Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q61315 (APC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenomatous polyposis coli protein

Short name=Protein APC
Short name=mAPC
Gene names
Name:Apc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2845 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration By similarity. 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 By similarity. Ref.8

Subunit structure

Forms homooligomers and heterooligomers with APC2. Interacts with PDZ domains of DLG1 and DLG3. Associates with catenins. Binds axin. Interacts with MAPRE2 and MAPRE3 (via C-terminus). Found in a complex consisting of ARHGEF4, APC and CTNNB1. Interacts with ARHGEF4 (via N-terminus) By similarity. Interacts with MAPRE1 (via C-terminus); probably required for APC targeting to the growing microtubule plus ends. Interacts with DIAPH1 and DIAPH2. Interacts with SCRIB; may mediate targeting to adherens junctions of epithelial cells. Interacts with SPATA13 (via N-terminus and SH3 domain). Interacts with ASAP1 (via SH3 domain) By similarity. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B. Interacts at the cell membrane with AMER1 and AMER2 (via ARM repeats) By similarity. Ref.6 Ref.7

Subcellular location

Cell junctionadherens junction By similarity. Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle membrane By similarity. Cytoplasm By similarity. Cell membrane By similarity. 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 By similarity.

Tissue specificity

Expressed in liver, spleen, kidney, heart, lung, brain, stomach, intestine, testis and ovary.

Domain

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

Post-translational modification

Phosphorylated by GSK3B By similarity.

Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID By similarity.

Sequence similarities

Belongs to the adenomatous polyposis coli (APC) family.

Contains 7 ARM repeats.

Ontologies

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

Inferred from mutant phenotype PubMed 16025118. Source: MGI

Wnt signaling pathway

Inferred from direct assay PubMed 10346819. Source: MGI

anterior/posterior pattern specification

Inferred from mutant phenotype PubMed 12645927. Source: MGI

axis specification

Inferred from mutant phenotype PubMed 12645927. Source: MGI

axonogenesis

Inferred from mutant phenotype PubMed 15207235PubMed 18716223. Source: MGI

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 16887818. Source: MGI

canonical Wnt signaling pathway involved in negative regulation of apoptotic process

Inferred from genetic interaction PubMed 17377531. Source: MGI

canonical Wnt signaling pathway involved in positive regulation of apoptotic process

Inferred from genetic interaction PubMed 17377531. Source: MGI

cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration

Inferred from mutant phenotype PubMed 15198980. Source: MGI

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome organization

Inferred from mutant phenotype PubMed 17200209. Source: MGI

cytoplasmic microtubule organization

Inferred from genetic interaction PubMed 18716223. Source: MGI

dorsal/ventral pattern formation

Inferred from mutant phenotype PubMed 12645927. Source: MGI

hair follicle development

Inferred from mutant phenotype PubMed 17002498. Source: MGI

kidney development

Inferred from mutant phenotype PubMed 15550389. Source: MGI

metaphase/anaphase transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 15767571PubMed 16025118. Source: MGI

mitotic cytokinesis

Inferred from mutant phenotype PubMed 17570218PubMed 17893240. Source: MGI

muscle cell cellular homeostasis

Inferred from genetic interaction PubMed 18056981. Source: MGI

negative regulation of MAPK cascade

Inferred from mutant phenotype PubMed 16478791. Source: MGI

negative regulation of Wnt signaling pathway

Inferred from mutant phenotype PubMed 11756652PubMed 15198980PubMed 15550389PubMed 15563600PubMed 16740478PubMed 16887818PubMed 17363566. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 11756652PubMed 16950562. Source: MGI

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 11756652PubMed 15198980PubMed 15563600. Source: MGI

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 9060821. Source: MGI

negative regulation of epithelial cell proliferation involved in prostate gland development

Inferred from mutant phenotype PubMed 17363566. Source: MGI

negative regulation of microtubule depolymerization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of odontogenesis

