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Adenomatous polyposis coli protein (Protein APC) (mAPC)

 APC_MOUSE               Reviewed;        2845 AA.
Q61315; Q62044;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=Adenomatous polyposis coli protein;
Short=Protein APC;
Short=mAPC;
Name=Apc;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS.
STRAIN=C57BL/6J, and CAST/EiJ; TISSUE=Brain;
PubMed=1350108; DOI=10.1126/science.1350108;
Su L.-K., Kinzler K.W., Vogelstein B., Preisinger A.C., Moser A.R.,
Luongo C., Gould K.A., Dove W.F.;
"Multiple intestinal neoplasia caused by a mutation in the murine
homolog of the APC gene.";
Science 256:668-670(1992).
[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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
STRAIN=BALB/cJ; TISSUE=Liver;
Dicker F., Lambertz S., Reitmair A., Ballhausen W.G.;
"The murine APC gene: alternative splicing of 5' untranslated region
segments.";
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 1795-1810, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
ALTERNATIVE SPLICING.
PubMed=8242607;
Oshima M., Sugiyama H., Kitagawa K., Taketo M.;
"APC gene messenger RNA: novel isoforms that lack exon 7.";
Cancer Res. 53:5589-5591(1993).
[6]
INTERACTION WITH DIAPH1; DIAPH2 AND MAPRE1.
PubMed=15311282; DOI=10.1038/ncb1160;
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.;
"EB1 and APC bind to mDia to stabilize microtubules downstream of Rho
and promote cell migration.";
Nat. Cell Biol. 6:820-830(2004).
[7]
INTERACTION WITH SCRIB.
PubMed=16611247; DOI=10.1111/j.1365-2443.2006.00954.x;
Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K.,
Yasugi T., Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T.,
Taketani Y.;
"Human scribble, a novel tumor suppressor identified as a target of
high-risk HPV E6 for ubiquitin-mediated degradation, interacts with
adenomatous polyposis coli.";
Genes Cells 11:453-464(2006).
[8]
FUNCTION.
PubMed=19893577; DOI=10.1038/embor.2009.233;
Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M.,
Ohwada S., Akiyama T.;
"The adenomatous polyposis coli-associated exchange factors Asef and
Asef2 are required for adenoma formation in Apc(Min/+)mice.";
EMBO Rep. 10:1355-1362(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-109; SER-778;
SER-1036; SER-1370; SER-1391; SER-1394; THR-1437; SER-1772; SER-1859;
SER-1862; SER-1969; SER-1971; SER-2125; THR-2151; SER-2674 AND
SER-2726, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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).
{ECO:0000250|UniProtKB:P25054, ECO:0000269|PubMed:19893577}.
-!- SUBUNIT: 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 (PubMed:15311282).
Interacts with DIAPH1 and DIAPH2 (PubMed:15311282). Interacts with
SCRIB; may mediate targeting to adherens junctions of epithelial
cells (PubMed:16611247). 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). Interacts with KHDRBS1
(By similarity). 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') (By
similarity). {ECO:0000250|UniProtKB:P25054,
ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:16611247}.
-!- SUBCELLULAR LOCATION: Cell junction, adherens junction
{ECO:0000250|UniProtKB:P25054}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P25054}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:P25054}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:P25054}. Cytoplasm
{ECO:0000250|UniProtKB:P25054}. Cell membrane
{ECO:0000250|UniProtKB:P25054}. 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 phosphorylated form
to the cell membrane. {ECO:0000250|UniProtKB:P25054}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q61315-1; Sequence=Displayed;
Name=2;
IsoId=Q61315-2; Sequence=VSP_004116;
Name=3;
IsoId=Q61315-3; Sequence=VSP_004117;
Name=4;
IsoId=Q61315-4; Sequence=VSP_004116, VSP_004117;
-!- 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. {ECO:0000250}.
-!- PTM: Phosphorylated by GSK3B. {ECO:0000250}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
Ubiquitination is facilitated by Axin. Deubiquitinated by
ZRANB1/TRABID (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC)
family. {ECO:0000305}.
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EMBL; M88127; AAB59632.1; -; mRNA.
EMBL; U02937; AAA03443.1; -; Unassigned_DNA.
PIR; I49505; I49505.
UniGene; Mm.384171; -.
PDB; 1VJ6; NMR; -; B=2834-2845.
PDBsum; 1VJ6; -.
ProteinModelPortal; Q61315; -.
SMR; Q61315; -.
CORUM; Q61315; -.
ELM; Q61315; -.
IntAct; Q61315; 3.
STRING; 10090.ENSMUSP00000078337; -.
iPTMnet; Q61315; -.
PhosphoSitePlus; Q61315; -.
PaxDb; Q61315; -.
PeptideAtlas; Q61315; -.
PRIDE; Q61315; -.
MGI; MGI:88039; Apc.
eggNOG; KOG2122; Eukaryota.
eggNOG; ENOG410XR2V; LUCA.
