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Catenin alpha-1 (Alpha E-catenin) (Cadherin-associated protein) (Renal carcinoma antigen NY-REN-13)

 CTNA1_HUMAN             Reviewed;         906 AA.
P35221; Q12795; Q8N1C0;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 186.
RecName: Full=Catenin alpha-1;
AltName: Full=Alpha E-catenin;
AltName: Full=Cadherin-associated protein;
AltName: Full=Renal carcinoma antigen NY-REN-13;
Name=CTNNA1;
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).
TISSUE=Brain;
PubMed=8404069;
Furukawa Y., Nakatsuru S., Nagafuchi A., Tsukita S., Muto T.,
Nakamura Y., Horii A.;
"Structure, expression and chromosome assignment of the human catenin
(cadherin-associated protein) alpha 1 gene (CTNNA1).";
Cytogenet. Cell Genet. 65:74-78(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon, and Lung;
PubMed=8323564; DOI=10.1006/bbrc.1993.1710;
Oda T., Kanai Y., Shimoyama Y., Nagafuchi A., Tsukita S.,
Hirohashi S.;
"Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a
human cancer cell line.";
Biochem. Biophys. Res. Commun. 193:897-904(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon;
PubMed=7945318; DOI=10.1006/bbrc.1994.2381;
Rimm D.L., Kebriaei P., Morrow J.S.;
"Molecular cloning reveals alternative splice forms of human alpha(E)-
catenin.";
Biochem. Biophys. Res. Commun. 203:1691-1699(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, AND
SUBCELLULAR LOCATION (ISOFORM 3).
TISSUE=Hippocampus;
PubMed=21708131; DOI=10.1016/j.bbrc.2011.06.085;
Kask M., Pruunsild P., Timmusk T.;
"Bidirectional transcription from human LRRTM2/CTNNA1 and
LRRTM1/CTNNA2 gene loci leads to expression of N-terminally truncated
CTNNA1 and CTNNA2 isoforms.";
Biochem. Biophys. Res. Commun. 411:56-61(2011).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nollet F.H., Vanpoucke G.G., van Roy F.M.;
"Genomic organization of the human alphaE-catenin gene (CTNNA1).";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-179 AND SER-219.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Lung;
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).
[10]
PROTEIN SEQUENCE OF 2-12; 166-178 AND 617-623, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 159-250.
TISSUE=Prostate;
PubMed=8188230; DOI=10.1006/geno.1994.1042;
McPherson J.D., Morton R.A., Ewing C.M., Wasmuth J.J., Overhauser J.,
Nagafuchi A., Tsukita S., Isaacs W.B.;
"Assignment of the human alpha-catenin gene (CTNNA1) to chromosome
5q21-q22.";
Genomics 19:188-190(1994).
[12]
IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
Butz S., Kemler R.;
"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
adhesion.";
FEBS Lett. 355:195-200(1994).
[13]
SUBUNIT, AND INTERACTION WITH CTNNB1.
PubMed=9341178; DOI=10.1074/jbc.272.43.27301;
Koslov E.R., Maupin P., Pradhan D., Morrow J.S., Rimm D.L.;
"Alpha-catenin can form asymmetric homodimeric complexes and/or
heterodimeric complexes with beta-catenin.";
J. Biol. Chem. 272:27301-27306(1997).
[14]
INTERACTION WITH JUP; CTNNB1 AND ALPHA-ACTININ.
PubMed=9152027;
Nieset J.E., Redfield A.R., Jin F., Knudsen K.A., Johnson K.R.,
Wheelock M.J.;
"Characterization of the interactions of alpha-catenin with alpha-
actinin and beta-catenin/plakoglobin.";
J. Cell Sci. 110:1013-1022(1997).
[15]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[16]
INTERACTION WITH AJUBA.
PubMed=12417594; DOI=10.1074/jbc.M205391200;
Marie H., Pratt S.J., Betson M., Epple H., Kittler J.T., Meek L.,
Moss S.J., Troyanovsky S., Attwell D., Longmore G.D., Braga V.M.;
"The LIM protein Ajuba is recruited to cadherin-dependent cell
junctions through an association with alpha-catenin.";
J. Biol. Chem. 278:1220-1228(2003).
[17]
SUMOYLATION.
PubMed=15561718; DOI=10.1074/jbc.M411718200;
Gocke C.B., Yu H., Kang J.;
"Systematic identification and analysis of mammalian small ubiquitin-
like modifier substrates.";
J. Biol. Chem. 280:5004-5012(2005).
[18]
INTERACTION WITH ARHGAP21.
