ID G3XAM7_HUMAN Unreviewed; 841 AA. AC G3XAM7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 02-SEP-2026, entry version 118. DE RecName: Full=Catenin alpha-1 {ECO:0000256|ARBA:ARBA00044775}; GN Name=CTNNA1 {ECO:0000313|Ensembl:ENSP00000427821.1}; 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 {ECO:0000313|Ensembl:ENSP00000427821.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000427821.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11237011; DOI=10.1038/35057062; RG International Human Genome Sequencing Consortium; RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J., RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K., RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P., RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J., RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C., RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J., RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C., RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I., RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S., RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S., RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S., RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A., RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R., RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A., RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W., RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T., RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E., RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B., RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L., RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y., RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C., RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W., RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P., RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M., RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A., RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A., RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M., RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R., RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A., RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J., RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N., RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L., RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G., RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R., RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G., RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W., RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J., RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M., RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J., RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E., RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J., RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F., RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A., RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K., RA Shizuya H., Choi S., Chen Y.J.; RT "Initial sequencing and analysis of the human genome."; RL Nature 409:860-921(2001). RN [2] {ECO:0000313|Ensembl:ENSP00000427821.1, ECO:0000313|Proteomes:UP000005640} 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 [3] {ECO:0000313|Ensembl:ENSP00000427821.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496913; DOI=10.1038/nature03001; RG International Human Genome Sequencing Consortium; RT "Finishing the euchromatic sequence of the human genome."; RL Nature 431:931-945(2004). RN [4] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [5] {ECO:0007829|PubMed:16964243} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [6] {ECO:0007829|PubMed:16807684} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [7] {ECO:0007829|PubMed:17487921} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [8] {ECO:0007829|PubMed:18220336} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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.; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [10] {ECO:0007829|PubMed:18318008} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [11] {ECO:0007829|PubMed:19413330} 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 [12] {ECO:0007829|PubMed:19369195} RP IDENTIFICATION BY 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 [13] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [14] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [15] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [16] {ECO:0007829|PubMed:21406692} 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 [17] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; 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 [18] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [19] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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 [20] {ECO:0000313|Ensembl:ENSP00000427821.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton CC {ECO:0000256|ARBA:ARBA00004245}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family. CC {ECO:0000256|ARBA:ARBA00008376}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; KF458015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001277236.1; NM_001290307.3. DR AlphaFoldDB; G3XAM7; -. DR SMR; G3XAM7; -. DR ProteomicsDB; 33790; -. DR Antibodypedia; 3431; 794 antibodies from 47 providers. DR DNASU; 1495; -. DR Ensembl; ENST00000518825.5; ENSP00000427821.1; ENSG00000044115.22. DR Ensembl; ENST00000627109.2; ENSP00000486200.1; ENSG00000044115.22. DR GeneID; 1495; -. DR UCSC; uc003ldj.4; human. DR CTD; 1495; -. DR DisGeNET; 1495; -. DR HGNC; HGNC:2509; CTNNA1. DR OpenTargets; ENSG00000044115; -. DR VEuPathDB; HostDB:ENSG00000044115; -. DR GeneTree; ENSGT01030000234543; -. DR OrthoDB; 6376697at2759; -. DR BioGRID-ORCS; 1495; 38 hits in 1168 CRISPR screens. DR ChiTaRS; CTNNA1; human. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000044115; Expressed in colonic epithelium and 210 other cell types or tissues. DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro. DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProtKB-ARBA. DR GO; GO:0098797; C:plasma membrane protein complex; IEA:UniProtKB-ARBA. DR GO; GO:0051015; F:actin filament binding; IEA:InterPro. DR GO; GO:0045296; F:cadherin binding; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR FunFam; 1.20.120.230:FF:000006; Catenin alpha 1; 1. DR FunFam; 1.20.120.230:FF:000007; Catenin alpha 1; 1. DR FunFam; 1.20.120.230:FF:000008; Catenin alpha 1; 1. DR FunFam; 1.20.120.230:FF:000011; Catenin alpha 1; 1. DR FunFam; 1.20.120.230:FF:000012; Catenin alpha-2 isoform 1; 1. DR Gene3D; 6.10.250.2510; -; 1. DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 5. DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf. DR InterPro; IPR001033; Alpha_catenin. DR InterPro; IPR006077; Vinculin/catenin. DR InterPro; IPR000633; Vinculin_CS. DR PANTHER; PTHR18914; ALPHA CATENIN; 1. DR PANTHER; PTHR18914:SF24; CATENIN ALPHA-1; 1. DR Pfam; PF01044; Vinculin; 1. DR PRINTS; PR00805; ALPHACATENIN. DR SUPFAM; SSF47220; alpha-catenin/vinculin-like; 4. DR PROSITE; PS00663; VINCULIN_1; 1. PE 1: Evidence at protein level; KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889}; KW Cell junction {ECO:0000256|ARBA:ARBA00022949}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Proteomics identification {ECO:0007829|PeptideAtlas:G3XAM7, KW ECO:0007829|ProteomicsDB:G3XAM7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. SQ SEQUENCE 841 AA; 92722 MW; C5168109B1E7B113 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 GNCDTCGALQ GLKGWPPPLC WPLTGWTAPC P //