HOGENOM; HOG000033986; -.
HOVERGEN; HBG004264; -.
InParanoid; Q61315; -.
PhylomeDB; Q61315; -.
ChiTaRS; Apc; mouse.
EvolutionaryTrace; Q61315; -.
PRO; PR:Q61315; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_APC; -.
GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0044295; C:axonal growth cone; IDA:MGI.
GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
GO; GO:0016342; C:catenin complex; ISO:MGI.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0031253; C:cell projection membrane; IDA:MGI.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0030426; C:growth cone; IDA:MGI.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
GO; GO:0070840; F:dynein complex binding; IPI:CAFA.
GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:CAFA.
GO; GO:0019887; F:protein kinase regulator activity; ISS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0009798; P:axis specification; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; IGI:MGI.
GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; IGI:MGI.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0051276; P:chromosome organization; IMP:MGI.
GO; GO:0031122; P:cytoplasmic microtubule organization; IGI:MGI.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
GO; GO:0001942; P:hair follicle development; IMP:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:CAFA.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:MGI.
GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; ISO:MGI.
GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:MGI.
GO; GO:0042483; P:negative regulation of odontogenesis; IMP:MGI.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:MGI.
GO; GO:0007389; P:pattern specification process; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:MGI.
GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
GO; GO:0051781; P:positive regulation of cell division; IMP:MGI.
GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IGI:MGI.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:CAFA.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:MGI.
GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:MGI.
GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
GO; GO:0045595; P:regulation of cell differentiation; IGI:MGI.
GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IMP:MGI.
GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:MGI.
GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
Gene3D; 1.25.10.10; -; 3.
InterPro; IPR026836; APC.
InterPro; IPR009240; APC_15aa_rpt.
InterPro; IPR009234; APC_basic_dom.
InterPro; IPR026831; APC_dom.
InterPro; IPR026818; Apc_fam.
InterPro; IPR032038; APC_N.
InterPro; IPR036149; APC_N_sf.
InterPro; IPR009223; APC_rpt.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR009232; EB1-bd.
InterPro; IPR009224; SAMP.
PANTHER; PTHR12607; PTHR12607; 1.
PANTHER; PTHR12607:SF11; PTHR12607:SF11; 1.
Pfam; PF05972; APC_15aa; 3.
Pfam; PF05956; APC_basic; 1.
Pfam; PF16689; APC_N_CC; 1.
Pfam; PF05923; APC_r; 7.
Pfam; PF00514; Arm; 2.
Pfam; PF05937; EB1_binding; 1.
Pfam; PF05924; SAMP; 3.
SMART; SM00185; ARM; 7.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF58050; SSF58050; 1.
SUPFAM; SSF82931; SSF82931; 1.
PROSITE; PS50176; ARM_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell junction;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
Microtubule; Phosphoprotein; Reference proteome; Repeat;
Tumor suppressor; Ubl conjugation; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P25054}.
CHAIN 2 2845 Adenomatous polyposis coli protein.
/FTId=PRO_0000064628.
REPEAT 451 493 ARM 1.
REPEAT 503 545 ARM 2.
REPEAT 546 589 ARM 3.
REPEAT 590 636 ARM 4.
REPEAT 637 681 ARM 5.
REPEAT 682 723 ARM 6.
REPEAT 724 765 ARM 7.
REGION 1864 1891 Highly charged.
COILED 2 61 {ECO:0000255}.
COILED 125 245 {ECO:0000255}.
MOTIF 2805 2808 Microtubule tip localization signal.
MOTIF 2843 2845 PDZ-binding. {ECO:0000250}.
COMPBIAS 1 728 Leu-rich.
COMPBIAS 739 2834 Ser-rich.
COMPBIAS 1130 1156 Asp/Glu-rich (acidic).
COMPBIAS 1556 1575 Asp/Glu-rich (acidic).
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 742 742 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 746 746 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 778 778 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 906 906 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 985 985 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 1036 1036 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1040 1040 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 1359 1359 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 1370 1370 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1384 1384 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 1391 1391 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1394 1394 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1437 1437 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1565 1565 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 1772 1772 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1859 1859 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1861 1861 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 1862 1862 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1969 1969 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1971 1971 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2087 2087 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2092 2092 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2125 2125 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2129 2129 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2130 2130 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2132 2132 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2151 2151 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2260 2260 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 2270 2270 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 2283 2283 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 2473 2473 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 2535 2535 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 2569 2569 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 2671 2671 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 2674 2674 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2679 2679 Phosphothreonine.
{ECO:0000250|UniProtKB:P25054}.
MOD_RES 2713 2713 Phosphoserine.
{ECO:0000250|UniProtKB:P70478}.
MOD_RES 2726 2726 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2791 2791 Phosphoserine.
{ECO:0000250|UniProtKB:P25054}.
VAR_SEQ 243 276 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:1350108}.
/FTId=VSP_004116.
VAR_SEQ 310 410 Missing (in isoform 3 and isoform 4).
