CTNA1_HUMAN
ID CTNA1_HUMAN Reviewed; 906 AA.
AC P35221; Q12795; Q8N1C0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Catenin alpha-1;
DE AltName: Full=Alpha E-catenin;
DE AltName: Full=Cadherin-associated protein;
DE AltName: Full=Renal carcinoma antigen NY-REN-13;
GN Name=CTNNA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8404069; DOI=10.1159/000133603;
RA Furukawa Y., Nakatsuru S., Nagafuchi A., Tsukita S., Muto T., Nakamura Y.,
RA Horii A.;
RT "Structure, expression and chromosome assignment of the human catenin
RT (cadherin-associated protein) alpha 1 gene (CTNNA1).";
RL Cytogenet. Cell Genet. 65:74-78(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Lung;
RX PubMed=8323564; DOI=10.1006/bbrc.1993.1710;
RA Oda T., Kanai Y., Shimoyama Y., Nagafuchi A., Tsukita S., Hirohashi S.;
RT "Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a human
RT cancer cell line.";
RL Biochem. Biophys. Res. Commun. 193:897-904(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon;
RX PubMed=7945318; DOI=10.1006/bbrc.1994.2381;
RA Rimm D.L., Kebriaei P., Morrow J.S.;
RT "Molecular cloning reveals alternative splice forms of human alpha(E)-
RT catenin.";
RL Biochem. Biophys. Res. Commun. 203:1691-1699(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, AND
RP SUBCELLULAR LOCATION (ISOFORM 3).
RC TISSUE=Hippocampus;
RX PubMed=21708131; DOI=10.1016/j.bbrc.2011.06.085;
RA Kask M., Pruunsild P., Timmusk T.;
RT "Bidirectional transcription from human LRRTM2/CTNNA1 and LRRTM1/CTNNA2
RT gene loci leads to expression of N-terminally truncated CTNNA1 and CTNNA2
RT isoforms.";
RL Biochem. Biophys. Res. Commun. 411:56-61(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nollet F.H., Vanpoucke G.G., van Roy F.M.;
RT "Genomic organization of the human alphaE-catenin gene (CTNNA1).";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-179 AND SER-219.
RG NIEHS SNPs program;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-12; 166-178 AND 617-623, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 159-250.
RC TISSUE=Prostate;
RX PubMed=8188230; DOI=10.1006/geno.1994.1042;
RA McPherson J.D., Morton R.A., Ewing C.M., Wasmuth J.J., Overhauser J.,
RA Nagafuchi A., Tsukita S., Isaacs W.B.;
RT "Assignment of the human alpha-catenin gene (CTNNA1) to chromosome 5q21-
RT q22.";
RL Genomics 19:188-190(1994).
RN [12]
RP IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA Butz S., Kemler R.;
RT "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT adhesion.";
RL FEBS Lett. 355:195-200(1994).
RN [13]
RP SUBUNIT, AND INTERACTION WITH CTNNB1.
RX PubMed=9341178; DOI=10.1074/jbc.272.43.27301;
RA Koslov E.R., Maupin P., Pradhan D., Morrow J.S., Rimm D.L.;
RT "Alpha-catenin can form asymmetric homodimeric complexes and/or
RT heterodimeric complexes with beta-catenin.";
RL J. Biol. Chem. 272:27301-27306(1997).
RN [14]
RP INTERACTION WITH JUP; CTNNB1 AND ALPHA-ACTININ.
RX PubMed=9152027; DOI=10.1242/jcs.110.8.1013;
RA Nieset J.E., Redfield A.R., Jin F., Knudsen K.A., Johnson K.R.,
RA Wheelock M.J.;
RT "Characterization of the interactions of alpha-catenin with alpha-actinin
RT and beta-catenin/plakoglobin.";
RL J. Cell Sci. 110:1013-1022(1997).
RN [15]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [16]
RP INTERACTION WITH AJUBA.
