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Adenomatous polyposis coli protein 2 (Adenomatous polyposis coli protein-like) (APC-like)

 APCL_HUMAN              Reviewed;        2303 AA.
O95996; Q05BW4; Q9UBZ1; Q9UEM8; Q9UQJ8; Q9UQJ9; Q9Y632;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
13-FEB-2019, entry version 148.
RecName: Full=Adenomatous polyposis coli protein 2;
AltName: Full=Adenomatous polyposis coli protein-like;
Short=APC-like;
Name=APC2; Synonyms=APCL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
CTNNB1, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9823329;
Nakagawa H., Murata Y., Koyama K., Fujiyama A., Miyoshi Y., Monden M.,
Akiyama T., Nakamura Y.;
"Identification of a brain-specific APC homologue, APCL, and its
interaction with beta-catenin.";
Cancer Res. 58:5176-5181(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=10551328; DOI=10.1111/j.1349-7006.1999.tb00845.x;
Nakagawa H., Koyama K., Monden M., Nakamura Y.;
"Analysis of APCL, a brain-specific adenomatous polyposis coli
homologue, for mutations and expression in brain tumors.";
Jpn. J. Cancer Res. 90:982-986(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1521 (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [GENOMIC DNA] OF 34-86 AND 476-555 (ISOFORM 2).
Carr I.M., Markham A.F., Colleta P.L., Wai L., Askham J., Morrison E.,
Meredith D.M.;
"APC2 alternatively spliced cDNA sequence.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-731 (ISOFORM 3), NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 618-2303 (ISOFORM 3), FUNCTION, INTERACTION WITH
AXIN2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Kidney;
PubMed=10021369; DOI=10.1016/S0960-9822(99)80024-4;
van Es J.H., Kirkpatrick C., van de Wetering M., Molenaar M.,
Miles A., Kuipers J., Destree O., Peifer M., Clevers H.;
"Identification of APC2, a homologue of the adenomatous polyposis coli
tumour suppressor.";
Curr. Biol. 9:105-108(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-702 (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH TP53BP2, AND SUBCELLULAR LOCATION.
PubMed=10646860;
Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
"APCL, a central nervous system-specific homologue of adenomatous
polyposis coli tumor suppressor, binds to p53-binding protein 2 and
translocates it to the perinucleus.";
Cancer Res. 60:101-105(2000).
[8]
INTERACTION WITH MAPRE1 AND MAPRE3, AND SUBCELLULAR LOCATION.
TISSUE=Fetal brain;
PubMed=10644998; DOI=10.1038/sj.onc.1203308;
Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
"EB3, a novel member of the EB1 family preferentially expressed in the
central nervous system, binds to a CNS-specific APC homologue.";
Oncogene 19:210-216(2000).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, AND TISSUE
SPECIFICITY.
PubMed=11691822;
Jarrett C.R., Blancato J., Cao T., Bressette D.S., Cepeda M.,
Young P.E., King C.R., Byers S.W.;
"Human APC2 localization and allelic imbalance.";
Cancer Res. 61:7978-7984(2001).
[10]
INVOLVEMENT IN SOTOS3, FUNCTION, SUBCELLULAR LOCATION, AND REGION.
PubMed=25753423; DOI=10.1016/j.celrep.2015.02.011;
Almuriekhi M., Shintani T., Fahiminiya S., Fujikawa A., Kuboyama K.,
Takeuchi Y., Nawaz Z., Nadaf J., Kamel H., Kitam A.K., Samiha Z.,
Mahmoud L., Ben-Omran T., Majewski J., Noda M.;
"Loss-of-function mutation in APC2 causes Sotos syndrome features.";
Cell Rep. 0:0-0(2015).
[11]
VARIANTS [LARGE SCALE ANALYSIS] SER-562 AND SER-2003.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[12] {ECO:0000305}
VARIANT ASN-1921.
PubMed=29120066; DOI=10.1111/cge.13171;
Mejecase C., Mohand-Said S., El Shamieh S., Antonio A., Condroyer C.,
Blanchard S., Letexier M., Saraiva J.P., Sahel J.A., Audo I.,
Zeitz C.;
"A novel nonsense variant in REEP6 is involved in a sporadic rod-cone
dystrophy case.";
Clin. Genet. 93:707-711(2018).