PubMed=16184169; DOI=10.1038/ncb1308;
Sousa S., Cabanes D., Archambaud C., Colland F., Lemichez E.,
Popoff M., Boisson-Dupuis S., Gouin E., Lecuit M., Legrain P.,
Cossart P.;
"ARHGAP10 is necessary for alpha-catenin recruitment at adherens
junctions and for Listeria invasion.";
Nat. Cell Biol. 7:954-960(2005).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
INTERACTION WITH LIMA1.
PubMed=18093941; DOI=10.1073/pnas.0710504105;
Abe K., Takeichi M.;
"EPLIN mediates linkage of the cadherin catenin complex to F-actin and
stabilizes the circumferential actin belt.";
Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-634; SER-641 AND
SER-652, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-268; SER-295;
SER-297; THR-634; SER-641 AND SER-851, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
POSSIBLE INVOLVEMENT IN HDGC.
PubMed=26182300; DOI=10.1001/jamaoncol.2014.168;
Hansford S., Kaurah P., Li-Chang H., Woo M., Senz J., Pinheiro H.,
Schrader K.A., Schaeffer D.F., Shumansky K., Zogopoulos G.,
Santos T.A., Claro I., Carvalho J., Nielsen C., Padilla S., Lum A.,
Talhouk A., Baker-Lange K., Richardson S., Lewis I., Lindor N.M.,
Pennell E., MacMillan A., Fernandez B., Keller G., Lynch H.,
Shah S.P., Guilford P., Gallinger S., Corso G., Roviello F.,
Caldas C., Oliveira C., Pharoah P.D., Huntsman D.G.;
"Hereditary diffuse gastric cancer syndrome: CDH1 mutations and
beyond.";
JAMA Oncol. 1:23-32(2015).
[36]
FUNCTION, PHOSPHORYLATION AT SER-641; SER-652; SER-655 AND THR-658,
AND MUTAGENESIS OF SER-641; 652-SER--THR-658 AND SER-652.
PubMed=25653389; DOI=10.1242/jcs.163824;
Escobar D.J., Desai R., Ishiyama N., Folmsbee S.S., Novak M.N.,
Flozak A.S., Daugherty R.L., Mo R., Nanavati D., Sarpal R.,
Leckband D., Ikura M., Tepass U., Gottardi C.J.;
"alpha-Catenin phosphorylation promotes intercellular adhesion through
a dual-kinase mechanism.";
J. Cell Sci. 128:1150-1165(2015).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-57 AND LYS-797, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[38]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 377-632, PARTIAL PROTEIN
SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11447106; DOI=10.1093/emboj/20.14.3645;
Yang J., Dokurno P., Tonks N.K., Barford D.;
"Crystal structure of the M-fragment of alpha-catenin: implications
for modulation of cell adhesion.";
EMBO J. 20:3645-3656(2001).
[39]
INVOLVEMENT IN MDPT2, VARIANTS MDPT2 CYS-54; LYS-307; SER-318 AND
MET-431, AND INTERACTION WITH VCL.
PubMed=26691986; DOI=10.1038/ng.3474;
Saksens N.T., Krebs M.P., Schoenmaker-Koller F.E., Hicks W., Yu M.,
Shi L., Rowe L., Collin G.B., Charette J.R., Letteboer S.J.,
Neveling K., van Moorsel T.W., Abu-Ltaif S., De Baere E., Walraedt S.,
Banfi S., Simonelli F., Cremers F.P., Boon C.J., Roepman R.,
Leroy B.P., Peachey N.S., Hoyng C.B., Nishina P.M.,
den Hollander A.I.;
"Mutations in CTNNA1 cause butterfly-shaped pigment dystrophy and
perturbed retinal pigment epithelium integrity.";
Nat. Genet. 48:144-151(2016).
[40]
POSSIBLE INVOLVEMENT IN HDGC.