RX PubMed=12417594; DOI=10.1074/jbc.m205391200;
RA Marie H., Pratt S.J., Betson M., Epple H., Kittler J.T., Meek L.,
RA Moss S.J., Troyanovsky S., Attwell D., Longmore G.D., Braga V.M.;
RT "The LIM protein Ajuba is recruited to cadherin-dependent cell junctions
RT through an association with alpha-catenin.";
RL J. Biol. Chem. 278:1220-1228(2003).
RN [17]
RP SUMOYLATION.
RX PubMed=15561718; DOI=10.1074/jbc.m411718200;
RA Gocke C.B., Yu H., Kang J.;
RT "Systematic identification and analysis of mammalian small ubiquitin-like
RT modifier substrates.";
RL J. Biol. Chem. 280:5004-5012(2005).
RN [18]
RP INTERACTION WITH ARHGAP21.
RX PubMed=16184169; DOI=10.1038/ncb1308;
RA Sousa S., Cabanes D., Archambaud C., Colland F., Lemichez E., Popoff M.,
RA Boisson-Dupuis S., Gouin E., Lecuit M., Legrain P., Cossart P.;
RT "ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions
RT and for Listeria invasion.";
RL Nat. Cell Biol. 7:954-960(2005).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP INTERACTION WITH LIMA1.
RX PubMed=18093941; DOI=10.1073/pnas.0710504105;
RA Abe K., Takeichi M.;
RT "EPLIN mediates linkage of the cadherin catenin complex to F-actin and
RT stabilizes the circumferential actin belt.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-634; SER-641 AND SER-652, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-268; SER-295;
RP SER-297; THR-634; SER-641 AND SER-851, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [35]
RP POSSIBLE INVOLVEMENT IN HDGC.
RX PubMed=26182300; DOI=10.1001/jamaoncol.2014.168;
RA Hansford S., Kaurah P., Li-Chang H., Woo M., Senz J., Pinheiro H.,
RA Schrader K.A., Schaeffer D.F., Shumansky K., Zogopoulos G., Santos T.A.,
RA Claro I., Carvalho J., Nielsen C., Padilla S., Lum A., Talhouk A.,
RA Baker-Lange K., Richardson S., Lewis I., Lindor N.M., Pennell E.,
RA MacMillan A., Fernandez B., Keller G., Lynch H., Shah S.P., Guilford P.,
RA Gallinger S., Corso G., Roviello F., Caldas C., Oliveira C., Pharoah P.D.,
RA Huntsman D.G.;
RT "Hereditary diffuse gastric cancer syndrome: CDH1 mutations and beyond.";
RL JAMA Oncol. 1:23-32(2015).
RN [36]
RP FUNCTION, PHOSPHORYLATION AT SER-641; SER-652; SER-655 AND THR-658, AND
RP MUTAGENESIS OF SER-641; 652-SER--THR-658 AND SER-652.
RX PubMed=25653389; DOI=10.1242/jcs.163824;
RA Escobar D.J., Desai R., Ishiyama N., Folmsbee S.S., Novak M.N.,
RA Flozak A.S., Daugherty R.L., Mo R., Nanavati D., Sarpal R., Leckband D.,
RA Ikura M., Tepass U., Gottardi C.J.;
RT "alpha-Catenin phosphorylation promotes intercellular adhesion through a
RT dual-kinase mechanism.";
RL J. Cell Sci. 128:1150-1165(2015).
RN [37]
RP IDENTIFICATION IN A CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=28051089; DOI=10.1038/mi.2016.120;
RA Caldwell J.M., Collins M.H., Kemme K.A., Sherrill J.D., Wen T., Rochman M.,
RA Stucke E.M., Amin L., Tai H., Putnam P.E., Jimenez-Dalmaroni M.J.,
RA Wormald M.R., Porollo A., Abonia J.P., Rothenberg M.E.;
RT "Cadherin 26 is an alpha integrin-binding epithelial receptor regulated
RT during allergic inflammation.";
RL Mucosal Immunol. 10:1190-1201(2017).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-57 AND LYS-797, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 377-632, PARTIAL PROTEIN SEQUENCE,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11447106; DOI=10.1093/emboj/20.14.3645;
RA Yang J., Dokurno P., Tonks N.K., Barford D.;
RT "Crystal structure of the M-fragment of alpha-catenin: implications for
RT modulation of cell adhesion.";
RL EMBO J. 20:3645-3656(2001).