-!- FUNCTION: Stabilizes microtubules and may regulate actin fiber
dynamics through the activation of Rho family GTPases
(PubMed:25753423). May also function in Wnt signaling by promoting
the rapid degradation of CTNNB1 (PubMed:10021369, PubMed:11691822,
PubMed:9823329). {ECO:0000269|PubMed:10021369,
ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423,
ECO:0000269|PubMed:9823329}.
-!- SUBUNIT: Interacts with PSRC1 (By similarity). Interacts with APC,
CTNNB1, MAPRE1, MAPRE3, TP53BP2 and possibly with AXIN2.
{ECO:0000250, ECO:0000269|PubMed:10021369,
ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:10646860,
ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:9823329}.
-!- INTERACTION:
Q15691:MAPRE1; NbExp=3; IntAct=EBI-1053045, EBI-1004115;
Q9UPY8:MAPRE3; NbExp=7; IntAct=EBI-1053045, EBI-726739;
Q13625:TP53BP2; NbExp=4; IntAct=EBI-1053045, EBI-77642;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11691822,
ECO:0000269|PubMed:25753423}. Golgi apparatus
{ECO:0000269|PubMed:11691822}. Cytoplasm
{ECO:0000269|PubMed:11691822}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:10646860}. Note=Associated with actin
filaments (PubMed:11691822, PubMed:25753423). Associated with
microtubule network (PubMed:10644998, PubMed:11691822,
PubMed:25753423). {ECO:0000269|PubMed:10644998,
ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:25753423}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O95996-1; Sequence=Displayed;
Name=2;
IsoId=O95996-2; Sequence=VSP_030106;
Name=3;
IsoId=O95996-3; Sequence=VSP_030107;
-!- TISSUE SPECIFICITY: Widely expressed (at protein level).
Specifically expressed in the CNS. {ECO:0000269|PubMed:10021369,
ECO:0000269|PubMed:11691822, ECO:0000269|PubMed:9823329}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal brain.
{ECO:0000269|PubMed:10021369}.
-!- DISEASE: Sotos syndrome 3 (SOTOS3) [MIM:617169]: A form of Sotos
syndrome, a childhood overgrowth syndrome characterized by
prenatal and postnatal overgrowth, developmental delay, mental
retardation, advanced bone age, and abnormal craniofacial
morphology. SOTOS3 patients do not have advanced bone age,
hypotonia, seizures, or autism. SOTOS3 transmission pattern is
consistent with autosomal recessive inheritance.
{ECO:0000269|PubMed:25753423}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC)
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD28183.1; Type=Frameshift; Positions=1322, 1338; Evidence={ECO:0000305};
Sequence=AAF01784.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
Sequence=CAA10317.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAB61207.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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EMBL; AB012162; BAA34611.1; -; mRNA.
EMBL; AB022529; BAA75469.1; -; Genomic_DNA.
EMBL; CH471139; EAW69498.1; -; Genomic_DNA.
EMBL; AF110334; AAD28183.1; ALT_FRAME; mRNA.
EMBL; AF110335; AAD29273.1; -; Genomic_DNA.
EMBL; AF110337; AAD29274.1; -; Genomic_DNA.
EMBL; AF110336; AAD29274.1; JOINED; Genomic_DNA.
EMBL; AF128222; AAF01784.1; ALT_SEQ; mRNA.
EMBL; AJ012652; CAB61207.1; ALT_SEQ; mRNA.
EMBL; AJ131187; CAA10317.1; ALT_INIT; Genomic_DNA.
EMBL; BC032573; AAH32573.1; -; mRNA.
CCDS; CCDS12068.1; -. [O95996-1]
RefSeq; NP_005874.1; NM_005883.2. [O95996-1]
RefSeq; XP_006722672.1; XM_006722609.3. [O95996-1]
UniGene; Hs.446376; -.
ProteinModelPortal; O95996; -.
SMR; O95996; -.
BioGrid; 115585; 6.
