helixi343 – 350Combined sources8
Helixi353 – 360Combined sources8
Helixi377 – 393Combined sources17
Helixi407 – 425Combined sources19
Beta strandi429 – 431Combined sources3
Helixi433 – 435Combined sources3
Helixi441 – 444Combined sources4
Helixi446 – 457Combined sources12
Helixi460 – 468Combined sources9
Helixi471 – 486Combined sources16
Helixi492 – 508Combined sources17
Helixi513 – 521Combined sources9
Helixi523 – 531Combined sources9
Helixi532 – 534Combined sources3
Helixi538 – 552Combined sources15
Helixi557 – 565Combined sources9
Helixi568 – 578Combined sources11
Helixi582 – 596Combined sources15
Helixi600 – 608Combined sources9
Helixi612 – 619Combined sources8
Beta strandi625 – 627Combined sources3
Helixi630 – 646Combined sources17
Helixi650 – 657Combined sources8
Turni658 – 660Combined sources3
Helixi661 – 668Combined sources8
Helixi674 – 687Combined sources14
Helixi692 – 700Combined sources9
Helixi703 – 708Combined sources6
Turni709 – 712Combined sources4
Helixi716 – 730Combined sources15
Helixi735 – 737Combined sources3
Turni1027 – 1030Combined sources4
Helixi1470 – 1479Combined sources10
Helixi1520 – 1524Combined sources5
Helixi2036 – 2045Combined sources10
Beta strandi2840 – 2842Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4YJEX-ray1.90A407-751[»]
4YJLX-ray2.10A/B/C/D/E/F407-751[»]
4YK6X-ray1.70A407-751[»]
DisProtiDP00519.
ProteinModelPortaliP25054.
SMRiP25054.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25054.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati453 – 495ARM 1Add BLAST43
Repeati505 – 547ARM 2Add BLAST43
Repeati548 – 591ARM 3Add BLAST44
Repeati592 – 638ARM 4Add BLAST47
Repeati639 – 683ARM 5Add BLAST45
Repeati684 – 725ARM 6Add BLAST42
Repeati726 – 767ARM 7Add BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni960 – 1337Responsible for down-regulation through a process mediated by direct ubiquitinationAdd BLAST378
Regioni1866 – 1893Highly chargedAdd BLAST28

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2 – 61Sequence analysisAdd BLAST60
Coiled coili127 – 248Sequence analysisAdd BLAST122

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2803 – 2806Microtubule tip localization signal4
Motifi2841 – 2843PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 730Leu-richAdd BLAST730
Compositional biasi731 – 2832Ser-richAdd BLAST2102
Compositional biasi1131 – 1156Asp/Glu-rich (acidic)Add BLAST26
Compositional biasi1558 – 1577Asp/Glu-rich (acidic)Add BLAST20

Domaini

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

Sequence similaritiesi

Belongs to the adenomatous polyposis coli (APC) family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG2122. Eukaryota.
ENOG410XR2V. LUCA.
GeneTreeiENSGT00530000063749.
HOVERGENiHBG004264.
InParanoidiP25054.
KOiK02085.
OMAiPRVYCVE.
OrthoDBiEOG091G00D4.
PhylomeDBiP25054.
TreeFamiTF106496.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiView protein in InterPro
IPR026836. APC.
IPR009240. APC_15aa_rpt.
IPR009234. APC_basic_dom.
IPR026831. APC_dom.
IPR026818. Apc_fam.
IPR032038. APC_N.
IPR009223. APC_rpt.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR009232. EB1-bd.
IPR009224. SAMP.
PANTHERiPTHR12607. PTHR12607. 1 hit.
PTHR12607:SF13. PTHR12607:SF13. 1 hit.
PfamiView protein in Pfam
PF05972. APC_15aa. 3 hits.
PF05956. APC_basic. 1 hit.
PF16689. APC_N_CC. 1 hit.
PF05923. APC_r. 7 hits.
PF00514. Arm. 2 hits.
PF05937. EB1_binding. 1 hit.
PF05924. SAMP. 3 hits.
SMARTiView protein in SMART
SM00185. ARM. 7 hits.
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF58050. SSF58050. 1 hit.
SSF82931. SSF82931. 1 hit.
PROSITEiView protein in PROSITE
PS50176. ARM_REPEAT. 1 hit.