RN [40]
RP INVOLVEMENT IN MDPT2, VARIANTS MDPT2 CYS-54; LYS-307; SER-318 AND MET-431,
RP AND INTERACTION WITH VCL.
RX PubMed=26691986; DOI=10.1038/ng.3474;
RA Saksens N.T., Krebs M.P., Schoenmaker-Koller F.E., Hicks W., Yu M., Shi L.,
RA Rowe L., Collin G.B., Charette J.R., Letteboer S.J., Neveling K.,
RA van Moorsel T.W., Abu-Ltaif S., De Baere E., Walraedt S., Banfi S.,
RA Simonelli F., Cremers F.P., Boon C.J., Roepman R., Leroy B.P.,
RA Peachey N.S., Hoyng C.B., Nishina P.M., den Hollander A.I.;
RT "Mutations in CTNNA1 cause butterfly-shaped pigment dystrophy and perturbed
RT retinal pigment epithelium integrity.";
RL Nat. Genet. 48:144-151(2016).
RN [41]
RP POSSIBLE INVOLVEMENT IN HDGC.
RX PubMed=23208944; DOI=10.1002/path.4152;
RA Majewski I.J., Kluijt I., Cats A., Scerri T.S., de Jong D., Kluin R.J.,
RA Hansford S., Hogervorst F.B., Bosma A.J., Hofland I., Winter M.,
RA Huntsman D., Jonkers J., Bahlo M., Bernards R.;
RT "An alpha-E-catenin (CTNNA1) mutation in hereditary diffuse gastric
RT cancer.";
RL J. Pathol. 229:621-629(2013).
CC -!- FUNCTION: Associates with the cytoplasmic domain of a variety of
CC cadherins. The association of catenins to cadherins produces a complex
CC which is linked to the actin filament network, and which seems to be of
CC primary importance for cadherins cell-adhesion properties. Can
CC associate with both E- and N-cadherins. Originally believed to be a
CC stable component of E-cadherin/catenin adhesion complexes and to
CC mediate the linkage of cadherins to the actin cytoskeleton at adherens
CC junctions. In contrast, cortical actin was found to be much more
CC dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to
CC bind to F-actin when assembled in the complex suggesting a different
CC linkage between actin and adherens junctions components. The
CC homodimeric form may regulate actin filament assembly and inhibit actin
CC branching by competing with the Arp2/3 complex for binding to actin
CC filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-
CC dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). May
CC play a crucial role in cell differentiation.
CC {ECO:0000250|UniProtKB:P26231, ECO:0000269|PubMed:25653389}.
CC -!- SUBUNIT: Monomer and homodimer; the monomer preferentially binds to
CC CTNNB1 and the homodimer to actin (By similarity). Component of an
CC cadherin:catenin adhesion complex composed of at least of CDH26, beta-
CC catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1
CC (PubMed:28051089). Possible component of an E-cadherin/ catenin
CC adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1
CC or gamma-catenin/JUP; the complex is located to adherens junctions (By
CC similarity). The stable association of CTNNA1 is controversial as
CC CTNNA1 was shown not to bind to F-actin when assembled in the complex
CC (By similarity). Alternatively, the CTNNA1-containing complex may be
CC linked to F-actin by other proteins such as LIMA1 (By similarity).
CC Binds AFDN and F-actin (By similarity). Interacts with ARHGAP21
CC (PubMed:16184169). Interacts with AJUBA (PubMed:12417594). Interacts
CC with LIMA1 (PubMed:18093941). Interacts with vinculin/VCL
CC (PubMed:26691986). {ECO:0000250|UniProtKB:P26231,
CC ECO:0000269|PubMed:12417594, ECO:0000269|PubMed:16184169,
CC ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:26691986,
CC ECO:0000269|PubMed:28051089}.