ComplexPortal; CPX-440; Beta-catenin destruction core complex, variant 4.
ComplexPortal; CPX-442; Beta-catenin destruction core complex, variant 6.
ComplexPortal; CPX-443; Beta-catenin destruction core complex, variant 8.
ComplexPortal; CPX-99; Beta-catenin destruction core complex, variant 2.
ELM; O95996; -.
IntAct; O95996; 5.
MINT; O95996; -.
STRING; 9606.ENSP00000233607; -.
CarbonylDB; O95996; -.
iPTMnet; O95996; -.
PhosphoSitePlus; O95996; -.
BioMuta; APC2; -.
jPOST; O95996; -.
PaxDb; O95996; -.
PeptideAtlas; O95996; -.
PRIDE; O95996; -.
ProteomicsDB; 51171; -.
ProteomicsDB; 51172; -. [O95996-2]
ProteomicsDB; 51173; -. [O95996-3]
Ensembl; ENST00000233607; ENSP00000233607; ENSG00000115266. [O95996-1]
Ensembl; ENST00000535453; ENSP00000442954; ENSG00000115266. [O95996-1]
GeneID; 10297; -.
KEGG; hsa:10297; -.
UCSC; uc002lsr.1; human. [O95996-1]
CTD; 10297; -.
DisGeNET; 10297; -.
EuPathDB; HostDB:ENSG00000115266.11; -.
GeneCards; APC2; -.
H-InvDB; HIX0039920; -.
HGNC; HGNC:24036; APC2.
HPA; HPA078002; -.
MalaCards; APC2; -.
MIM; 612034; gene.
MIM; 617169; phenotype.
neXtProt; NX_O95996; -.
OpenTargets; ENSG00000115266; -.
Orphanet; 821; Sotos syndrome.
PharmGKB; PA134906843; -.
eggNOG; KOG2122; Eukaryota.
eggNOG; ENOG410XR2V; LUCA.
GeneTree; ENSGT00530000063749; -.
HOVERGEN; HBG104821; -.
InParanoid; O95996; -.
KO; K02085; -.
OMA; VETQFSM; -.
OrthoDB; 31524at2759; -.
PhylomeDB; O95996; -.
TreeFam; TF106496; -.
SignaLink; O95996; -.
SIGNOR; O95996; -.
GenomeRNAi; 10297; -.
PRO; PR:O95996; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000115266; Expressed in 173 organ(s), highest expression level in paraflocculus.
ExpressionAtlas; O95996; baseline and differential.
Genevisible; O95996; HS.
GO; GO:0005884; C:actin filament; IDA:BHF-UCL.
GO; GO:0030877; C:beta-catenin destruction complex; IBA:GO_Central.
GO; GO:0016342; C:catenin complex; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0031258; C:lamellipodium membrane; IDA:BHF-UCL.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
GO; GO:0030496; C:midbody; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0098794; C:postsynapse; IEA:Ensembl.
GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
GO; GO:0045295; F:gamma-catenin binding; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
GO; GO:0007389; P:pattern specification process; IBA:GO_Central.
GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR026837; APC2.
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; IPR009224; SAMP.
PANTHER; PTHR12607; PTHR12607; 1.
PANTHER; PTHR12607:SF3; PTHR12607:SF3; 1.
Pfam; PF05956; APC_basic; 1.
Pfam; PF16689; APC_N_CC; 1.
Pfam; PF05923; APC_r; 4.
Pfam; PF00514; Arm; 1.
Pfam; PF05924; SAMP; 2.
SMART; SM00185; ARM; 6.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF58050; SSF58050; 1.
SUPFAM; SSF82931; SSF82931; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Golgi apparatus; Microtubule; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Wnt signaling pathway.
CHAIN 1 2303 Adenomatous polyposis coli protein 2.
/FTId=PRO_0000313686.
REPEAT 302 341 ARM 1.
REPEAT 479 518 ARM 2.
REPEAT 522 562 ARM 3.
REPEAT 566 609 ARM 4.
REPEAT 615 654 ARM 5.
REPEAT 657 696 ARM 6.
REPEAT 1058 1077 1.
REPEAT 1150 1169 2.
