GJA1
entrez
2697
canonical
uniprot
P17302
canonical
ensembl
ENSG00000152661
resolver
ensp
ENSP00000282561
resolver
ensp
ENSP00000497283
resolver
ensp
ENSP00000497367
resolver
ensp
ENSP00000497565
resolver
ensp
ENSP00000568992
resolver
ensp
ENSP00000582119
resolver
ensp
ENSP00000582120
resolver
enst
ENST00000282561
resolver
enst
ENST00000647564
resolver
enst
ENST00000649003
resolver
enst
ENST00000650427
resolver
enst
ENST00000898933
resolver
enst
ENST00000912060
resolver
enst
ENST00000912061
resolver
genesymbol
GJA1
resolver
genesymbol_syn
GJAL
resolver
hgnc
HGNC:4274
resolver
uniprot
B2R5U9
resolver
uniprot
Q6FHU1
resolver
uniprot
Q9Y5I8
resolver
uniprot_entry
CXA1_HUMAN
resolver
uniprot_sec
B2R5U9
resolver
uniprot_sec
Q6FHU1
resolver
uniprot_sec
Q9Y5I8
resolver
amino_acid_sequence
MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVDMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSIFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATSGALSPAKDCGSQKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNSKKLAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI
uniprot
proteins
disease_involvement
DISEASE: Oculodentodigital dysplasia (ODDD) [MIM:164200]: A disease characterized by a typical facial appearance and variable involvement of the eyes, dentition, and fingers. Characteristic facial features include a narrow, pinched nose with hypoplastic alae nasi, prominent columella and thin anteverted nares together with a narrow nasal bridge, and prominent epicanthic folds giving the impression of hypertelorism. The teeth are usually small and carious. Typical eye findings include microphthalmia and microcornea. The characteristic digital malformation is complete syndactyly of the fourth and fifth fingers (syndactyly type III) but the third finger may be involved and associated camptodactyly is a common finding. Cardiac abnormalities are observed in rare instances. {ECO:0000269|PubMed:16816024}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Oculodentodigital dysplasia, autosomal recessive (ODDD-AR) [MIM:257850]: A disease characterized by a typical facial appearance and variable involvement of the eyes, dentition, and fingers. Characteristic facial features include a narrow, pinched nose with hypoplastic alae nasi, prominent columella and thin anteverted nares together with a narrow nasal bridge, and prominent epicanthic folds giving the impression of hypertelorism. The teeth are usually small and carious. Typical eye findings include microphthalmia and microcornea. The characteristic digital malformation is complete syndactyly of the fourth and fifth fingers (syndactyly type III) but the third finger may be involved and associated camptodactyly is a common finding. Cardiac abnormalities are observed in rare instances. {ECO:0000269|PubMed:16816024}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Syndactyly 3 (SDTY3) [MIM:186100]: A form of syndactyly, a congenital anomaly of the hand or foot marked by persistence of the webbing between adjacent digits that are more or less completely attached. In SDTY3, there is usually complete and bilateral syndactyly between the fourth and fifth fingers. Usually it is soft tissue syndactyly but occasionally the distal phalanges are fused. The fifth finger is short with absent or rudimentary middle phalanx. The feet are not affected. {ECO:0000269|PubMed:14729836}. Note=The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Hypoplastic left heart syndrome 1 (HLHS1) [MIM:241550]: A syndrome due to defective development of the aorta proximal to the entrance of the ductus arteriosus, and hypoplasia of the left ventricle and mitral valve. As a result of the abnormal circulation, the ductus arteriosus and foramen ovale are patent and the right atrium, right ventricle, and pulmonary artery are enlarged. {ECO:0000269|PubMed:11470490}. Note=The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Hallermann-Streiff syndrome (HSS) [MIM:234100]: A disorder characterized by a typical skull shape (brachycephaly with frontal bossing), hypotrichosis, microphthalmia, cataracts, beaked nose, micrognathia, skin atrophy, dental anomalies and proportionate short stature. Intellectual disability is present in a minority of cases. {ECO:0000269|PubMed:14974090}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Craniometaphyseal dysplasia, autosomal recessive (CMDR) [MIM:218400]: An osteochondrodysplasia characterized by hyperostosis and sclerosis of the craniofacial bones associated with abnormal modeling of the metaphyses. Sclerosis of the skull may lead to asymmetry of the mandible, as well as to cranial nerve compression, that may finally result in hearing loss and facial palsy. {ECO:0000269|PubMed:23951358}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Erythrokeratodermia variabilis et progressiva 3 (EKVP3) [MIM:617525]: A form of erythrokeratodermia variabilis et progressiva, a genodermatosis characterized by the coexistence of two independent skin lesions: transient erythema and hyperkeratosis that is usually localized but occasionally occurs in its generalized form. Clinical presentation varies significantly within a family and from one family to another. Palmoplantar keratoderma is present in around 50% of cases. {ECO:0000269|PubMed:25398053}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Palmoplantar keratoderma and congenital alopecia 1 (PPKCA1) [MIM:104100]: A rare autosomal dominant disorder characterized by severe hyperkeratosis of the palms and soles, and congenital hypotrichosis or alopecia. Dystrophic nail changes occur in some patients. {ECO:0000269|PubMed:25168385}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Structural component of the gap junction, a specialized intercellular structure consisting of a cluster of closely packed pairs of transmembrane channels, the connexons, that allow passage of small molecules and electrical signals between neighboring cells (By similarity). Forms homotypic and heterotypic channels gated by transjunctional voltage (By similarity). May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph (Probable). Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract (By similarity). May play a role in the conductive system of ventricular myocardium and heart morphogenesis (By similarity). May play a role in cell growth inhibition through the regulation of NOV expression and localization (By similarity). Involved in intercellular innate immune signaling (PubMed:24077100, PubMed:31992625, PubMed:40010341). Mediates translocation of 2',3'-cGAMP and 2',5'-oligoadenylates (2-5A) second messengers from virus-infected cells to macrophages and uninfected neighboring cells to propagate and amplify the antiviral immune response (PubMed:24077100, PubMed:31992625, PubMed:40010341). {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P23242, ECO:0000269|PubMed:24077100, ECO:0000269|PubMed:31992625, ECO:0000269|PubMed:40010341, ECO:0000305|PubMed:11741837}.