PubMed=23208944; DOI=10.1002/path.4152;
Majewski I.J., Kluijt I., Cats A., Scerri T.S., de Jong D.,
Kluin R.J., Hansford S., Hogervorst F.B., Bosma A.J., Hofland I.,
Winter M., Huntsman D., Jonkers J., Bahlo M., Bernards R.;
"An alpha-E-catenin (CTNNA1) mutation in hereditary diffuse gastric
cancer.";
J. Pathol. 229:621-629(2013).
-!- FUNCTION: Associates with the cytoplasmic domain of a variety of
cadherins. The association of catenins to cadherins produces a
complex which is linked to the actin filament network, and which
seems to be of primary importance for cadherins cell-adhesion
properties. Can associate with both E- and N-cadherins. Originally
believed to be a stable component of E-cadherin/catenin adhesion
complexes and to mediate the linkage of cadherins to the actin
cytoskeleton at adherens junctions. In contrast, cortical actin
was found to be much more dynamic than E-cadherin/catenin
complexes and CTNNA1 was shown not to bind to F-actin when
assembled in the complex suggesting a different linkage between
actin and adherens junctions components. The homodimeric form may
regulate actin filament assembly and inhibit actin branching by
competing with the Arp2/3 complex for binding to actin filaments.
May play a crucial role in cell differentiation.
{ECO:0000269|PubMed:25653389}.
-!- SUBUNIT: Monomer and homodimer; the monomer preferentially binds
to CTNNB1 and the homodimer to actin. Binds AFDN and F-actin.
Possible component of an E-cadherin/ catenin adhesion complex
together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-
catenin/JUP; the complex is located to adherens junctions. The
stable association of CTNNA1 is controversial as CTNNA1 was shown
not to bind to F-actin when assembled in the complex.
Alternatively, the CTNNA1-containing complex may be linked to F-
actin by other proteins such as LIMA1. Interacts with ARHGAP21 and
with AJUBA. Interacts with LIMA1 (By similarity). Interacts with
vinculin/VCL (PubMed:26691986). {ECO:0000250|UniProtKB:P26231,
ECO:0000269|PubMed:26691986}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-701918, EBI-701918;
P25054:APC; NbExp=3; IntAct=EBI-701918, EBI-727707;
P32121:ARRB2; NbExp=3; IntAct=EBI-701918, EBI-714559;
P12830:CDH1; NbExp=6; IntAct=EBI-701918, EBI-727477;
Q5VT06:CEP350; NbExp=5; IntAct=EBI-701918, EBI-947346;
P35222:CTNNB1; NbExp=3; IntAct=EBI-701918, EBI-491549;
Q9H8V3:ECT2; NbExp=3; IntAct=EBI-701918, EBI-1054039;
P00533:EGFR; NbExp=4; IntAct=EBI-701918, EBI-297353;
P14923:JUP; NbExp=2; IntAct=EBI-701918, EBI-702484;
Q9UHB6:LIMA1; NbExp=2; IntAct=EBI-701918, EBI-351479;
Q9ERG0-2:Lima1 (xeno); NbExp=2; IntAct=EBI-7053242, EBI-15677021;
P25963:NFKBIA; NbExp=5; IntAct=EBI-701918, EBI-307386;
Q9H0H5:RACGAP1; NbExp=2; IntAct=EBI-701918, EBI-717233;
P18206-2:VCL; NbExp=2; IntAct=EBI-701918, EBI-11027067;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton. Cell
junction, adherens junction. Cell membrane; Peripheral membrane
protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell
boundaries and probably at cell-matrix boundaries.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane
{ECO:0000269|PubMed:21708131}; Peripheral membrane protein
{ECO:0000269|PubMed:21708131}; Cytoplasmic side
{ECO:0000269|PubMed:21708131}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=CTNNA1a;
IsoId=P35221-1; Sequence=Displayed;
Name=2;
IsoId=P35221-2; Sequence=VSP_017494;
Name=3; Synonyms=CTNNA1b;
IsoId=P35221-3; Sequence=VSP_047810;
Note=Expressed at high levels in the nervous system. Lacks the
beta-catenin interaction domain.;
-!- TISSUE SPECIFICITY: Expressed ubiquitously in normal tissues.
-!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
-!- PTM: Phosphorylation seems to contribute to the strength of cell-
cell adhesion rather than to the basic capacity for cell-cell
adhesion. {ECO:0000250|UniProtKB:P26231}.
-!- DISEASE: Note=Germline CTNNA1 truncating mutations have been
detected in patients with hereditary diffuse gastric cancer (HDGC)
and may play a role in disease susceptibility. Diffuse gastric
cancer is a malignant disease characterized by poorly
differentiated infiltrating lesions resulting in thickening of the
stomach. Malignant tumors start in the stomach, can spread to the
esophagus or the small intestine, and can extend through the
stomach wall to nearby lymph nodes and organs. It also can
metastasize to other parts of the body.
{ECO:0000269|PubMed:23208944, ECO:0000269|PubMed:26182300}.