REPEAT 1263 1282 3.
REPEAT 1391 1410 4.
REPEAT 1568 1587 5.
REGION 1058 1587 5 X 20 AA approximate repeat of F-X-V-E-
X-T-P-X-C-F-S-R-X-S-S-L-S-S-L-S.
REGION 1058 1587 Interaction with CTNNB1.
{ECO:0000269|PubMed:9823329}.
REGION 1821 1900 Required for localization to microtubules
and function in microtubule
stabilization.
{ECO:0000269|PubMed:25753423}.
REGION 2067 2144 Interaction with MAPRE1 and MAPRE3.
{ECO:0000269|PubMed:10644998}.
COILED 8 59 {ECO:0000255}.
COILED 840 864 {ECO:0000255}.
COMPBIAS 1145 1196 Ser-rich.
COMPBIAS 1518 1622 Pro-rich.
COMPBIAS 1765 1953 Pro-rich.
MOD_RES 1585 1585 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1K7}.
MOD_RES 1587 1587 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1K7}.
VAR_SEQ 168 441 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_030106.
VAR_SEQ 175 175 Missing (in isoform 3).
{ECO:0000303|PubMed:10021369}.
/FTId=VSP_030107.
VARIANT 562 562 A -> S (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_037703.
VARIANT 1921 1921 H -> N. {ECO:0000269|PubMed:29120066}.
/FTId=VAR_081224.
VARIANT 2003 2003 G -> S (in a breast cancer sample;
somatic mutation; dbSNP:rs1288757495).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_037704.
VARIANT 2241 2241 S -> A (in dbSNP:rs265277).
/FTId=VAR_037705.
CONFLICT 463 463 Missing (in Ref. 4; AAD28183).
{ECO:0000305}.
CONFLICT 526 527 KV -> NL (in Ref. 4; AAD28183/AAD29274).
{ECO:0000305}.
CONFLICT 566 566 E -> A (in Ref. 5; AAF01784/CAB61207).
{ECO:0000305}.
CONFLICT 816 816 L -> Q (in Ref. 4; AAD28183).
{ECO:0000305}.
CONFLICT 971 971 L -> P (in Ref. 4; AAD28183).
{ECO:0000305}.
CONFLICT 1106 1106 S -> I (in Ref. 4; AAD28183).
{ECO:0000305}.
CONFLICT 1140 1140 E -> G (in Ref. 5; CAA10317).
{ECO:0000305}.
CONFLICT 1188 1188 Q -> H (in Ref. 4; AAD28183).
{ECO:0000305}.
CONFLICT 1361 1361 A -> G (in Ref. 4; AAD28183).
{ECO:0000305}.
CONFLICT 1456 1456 R -> P (in Ref. 4; AAD28183).
{ECO:0000305}.
CONFLICT 1515 1515 D -> V (in Ref. 4; AAD28183).
{ECO:0000305}.
CONFLICT 2219 2219 A -> V (in Ref. 5; CAA10317).
{ECO:0000305}.