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. AlignAdd to basket

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

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

« Hide

        10         20         30         40         50
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ 
        60         70         80         90        100
LQGSIEDEAM ASSGQIDLLE RLKELNLDSS NFPGVKLRSK MSLRSYGSRE 
       110        120        130        140        150
GSVSSRSGEC SPVPMGSFPR RGFVNGSRES TGYLEELEKE RSLLLADLDK 
       160        170        180        190        200
EEKEKDWYYA QLQNLTKRID SLPLTENFSL QTDMTRRQLE YEARQIRVAM 
       210        220        230        240        250
EEQLGTCQDM EKRAQRRIAR IQQIEKDILR IRQLLQSQAT EAERSSQNKH 
       260        270        280        290        300
ETGSHDAERQ NEGQGVGEIN MATSGNGQGS TTRMDHETAS VLSSSSTHSA 
       310        320        330        340        350
PRRLTSHLGT KVEMVYSLLS MLGTHDKDDM SRTLLAMSSS QDSCISMRQS 
       360        370        380        390        400
GCLPLLIQLL HGNDKDSVLL GNSRGSKEAR ARASAALHNI IHSQPDDKRG 
       410        420        430        440        450
RREIRVLHLL EQIRAYCETC WEWQEAHEPG MDQDKNPMPA PVEHQICPAV 
       460        470        480        490        500
CVLMKLSFDE EHRHAMNELG GLQAIAELLQ VDCEMYGLTN DHYSITLRRY 
       510        520        530        540        550
AGMALTNLTF GDVANKATLC SMKGCMRALV AQLKSESEDL QQVIASVLRN 
       560        570        580        590        600
LSWRADVNSK KTLREVGSVK ALMECALEVK KESTLKSVLS ALWNLSAHCT 
       610        620        630        640        650
ENKADICAVD GALAFLVGTL TYRSQTNTLA IIESGGGILR NVSSLIATNE 
       660        670        680        690        700
DHRQILRENN CLQTLLQHLK SHSLTIVSNA CGTLWNLSAR NPKDQEALWD 
       710        720        730        740        750
MGAVSMLKNL IHSKHKMIAM GSAAALRNLM ANRPAKYKDA NIMSPGSSLP 
       760        770        780        790        800
SLHVRKQKAL EAELDAQHLS ETFDNIDNLS PKASHRSKQR HKQSLYGDYV 
       810        820        830        840        850
FDTNRHDDNR SDNFNTGNMT VLSPYLNTTV LPSSSSSRGS LDSSRSEKDR 
       860        870        880        890        900
SLERERGIGL GNYHPATENP GTSSKRGLQI STTAAQIAKV MEEVSAIHTS 
       910        920        930        940        950
QEDRSSGSTT ELHCVTDERN ALRRSSAAHT HSNTYNFTKS ENSNRTCSMP 
       960        970        980        990       1000
YAKLEYKRSS NDSLNSVSSS DGYGKRGQMK PSIESYSEDD ESKFCSYGQY 
      1010       1020       1030       1040       1050
PADLAHKIHS ANHMDDNDGE LDTPINYSLK YSDEQLNSGR QSPSQNERWA 
      1060       1070       1080       1090       1100
RPKHIIEDEI KQSEQRQSRN QSTTYPVYTE STDDKHLKFQ PHFGQQECVS 
      1110       1120       1130       1140       1150
PYRSRGANGS ETNRVGSNHG INQNVSQSLC QEDDYEDDKP TNYSERYSEE 
      1160       1170       1180       1190       1200
EQHEEEERPT NYSIKYNEEK RHVDQPIDYS LKYATDIPSS QKQSFSFSKS 
      1210       1220       1230       1240       1250
SSGQSSKTEH MSSSSENTST PSSNAKRQNQ LHPSSAQSRS GQPQKAATCK 
      1260       1270       1280       1290       1300
VSSINQETIQ TYCVEDTPIC FSRCSSLSSL SSAEDEIGCN QTTQEADSAN 
      1310       1320       1330       1340       1350
TLQIAEIKEK IGTRSAEDPV SEVPAVSQHP RTKSSRLQGS SLSSESARHK 
      1360       1370       1380       1390       1400
AVEFSSGAKS PSKSGAQTPK SPPEHYVQET PLMFSRCTSV SSLDSFESRS 
      1410       1420       1430       1440       1450
