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Q61315

- APC_MOUSE

UniProt

Q61315 - APC_MOUSE

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Protein

Adenomatous polyposis coli protein

Gene

Apc

Organism
Mus musculus (Mouse)
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 (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 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
Complete GO annotation...

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. axon Source: MGI
  2. axonal growth cone Source: MGI
  3. beta-catenin destruction complex Source: UniProtKB
  4. cell junction Source: UniProtKB-KW
  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
Complete GO annotation...

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. 3 interactions.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ
60 70 80 90 100
LQGSIEDETM TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS
110 120 130 140 150
VSSRSGECSP VPMGSFPRRT FVNGSRESTG YLEELEKERS LLLADLDKEE
160 170 180 190 200
KEKDWYYAQL QNLTKRIDSL PLTENFSLQT DMTRRQLEYE ARQIRAAMEE
210 220 230 240 250
QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA ERSSQSRHDA
260 270 280 290 300
ASHEAGRQHE GHGVAESNTA ASSSGQSPAT RVDHETASVL SSSGTHSAPR
310 320 330 340 350
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC
360 370 380 390 400
LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR
410 420 430 440 450
EIRVLHLLEQ IRAYCETCWE WQEAHEQGMD QDKNPMPAPV EHQICPAVCV
460 470 480 490 500
LMKLSFDEEH RHAMNELGGL QAIAELLQVD CEMYGLTNDH YSVTLRRYAG
510 520 530 540 550
MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ VIASVLRNLS
560 570 580 590 600
WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
610 620 630 640 650
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH
660 670 680 690 700
RQILRENNCL QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG
710 720 730 740 750
AVSMLKNLIH SKHKMIAMGS AAALRNLMAN RPAKYKDANI MSPGSSLPSL
760 770 780 790 800
HVRKQKALEA ELDAQHLSET FDNIDNLSPK ASHRSKQRHK QNLYGDYAFD
810 820 830 840 850
ANRHDDSRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD SSRSEKDRSL
860 870 880 890 900
ERERGIGLSA YHPTTENAGT SSKRGLQITT TAAQIAKVME EVSAIHTSQD
910 920 930 940 950
DRSSASTTEF HCVADDRSAA RRSSASHTHS NTYNFTKSEN SNRTCSMPYA
960 970 980 990 1000
KVEYKRSSND SLNSVTSSDG YGKRGQMKPS VESYSEDDES KFCSYGQYPA
1010 1020 1030 1040 1050
DLAHKIHSAN HMDDNDGELD TPINYSLKYS DEQLNSGRQS PSQNERWARP
1060 1070 1080 1090 1100
KHVIEDEIKQ NEQRQARSQN TSYPVYSENT DDKHLKFQPH FGQQECVSPY
1110 1120 1130 1140 1150
RSRGTSGSET NRMGSSHAIN QNVNQSLCQE DDYEDDKPTN YSERYSEEEQ
1160 1170 1180 1190 1200
HEEEEERPTN YSIKYNEEKH HVDQPIDYSL KYATDISSSQ KPSFSFSKNS
1210 1220 1230 1240 1250
SAQSTKPEHL SPSSENTAVP PSNAKRQNQL RPSSAQRNGQ TQKGTTCKVP
1260 1270 1280 1290 1300
SINQETIQTY CVEDTPICFS RCSSLSSLSS ADDEIGCDQT TQEADSANTL
1310 1320 1330 1340 1350
QTAEVKENDV TRSAEDPATE VPAVSQNARA KPSRLQASGL SSESTRHNKA
1360 1370 1380 1390 1400
VEFSSGAKSP SKSGAQTPKS PPEHYVQETP LVFSRCTSVS SLDSFESRSI
1410 1420 1430 1440 1450
ASSVQSEPCS GMVSGIISPS DLPDSPGQTM PPSRSKTPPP PPQTVQAKRE
1460 1470 1480 1490 1500
VPKSKVPAAE KRESGPKQTA VNAAVQRVQV LPDVDTLLHF ATESTPDGFS
1510 1520 1530 1540 1550
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETESEQ PEESNENQDK
1560 1570 1580 1590 1600
EVEKPDSEKD LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP
1610 1620 1630 1640 1650
PPVARKPSQL PVYKLLPAQN RLQAQKHVSF TPGDDVPRVY CVEGTPINFS
1660 1670 1680 1690 1700
TATSLSDLTI ESPPNELATG DGVRAGIQSG EFEKRDTIPT EGRSTDDAQR
1710 1720 1730 1740 1750
GKISSIVTPD LDDNKAEEGD ILAECINSAM PKGKSHKPFR VKKIMDQVQQ
1760 1770 1780 1790 1800
ASSTSSGANK NQVDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
1810 1820 1830 1840 1850
ETFSDNKDSK KPSLQTNAKA FNEKLPNNED RVRGTFALDS PHHYTPIEGT
1860 1870 1880 1890 1900
PYCFSRNDSL SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCRPEPNS
1910 1920 1930 1940 1950
SQQAASKSQA SIKHPANRAQ SKPVLQKQPT FPQSSKDGPD RGAATDEKLQ
1960 1970 1980 1990 2000
NLAIENTPVC FSRNSSLSSL SDIDQENNNN KESEPIKEAE PANSQGEPSK
2010 2020 2030 2040 2050
PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLQE CISSAMPKKK
2060 2070 2080 2090 2100
RPSRLKSESE KQSPRKVGGI LAEDLTLDLK DLQRPDSEHA FSPGSENFDW
2110 2120 2130 2140 2150
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GISLGSPFHL
2160 2170 2180 2190 2200
TPDQEEKPFT SNKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT
2210 2220 2230 2240 2250
GKIRSNSEIS SQMKQPLPTN MPSISRGRTM IHIPGLRNSS SSTSPVSKKG
2260 2270 2280 2290 2300
PPLKTPASKS PSEGPGATTS PRGTKPAGKS ELSPITRQTS QISGSNKGSS
2310 2320 2330 2340 2350
RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISPPN KLSQLPRTSS
2360 2370 2380 2390 2400
PSTASTKSSG SGKMSYTSPG RQLSQQNLTK QASLSKNASS IPRSESASKG
2410 2420 2430 2440 2450
LNQMSNGNGS NKKVELSRMS STKSSGSESD SSERPALVRQ STFIKEAPSP
2460 2470 2480 2490 2500
TLRRKLEESA SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ
2510 2520 2530 2540 2550
AGGWRKLPPN LSPTIEYNDG RPTKRHDIAR SHSESPSRLP INRAGTWKRE
2560 2570 2580 2590 2600
HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDER HVSSMPAPRQ
2610 2620 2630 2640 2650
MKENQVPTKG TWRKIKESDI SPTGMASQSA SSGAASGAES KPLIYQMAPP
2660 2670 2680 2690 2700
VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKG SSSIKDSKDS
2710 2720 2730 2740 2750
KDTHGKQSVG SGSPVQTVGL ETRLNSFVQV EAPEQKGTEA KPGQSNPVSI
2760 2770 2780 2790 2800
AETAETCIAE RTPFSSSSSS KHSSPSGTVA ARVTPFNYNP SPRKSSADST
2810 2820 2830 2840
SARPSQIPTP VSTNTKKRDS KTDITESSGA QSPKRHSGSY LVTSV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 3 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: November 26, 2014
This is version 134 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