Inferred from mutant phenotype PubMed 17002498. Source: MGI

pattern specification process

Inferred from mutant phenotype PubMed 16740478. Source: MGI

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 17227893. Source: MGI

positive regulation of cell adhesion

Inferred from mutant phenotype PubMed 16368433. Source: MGI

positive regulation of cell differentiation

Inferred from mutant phenotype PubMed 15198980PubMed 16709231. Source: MGI

positive regulation of cell division

Inferred from mutant phenotype PubMed 16950562. Source: MGI

positive regulation of cell migration

Inferred from mutant phenotype PubMed 17192415. Source: MGI

positive regulation of epithelial cell differentiation

Inferred from genetic interaction PubMed 15314168. Source: MGI

positive regulation of microtubule polymerization

Inferred from mutant phenotype PubMed 16525027. Source: MGI

positive regulation of protein catabolic process

Inferred from mutant phenotype PubMed 16478791. Source: MGI

protein complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

proximal/distal pattern formation

Inferred from mutant phenotype PubMed 16887818. Source: MGI

regulation of attachment of spindle microtubules to kinetochore

Inferred from mutant phenotype PubMed 17227893. Source: MGI

regulation of cell cycle

Inferred from mutant phenotype PubMed 8988060. Source: MGI

regulation of cell differentiation

Inferred from genetic interaction PubMed 17377531. Source: MGI

regulation of cell migration

Inferred from mutant phenotype PubMed 9371501. Source: MGI

regulation of epithelial cell differentiation

Inferred from mutant phenotype PubMed 9771477. Source: MGI

regulation of microtubule-based process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of nitrogen compound metabolic process

Inferred from mutant phenotype PubMed 16740478. Source: MGI

regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 15802266. Source: MGI

regulation of osteoclast differentiation

Inferred from mutant phenotype PubMed 15802266. Source: MGI

retina development in camera-type eye

Inferred from mutant phenotype PubMed 10982921. Source: MGI

skin development

Inferred from mutant phenotype PubMed 9453487. Source: MGI

somatic stem cell maintenance

Inferred from mutant phenotype PubMed 1541640. Source: MGI

stem cell maintenance

Inferred from mutant phenotype PubMed 18725524. Source: MGI

thymus development

Inferred from mutant phenotype PubMed 16025118PubMed 17002498. Source: MGI

   Cellular_componentScrib-APC-beta-catenin complex

Inferred from direct assay Ref.7. Source: BHF-UCL

adherens junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

axon

Inferred from direct assay PubMed 15207235. Source: MGI

axonal growth cone

Inferred from direct assay PubMed 18716223. Source: MGI

beta-catenin destruction complex

Inferred from sequence or structural similarity. Source: UniProtKB

cell projection

Inferred from direct assay PubMed 16525027. Source: MGI

cell projection membrane

Inferred from direct assay PubMed 16621792. Source: MGI

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic microtubule

Inferred from direct assay PubMed 16525027PubMed 16621792. Source: MGI

growth cone

Inferred from direct assay PubMed 15207235. Source: MGI

kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule plus-end

Inferred from direct assay PubMed 18716223. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule plus-end binding

Inferred from sequence or structural similarity. Source: UniProtKB

protease binding

Inferred from physical interaction PubMed 18281465. Source: BHF-UCL

protein kinase regulator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q61315-1)

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 2 (identifier: Q61315-2)

The sequence of this isoform differs from the canonical sequence as follows:
     243-276: Missing.
Isoform 3 (identifier: Q61315-3)

The sequence of this isoform differs from the canonical sequence as follows:
     310-410: Missing.
Isoform 4 (identifier: Q61315-4)

The sequence of this isoform differs from the canonical sequence as follows:
     243-276: Missing.
     310-410: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 28452844Adenomatous polyposis coli protein
PRO_0000064628