IASSVQSEPC SGMVSGIISP SDLPDSPGQT MPPSRSKTPP PPPQTAQTKR 
      1460       1470       1480       1490       1500
EVPKNKAPTA EKRESGPKQA AVNAAVQRVQ VLPDADTLLH FATESTPDGF 
      1510       1520       1530       1540       1550
SCSSSLSALS LDEPFIQKDV ELRIMPPVQE NDNGNETESE QPKESNENQE 
      1560       1570       1580       1590       1600
KEAEKTIDSE KDLLDDSDDD DIEILEECII SAMPTKSSRK AKKPAQTASK 
      1610       1620       1630       1640       1650
LPPPVARKPS QLPVYKLLPS QNRLQPQKHV SFTPGDDMPR VYCVEGTPIN 
      1660       1670       1680       1690       1700
FSTATSLSDL TIESPPNELA AGEGVRGGAQ SGEFEKRDTI PTEGRSTDEA 
      1710       1720       1730       1740       1750
QGGKTSSVTI PELDDNKAEE GDILAECINS AMPKGKSHKP FRVKKIMDQV 
      1760       1770       1780       1790       1800
QQASASSSAP NKNQLDGKKK KPTSPVKPIP QNTEYRTRVR KNADSKNNLN 
      1810       1820       1830       1840       1850
AERVFSDNKD SKKQNLKNNS KVFNDKLPNN EDRVRGSFAF DSPHHYTPIE 
      1860       1870       1880       1890       1900
GTPYCFSRND SLSSLDFDDD DVDLSREKAE LRKAKENKES EAKVTSHTEL 
      1910       1920       1930       1940       1950
TSNQQSANKT QAIAKQPINR GQPKPILQKQ STFPQSSKDI PDRGAATDEK 
      1960       1970       1980       1990       2000
LQNFAIENTP VCFSHNSSLS SLSDIDQENN NKENEPIKET EPPDSQGEPS 
      2010       2020       2030       2040       2050
KPQASGYAPK SFHVEDTPVC FSRNSSLSSL SIDSEDDLLQ ECISSAMPKK 
      2060       2070       2080       2090       2100
KKPSRLKGDN EKHSPRNMGG ILGEDLTLDL KDIQRPDSEH GLSPDSENFD 
      2110       2120       2130       2140       2150
WKAIQEGANS IVSSLHQAAA AACLSRQASS DSDSILSLKS GISLGSPFHL 
      2160       2170       2180       2190       2200
TPDQEEKPFT SNKGPRILKP GEKSTLETKK IESESKGIKG GKKVYKSLIT 
      2210       2220       2230       2240       2250
GKVRSNSEIS GQMKQPLQAN MPSISRGRTM IHIPGVRNSS SSTSPVSKKG 
      2260       2270       2280       2290       2300
PPLKTPASKS PSEGQTATTS PRGAKPSVKS ELSPVARQTS QIGGSSKAPS 
      2310       2320       2330       2340       2350
RSGSRDSTPS RPAQQPLSRP IQSPGRNSIS PGRNGISPPN KLSQLPRTSS 
      2360       2370       2380       2390       2400
PSTASTKSSG SGKMSYTSPG RQMSQQNLTK QTGLSKNASS IPRSESASKG 
      2410       2420       2430       2440       2450
LNQMNNGNGA NKKVELSRMS STKSSGSESD RSERPVLVRQ STFIKEAPSP 
      2460       2470       2480       2490       2500
TLRRKLEESA SFESLSPSSR PASPTRSQAQ TPVLSPSLPD MSLSTHSSVQ 
      2510       2520       2530       2540       2550
AGGWRKLPPN LSPTIEYNDG RPAKRHDIAR SHSESPSRLP INRSGTWKRE 
      2560       2570       2580       2590       2600
HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDEK HVNSISGTKQ 
      2610       2620       2630       2640       2650
SKENQVSAKG TWRKIKENEF SPTNSTSQTV SSGATNGAES KTLIYQMAPA 
      2660       2670       2680       2690       2700
VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKA NPNIKDSKDN 
      2710       2720       2730       2740       2750
QAKQNVGNGS VPMRTVGLEN RLNSFIQVDA PDQKGTEIKP GQNNPVPVSE 
      2760       2770       2780       2790       2800
TNESSIVERT PFSSSSSSKH SSPSGTVAAR VTPFNYNPSP RKSSADSTSA 
      2810       2820       2830       2840 
RPSQIPTPVN NNTKKRDSKT DSTESSGTQS PKRHSGSYLV TSV
Length:2,843
Mass (Da):311,646
Last modified:May 16, 2006 - v2
Checksum:i77E194AE4A91DC5A
GO
Isoform Short (identifier: P25054-2) [UniParc]FASTAAdd to basket