-!- DISEASE: Macular dystrophy, patterned, 2 (MDPT2) [MIM:608970]: A
form of retinal patterned dystrophy, a heterogeneous group of
macular disorders caused by abnormal accumulation of lipofuscin in
the retinal pigment epithelium. Lipofuscin distribution can show
various shapes that define different types of macular dystrophy,
including reticular (fishnet-like) dystrophy, macroreticular
(spider-shaped) dystrophy and butterfly-shaped pigment dystrophy.
MDPT2 is an autosomal dominant form characterized by bilateral
accumulation of pigment in the macular area that resembles the
wings of a butterfly. {ECO:0000269|PubMed:26691986}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ctnna1/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D14705; BAA03530.1; -; mRNA.
EMBL; D13866; BAA02979.1; -; mRNA.
EMBL; L23805; AAA86430.1; -; mRNA.
EMBL; U03100; AAA18949.1; -; mRNA.
EMBL; HQ589335; AEF32483.1; -; mRNA.
EMBL; AF102803; AAC99459.1; -; Genomic_DNA.
EMBL; AF102787; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102788; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102789; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102790; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102791; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102792; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102793; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102794; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102795; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102796; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102797; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102798; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102799; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102800; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102801; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AF102802; AAC99459.1; JOINED; Genomic_DNA.
EMBL; AY884207; AAW56940.1; -; Genomic_DNA.
EMBL; AC010453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC034243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC113340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW62124.1; -; Genomic_DNA.
EMBL; BC000385; AAH00385.1; -; mRNA.
EMBL; BC031262; AAH31262.1; -; mRNA.
EMBL; L22080; AAA35502.1; -; mRNA.
CCDS; CCDS34243.1; -. [P35221-1]
CCDS; CCDS75315.1; -. [P35221-3]
PIR; JC2542; JC2542.
PIR; JN0607; JN0607.
RefSeq; NP_001277236.1; NM_001290307.2.
RefSeq; NP_001277238.1; NM_001290309.2.
RefSeq; NP_001277239.1; NM_001290310.2.
RefSeq; NP_001277241.1; NM_001290312.1. [P35221-3]
RefSeq; NP_001310911.1; NM_001323982.1. [P35221-1]
RefSeq; NP_001310912.1; NM_001323983.1. [P35221-1]
RefSeq; NP_001310913.1; NM_001323984.1. [P35221-1]
RefSeq; NP_001310916.1; NM_001323987.1. [P35221-3]
RefSeq; NP_001310917.1; NM_001323988.1. [P35221-3]
RefSeq; NP_001310918.1; NM_001323989.1. [P35221-3]
RefSeq; NP_001310919.1; NM_001323990.1. [P35221-3]
RefSeq; NP_001310920.1; NM_001323991.1. [P35221-3]
RefSeq; NP_001310921.1; NM_001323992.1. [P35221-3]
RefSeq; NP_001310922.1; NM_001323993.1. [P35221-3]
RefSeq; NP_001310923.1; NM_001323994.1. [P35221-3]
RefSeq; NP_001310924.1; NM_001323995.1. [P35221-3]
RefSeq; NP_001310925.1; NM_001323996.1. [P35221-3]
RefSeq; NP_001310926.1; NM_001323997.1. [P35221-3]
RefSeq; NP_001310927.1; NM_001323998.1. [P35221-3]
RefSeq; NP_001310928.1; NM_001323999.1. [P35221-3]
RefSeq; NP_001310929.1; NM_001324000.1. [P35221-3]
RefSeq; NP_001894.2; NM_001903.4. [P35221-1]
UniGene; Hs.445981; -.
PDB; 1H6G; X-ray; 2.20 A; A/B=377-632.
PDB; 4EHP; X-ray; 2.66 A; B=277-382.
PDB; 4IGG; X-ray; 3.66 A; A/B=82-906.
PDBsum; 1H6G; -.
PDBsum; 4EHP; -.
PDBsum; 4IGG; -.
ProteinModelPortal; P35221; -.
SMR; P35221; -.
BioGrid; 107876; 83.
CORUM; P35221; -.
DIP; DIP-515N; -.
IntAct; P35221; 71.
MINT; MINT-4998962; -.
STRING; 9606.ENSP00000304669; -.
iPTMnet; P35221; -.
PhosphoSitePlus; P35221; -.
SwissPalm; P35221; -.
BioMuta; CTNNA1; -.
DMDM; 461853; -.
EPD; P35221; -.
MaxQB; P35221; -.