Regions

Repeat451 – 49343ARM 1
Repeat503 – 54543ARM 2
Repeat546 – 58944ARM 3
Repeat590 – 63647ARM 4
Repeat637 – 68145ARM 5
Repeat682 – 72342ARM 6
Repeat724 – 76542ARM 7
Region1864 – 189128Highly charged
Coiled coil2 – 6160 Potential
Coiled coil125 – 245121 Potential
Motif2805 – 28084Microtubule tip localization signal
Motif2843 – 28453PDZ-binding By similarity
Compositional bias1 – 728728Leu-rich
Compositional bias739 – 28342096Ser-rich
Compositional bias1130 – 115627Asp/Glu-rich (acidic)
Compositional bias1556 – 157520Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue7421Phosphoserine By similarity
Modified residue7781Phosphoserine By similarity
Modified residue10401Phosphoserine By similarity
Modified residue13591Phosphoserine By similarity
Modified residue18591Phosphoserine By similarity
Modified residue18611Phosphoserine By similarity
Modified residue18621Phosphoserine By similarity
Modified residue21511Phosphothreonine By similarity
Modified residue22601Phosphoserine By similarity
Modified residue22701Phosphoserine By similarity
Modified residue22831Phosphoserine By similarity
Modified residue24731Phosphoserine By similarity
Modified residue25351Phosphoserine By similarity
Modified residue26711Phosphoserine By similarity
Modified residue26741Phosphoserine By similarity
Modified residue26791Phosphothreonine By similarity
Modified residue27911Phosphoserine By similarity

Natural variations

Alternative sequence243 – 27634Missing in isoform 2 and isoform 4.
VSP_004116
Alternative sequence310 – 410101Missing in isoform 3 and isoform 4.
VSP_004117
Natural variant1201T → A in strain: CAST/Ei.
Natural variant4931V → I in strain: CAST/Ei.
Natural variant7971Y → F in strain: CAST/Ei.
Natural variant13301A → T in strain: CAST/Ei.
Natural variant16181A → S in strain: CAST/Ei.
Natural variant22941G → A in strain: CAST/Ei.
Natural variant24961H → Q in strain: CAST/Ei.
Natural variant25231T → A in strain: CAST/Ei.
Natural variant28131T → S in strain: CAST/Ei.

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 145CA73CF570A499

FASTA2,845311,089
        10         20         30         40         50         60 
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDETM 

        70         80         90        100        110        120 
TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRT 

       130        140        150        160        170        180 
FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT 

       190        200        210        220        230        240 
DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA 

       250        260        270        280        290        300 
ERSSQSRHDA ASHEAGRQHE GHGVAESNTA ASSSGQSPAT RVDHETASVL SSSGTHSAPR 

       310        320        330        340        350        360 
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG 

       370        380        390        400        410        420 
NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE 

       430        440        450        460        470        480 
WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD 

       490        500        510        520        530        540 
CEMYGLTNDH YSVTLRRYAG MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ 

       550        560        570        580        590        600 
VIASVLRNLS WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN 

       610        620        630        640        650        660 
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH RQILRENNCL 

       670        680        690        700        710        720 
QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG AVSMLKNLIH SKHKMIAMGS 

       730        740        750        760        770        780 
AAALRNLMAN RPAKYKDANI MSPGSSLPSL HVRKQKALEA ELDAQHLSET FDNIDNLSPK 

       790        800        810        820        830        840 
ASHRSKQRHK QNLYGDYAFD ANRHDDSRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD 

       850        860        870        880        890        900 
SSRSEKDRSL ERERGIGLSA YHPTTENAGT SSKRGLQITT TAAQIAKVME EVSAIHTSQD 

       910        920        930        940        950        960 
DRSSASTTEF HCVADDRSAA RRSSASHTHS NTYNFTKSEN SNRTCSMPYA KVEYKRSSND 

       970        980        990       1000       1010       1020 
SLNSVTSSDG YGKRGQMKPS VESYSEDDES KFCSYGQYPA DLAHKIHSAN HMDDNDGELD 

      1030       1040       1050       1060       1070       1080 
TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQARSQN TSYPVYSENT 

      1090       1100       1110       1120       1130       1140 
DDKHLKFQPH FGQQECVSPY RSRGTSGSET NRMGSSHAIN QNVNQSLCQE DDYEDDKPTN 

      1150       1160       1170       1180       1190       1200 
YSERYSEEEQ HEEEEERPTN YSIKYNEEKH HVDQPIDYSL KYATDISSSQ KPSFSFSKNS 

      1210       1220       1230       1240       1250       1260 
SAQSTKPEHL SPSSENTAVP PSNAKRQNQL RPSSAQRNGQ TQKGTTCKVP SINQETIQTY 

      1270       1280       1290       1300       1310       1320 
CVEDTPICFS RCSSLSSLSS ADDEIGCDQT TQEADSANTL QTAEVKENDV TRSAEDPATE 

      1330       1340       1350       1360       1370       1380 
VPAVSQNARA KPSRLQASGL SSESTRHNKA VEFSSGAKSP SKSGAQTPKS PPEHYVQETP 

      1390       1400       1410       1420       1430       1440 
LVFSRCTSVS SLDSFESRSI ASSVQSEPCS GMVSGIISPS DLPDSPGQTM PPSRSKTPPP 

      1450       1460       1470       1480       1490       1500 
PPQTVQAKRE VPKSKVPAAE KRESGPKQTA VNAAVQRVQV LPDVDTLLHF ATESTPDGFS 

      1510       1520       1530       1540       1550       1560 
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETESEQ PEESNENQDK EVEKPDSEKD 

      1570       1580       1590       1600       1610       1620 
LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPAQN 

      1630       1640       1650       1660       1670       1680 
RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELATG DGVRAGIQSG 

      1690       1700       1710       1720       1730       1740 
EFEKRDTIPT EGRSTDDAQR GKISSIVTPD LDDNKAEEGD ILAECINSAM PKGKSHKPFR 

      1750       1760       1770       1780       1790       1800 
VKKIMDQVQQ ASSTSSGANK NQVDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE 

      1810       1820       1830       1840       1850       1860 
ETFSDNKDSK KPSLQTNAKA FNEKLPNNED RVRGTFALDS PHHYTPIEGT PYCFSRNDSL 

      1870       1880       1890       1900       1910       1920 
SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCRPEPNS SQQAASKSQA SIKHPANRAQ 

      1930       1940       1950       1960       1970       1980 
SKPVLQKQPT FPQSSKDGPD RGAATDEKLQ NLAIENTPVC FSRNSSLSSL SDIDQENNNN 

      1990       2000       2010       2020       2030       2040 
KESEPIKEAE PANSQGEPSK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLQE 

      2050       2060       2070       2080       2090       2100 
CISSAMPKKK RPSRLKSESE KQSPRKVGGI LAEDLTLDLK DLQRPDSEHA FSPGSENFDW 

      2110       2120       2130       2140       2150       2160 
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT 

      2170       2180       2190       2200       2210       2220 
SNKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLPTN 

      2230       2240       2250       2260       2270       2280 
MPSISRGRTM IHIPGLRNSS SSTSPVSKKG PPLKTPASKS PSEGPGATTS PRGTKPAGKS 

      2290       2300       2310       2320       2330       2340 
ELSPITRQTS QISGSNKGSS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISPPN 

      2350       2360       2370       2380       2390       2400 
KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLTK QASLSKNASS IPRSESASKG 

      2410       2420       2430       2440       2450       2460 
LNQMSNGNGS NKKVELSRMS STKSSGSESD SSERPALVRQ STFIKEAPSP TLRRKLEESA 

      2470       2480       2490       2500       2510       2520 
SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYNDG 

      2530       2540       2550       2560       2570       2580 
RPTKRHDIAR SHSESPSRLP INRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES 

      2590       2600       2610       2620       2630       2640 
SEKAKSEDER HVSSMPAPRQ MKENQVPTKG TWRKIKESDI SPTGMASQSA SSGAASGAES 

      2650       2660       2670       2680       2690       2700 
KPLIYQMAPP VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKG SSSIKDSKDS 

      2710       2720       2730       2740       2750       2760 
KDTHGKQSVG SGSPVQTVGL ETRLNSFVQV EAPEQKGTEA KPGQSNPVSI AETAETCIAE 

      2770       2780       2790       2800       2810       2820 
RTPFSSSSSS KHSSPSGTVA ARVTPFNYNP SPRKSSADST SARPSQIPTP VSTNTKKRDS 

      2830       2840 
KTDITESSGA QSPKRHSGSY LVTSV 

« Hide

Isoform 2 [UniParc].