CC -!- INTERACTION:
CC P35221; P25054: APC; NbExp=3; IntAct=EBI-701918, EBI-727707;
CC P35221; P12830: CDH1; NbExp=6; IntAct=EBI-701918, EBI-727477;
CC P35221; Q5VT06: CEP350; NbExp=5; IntAct=EBI-701918, EBI-947346;
CC P35221; P35221: CTNNA1; NbExp=3; IntAct=EBI-701918, EBI-701918;
CC P35221; P35222: CTNNB1; NbExp=5; IntAct=EBI-701918, EBI-491549;
CC P35221; Q9H8V3: ECT2; NbExp=3; IntAct=EBI-701918, EBI-1054039;
CC P35221; Q9UHB6: LIMA1; NbExp=2; IntAct=EBI-701918, EBI-351479;
CC P35221; P25963: NFKBIA; NbExp=5; IntAct=EBI-701918, EBI-307386;
CC P35221; Q9H0H5: RACGAP1; NbExp=2; IntAct=EBI-701918, EBI-717233;
CC P35221; P18206-2: VCL; NbExp=2; IntAct=EBI-701918, EBI-11027067;
CC P35221; Q9ERG0-2: Lima1; Xeno; NbExp=2; IntAct=EBI-701918, EBI-15677021;
CC P35221-1; Q9ERG0-2: Lima1; Xeno; NbExp=2; IntAct=EBI-7053242, EBI-15677021;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton. Cell
CC junction, adherens junction. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell
CC boundaries and probably at cell-matrix boundaries.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane
CC {ECO:0000269|PubMed:21708131}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21708131}; Cytoplasmic side
CC {ECO:0000269|PubMed:21708131}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CTNNA1a;
CC IsoId=P35221-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35221-2; Sequence=VSP_017494;
CC Name=3; Synonyms=CTNNA1b;
CC IsoId=P35221-3; Sequence=VSP_047810;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in normal tissues.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.
CC -!- PTM: Phosphorylation seems to contribute to the strength of cell-cell
CC adhesion rather than to the basic capacity for cell-cell adhesion.
CC {ECO:0000250|UniProtKB:P26231}.
CC -!- DISEASE: Note=Germline CTNNA1 truncating mutations have been detected
CC in patients with hereditary diffuse gastric cancer (HDGC) and may play
CC a role in disease susceptibility. Diffuse gastric cancer is a malignant
CC disease characterized by poorly differentiated infiltrating lesions
CC resulting in thickening of the stomach. Malignant tumors start in the
CC stomach, can spread to the esophagus or the small intestine, and can
CC extend through the stomach wall to nearby lymph nodes and organs. It
CC also can metastasize to other parts of the body.
CC {ECO:0000269|PubMed:23208944, ECO:0000269|PubMed:26182300}.
CC -!- DISEASE: Macular dystrophy, patterned, 2 (MDPT2) [MIM:608970]: A form
CC of retinal patterned dystrophy, a heterogeneous group of macular
CC disorders caused by abnormal accumulation of lipofuscin in the retinal
CC pigment epithelium. Lipofuscin distribution can show various shapes
CC that define different types of macular dystrophy, including reticular
CC (fishnet-like) dystrophy, macroreticular (spider-shaped) dystrophy and
CC butterfly-shaped pigment dystrophy. MDPT2 is an autosomal dominant form
CC characterized by bilateral accumulation of pigment in the macular area
CC that resembles the wings of a butterfly. {ECO:0000269|PubMed:26691986}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Expressed at high levels in the nervous
CC system. Lacks the beta-catenin interaction domain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ctnna1/";
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DR EMBL; D14705; BAA03530.1; -; mRNA.
DR EMBL; D13866; BAA02979.1; -; mRNA.
DR EMBL; L23805; AAA86430.1; -; mRNA.
DR EMBL; U03100; AAA18949.1; -; mRNA.
DR EMBL; HQ589335; AEF32483.1; -; mRNA.
DR EMBL; AF102803; AAC99459.1; -; Genomic_DNA.
DR EMBL; AF102787; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102788; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102789; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102790; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102791; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102792; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102793; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102794; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102795; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102796; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102797; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102798; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102799; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102800; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102801; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AF102802; AAC99459.1; JOINED; Genomic_DNA.
DR EMBL; AY884207; AAW56940.1; -; Genomic_DNA.