uniprot
proteins
mass_dalton
43008
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-368 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity (By similarity). Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates gap junction assembly. Phosphorylation at Ser-368 by PRKCD triggers its internalization into small vesicles leading to proteasome-mediated degradation (By similarity). Phosphorylation by MAPK1/MAPK3 at Ser-279 and Ser-282 leads to increased ubiquitination and lysosomal degradation (By similarity). {ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P23242, ECO:0000250|UniProtKB:Q6TYA7, ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14702389, ECO:0000269|PubMed:15605363}.; PTM: Ubiquitination results in lysosomal degradation. {ECO:0000250|UniProtKB:P23242}.; PTM: Sumoylated with SUMO1, SUMO2 and SUMO3, which may regulate the level of functional Cx43 gap junctions at the plasma membrane. May be desumoylated by SENP1 or SENP2. {ECO:0000269|PubMed:22411987}.; PTM: S-nitrosylation at Cys-271 is enriched at the muscle endothelial gap junction in arteries, it augments channel permeability and may regulate of smooth muscle cell to endothelial cell communication. {ECO:0000250|UniProtKB:P23242}.; PTM: Acetylated in the developing cortex; leading to delocalization from the cell membrane. {ECO:0000250|UniProtKB:P23242}.
uniprot
proteins
protein_family
Alpha-type (group II) subfamily
uniprot
proteins
protein_family
Connexin family
uniprot
proteins
pubmed
10581143
uniprot
proteins
pubmed
10764404
uniprot
proteins
pubmed
11470490
uniprot
proteins
pubmed
11741837
uniprot
proteins
pubmed
12270943
uniprot
proteins
pubmed
12457340
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14702389
uniprot
proteins
pubmed
14729836
uniprot
proteins
pubmed
14974090
uniprot
proteins
pubmed
15108203
uniprot
proteins
pubmed
15181016
uniprot
proteins
pubmed
15213231
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15605363
uniprot
proteins
pubmed
15637728
uniprot
proteins
pubmed
15757815
uniprot
proteins
pubmed
15978203
uniprot
proteins
pubmed
16112082
uniprot
proteins
pubmed
16219735
uniprot
proteins
pubmed
16222672
uniprot
proteins
pubmed
16378922
uniprot
proteins
pubmed
1646158
uniprot
proteins
pubmed
16709485
uniprot
proteins
pubmed
16813608
uniprot
proteins
pubmed
16816024
uniprot
proteins
pubmed
1696265
uniprot
proteins
pubmed
17509830
uniprot
proteins
pubmed
18161618
uniprot
proteins
pubmed
18662195
uniprot
proteins
pubmed
19338053
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21670345
uniprot
proteins
pubmed
22411987
uniprot
proteins
pubmed
23550541
uniprot
proteins
pubmed
23951358
uniprot
proteins
pubmed
24077100
uniprot
proteins
pubmed
24508941
uniprot
proteins
pubmed
25168385
uniprot
proteins
pubmed
25225338
uniprot
proteins
pubmed
25398053
uniprot
proteins
pubmed
26604139
uniprot
proteins
pubmed
28258662
uniprot
proteins
pubmed
31992625
uniprot
proteins
pubmed
34905516
uniprot
proteins
pubmed
38375917
uniprot
proteins
pubmed
40010341
uniprot
proteins
pubmed
7715640
uniprot
proteins
pubmed
8873667
uniprot
proteins
pubmed
9155619
uniprot
proteins
pubmed
9430691
uniprot
proteins
pubmed
9443444
uniprot
proteins
sequence_length
382
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22411987, ECO:0000269|PubMed:25398053}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000269|PubMed:22411987, ECO:0000269|PubMed:25225338, ECO:0000269|PubMed:25398053, ECO:0000269|PubMed:38375917}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}. Cell junction {ECO:0000269|PubMed:26604139, ECO:0000269|PubMed:34905516}. Note=Localizes at the intercalated disk (ICD) between two adjacent cardiomyocytes and the proper localization at ICD is dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}.
uniprot
proteins
transmembrane_region
TRANSMEM 24..44; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 77..97; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 156..176; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 208..228; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins