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Q61315

- APC_MOUSE

UniProt

Q61315 - APC_MOUSE

Protein

Adenomatous polyposis coli protein

Gene

Apc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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 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.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Biological processi

    Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenomatous polyposis coli protein
    Short name:
    Protein APC
    Short name:
    mAPC
    Gene namesi
    Name:Apc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:88039. Apc.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB-SubCell
    2. axon Source: MGI
    3. axonal growth cone Source: MGI
    4. beta-catenin destruction complex Source: UniProtKB
    5. cell projection Source: MGI
    6. cell projection membrane Source: MGI
    7. centrosome Source: UniProtKB
    8. cytoplasm Source: UniProtKB
    9. growth cone Source: MGI
    10. kinetochore Source: UniProtKB
    11. lamellipodium Source: UniProtKB
    12. microtubule Source: UniProtKB-KW
    13. nucleus Source: UniProtKB
    14. plasma membrane Source: UniProtKB
    15. ruffle membrane Source: UniProtKB
    16. Scrib-APC-beta-catenin complex Source: BHF-UCL

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 28452844Adenomatous polyposis coli proteinPRO_0000064628Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei742 – 7421PhosphoserineBy similarity
    Modified residuei778 – 7781PhosphoserineBy similarity
    Modified residuei1040 – 10401PhosphoserineBy similarity
    Modified residuei1359 – 13591PhosphoserineBy similarity
    Modified residuei1859 – 18591PhosphoserineBy similarity
    Modified residuei1861 – 18611PhosphoserineBy similarity
    Modified residuei1862 – 18621PhosphoserineBy similarity
    Modified residuei2151 – 21511PhosphothreonineBy similarity
    Modified residuei2260 – 22601PhosphoserineBy similarity
    Modified residuei2270 – 22701PhosphoserineBy similarity
    Modified residuei2283 – 22831PhosphoserineBy similarity
    Modified residuei2473 – 24731PhosphoserineBy similarity
    Modified residuei2535 – 25351PhosphoserineBy similarity
    Modified residuei2671 – 26711PhosphoserineBy similarity
    Modified residuei2674 – 26741PhosphoserineBy similarity
    Modified residuei2679 – 26791PhosphothreonineBy similarity
    Modified residuei2791 – 27911PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ61315.
    PaxDbiQ61315.
    PRIDEiQ61315.

    PTM databases

    PhosphoSiteiQ61315.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    CleanExiMM_APC.
    GenevestigatoriQ61315.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    IntActiQ61315. 2 interactions.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VJ6NMR-B2834-2845[»]
    ProteinModelPortaliQ61315.
    SMRiQ61315. Positions 2-55, 128-237, 324-734, 1485-1527.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61315.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati451 – 49343ARM 1Add
    BLAST
    Repeati503 – 54543ARM 2Add
    BLAST
    Repeati546 – 58944ARM 3Add
    BLAST
    Repeati590 – 63647ARM 4Add
    BLAST
    Repeati637 – 68145ARM 5Add
    BLAST
    Repeati682 – 72342ARM 6Add
    BLAST
    Repeati724 – 76542ARM 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1864 – 189128Highly chargedAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2 – 6160Sequence AnalysisAdd
    BLAST
    Coiled coili125 – 245121Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2805 – 28084Microtubule tip localization signal
    Motifi2843 – 28453PDZ-bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 728728Leu-richAdd
    BLAST
    Compositional biasi739 – 28342096Ser-richAdd
    BLAST
    Compositional biasi1130 – 115627Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi1556 – 157520Asp/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

    Sequence similaritiesi

    Contains 7 ARM repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG259696.
    HOGENOMiHOG000033986.
    HOVERGENiHBG004264.
    InParanoidiQ61315.
    PhylomeDBiQ61315.