DR EMBL; AC010453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62124.1; -; Genomic_DNA.
DR EMBL; BC000385; AAH00385.1; -; mRNA.
DR EMBL; BC031262; AAH31262.1; -; mRNA.
DR EMBL; L22080; AAA35502.1; -; mRNA.
DR CCDS; CCDS34243.1; -. [P35221-1]
DR CCDS; CCDS75315.1; -. [P35221-3]
DR PIR; JC2542; JC2542.
DR PIR; JN0607; JN0607.
DR RefSeq; NP_001277236.1; NM_001290307.2.
DR RefSeq; NP_001277238.1; NM_001290309.2.
DR RefSeq; NP_001277239.1; NM_001290310.2.
DR RefSeq; NP_001277241.1; NM_001290312.1. [P35221-3]
DR RefSeq; NP_001310911.1; NM_001323982.1. [P35221-1]
DR RefSeq; NP_001310912.1; NM_001323983.1. [P35221-1]
DR RefSeq; NP_001310913.1; NM_001323984.1. [P35221-1]
DR RefSeq; NP_001310916.1; NM_001323987.1. [P35221-3]
DR RefSeq; NP_001310917.1; NM_001323988.1. [P35221-3]
DR RefSeq; NP_001310918.1; NM_001323989.1. [P35221-3]
DR RefSeq; NP_001310919.1; NM_001323990.1. [P35221-3]
DR RefSeq; NP_001310920.1; NM_001323991.1. [P35221-3]
DR RefSeq; NP_001310921.1; NM_001323992.1. [P35221-3]
DR RefSeq; NP_001310922.1; NM_001323993.1. [P35221-3]
DR RefSeq; NP_001310923.1; NM_001323994.1. [P35221-3]
DR RefSeq; NP_001310924.1; NM_001323995.1. [P35221-3]
DR RefSeq; NP_001310925.1; NM_001323996.1. [P35221-3]
DR RefSeq; NP_001310926.1; NM_001323997.1. [P35221-3]
DR RefSeq; NP_001310927.1; NM_001323998.1. [P35221-3]
DR RefSeq; NP_001310928.1; NM_001323999.1. [P35221-3]
DR RefSeq; NP_001310929.1; NM_001324000.1. [P35221-3]
DR RefSeq; NP_001894.2; NM_001903.4. [P35221-1]
DR PDB; 1H6G; X-ray; 2.20 A; A/B=377-632.
DR PDB; 4EHP; X-ray; 2.66 A; B=277-382.
DR PDB; 4IGG; X-ray; 3.66 A; A/B=82-906.
DR PDB; 6UPV; EM; 3.20 A; L/M=1-906.
DR PDB; 6V2O; X-ray; 1.27 A; C=850-859.
DR PDB; 6V2P; X-ray; 1.30 A; C=850-859.
DR PDBsum; 1H6G; -.
DR PDBsum; 4EHP; -.
DR PDBsum; 4IGG; -.
DR PDBsum; 6UPV; -.
DR PDBsum; 6V2O; -.
DR PDBsum; 6V2P; -.
DR AlphaFoldDB; P35221; -.
DR SMR; P35221; -.
DR BioGRID; 107876; 255.
DR CORUM; P35221; -.
DR DIP; DIP-515N; -.
DR IntAct; P35221; 107.
DR MINT; P35221; -.
DR STRING; 9606.ENSP00000304669; -.
DR ChEMBL; CHEMBL4295748; -.
DR iPTMnet; P35221; -.
DR MetOSite; P35221; -.
DR PhosphoSitePlus; P35221; -.
DR SwissPalm; P35221; -.
DR BioMuta; CTNNA1; -.
DR DMDM; 461853; -.
DR CPTAC; CPTAC-1750; -.
DR EPD; P35221; -.
DR jPOST; P35221; -.
DR MassIVE; P35221; -.
DR MaxQB; P35221; -.
DR PaxDb; P35221; -.
DR PeptideAtlas; P35221; -.
DR PRIDE; P35221; -.
DR ProteomicsDB; 54986; -. [P35221-1]
DR ProteomicsDB; 54987; -. [P35221-2]
DR ProteomicsDB; 71584; -.