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti184M → L in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti184M → L in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti970S → N in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti970S → N in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti1309E → G in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti1309E → G in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti1325 – 1331AVSQHPR → SSVHSTLE in AAA60353 (PubMed:1678319).Curated7
Sequence conflicti1325 – 1331AVSQHPR → SSVHSTLE in AAA60354 (PubMed:1678319).Curated7
Sequence conflicti1355S → P in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti1355S → P in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti1591A → G in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti1591A → G in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti2723N → T in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti2723N → T in AAA60354 (PubMed:1678319).Curated1
Sequence conflicti2755S → P in AAA60353 (PubMed:1678319).Curated1
Sequence conflicti2755S → P in AAA60354 (PubMed:1678319).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00961399R → W in FAP; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139196838Ensembl.1
Natural variantiVAR_005032171S → I in FAP. 1 Publication1
Natural variantiVAR_005033414R → C in FAP. Corresponds to variant dbSNP:rs137854567Ensembl.1
Natural variantiVAR_009614722S → G in FAP. 1 Publication1
Natural variantiVAR_005034784S → T in FAP. 1
Natural variantiVAR_005035817G → C in gastric cancer. 1
Natural variantiVAR_053976870P → S. Corresponds to variant dbSNP:rs33974176Ensembl.1
Natural variantiVAR_005036880I → T in colorectal carcinoma and gastric cancer; from a patient with MMRCS. 1 Publication1
Natural variantiVAR_012975890V → I in colorectal carcinoma; from a patient with MMRCS. 1 PublicationCorresponds to variant dbSNP:rs779998847Ensembl.1
Natural variantiVAR_005037906S → Y in colorectal tumor. 1
Natural variantiVAR_005038911E → G in FAP and colorectal tumor. 1
Natural variantiVAR_005039942N → D in gastric cancer. 1
Natural variantiVAR_0050401027Y → C in colorectal tumor. Corresponds to variant dbSNP:rs869312784Ensembl.1
Natural variantiVAR_0096151057E → G in non-FAP; unknown pathological significance. 1 Publication1
Natural variantiVAR_0050411118N → D1 PublicationCorresponds to variant dbSNP:rs140493115Ensembl.1
Natural variantiVAR_0050421120G → E in gastric cancer. Corresponds to variant dbSNP:rs28933379Ensembl.1
Natural variantiVAR_0089921171R → C1 PublicationCorresponds to variant dbSNP:rs201830995Ensembl.1
Natural variantiVAR_0050431171R → H in gastric cancer. Corresponds to variant dbSNP:rs372481703Ensembl.1
Natural variantiVAR_0050441176P → L in FAP. 1
Natural variantiVAR_0096161184A → P in FAP. 1 Publication1
Natural variantiVAR_0050451197F → S in gastric cancer. 1
Natural variantiVAR_0357941254I → F in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0050461259I → T in gastric cancer. 1