PaxDb; P35221; -.
PeptideAtlas; P35221; -.
PRIDE; P35221; -.
DNASU; 1495; -.
Ensembl; ENST00000302763; ENSP00000304669; ENSG00000044115. [P35221-1]
Ensembl; ENST00000540387; ENSP00000438476; ENSG00000044115. [P35221-3]
GeneID; 1495; -.
KEGG; hsa:1495; -.
UCSC; uc003ldh.4; human. [P35221-1]
CTD; 1495; -.
DisGeNET; 1495; -.
EuPathDB; HostDB:ENSG00000044115.20; -.
GeneCards; CTNNA1; -.
HGNC; HGNC:2509; CTNNA1.
HPA; CAB021089; -.
HPA; HPA046119; -.
HPA; HPA063535; -.
MalaCards; CTNNA1; -.
MIM; 116805; gene.
MIM; 608970; phenotype.
neXtProt; NX_P35221; -.
OpenTargets; ENSG00000044115; -.
PharmGKB; PA27008; -.
eggNOG; KOG3681; Eukaryota.
eggNOG; ENOG410XSRU; LUCA.
GeneTree; ENSGT00550000074411; -.
HOGENOM; HOG000280724; -.
HOVERGEN; HBG000069; -.
InParanoid; P35221; -.
KO; K05691; -.
OMA; HHKDQMA; -.
OrthoDB; EOG091G01KR; -.
PhylomeDB; P35221; -.
TreeFam; TF313686; -.
Reactome; R-HSA-375170; CDO in myogenesis.
Reactome; R-HSA-418990; Adherens junctions interactions.
Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
SIGNOR; P35221; -.
ChiTaRS; CTNNA1; human.
EvolutionaryTrace; P35221; -.
GeneWiki; Catenin_(cadherin-associated_protein),_alpha_1; -.
GenomeRNAi; 1495; -.
PRO; PR:P35221; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000044115; -.
CleanEx; HS_CTNNA1; -.
ExpressionAtlas; P35221; baseline and differential.
Genevisible; P35221; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
GO; GO:0016342; C:catenin complex; IDA:BHF-UCL.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005915; C:zonula adherens; IEA:Ensembl.
GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
GO; GO:0007015; P:actin filament organization; IEA:InterPro.
GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0043297; P:apical junction assembly; NAS:UniProtKB.
GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB.
GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
GO; GO:0016264; P:gap junction assembly; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
InterPro; IPR001033; Alpha_catenin.
InterPro; IPR030047; CTNNA1.
InterPro; IPR006077; Vinculin/catenin.
InterPro; IPR000633; Vinculin_CS.
PANTHER; PTHR18914; PTHR18914; 1.
PANTHER; PTHR18914:SF24; PTHR18914:SF24; 1.
Pfam; PF01044; Vinculin; 2.
PRINTS; PR00805; ALPHACATENIN.
SUPFAM; SSF47220; SSF47220; 4.
PROSITE; PS00663; VINCULIN_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell adhesion;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Isopeptide bond; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.10}.
CHAIN 2 906 Catenin alpha-1.
/FTId=PRO_0000064261.
REGION 2 228 Involved in homodimerization.
REGION 97 148 Interaction with JUP and CTNNB1.
{ECO:0000269|PubMed:9152027}.
REGION 325 394 Interaction with alpha-actinin.
MOD_RES 2 2 N-acetylthreonine. {ECO:0000269|Ref.10}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 634 634 Phosphothreonine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 641 641 Phosphoserine; by CK2.
{ECO:0000244|PubMed:16807684,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:25653389}.
MOD_RES 645 645 Phosphothreonine.
{ECO:0000244|PubMed:18318008}.
MOD_RES 652 652 Phosphoserine; by CK1.
{ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:25653389}.
MOD_RES 655 655 Phosphoserine; by CK1.
{ECO:0000269|PubMed:25653389}.
MOD_RES 658 658 Phosphothreonine; by CK1.
{ECO:0000269|PubMed:25653389}.
MOD_RES 851 851 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CROSSLNK 57 57 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 797 797 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 370 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:21708131}.
/FTId=VSP_047810.
VAR_SEQ 811 811 G -> GNCDTCGALQGLKGWPPPLCLATHW (in
isoform 2). {ECO:0000303|PubMed:7945318}.
/FTId=VSP_017494.
VARIANT 54 54 R -> C (in MDPT2; no effect on VCL-
binding; dbSNP:rs781520852).