DR Antibodypedia; 3431; 788 antibodies from 44 providers.
DR DNASU; 1495; -.
DR Ensembl; ENST00000302763.12; ENSP00000304669.7; ENSG00000044115.21. [P35221-1]
DR Ensembl; ENST00000540387.5; ENSP00000438476.1; ENSG00000044115.21. [P35221-3]
DR GeneID; 1495; -.
DR KEGG; hsa:1495; -.
DR MANE-Select; ENST00000302763.12; ENSP00000304669.7; NM_001903.5; NP_001894.2.
DR UCSC; uc003ldh.4; human. [P35221-1]
DR CTD; 1495; -.
DR DisGeNET; 1495; -.
DR GeneCards; CTNNA1; -.
DR HGNC; HGNC:2509; CTNNA1.
DR HPA; ENSG00000044115; Low tissue specificity.
DR MalaCards; CTNNA1; -.
DR MIM; 116805; gene.
DR MIM; 608970; phenotype.
DR neXtProt; NX_P35221; -.
DR OpenTargets; ENSG00000044115; -.
DR Orphanet; 99001; Butterfly-shaped pigment dystrophy.
DR Orphanet; 26106; Hereditary diffuse gastric cancer.
DR PharmGKB; PA27008; -.
DR VEuPathDB; HostDB:ENSG00000044115; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; P35221; -.
DR OMA; DIGHRDQ; -.
DR OrthoDB; 953344at2759; -.
DR PhylomeDB; P35221; -.
DR TreeFam; TF313686; -.
DR PathwayCommons; P35221; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-525793; Myogenesis.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR SignaLink; P35221; -.
DR SIGNOR; P35221; -.
DR BioGRID-ORCS; 1495; 36 hits in 1084 CRISPR screens.
DR ChiTaRS; CTNNA1; human.
DR EvolutionaryTrace; P35221; -.
DR GeneWiki; Catenin_(cadherin-associated_protein),_alpha_1; -.
DR GenomeRNAi; 1495; -.
DR Pharos; P35221; Tbio.
DR PRO; PR:P35221; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P35221; protein.
DR Bgee; ENSG00000044115; Expressed in colonic epithelium and 208 other tissues.
DR ExpressionAtlas; P35221; baseline and differential.
DR Genevisible; P35221; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016600; C:flotillin complex; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005915; C:zonula adherens; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
DR GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0043297; P:apical junction assembly; NAS:UniProtKB.
DR GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0016264; P:gap junction assembly; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR030047; CTNNA1/CTNNA3.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR18914:SF24; PTHR18914:SF24; 1.
DR Pfam; PF01044; Vinculin; 2.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 4.
DR PROSITE; PS00663; VINCULIN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.10"
FT CHAIN 2..906
FT /note="Catenin alpha-1"
FT /id="PRO_0000064261"
FT REGION 2..228
FT /note="Involved in homodimerization"
FT REGION 97..148
FT /note="Interaction with JUP and CTNNB1"
FT /evidence="ECO:0000269|PubMed:9152027"
FT REGION 325..394
FT /note="Interaction with alpha-actinin"
FT REGION 864..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 634
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 641
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:25653389,
FT ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18318008"
FT MOD_RES 652
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:25653389,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 655
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:25653389"
FT MOD_RES 658
FT /note="Phosphothreonine; by CK1"
FT /evidence="ECO:0000269|PubMed:25653389"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..370
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:21708131"
FT /id="VSP_047810"
FT VAR_SEQ 811
FT /note="G -> GNCDTCGALQGLKGWPPPLCLATHW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7945318"
FT /id="VSP_017494"
FT VARIANT 54
FT /note="R -> C (in MDPT2; no effect on VCL-binding;
FT dbSNP:rs781520852)"
FT /evidence="ECO:0000269|PubMed:26691986"
FT /id="VAR_076586"
FT VARIANT 179
FT /note="A -> V (in dbSNP:rs28363394)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_022303"
FT VARIANT 219
FT /note="P -> S (in dbSNP:rs28363406)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_022304"
FT VARIANT 307
FT /note="E -> K (in MDPT2; no effect on VCL-binding;
FT dbSNP:rs869320697)"
FT /evidence="ECO:0000269|PubMed:26691986"
FT /id="VAR_076587"
FT VARIANT 318
FT /note="L -> S (in MDPT2; no effect on VCL-binding;
FT dbSNP:rs869320696)"
FT /evidence="ECO:0000269|PubMed:26691986"
FT /id="VAR_076588"
FT VARIANT 431
FT /note="I -> M (in MDPT2; no effect on VCL-binding;
FT dbSNP:rs755215402)"
FT /evidence="ECO:0000269|PubMed:26691986"
FT /id="VAR_076589"
FT MUTAGEN 641
FT /note="S->A: Abolishes phosphorylation by CK2. No effect on
FT phosphorylation by CK1."