{ECO:0000305}.
/FTId=VSP_004117.
VARIANT 120 120 T -> A (in strain: CAST/Ei).
VARIANT 493 493 V -> I (in strain: CAST/Ei).
VARIANT 797 797 Y -> F (in strain: CAST/Ei).
VARIANT 1330 1330 A -> T (in strain: CAST/Ei).
VARIANT 1618 1618 A -> S (in strain: CAST/Ei).
VARIANT 2294 2294 G -> A (in strain: CAST/Ei).
VARIANT 2496 2496 H -> Q (in strain: CAST/Ei).
VARIANT 2523 2523 T -> A (in strain: CAST/Ei).
VARIANT 2813 2813 T -> S (in strain: CAST/Ei).
SEQUENCE 2845 AA; 311089 MW; 145CA73CF570A499 CRC64;
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDETM
TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRT
FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT
DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA
ERSSQSRHDA ASHEAGRQHE GHGVAESNTA ASSSGQSPAT RVDHETASVL SSSGTHSAPR
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG
NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE
WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD
CEMYGLTNDH YSVTLRRYAG MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ
VIASVLRNLS WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH RQILRENNCL
QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG AVSMLKNLIH SKHKMIAMGS
AAALRNLMAN RPAKYKDANI MSPGSSLPSL HVRKQKALEA ELDAQHLSET FDNIDNLSPK
ASHRSKQRHK QNLYGDYAFD ANRHDDSRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD
SSRSEKDRSL ERERGIGLSA YHPTTENAGT SSKRGLQITT TAAQIAKVME EVSAIHTSQD
DRSSASTTEF HCVADDRSAA RRSSASHTHS NTYNFTKSEN SNRTCSMPYA KVEYKRSSND
SLNSVTSSDG YGKRGQMKPS VESYSEDDES KFCSYGQYPA DLAHKIHSAN HMDDNDGELD
TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQARSQN TSYPVYSENT
DDKHLKFQPH FGQQECVSPY RSRGTSGSET NRMGSSHAIN QNVNQSLCQE DDYEDDKPTN
YSERYSEEEQ HEEEEERPTN YSIKYNEEKH HVDQPIDYSL KYATDISSSQ KPSFSFSKNS
SAQSTKPEHL SPSSENTAVP PSNAKRQNQL RPSSAQRNGQ TQKGTTCKVP SINQETIQTY
CVEDTPICFS RCSSLSSLSS ADDEIGCDQT TQEADSANTL QTAEVKENDV TRSAEDPATE
VPAVSQNARA KPSRLQASGL SSESTRHNKA VEFSSGAKSP SKSGAQTPKS PPEHYVQETP
LVFSRCTSVS SLDSFESRSI ASSVQSEPCS GMVSGIISPS DLPDSPGQTM PPSRSKTPPP
PPQTVQAKRE VPKSKVPAAE KRESGPKQTA VNAAVQRVQV LPDVDTLLHF ATESTPDGFS
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETESEQ PEESNENQDK EVEKPDSEKD
LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPAQN
RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELATG DGVRAGIQSG
EFEKRDTIPT EGRSTDDAQR GKISSIVTPD LDDNKAEEGD ILAECINSAM PKGKSHKPFR
VKKIMDQVQQ ASSTSSGANK NQVDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
ETFSDNKDSK KPSLQTNAKA FNEKLPNNED RVRGTFALDS PHHYTPIEGT PYCFSRNDSL
SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCRPEPNS SQQAASKSQA SIKHPANRAQ
SKPVLQKQPT FPQSSKDGPD RGAATDEKLQ NLAIENTPVC FSRNSSLSSL SDIDQENNNN
KESEPIKEAE PANSQGEPSK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLQE
CISSAMPKKK RPSRLKSESE KQSPRKVGGI LAEDLTLDLK DLQRPDSEHA FSPGSENFDW
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT
SNKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLPTN
MPSISRGRTM IHIPGLRNSS SSTSPVSKKG PPLKTPASKS PSEGPGATTS PRGTKPAGKS
ELSPITRQTS QISGSNKGSS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISPPN
KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLTK QASLSKNASS IPRSESASKG
LNQMSNGNGS NKKVELSRMS STKSSGSESD SSERPALVRQ STFIKEAPSP TLRRKLEESA
SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYNDG
RPTKRHDIAR SHSESPSRLP INRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES
SEKAKSEDER HVSSMPAPRQ MKENQVPTKG TWRKIKESDI SPTGMASQSA SSGAASGAES
KPLIYQMAPP VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKG SSSIKDSKDS
KDTHGKQSVG SGSPVQTVGL ETRLNSFVQV EAPEQKGTEA KPGQSNPVSI AETAETCIAE
RTPFSSSSSS KHSSPSGTVA ARVTPFNYNP SPRKSSADST SARPSQIPTP VSTNTKKRDS
KTDITESSGA QSPKRHSGSY LVTSV


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