SEQUENCE 2303 AA; 243949 MW; 7BF940183ACD643D CRC64;
MASSVAPYEQ LVRQVEALKA ENSHLRQELR DNSSHLSKLE TETSGMKEVL KHLQGKLEQE
ARVLVSSGQT EVLEQLKALQ MDITSLYNLK FQPPTLGPEP AARTPEGSPV HGSGPSKDSF
GELSRATIRL LEELDRERCF LLNEIEKEEK EKLWYYSQLQ GLSKRLDELP HVETQFSMQM
DLIRQQLEFE AQHIRSLMEE RFGTSDEMVQ RAQIRASRLE QIDKELLEAQ DRVQQTEPQA
LLAVKSVPVD EDPETEVPTH PEDGTPQPGN SKVEVVFWLL SMLATRDQED TARTLLAMSS
SPESCVAMRR SGCLPLLLQI LHGTEAAAGG RAGAPGAPGA KDARMRANAA LHNIVFSQPD
QGLARKEMRV LHVLEQIRAY CETCWDWLQA RDGGPEGGGA GSAPIPIEPQ ICQATCAVMK
LSFDEEYRRA MNELGGLQAV AELLQVDYEM HKMTRDPLNL ALRRYAGMTL TNLTFGDVAN
KATLCARRGC MEAIVAQLAS DSEELHQVVS SILRNLSWRA DINSKKVLRE AGSVTALVQC
VLRATKESTL KSVLSALWNL SAHSTENKAA ICQVDGALGF LVSTLTYKCQ SNSLAIIESG
GGILRNVSSL VATREDYRQV LRDHNCLQTL LQHLTSHSLT IVSNACGTLW NLSARSARDQ
ELLWDLGAVG MLRNLVHSKH KMIAMGSAAA LRNLLAHRPA KHQAAATAVS PGSCVPSLYV
RKQRALEAEL DARHLAQALE HLEKQGPPAA EAATKKPLPP LRHLDGLAQD YASDSGCFDD
DDAPSSLAAA AATGEPASPA ALSLFLGSPF LQGQALARTP PTRRGGKEAE KDTSGEAAVA
AKAKAKLALA VARIDQLVED ISALHTSSDD SFSLSSGDPG QEAPREGRAQ SCSPCRGPEG
GRREAGSRAH PLLRLKAAHA SLSNDSLNSG SASDGYCPRE HMLPCPLAAL ASRREDPRCG
QPRPSRLDLD LPGCQAEPPA REATSADARV RTIKLSPTYQ HVPLLEGASR AGAEPLAGPG
ISPGARKQAW LPADHLSKVP EKLAAAPLSV ASKALQKLAA QEGPLSLSRC SSLSSLSSAG
RPGPSEGGDL DDSDSSLEGL EEAGPSEAEL DSTWRAPGAT SLPVAIPAPR RNRGRGLGVE
DATPSSSSEN YVQETPLVLS RCSSVSSLGS FESPSIASSI PSEPCSGQGS GTISPSELPD
SPGQTMPPSR SKTPPLAPAP QGPPEATQFS LQWESYVKRF LDIADCRERC RLPSELDAGS
VRFTVEKPDE NFSCASSLSA LALHEHYVQQ DVELRLLPSA CPERGGGAGG AGLHFAGHRR
REEGPAPTGS RPRGAADQEL ELLRECLGAA VPARLRKVAS ALVPGRRALP VPVYMLVPAP
APAQEDDSCT DSAEGTPVNF SSAASLSDET LQGPPRDQPG GPAGRQRPTG RPTSARQAMG
HRHKAGGAGR SAEQSRGAGK NRAGLELPLG RPPSAPADKD GSKPGRTRGD GALQSLCLTT
PTEEAVYCFY GNDSDEEPPA AAPTPTHRRT SAIPRAFTRE RPQGRKEAPA PSKAAPAAPP
PARTQPSLIA DETPPCYSLS SSASSLSEPE PSEPPAVHPR GREPAVTKDP GPGGGRDSSP
SPRAAEELLQ RCISSALPRR RPPVSGLRRR KPRATRLDER PAEGSRERGE EAAGSDRASD
LDSVEWRAIQ EGANSIVTWL HQAAAATREA SSESDSILSF VSGLSVGSTL QPPKHRKGRQ
AEGEMGSARR PEKRGAASVK TSGSPRSPAG PEKPRGTQKT TPGVPAVLRG RTVIYVPSPA
PRAQPKGTPG PRATPRKVAP PCLAQPAAPA KVPSPGQQRS RSLHRPAKTS ELATLSQPPR
SATPPARLAK TPSSSSSQTS PASQPLPRKR PPVTQAAGAL PGPGASPVPK TPARTLLAKQ
HKTQRSPVRI PFMQRPARRG PPPLARAVPE PGPRGRAGTE AGPGARGGRL GLVRVASALS
SGSESSDRSG FRRQLTFIKE SPGLRRRRSE LSSAESAASA PQGASPRRGR PALPAVFLCS
SRCEELRAAP RQGPAPARQR PPAARPSPGE RPARRTTSES PSRLPVRAPA ARPETVKRYA
SLPHISVARR PDGAVPAAPA SADAARRSSD GEPRPLPRVA APGTTWRRIR DEDVPHILRS
TLPATALPLR GSTPEDAPAG PPPRKTSDAV VQTEEVAAPK TNSSTSPSLE TREPPGAPAG
GQLSLLGSDV DGPSLAKAPI SAPFVHEGLG VAVGGFPASR HGSPSRSARV PPFNYVPSPM
VVAATTDSAA EKAPATASAT LLE


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[APC2 APCL] Adenomatous polyposis coli protein 2 (Adenomatous polyposis coli protein-like) (APC-like)
[APC DP2.5] Adenomatous polyposis coli protein (Protein APC) (Deleted in polyposis 2.5)