FT /evidence="ECO:0000269|PubMed:25653389"
FT MUTAGEN 641
FT /note="S->D: Enhances phosphorylation by CK1."
FT /evidence="ECO:0000269|PubMed:25653389"
FT MUTAGEN 652..658
FT /note="SRTSVQT->ARTAVQA: Abolishes phosphorylation by CK1.
FT No effect on phosphorylation by CK2."
FT /evidence="ECO:0000269|PubMed:25653389"
FT MUTAGEN 652
FT /note="S->A: Abolishes phosphorylation by CK1."
FT /evidence="ECO:0000269|PubMed:25653389"
FT CONFLICT 92
FT /note="A -> V (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="R -> P (in Ref. 3; AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="I -> N (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="K -> S (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="Q -> K (in Ref. 1; BAA03530)"
FT /evidence="ECO:0000305"
FT CONFLICT 344..348
FT /note="LQDLL -> CRTCV (in Ref. 3; AAA86430)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="L -> G (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="L -> TW (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="A -> P (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="R -> E (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="A -> R (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="A -> R (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="Q -> H (in Ref. 1; BAA03530)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="W -> M (in Ref. 3; AAA86430/AAA18949)"
FT /evidence="ECO:0000305"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:4EHP"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4EHP"
FT HELIX 305..316
FT /evidence="ECO:0007829|PDB:4EHP"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4EHP"
FT HELIX 328..352
FT /evidence="ECO:0007829|PDB:4EHP"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4EHP"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:1H6G"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 413..438
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 444..473
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 478..506
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 509..531
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 535..559
FT /evidence="ECO:0007829|PDB:1H6G"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 567..581
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 583..598
FT /evidence="ECO:0007829|PDB:1H6G"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 608..630
FT /evidence="ECO:0007829|PDB:1H6G"
FT HELIX 700..703
FT /evidence="ECO:0007829|PDB:6UPV"
FT HELIX 713..727
FT /evidence="ECO:0007829|PDB:6UPV"
FT TURN 728..732
FT /evidence="ECO:0007829|PDB:6UPV"
FT HELIX 739..766
FT /evidence="ECO:0007829|PDB:6UPV"
FT TURN 770..772
FT /evidence="ECO:0007829|PDB:6UPV"
FT HELIX 773..775
FT /evidence="ECO:0007829|PDB:6UPV"
FT HELIX 777..804
FT /evidence="ECO:0007829|PDB:6UPV"
FT TURN 806..808
FT /evidence="ECO:0007829|PDB:6UPV"
FT TURN 812..814
FT /evidence="ECO:0007829|PDB:6UPV"
FT HELIX 816..826
FT /evidence="ECO:0007829|PDB:6UPV"
FT TURN 827..829
FT /evidence="ECO:0007829|PDB:6UPV"
FT TURN 832..834
FT /evidence="ECO:0007829|PDB:6UPV"
FT HELIX 835..841
FT /evidence="ECO:0007829|PDB:6UPV"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:6UPV"
FT TURN 847..849
FT /evidence="ECO:0007829|PDB:6UPV"
FT HELIX 850..852
FT /evidence="ECO:0007829|PDB:6UPV"
FT TURN 856..858
FT /evidence="ECO:0007829|PDB:6UPV"
SQ 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