Checksum: 26917A1088E0B295
Show »

FASTA2,811307,676
Isoform 3 [UniParc].

Checksum: 7E887CE032058082
Show »

FASTA2,744299,882
Isoform 4 [UniParc].

Checksum: 76584921956DDB03
Show »

FASTA2,710296,469

References

[1]"Multiple intestinal neoplasia caused by a mutation in the murine homolog of the APC gene."
Su L.-K., Kinzler K.W., Vogelstein B., Preisinger A.C., Moser A.R., Luongo C., Gould K.A., Dove W.F.
Science 256:668-670(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS.
Strain: C57BL/6J and CAST/Ei.
Tissue: Brain.
[2]Erratum
Su L.-K., Kinzler K.W., Vogelstein B., Preisinger A.C., Moser A.R., Luongo C., Gould K.A., Dove W.F.
Science 256:1114-1114(1992)
[3]"The murine APC gene: alternative splicing of 5' untranslated region segments."
Dicker F., Lambertz S., Reitmair A., Ballhausen W.G.
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
Strain: BALB/c.
Tissue: Liver.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1795-1810, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"APC gene messenger RNA: novel isoforms that lack exon 7."
Oshima M., Sugiyama H., Kitagawa K., Taketo M.
Cancer Res. 53:5589-5591(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[6]"EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration."
Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., Chen M., Wallar B.J., Alberts A.S., Gundersen G.G.
Nat. Cell Biol. 6:820-830(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DIAPH1; DIAPH2 AND MAPRE1.
[7]"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: INTERACTION WITH SCRIB.
[8]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88127 mRNA. Translation: AAB59632.1.
U02937 Unassigned DNA. Translation: AAA03443.1.
PIRI49505.
UniGeneMm.384171.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VJ6NMR-B2834-2845[»]
ProteinModelPortalQ61315.
SMRQ61315. Positions 2-55, 128-237, 324-734, 1485-1527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61315. 2 interactions.

PTM databases

PhosphoSiteQ61315.

Proteomic databases

PaxDbQ61315.
PRIDEQ61315.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:88039. Apc.

Phylogenomic databases

eggNOGNOG259696.
HOGENOMHOG000033986.
HOVERGENHBG004264.
InParanoidQ61315.
PhylomeDBQ61315.

Gene expression databases

CleanExMM_APC.
GenevestigatorQ61315.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR026836. APC.
IPR009240. APC_15aa_rpt.
IPR009234. APC_basic_dom.
IPR009223. APC_Cys-rich_rpt.
IPR026831. APC_dom.
IPR026818. Apc_fam.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR009232. EB1-bd.
IPR009224. SAMP.
[Graphical view]
PANTHERPTHR12607. PTHR12607. 1 hit.
PTHR12607:SF2. PTHR12607:SF2. 1 hit.
PfamPF05972. APC_15aa. 4 hits.
PF05956. APC_basic. 1 hit.
PF05923. APC_crr. 7 hits.
PF00514. Arm. 3 hits.
PF05937. EB1_binding. 1 hit.
PF05924. SAMP. 3 hits.
PF11414. Suppressor_APC. 1 hit.
[Graphical view]
SMARTSM00185. ARM. 6 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPC. mouse.
EvolutionaryTraceQ61315.
PROQ61315.
SOURCESearch...

Entry information

Entry nameAPC_MOUSE
AccessionPrimary (citable) accession number: Q61315
Secondary accession number(s): Q62044
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot