ID CTNA2_HUMAN Reviewed; 953 AA. AC P26232; B3KXE5; B7Z2W7; B7Z352; B7Z898; Q4ZFW1; Q53R26; Q53R33; Q53T67; AC Q53T71; Q53TM8; Q7Z3L1; Q7Z3Y0; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 04-NOV-2026, entry version 217. DE RecName: Full=Catenin alpha-2; DE AltName: Full=Alpha N-catenin; DE AltName: Full=Alpha-catenin-related protein; GN Name=CTNNA2; Synonyms=CAPR; 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=8432524; DOI=10.1006/geno.1993.1004; RA Claverie J.-M., Hardelin J.-P., Legouis R., Levilliers J., Bougueleret L., RA Mattei M.-G., Petit C.; RT "Characterization and chromosomal assignment of a human cDNA encoding a RT protein related to the murine 102-kDa cadherin-associated protein (alpha- RT catenin)."; RL Genomics 15:13-20(1993). RN [2] RP SEQUENCE REVISION TO C-TERMINUS. RA Hardelin J.-P.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5). RC TISSUE=Brain, Hippocampus, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). RC TISSUE=Hippocampus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=PNS; 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 [8] RP INTERACTION WITH ZNF639, AND SUBCELLULAR LOCATION. RX PubMed=16182284; DOI=10.1016/j.yexcr.2005.06.018; RA Bogaerts S., Vanlandschoot A., van Hengel J., van Roy F.; RT "Nuclear translocation of alphaN-catenin by the novel zinc finger RT transcriptional repressor ZASC1."; RL Exp. Cell Res. 311:1-13(2005). RN [9] RP ALTERNATIVE SPLICING (ISOFORM 6). RX PubMed=18163523; DOI=10.1002/ajmg.b.30679; RA Mexal S., Berger R., Pearce L., Barton A., Logel J., Adams C.E., Ross R.G., RA Freedman R., Leonard S.; RT "Regulation of a novel alphaN-catenin splice variant in schizophrenic RT smokers."; RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 147:759-768(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640, AND IDENTIFICATION BY RP 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 [11] RP FUNCTION, INTERACTION WITH F-ACTIN, TISSUE SPECIFICITY, INVOLVEMENT IN RP CDCBM9, VARIANTS CDCBM9 494-ARG--PHE-953 DEL; 781-ARG--PHE-953 DEL AND RP 930-ARG--PHE-953 DEL, AND CHARACTERIZATION OF VARIANT CDCBM9 RP 781-ARG--PHE-953 DEL. RX PubMed=30013181; DOI=10.1038/s41588-018-0166-0; RA Schaffer A.E., Breuss M.W., Caglayan A.O., Al-Sanaa N., Al-Abdulwahed H.Y., RA Kaymakcalan H., Yilmaz C., Zaki M.S., Rosti R.O., Copeland B., Baek S.T., RA Musaev D., Scott E.C., Ben-Omran T., Kariminejad A., Kayserili H., RA Mojahedi F., Kara M., Cai N., Silhavy J.L., Elsharif S., Fenercioglu E., RA Barshop B.A., Kara B., Wang R., Stanley V., James K.N., Nachnani R., RA Kalur A., Megahed H., Incecik F., Danda S., Alanay Y., Faqeih E., RA Melikishvili G., Mansour L., Miller I., Sukhudyan B., Chelly J., RA Dobyns W.B., Bilguvar K., Jamra R.A., Gunel M., Gleeson J.G.; RT "Biallelic loss of human CTNNA2, encoding alphaN-catenin, leads to ARP2/3 RT complex overactivity and disordered cortical neuronal migration."; RL Nat. Genet. 50:1093-1101(2018). CC -!- FUNCTION: May function as a linker between cadherin adhesion receptors CC and the cytoskeleton to regulate cell-cell adhesion and differentiation CC in the nervous system (By similarity). Required for proper regulation CC of cortical neuronal migration and neurite growth (PubMed:30013181). It CC acts as a negative regulator of Arp2/3 complex activity and Arp2/3- CC mediated actin polymerization (PubMed:30013181). It thereby suppresses CC excessive actin branching which would impair neurite growth and CC stability (PubMed:30013181). Regulates morphological plasticity of CC synapses and cerebellar and hippocampal lamination during development. CC Functions in the control of startle modulation (By similarity). CC {ECO:0000250|UniProtKB:Q61301, ECO:0000269|PubMed:30013181}. CC -!- SUBUNIT: Interacts with CDH1 and CDH2 (By similarity). Interacts with CC ZNF639; recruits CTNNA2 to the nucleus (PubMed:16182284). Interacts CC with F-actin (PubMed:30013181). {ECO:0000250|UniProtKB:P30997, CC ECO:0000269|PubMed:16182284, ECO:0000269|PubMed:30013181}. CC -!- INTERACTION: CC P26232; Q02410: APBA1; NbExp=2; IntAct=EBI-3953920, EBI-368690; CC P26232; Q99767: APBA2; NbExp=2; IntAct=EBI-3953920, EBI-81711; CC P26232; P35222: CTNNB1; NbExp=5; IntAct=EBI-3953920, EBI-491549; CC P26232; Q12959: DLG1; NbExp=3; IntAct=EBI-3953920, EBI-357481; CC P26232; Q92796: DLG3; NbExp=3; IntAct=EBI-3953920, EBI-80440; CC P26232; P78352: DLG4; NbExp=3; IntAct=EBI-3953920, EBI-80389; CC P26232; Q68DX3: FRMPD2; NbExp=3; IntAct=EBI-3953920, EBI-53993476; CC P26232; A4D2P6: GRID2IP; NbExp=2; IntAct=EBI-3953920, EBI-15893226; CC P26232; Q9Y3R0: GRIP1; NbExp=5; IntAct=EBI-3953920, EBI-5349621; CC P26232; Q9C0E4: GRIP2; NbExp=5; IntAct=EBI-3953920, EBI-949557; CC P26232; Q14005: IL16; NbExp=3; IntAct=EBI-3953920, EBI-2831580; CC P26232; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-3953920, EBI-739832; CC P26232; Q8N448: LNX2; NbExp=2; IntAct=EBI-3953920, EBI-2340947; CC P26232; Q96QZ7: MAGI1; NbExp=2; IntAct=EBI-3953920, EBI-924464; CC P26232; Q86UL8: MAGI2; NbExp=5; IntAct=EBI-3953920, EBI-311035; CC P26232; O75970: MPDZ; NbExp=3; IntAct=EBI-3953920, EBI-821405; CC P26232; Q86UT5: NHERF4; NbExp=2; IntAct=EBI-3953920, EBI-8744528; CC P26232; Q8NI35: PATJ; NbExp=9; IntAct=EBI-3953920, EBI-724390; CC P26232; Q5T2W1: PDZK1; NbExp=3; IntAct=EBI-3953920, EBI-349819; CC P26232; Q14160: SCRIB; NbExp=3; IntAct=EBI-3953920, EBI-357345; CC P26232; O14907: TAX1BP3; NbExp=5; IntAct=EBI-3953920, EBI-723259; CC P26232; Q07157: TJP1; NbExp=2; IntAct=EBI-3953920, EBI-79553; CC P26232; Q9P202: WHRN; NbExp=3; IntAct=EBI-3953920, EBI-310886; CC P26232; Q9UID6: ZNF639; NbExp=7; IntAct=EBI-3953920, EBI-947476; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q61301}; CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q61301}; Cytoplasmic CC side {ECO:0000250|UniProtKB:Q61301}. Cytoplasm CC {ECO:0000269|PubMed:16182284}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q61301}. Cell junction, adherens junction CC {ECO:0000250|UniProtKB:Q61301}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q61301}. Nucleus {ECO:0000269|PubMed:16182284}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=AlphaN-catenin II; CC IsoId=P26232-1; Sequence=Displayed; CC Name=2; Synonyms=AlphaN-catenin I; CC IsoId=P26232-2; Sequence=VSP_020337; CC Name=3; CC IsoId=P26232-3; Sequence=VSP_038009; CC Name=4; CC IsoId=P26232-4; Sequence=VSP_038008, VSP_020337; CC Name=5; CC IsoId=P26232-5; Sequence=VSP_038007, VSP_020337; CC Name=6; Synonyms=AlphaN-catenin III; CC IsoId=P26232-6; Sequence=VSP_038005, VSP_038006, VSP_020337; CC -!- TISSUE SPECIFICITY: Expressed in neural tissues, with strongest CC expression in fetal and adult brain. Expressed in the developing CC cortical plate and marginal zone of 20-week-old human fetal brain. CC {ECO:0000269|PubMed:30013181}. CC -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 9 CC (CDCBM9) [MIM:618174]: An autosomal recessive disorder characterized by CC neurodevelopmental delay apparent from early infancy, acquired CC microcephaly, hypotonic cerebral palsy, inability to ambulate or speak, CC and intractable seizures. Brain imaging shows pachygyria with severe CC cortical gray matter thickening, paucity of gyri without an obvious CC posterior-anterior gradient or focal dysplasias, hypogenesis of the CC corpus callosum, and cerebellar hypoplasia. CC {ECO:0000269|PubMed:30013181}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family. CC {ECO:0000305}. 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; M94151; AAA58407.2; -; mRNA. DR EMBL; AK127226; BAG54457.1; -; mRNA. DR EMBL; AK295181; BAH12003.1; -; mRNA. DR EMBL; AK295493; BAH12088.1; -; mRNA. DR EMBL; AK303035; BAH13884.1; -; mRNA. DR EMBL; BX537769; CAD97832.1; -; mRNA. DR EMBL; AC008067; AAY15073.1; -; Genomic_DNA. DR EMBL; AC010975; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011741; AAX93241.1; -; Genomic_DNA. DR EMBL; AC011746; AAY15008.1; -; Genomic_DNA. DR EMBL; AC016670; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC016716; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093322; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC096573; AAY14758.1; -; Genomic_DNA. DR EMBL; AC096753; AAY14763.1; -; Genomic_DNA. DR EMBL; AC104780; AAX88946.1; -; Genomic_DNA. DR EMBL; FJ695201; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471053; EAW99564.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99565.1; -; Genomic_DNA. DR EMBL; BC052996; AAH52996.1; -; mRNA. DR CCDS; CCDS42703.2; -. [P26232-2] DR CCDS; CCDS54371.1; -. [P26232-3] DR CCDS; CCDS62944.1; -. [P26232-1] DR CCDS; CCDS62945.1; -. [P26232-6] DR CCDS; CCDS74531.1; -. [P26232-4] DR PIR; A45011; A45011. DR RefSeq; NP_001158355.1; NM_001164883.2. [P26232-3] DR RefSeq; NP_001269526.1; NM_001282597.3. [P26232-1] DR RefSeq; NP_001269527.1; NM_001282598.2. [P26232-5] DR RefSeq; NP_001269528.1; NM_001282599.2. [P26232-6] DR RefSeq; NP_001269529.1; NM_001282600.2. [P26232-4] DR RefSeq; NP_001307739.1; NM_001320810.2. DR RefSeq; NP_001386666.1; NM_001399737.1. [P26232-2] DR RefSeq; NP_004380.2; NM_004389.4. [P26232-2] DR RefSeq; XP_011530858.1; XM_011532556.3. [P26232-1] DR RefSeq; XP_016858892.1; XM_017003403.3. [P26232-2] DR RefSeq; XP_024308482.1; XM_024452714.2. [P26232-1] DR RefSeq; XP_024308483.1; XM_024452715.2. [P26232-1] DR RefSeq; XP_054196616.1; XM_054340641.1. [P26232-1] DR RefSeq; XP_054196617.1; XM_054340642.1. [P26232-1] DR RefSeq; XP_054196618.1; XM_054340643.1. [P26232-1] DR RefSeq; XP_054196619.1; XM_054340644.1. [P26232-2] DR PDB; 6DUW; X-ray; 2.20 A; A=651-953. DR AlphaFoldDB; P26232; -. DR EMDB; EMD-27717; -. DR SMR; P26232; -. DR BioGRID; 107877; 86. DR DIP; DIP-60979N; -. DR FunCoup; P26232; 1258. DR IntAct; P26232; 131. DR NDEx; IQUERY-CP-CTNNA2; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000384638; -. DR GlyGen; P26232; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P26232; -. DR PhosphoSitePlus; P26232; -. DR SwissPalm; P26232; -. DR BioMuta; CTNNA2; -. DR DMDM; 114152793; -. DR CPTAC; CPTAC-1756; -. DR jPOST; P26232; -. DR MassIVE; P26232; -. DR PaxDb; 9606-ENSP00000384638; -. DR PeptideAtlas; P26232; -. DR ProteomicsDB; 54314; -. [P26232-1] DR ProteomicsDB; 54315; -. [P26232-2] DR ProteomicsDB; 54316; -. [P26232-3] DR ProteomicsDB; 54317; -. [P26232-4] DR ProteomicsDB; 54318; -. [P26232-5] DR ProteomicsDB; 54319; -. [P26232-6] DR Pumba; P26232; -. DR TopDownProteomics; P26232-6; -. [P26232-6] DR Antibodypedia; 8335; 158 antibodies from 30 providers. DR DNASU; 1496; -. DR Ensembl; ENST00000343114.7; ENSP00000341500.3; ENSG00000066032.19. [P26232-6] DR Ensembl; ENST00000402739.9; ENSP00000384638.4; ENSG00000066032.19. [P26232-1] DR Ensembl; ENST00000466387.5; ENSP00000418191.1; ENSG00000066032.19. [P26232-2] DR Ensembl; ENST00000496558.5; ENSP00000419295.1; ENSG00000066032.19. [P26232-2] DR Ensembl; ENST00000541047.5; ENSP00000444675.2; ENSG00000066032.19. [P26232-4] DR Ensembl; ENST00000629316.2; ENSP00000486160.1; ENSG00000066032.19. [P26232-3] DR GeneID; 1496; -. DR KEGG; hsa:1496; -. DR MANE-Select; ENST00000402739.9; ENSP00000384638.4; NM_001282597.3; NP_001269526.1. DR UCSC; uc010yse.3; human. [P26232-1] DR AGR; HGNC:2510; -. DR ClinPGx; PA27013; -. DR CTD; 1496; -. DR DisGeNET; 1496; -. DR GeneCards; CTNNA2; -. DR HGNC; HGNC:2510; CTNNA2. DR HPA; ENSG00000066032; Group enriched (brain, epididymis, retina). DR MalaCards; CTNNA2; -. DR MIM; 114025; gene. DR MIM; 618174; phenotype. DR OpenTargets; ENSG00000066032; -. DR VEuPathDB; HostDB:ENSG00000066032; -. DR eggNOG; KOG3681; Eukaryota. DR GeneTree; ENSGT01030000234543; -. DR HOGENOM; CLU_015314_2_0_1; -. DR InParanoid; P26232; -. DR OMA; AARRQQX; -. DR OrthoDB; 6376697at2759; -. DR PAN-GO; P26232; 6 GO annotations based on evolutionary models. DR PhylomeDB; P26232; -. DR PathwayCommons; P26232; -. DR Reactome; R-HSA-525793; Myogenesis. DR SignaLink; P26232; -. DR SIGNOR; P26232; -. DR Agora; ENSG00000066032; -. DR BioGRID-ORCS; 1496; 15 hits in 1149 CRISPR screens. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; CTNNA2; human. DR GenomeRNAi; 1496; -. DR Pharos; P26232; Tbio. DR PRO; PR:P26232; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P26232; protein. DR Bgee; ENSG00000066032; Expressed in frontal pole and 150 other cell types or tissues. DR ExpressionAtlas; P26232; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro. DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0016342; C:catenin complex; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB. DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB. DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB. DR GO; GO:0048854; P:brain morphogenesis; ISS:UniProtKB. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB. DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB. DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IMP:UniProtKB. DR GO; GO:0060134; P:prepulse inhibition; ISS:UniProtKB. DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; ISS:UniProtKB. DR GO; GO:2001222; P:regulation of neuron migration; IMP:UniProtKB. DR GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB. DR GO; GO:0051823; P:regulation of synapse structural plasticity; ISS:UniProtKB. 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 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:SF23; CATENIN ALPHA-2; 1. DR Pfam; PF01044; Vinculin; 2. 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 3D-structure; Alternative splicing; Cell adhesion; Cell junction; KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; KW Developmental protein; Differentiation; Disease variant; Lissencephaly; KW Membrane; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome. FT CHAIN 1..953 FT /note="Catenin alpha-2" FT /id="PRO_0000064263" FT REGION 912..939 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 912..927 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 928..938 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 632 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q61301" FT MOD_RES 640 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 651 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61301" FT MOD_RES 901 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61301" FT MOD_RES 939 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61301" FT VAR_SEQ 1..368 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038008" FT VAR_SEQ 1..351 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_038005" FT VAR_SEQ 1 FT /note="M -> MSGLICLQYGLWHGQKIDFGGPRRLLQRNRGEGSM (in isoform FT 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038007" FT VAR_SEQ 352 FT /note="N -> MDGWRRPLQSVGKVCEKNMKTSEMHTMSGAQ (in isoform 6)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_038006" FT VAR_SEQ 766..858 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038009" FT VAR_SEQ 811..858 FT /note="Missing (in isoform 2, isoform 4, isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_020337" FT VARIANT 494..953 FT /note="Missing (in CDCBM9)" FT /evidence="ECO:0000269|PubMed:30013181" FT /id="VAR_081335" FT VARIANT 781..953 FT /note="Missing (in CDCBM9; loss-of-function variant FT resulting in decreased neurite length and impaired neuronal FT migration in patient-derived nerve cells; no protein FT detected in patient cells)" FT /evidence="ECO:0000269|PubMed:30013181" FT /id="VAR_081336" FT VARIANT 930..953 FT /note="Missing (in CDCBM9; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30013181" FT /id="VAR_081337" FT CONFLICT 122 FT /note="T -> A (in Ref. 3; BAH12003)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="E -> K (in Ref. 1; AAA58407)" FT /evidence="ECO:0000305" FT CONFLICT 309 FT /note="S -> SS (in Ref. 5; AAY15008)" FT /evidence="ECO:0000305" FT CONFLICT 651..652 FT /note="SR -> RG (in Ref. 1; AAA58407)" FT /evidence="ECO:0000305" FT HELIX 677..702 FT /evidence="ECO:0007829|PDB:6DUW" FT HELIX 710..729 FT /evidence="ECO:0007829|PDB:6DUW" FT HELIX 738..765 FT /evidence="ECO:0007829|PDB:6DUW" FT HELIX 769..792 FT /evidence="ECO:0007829|PDB:6DUW" FT STRAND 798..802 FT /evidence="ECO:0007829|PDB:6DUW" FT STRAND 805..809 FT /evidence="ECO:0007829|PDB:6DUW" FT HELIX 861..894 FT /evidence="ECO:0007829|PDB:6DUW" SQ SEQUENCE 953 AA; 105313 MW; 5FC88907B37E8A6C CRC64; MTSATSPIIL KWDPKSLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL AASVEQATQN FLEKGEQIAK ESQDLKEELV AAVEDVRKQG ETMRIASSEF ADDPCSSVKR GTMVRAARAL LSAVTRLLIL ADMADVMRLL SHLKIVEEAL EAVKNATNEQ DLANRFKEFG KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR DYVFKQVQEA IAGISNAAQA TSPTDEAKGH TGIGELAAAL NEFDNKIILD PMTFSEARFR PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNAVRQ ALQDLLSEYM NNTGRKEKGD PLNIAIDKMT KKTRDLRRQL RKAVMDHISD SFLETNVPLL VLIEAAKSGN EKEVKEYAQV FREHANKLVE VANLACSISN NEEGVKLVRM AATQIDSLCP QVINAALTLA ARPQSKVAQD NMDVFKDQWE KQVRVLTEAV DDITSVDDFL SVSENHILED VNKCVIALQE GDVDTLDRTA GAIRGRAARV IHIINAEMEN YEAGVYTEKV LEATKLLSET VMPRFAEQVE VAIEALSANV PQPFEENEFI DASRLVYDGV RDIRKAVLMI RTPEELEDDS DFEQEDYDVR SRTSVQTEDD QLIAGQSARA IMAQLPQEEK AKIAEQVEIF HQEKSKLDAE VAKWDDSGND IIVLAKQMCM IMMEMTDFTR GKGPLKNTSD VINAAKKIAE AGSRMDKLAR AVADQCPDSA CKQDLLAYLQ RIALYCHQLN ICSKVKAEVQ NLGGELIVSG TGVQSTFTTF YEVDCDVIDG GRASQLSTHL PTCAEGAPIG SGSSDSSMLD SATSLIQAAK NLMNAVVLTV KASYVASTKY QKVYGTAAVN SPVVSWKMKA PEKKPLVKRE KPEEFQTRVR RGSQKKHISP VQALSEFKAM DSF //