CTNNA1
entrez
1495
canonical
uniprot
P35221
canonical
ensembl
ENSG00000044115
resolver
ensp
ENSP00000304669
resolver
ensp
ENSP00000427821
resolver
ensp
ENSP00000438476
resolver
ensp
ENSP00000486200
resolver
ensp
ENSP00000559758
resolver
ensp
ENSP00000559760
resolver
ensp
ENSP00000559762
resolver
ensp
ENSP00000559771
resolver
ensp
ENSP00000559773
resolver
ensp
ENSP00000708777
resolver
enst
ENST00000518825
resolver
enst
ENST00000627109
resolver
genesymbol
CTNNA1
resolver
hgnc
HGNC:2509
resolver
uniprot
A0A384MDY0
resolver
uniprot
B4DKT9
resolver
uniprot
B4DU00
resolver
uniprot
G3XAM7
resolver
uniprot
Q12795
resolver
uniprot
Q8N1C0
resolver
uniprot_entry
A0A384MDY0_HUMAN
resolver
uniprot_entry
B4DKT9_HUMAN
resolver
uniprot_entry
B4DU00_HUMAN
resolver
uniprot_entry
CTNA1_HUMAN
resolver
uniprot_entry
G3XAM7_HUMAN
resolver
uniprot_sec
Q12795
resolver
uniprot_sec
Q8N1C0
resolver
amino_acid_sequence
MTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDVGHRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQATASDDASQHQGGGGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI
uniprot
proteins
disease_involvement
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 variants affecting the gene represented in this entry.
uniprot
proteins
function
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 (PubMed:40983751). 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. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). May play a crucial role in cell differentiation. {ECO:0000250|UniProtKB:P26231, ECO:0000269|PubMed:25653389, ECO:0000269|PubMed:40983751}.
uniprot
proteins
mass_dalton
100071
uniprot
proteins
mutagenesis
MUTAGEN 641; /note="S->A: Abolishes phosphorylation by CK2. No effect on phosphorylation by CK1."; /evidence="ECO:0000269|PubMed:25653389"; MUTAGEN 641; /note="S->D: Enhances phosphorylation by CK1."; /evidence="ECO:0000269|PubMed:25653389"; MUTAGEN 652..658; /note="SRTSVQT->ARTAVQA: Abolishes phosphorylation by CK1. No effect on phosphorylation by CK2."; /evidence="ECO:0000269|PubMed:25653389"; MUTAGEN 652; /note="S->A: Abolishes phosphorylation by CK1."; /evidence="ECO:0000269|PubMed:25653389
uniprot
proteins
post_translational_modification
PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.; PTM: Monoubiquitinated by UBE2O at multiple lysine residues leading to binding swith from beta-catenin to vinculin. {ECO:0000269|PubMed:40983751}.; 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}.
uniprot
proteins
protein_family
Vinculin/alpha-catenin family
uniprot
proteins
pubmed
10508479
uniprot
proteins
pubmed
11447106
uniprot
proteins
pubmed
12417594
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15561718
uniprot
proteins
pubmed
16184169
uniprot
proteins
pubmed
16807684
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17487921
uniprot
proteins
pubmed
18093941
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21708131
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23208944
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25653389
uniprot
proteins
pubmed
26182300
uniprot
proteins
pubmed
26691986
uniprot
proteins
pubmed
28051089
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
40983751
uniprot
proteins
pubmed
7945318
uniprot
proteins
pubmed
7982500
uniprot
proteins
pubmed
8188230
uniprot
proteins
pubmed
8323564
uniprot
proteins
pubmed
8404069
uniprot
proteins
pubmed
9152027
uniprot
proteins
pubmed
9341178
uniprot
proteins
sequence_length
906
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P26231}. Cell junction, adherens junction {ECO:0000269|PubMed:25653389}. Cell membrane {ECO:0000250|UniProtKB:P26231}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000250|UniProtKB:P26231}. Cell junction {ECO:0000269|PubMed:12417594, ECO:0000269|PubMed:16184169}. Cytoplasm {ECO:0000250|UniProtKB:Q9PVF8}. Nucleus {ECO:0000269|PubMed:16184169}. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries. {ECO:0000250|UniProtKB:P26231}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:21708131}; Peripheral membrane protein {ECO:0000269|PubMed:21708131}; Cytoplasmic side {ECO:0000269|PubMed:21708131}.
uniprot
proteins