    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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q61315-1) [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

    MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ     50
    LQGSIEDETM TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS 100
    VSSRSGECSP VPMGSFPRRT FVNGSRESTG YLEELEKERS LLLADLDKEE 150
    KEKDWYYAQL QNLTKRIDSL PLTENFSLQT DMTRRQLEYE ARQIRAAMEE 200
    QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA ERSSQSRHDA 250
    ASHEAGRQHE GHGVAESNTA ASSSGQSPAT RVDHETASVL SSSGTHSAPR 300
    RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC 350
    LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR 400
    EIRVLHLLEQ IRAYCETCWE WQEAHEQGMD QDKNPMPAPV EHQICPAVCV 450
    LMKLSFDEEH RHAMNELGGL QAIAELLQVD CEMYGLTNDH YSVTLRRYAG 500
    MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ VIASVLRNLS 550
    WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN 600
    KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH 650
    RQILRENNCL QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG 700
    AVSMLKNLIH SKHKMIAMGS AAALRNLMAN RPAKYKDANI MSPGSSLPSL 750
    HVRKQKALEA ELDAQHLSET FDNIDNLSPK ASHRSKQRHK QNLYGDYAFD 800
    ANRHDDSRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD SSRSEKDRSL 850
    ERERGIGLSA YHPTTENAGT SSKRGLQITT TAAQIAKVME EVSAIHTSQD 900
    DRSSASTTEF HCVADDRSAA RRSSASHTHS NTYNFTKSEN SNRTCSMPYA 950
    KVEYKRSSND SLNSVTSSDG YGKRGQMKPS VESYSEDDES KFCSYGQYPA 1000
    DLAHKIHSAN HMDDNDGELD TPINYSLKYS DEQLNSGRQS PSQNERWARP 1050
    KHVIEDEIKQ NEQRQARSQN TSYPVYSENT DDKHLKFQPH FGQQECVSPY 1100
    RSRGTSGSET NRMGSSHAIN QNVNQSLCQE DDYEDDKPTN YSERYSEEEQ 1150
    HEEEEERPTN YSIKYNEEKH HVDQPIDYSL KYATDISSSQ KPSFSFSKNS 1200
    SAQSTKPEHL SPSSENTAVP PSNAKRQNQL RPSSAQRNGQ TQKGTTCKVP 1250
    SINQETIQTY CVEDTPICFS RCSSLSSLSS ADDEIGCDQT TQEADSANTL 1300
    QTAEVKENDV TRSAEDPATE VPAVSQNARA KPSRLQASGL SSESTRHNKA 1350
    VEFSSGAKSP SKSGAQTPKS PPEHYVQETP LVFSRCTSVS SLDSFESRSI 1400
    ASSVQSEPCS GMVSGIISPS DLPDSPGQTM PPSRSKTPPP PPQTVQAKRE 1450
    VPKSKVPAAE KRESGPKQTA VNAAVQRVQV LPDVDTLLHF ATESTPDGFS 1500
    CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETESEQ PEESNENQDK 1550
    EVEKPDSEKD LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP 1600
    PPVARKPSQL PVYKLLPAQN RLQAQKHVSF TPGDDVPRVY CVEGTPINFS 1650
    TATSLSDLTI ESPPNELATG DGVRAGIQSG EFEKRDTIPT EGRSTDDAQR 1700
    GKISSIVTPD LDDNKAEEGD ILAECINSAM PKGKSHKPFR VKKIMDQVQQ 1750
    ASSTSSGANK NQVDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE 1800
    ETFSDNKDSK KPSLQTNAKA FNEKLPNNED RVRGTFALDS PHHYTPIEGT 1850
    PYCFSRNDSL SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCRPEPNS 1900
    SQQAASKSQA SIKHPANRAQ SKPVLQKQPT FPQSSKDGPD RGAATDEKLQ 1950
    NLAIENTPVC FSRNSSLSSL SDIDQENNNN KESEPIKEAE PANSQGEPSK 2000
    PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLQE CISSAMPKKK 2050
    RPSRLKSESE KQSPRKVGGI LAEDLTLDLK DLQRPDSEHA FSPGSENFDW 2100
    KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GISLGSPFHL 2150
    TPDQEEKPFT SNKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT 2200
    GKIRSNSEIS SQMKQPLPTN MPSISRGRTM IHIPGLRNSS SSTSPVSKKG 2250
    PPLKTPASKS PSEGPGATTS PRGTKPAGKS ELSPITRQTS QISGSNKGSS 2300
    RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISPPN KLSQLPRTSS 2350
    PSTASTKSSG SGKMSYTSPG RQLSQQNLTK QASLSKNASS IPRSESASKG 2400
    LNQMSNGNGS NKKVELSRMS STKSSGSESD SSERPALVRQ STFIKEAPSP 2450
    TLRRKLEESA SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ 2500
    AGGWRKLPPN LSPTIEYNDG RPTKRHDIAR SHSESPSRLP INRAGTWKRE 2550
    HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDER HVSSMPAPRQ 2600
    MKENQVPTKG TWRKIKESDI SPTGMASQSA SSGAASGAES KPLIYQMAPP 2650
    VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKG SSSIKDSKDS 2700
    KDTHGKQSVG SGSPVQTVGL ETRLNSFVQV EAPEQKGTEA KPGQSNPVSI 2750
    AETAETCIAE RTPFSSSSSS KHSSPSGTVA ARVTPFNYNP SPRKSSADST 2800
    SARPSQIPTP VSTNTKKRDS KTDITESSGA QSPKRHSGSY LVTSV 2845
    Length:2,845
    Mass (Da):311,089
    Last modified:November 1, 1996 - v1
    Checksum:i145CA73CF570A499
    GO
    Isoform 2 (identifier: Q61315-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,811
    Mass (Da):307,676
    Checksum:i26917A1088E0B295
    GO
    Isoform 3 (identifier: Q61315-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,744
    Mass (Da):299,882
    Checksum:i7E887CE032058082
    GO
    Isoform 4 (identifier: Q61315-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,710
    Mass (Da):296,469
    Checksum:i76584921956DDB03
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti120 – 1201T → A in strain: CAST/Ei.
    Natural varianti493 – 4931V → I in strain: CAST/Ei.
    Natural varianti797 – 7971Y → F in strain: CAST/Ei.
    Natural varianti1330 – 13301A → T in strain: CAST/Ei.
    Natural varianti1618 – 16181A → S in strain: CAST/Ei.
    Natural varianti2294 – 22941G → A in strain: CAST/Ei.
    Natural varianti2496 – 24961H → Q in strain: CAST/Ei.
    Natural varianti2523 – 25231T → A in strain: CAST/Ei.
    Natural varianti2813 – 28131T → S in strain: CAST/Ei.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei243 – 27634Missing in isoform 2 and isoform 4. 1 PublicationVSP_004116Add
    BLAST
    Alternative sequencei310 – 410101Missing in isoform 3 and isoform 4. CuratedVSP_004117Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88127 mRNA. Translation: AAB59632.1.
    U02937 Unassigned DNA. Translation: AAA03443.1.
    PIRiI49505.
    UniGeneiMm.384171.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88127 mRNA. Translation: AAB59632.1 .
    U02937 Unassigned DNA. Translation: AAA03443.1 .
    PIRi I49505.
    UniGenei Mm.384171.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VJ6 NMR - B 2834-2845 [» ]
    ProteinModelPortali Q61315.
    SMRi Q61315. Positions 2-55, 128-237, 324-734, 1485-1527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q61315. 2 interactions.

    PTM databases

    PhosphoSitei Q61315.

    Proteomic databases

    MaxQBi Q61315.
    PaxDbi Q61315.
    PRIDEi Q61315.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:88039. Apc.

    Phylogenomic databases

    eggNOGi NOG259696.
    HOGENOMi HOG000033986.
    HOVERGENi HBG004264.
    InParanoidi Q61315.
    PhylomeDBi Q61315.

    Miscellaneous databases

    ChiTaRSi APC. mouse.
    EvolutionaryTracei Q61315.
    PROi Q61315.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_APC.
    Genevestigatori Q61315.

    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

    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. "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.
    3. 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.
    4. "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.
    5. "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.
    6. "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.
    7. "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.

    Entry informationi

    Entry nameiAPC_MOUSE
    AccessioniPrimary (citable) accession number: Q61315
    Secondary accession number(s): Q62044
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3