{ECO:0000269|PubMed:26691986}.
/FTId=VAR_076586.
VARIANT 179 179 A -> V (in dbSNP:rs28363394).
{ECO:0000269|Ref.6}.
/FTId=VAR_022303.
VARIANT 219 219 P -> S (in dbSNP:rs28363406).
{ECO:0000269|Ref.6}.
/FTId=VAR_022304.
VARIANT 307 307 E -> K (in MDPT2; no effect on VCL-
binding; dbSNP:rs869320697).
{ECO:0000269|PubMed:26691986}.
/FTId=VAR_076587.
VARIANT 318 318 L -> S (in MDPT2; no effect on VCL-
binding; dbSNP:rs869320696).
{ECO:0000269|PubMed:26691986}.
/FTId=VAR_076588.
VARIANT 431 431 I -> M (in MDPT2; no effect on VCL-
binding; dbSNP:rs755215402).
{ECO:0000269|PubMed:26691986}.
/FTId=VAR_076589.
MUTAGEN 641 641 S->A: Abolishes phosphorylation by CK2.
No effect on phosphorylation by CK1.
{ECO:0000269|PubMed:25653389}.
MUTAGEN 641 641 S->D: Enhances phosphorylation by CK1.
{ECO:0000269|PubMed:25653389}.
MUTAGEN 652 658 SRTSVQT->ARTAVQA: Abolishes
phosphorylation by CK1. No effect on
phosphorylation by CK2.
{ECO:0000269|PubMed:25653389}.
MUTAGEN 652 652 S->A: Abolishes phosphorylation by CK1.
{ECO:0000269|PubMed:25653389}.
CONFLICT 92 92 A -> V (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 129 129 R -> P (in Ref. 3; AAA18949).
{ECO:0000305}.
CONFLICT 175 175 I -> N (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 216 216 K -> S (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 342 342 Q -> K (in Ref. 1; BAA03530).
{ECO:0000305}.
CONFLICT 344 348 LQDLL -> CRTCV (in Ref. 3; AAA86430).
{ECO:0000305}.
CONFLICT 460 460 L -> G (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 469 469 L -> TW (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 473 473 A -> P (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 653 653 R -> E (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 685 685 A -> R (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 764 764 A -> R (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
CONFLICT 789 789 Q -> H (in Ref. 1; BAA03530).
{ECO:0000305}.
CONFLICT 859 859 W -> M (in Ref. 3; AAA86430/AAA18949).
{ECO:0000305}.
HELIX 293 299 {ECO:0000244|PDB:4EHP}.
STRAND 300 302 {ECO:0000244|PDB:4EHP}.
HELIX 305 316 {ECO:0000244|PDB:4EHP}.
HELIX 325 327 {ECO:0000244|PDB:4EHP}.
HELIX 328 352 {ECO:0000244|PDB:4EHP}.
HELIX 353 355 {ECO:0000244|PDB:4EHP}.
HELIX 378 386 {ECO:0000244|PDB:1H6G}.
HELIX 387 389 {ECO:0000244|PDB:1H6G}.
TURN 393 395 {ECO:0000244|PDB:1H6G}.
HELIX 398 409 {ECO:0000244|PDB:1H6G}.
HELIX 413 438 {ECO:0000244|PDB:1H6G}.
HELIX 444 473 {ECO:0000244|PDB:1H6G}.
HELIX 478 506 {ECO:0000244|PDB:1H6G}.
HELIX 509 531 {ECO:0000244|PDB:1H6G}.
HELIX 535 559 {ECO:0000244|PDB:1H6G}.
TURN 560 562 {ECO:0000244|PDB:1H6G}.
HELIX 567 581 {ECO:0000244|PDB:1H6G}.
HELIX 583 598 {ECO:0000244|PDB:1H6G}.
STRAND 600 602 {ECO:0000244|PDB:1H6G}.
HELIX 608 630 {ECO:0000244|PDB:1H6G}.
SEQUENCE 906 AA; 100071 MW; 7AAE6F5DDBAF5099 CRC64;
MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKAAAGE FADDPCSSVK
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL
KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN
RDLIYKQLQQ AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER
SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA
QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA
QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR
TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED
DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC
MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL
QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS
TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF
KAMDSI


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CTNNBIP1 CTNNAL1 Gene catenin (cadherin-associated protein), alpha-like 1
EIAAB09849 Alpha N-catenin,Catenin alpha-2,Catna2,Ctnna2,Mouse,Mus musculus


 

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