[Apc2 APC APC2 apc2 D-APC2 d-APC2 dAPC2 dApc2 dapc2 Dm APC2 Dmel\CG6193 E-APC e-apc E-APC dAPC2 CG6193 Dmel_CG6193] Adenomatous polyposis coli 2 (Adenomatous polyposis coli 2, isoform A) (Adenomatous polyposis coli 2, isoform C) (Epithelial adenomatous polyposis coli)
[Apc] Adenomatous polyposis coli protein (Protein APC) (mAPC)
[apr-1 K04G2.8] Adenomatous polyposis coli protein-related protein 1 (APC-related protein 1)
[Apc] Adenomatous polyposis coli protein (Protein APC)
[Apc D-APC CG1451] Adenomatous polyposis coli
[MUTYH MYH] Adenine DNA glycosylase (EC 3.2.2.31) (MutY homolog) (hMYH)
[NTHL1 NTH1 OCTS3] Endonuclease III-like protein 1 (hNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[MAPRE2 RP1] Microtubule-associated protein RP/EB family member 2 (APC-binding protein EB2) (End-binding protein 2) (EB2)
[MAPRE1] Microtubule-associated protein RP/EB family member 1 (APC-binding protein EB1) (End-binding protein 1) (EB1)
[CTNNB1 CTNNB OK/SW-cl.35 PRO2286] Catenin beta-1 (Beta-catenin)
[Stk11 Lkb1] Serine/threonine-protein kinase STK11 (EC 2.7.11.1) (Liver kinase B1 homolog) (LKB1) (mLKB1)
[ASAP1 DDEF1 KIAA1249] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[SIAH1 HUMSIAH] E3 ubiquitin-protein ligase SIAH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1) (Seven in absentia homolog 1) (Siah-1) (Siah-1a)
[KHDRBS1 SAM68] KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)
[MAPRE3] Microtubule-associated protein RP/EB family member 3 (EB1 protein family member 3) (EBF3) (End-binding protein 3) (EB3) (RP3)
[SCRIB CRIB1 KIAA0147 LAP4 SCRB1 VARTUL] Protein scribble homolog (Scribble) (hScrib) (Protein LAP4)
[Ctnnb1 Catnb] Catenin beta-1 (Beta-catenin)
[Scrib Kiaa0147 Lap4 Scrib1] Protein scribble homolog (Scribble) (Protein LAP4)
[USP15 KIAA0529] Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15) (Unph-2) (Unph4)
[MSH2] DNA mismatch repair protein Msh2 (hMSH2) (MutS protein homolog 2)
[MMP9 CLG4B] Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9]
[MLH1 COCA2] DNA mismatch repair protein Mlh1 (MutL protein homolog 1)
[Mmp9 Clg4b] Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB)
[BMPR1A ACVRLK3 ALK3] Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (Serine/threonine-protein kinase receptor R5) (SKR5) (CD antigen CD292)
[POLD1 POLD] DNA polymerase delta catalytic subunit (EC 2.7.7.7) (EC 3.1.11.-) (DNA polymerase subunit delta p125)
[AXIN2] Axin-2 (Axin-like protein) (Axil) (Axis inhibition protein 2) (Conductin)
[pagP crcA ybeG b0622 JW0617] Lipid A palmitoyltransferase PagP (EC 2.3.1.251) (Lipid A acylation protein)
[SMAD4 DPC4 MADH4] Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4) (SMAD family member 4) (SMAD 4) (Smad4) (hSMAD4)

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