Natural variantiVAR_0050471292T → M1 PublicationCorresponds to variant dbSNP:rs371113837Ensembl.1
Natural variantiVAR_0176531296A → V in MDB; sporadic. 1 Publication1
Natural variantiVAR_0050481304I → V1 PublicationCorresponds to variant dbSNP:rs770157475Ensembl.1
Natural variantiVAR_0050491307I → K in 6% of Ashkenazi Jews; associated with slightly increased risk of colon and breast cancer. 4 PublicationsCorresponds to variant dbSNP:rs1801155Ensembl.1
Natural variantiVAR_0050501312G → E in gastric cancer. 1
Natural variantiVAR_0050511313T → A in FAP and colorectal tumor. Corresponds to variant dbSNP:rs863225349Ensembl.1
Natural variantiVAR_0096171317E → Q May contribute to colorectal tumor development. 1 PublicationCorresponds to variant dbSNP:rs1801166Ensembl.1
Natural variantiVAR_0050521326V → A in gastric cancer. 1
Natural variantiVAR_0050531348R → W in FAP. 1 Publication1
Natural variantiVAR_0651331395S → C in hepatoblastoma. 1 PublicationCorresponds to variant dbSNP:rs137854578Ensembl.1
Natural variantiVAR_0050541422D → H in colorectal tumor. 1
Natural variantiVAR_0176541472V → I in MDB; sporadic. 1 PublicationCorresponds to variant dbSNP:rs878853445Ensembl.1
Natural variantiVAR_0176551495S → G in MDB; sporadic. 1 Publication1
Natural variantiVAR_0201411496T → S. Corresponds to variant dbSNP:rs2229996Ensembl.1
Natural variantiVAR_0129761508A → V in colorectal carcinoma from a patient with MMRCS. 1 Publication1
Natural variantiVAR_0089931822V → D4 PublicationsCorresponds to variant dbSNP:rs459552Ensembl.1
Natural variantiVAR_0539771882R → T. Corresponds to variant dbSNP:rs34157245Ensembl.1
Natural variantiVAR_0201421973S → T. Corresponds to variant dbSNP:rs4987109Ensembl.1
Natural variantiVAR_0539782499V → L. Corresponds to variant dbSNP:rs33941929Ensembl.1
Natural variantiVAR_0050552502G → S1 PublicationCorresponds to variant dbSNP:rs2229995Ensembl.1
Natural variantiVAR_0050562621S → C in FAP. Corresponds to variant dbSNP:rs72541816Ensembl.1
Natural variantiVAR_0089942738I → T1 PublicationCorresponds to variant dbSNP:rs863224552Ensembl.1
Natural variantiVAR_0050572839L → F in FAP. Corresponds to variant dbSNP:rs876658156Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004115312 – 412Missing in isoform Short. 1 PublicationAdd BLAST101

Sequence databases

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

Genome annotation databases

EnsembliENST00000257430; ENSP00000257430; ENSG00000134982. [P25054-1]
ENST00000508376; ENSP00000427089; ENSG00000134982. [P25054-1]
GeneIDi324.
KEGGihsa:324.
UCSCiuc003kpy.5. human. [P25054-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiAPC_HUMAN
AccessioniPrimary (citable) accession number: P25054
Secondary accession number(s): D3DT03
, Q15162, Q15163, Q93042
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 16, 2006
Last modified: June 7, 2017
This is version 222 of the entry and version 2 of the sequence. See 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

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