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Gap junction alpha-1 protein (Connexin-43) (Cx43) (Gap junction 43 kDa heart protein)

 CXA1_HUMAN              Reviewed;         382 AA.
P17302; B2R5U9; Q6FHU1; Q9Y5I8;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 214.
RecName: Full=Gap junction alpha-1 protein;
AltName: Full=Connexin-43;
Short=Cx43;
AltName: Full=Gap junction 43 kDa heart protein;
Name=GJA1; Synonyms=GJAL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart muscle;
PubMed=1696265; DOI=10.1083/jcb.111.2.589;
Fishman G.I., Spray D.C., Leinwand L.A.;
"Molecular characterization and functional expression of the human
cardiac gap junction channel.";
J. Cell Biol. 111:589-598(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1646158; DOI=10.1016/0888-7543(91)90507-B;
Fishman G.I., Eddy R.L., Shows T.B., Rosenthal L., Leinwand L.A.;
"The human connexin gene family of gap junction proteins: distinct
chromosomal locations but similar structures.";
Genomics 10:250-256(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10581143; DOI=10.1053/euhj.1999.1718;
Haefliger J.-A., Goy J.J., Waeber G.;
"Sporadic cases of dilated cardiomyopathies associated with
atrioventricular conduction defects are not linked to mutation within
the connexins 40 and 43 genes.";
Eur. Heart J. 20:1843-1843(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
DISULFIDE BONDS.
PubMed=9430691; DOI=10.1074/jbc.273.3.1519;
Toyofuku T., Yabuki M., Otsu K., Kuzuya T., Hori M., Tada M.;
"Intercellular calcium signaling via gap junction in connexin-43-
transfected cells.";
J. Biol. Chem. 273:1519-1528(1998).
[10]
INTERACTION WITH NOV.
PubMed=15181016; DOI=10.1074/jbc.M404073200;
Gellhaus A., Dong X., Propson S., Maass K., Klein-Hitpass L.,
Kibschull M., Traub O., Willecke K., Perbal B., Lye S.J.,
Winterhager E.;
"Connexin43 interacts with NOV: a possible mechanism for negative
regulation of cell growth in choriocarcinoma cells.";
J. Biol. Chem. 279:36931-36942(2004).
[11]
INTERACTION WITH NOV.
PubMed=15213231; DOI=10.1074/jbc.M403952200;
Fu C.T., Bechberger J.F., Ozog M.A., Perbal B., Naus C.C.;
"CCN3 (NOV) interacts with connexin43 in C6 glioma cells: possible
mechanism of connexin-mediated growth suppression.";
J. Biol. Chem. 279:36943-36950(2004).
[12]
PHOSPHORYLATION AT SER-262.
PubMed=14702389; DOI=10.1242/jcs.00889;
Doble B.W., Dang X., Ping P., Fandrich R.R., Nickel B.E., Jin Y.,
Cattini P.A., Kardami E.;
"Phosphorylation of serine 262 in the gap junction protein connexin-43
regulates DNA synthesis in cell-cell contact forming cardiomyocytes.";
J. Cell Sci. 117:507-514(2004).
[13]
REVIEW.
PubMed=10764404; DOI=10.1161/01.RES.86.7.723;
Saffitz J.E., Laing J.G., Yamada K.A.;
"Connexin expression and turnover: implications for cardiac
excitability.";
Circ. Res. 86:723-728(2000).
[14]
SHOWS THAT HEART LATERALIZATION DEFECT ARE NOT DUE TO GJA1.
PubMed=8873667; DOI=10.1161/01.CIR.94.8.1909;
Gebbia M., Towbin J.A., Casey B.;
"Failure to detect connexin43 mutations in 38 cases of sporadic and
familial heterotaxy.";
Circulation 94:1909-1912(1996).
[15]
SHOWS THAT HEART LATERALIZATION DEFECT ARE NOT DUE TO GJA1.
PubMed=9155619;
Penman Splitt M., Tsai M.Y., Burn J., Goodship J.A.;
"Absence of mutations in the regulatory domain of the gap junction
protein connexin 43 in patients with visceroatrial heterotaxy.";
Heart 77:369-370(1997).
[16]
SHOWS THAT HEART LATERALIZATION DEFECT ARE NOT DUE TO GJA1.
PubMed=9443444; DOI=10.1161/01.CIR.97.1.117;
Toth T., Hajdu J., Marton T., Nagy B., Papp Z.;
"Connexin43 gene mutations and heterotaxy.";
Circulation 97:117-118(1998).
[17]
ASSOCIATION WITH NON-SYNDROMIC AUTOSOMAL RECESSIVE DEAFNESS, AND
TISSUE SPECIFICITY.
PubMed=11741837; DOI=10.1093/hmg/10.25.2945;
Liu X.Z., Xia X.J., Adams J., Chen Z.Y., Welch K.O., Tekin M.,
Ouyang X.M., Kristiansen A., Pandya A., Balkany T., Arnos K.S.,
Nance W.E.;
"Mutations in GJA1 (connexin 43) are associated with non-syndromic
autosomal recessive deafness.";
Hum. Mol. Genet. 10:2945-2951(2001).
[18]
PHOSPHORYLATION AT SER-325; SER-328 AND SER-330 BY CSNK1D/CK1, AND
INTERACTION WITH CSNK1D.
PubMed=12270943; DOI=10.1074/jbc.M209427200;
Cooper C.D., Lampe P.D.;
"Casein kinase 1 regulates connexin-43 gap junction assembly.";
J. Biol. Chem. 277:44962-44968(2002).
[19]
INTERACTION WITH RIC1.
PubMed=16112082; DOI=10.1016/j.bbrc.2005.08.019;
Akiyama M., Ishida N., Ogawa T., Yogo K., Takeya T.;
"Molecular cloning and functional analysis of a novel Cx43 partner
protein CIP150.";
Biochem. Biophys. Res. Commun. 335:1264-1271(2005).
[20]
PHOSPHORYLATION AT SER-255 AND SER-262.
PubMed=15605363; DOI=10.1002/mc.20072;
Arnold J.M., Phipps M.W., Chen J., Phipps J.;
"Cellular sublocalization of Cx43 and the establishment of functional
coupling in IMR-32 neuroblastoma cells.";
Mol. Carcinog. 42:159-169(2005).
[21]
INVOLVEMENT IN ODDD-AR.
PubMed=16816024; DOI=10.1136/jmg.2005.037655;
Richardson R.J., Joss S., Tomkin S., Ahmed M., Sheridan E.,
Dixon M.J.;
"A nonsense mutation in the first transmembrane domain of connexin 43
underlies autosomal recessive oculodentodigital syndrome.";
J. Med. Genet. 43:E37-E37(2006).
[22]
NON-ASSOCIATION WITH NON-SYNDROMIC AUTOSOMAL RECESSIVE DEAFNESS,
VARIANTS ODDD SER-17; PRO-18; ARG-21; GLU-22; THR-23; VAL-40; LYS-49;
PHE-52 INS; SER-76; VAL-90; CYS-98; ASN-102; THR-130; GLU-134;
ARG-138; HIS-202 AND LEU-216, AND VARIANT VAL-253.
PubMed=12457340; DOI=10.1086/346090;
Paznekas W.A., Boyadjiev S.A., Shapiro R.E., Daniels O., Wollnik B.,
Keegan C.E., Innis J.W., Dinulos M.B., Christian C., Hannibal M.C.,
Jabs E.W.;
"Connexin 43 (GJA1) mutations cause the pleiotropic phenotype of
oculodentodigital dysplasia.";
Am. J. Hum. Genet. 72:408-418(2003).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-314 AND
SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
SUMOYLATION AT LYS-144 AND LYS-237, AND SUBCELLULAR LOCATION.
PubMed=22411987; DOI=10.1074/jbc.M111.281832;
Kjenseth A., Fykerud T.A., Sirnes S., Bruun J., Yohannes Z.,
Kolberg M., Omori Y., Rivedal E., Leithe E.;
"The gap junction channel protein connexin 43 is covalently modified
and regulated by SUMOylation.";
J. Biol. Chem. 287:15851-15861(2012).
[25]
INVOLVEMENT IN PPKCA1, VARIANT PPKCA1 VAL-8, AND CHARACTERIZATION OF
VARIANT PPKCA1 VAL-8.
PubMed=25168385; DOI=10.1093/hmg/ddu442;
Wang H., Cao X., Lin Z., Lee M., Jia X., Ren Y., Dai L., Guan L.,
Zhang J., Lin X., Zhang J., Chen Q., Feng C., Zhou E.Y., Yin J.,
Xu G., Yang Y.;
"Exome sequencing reveals mutation in GJA1 as a cause of keratoderma-
hypotrichosis-leukonychia totalis syndrome.";
Hum. Mol. Genet. 24:243-250(2015).
[26]
INVOLVEMENT IN EKV, VARIANTS EKV VAL-44 AND ASP-227, AND
CHARACTERIZATION OF VARIANTS EKV VAL-44 AND ASP-227.
PubMed=25398053; DOI=10.1038/jid.2014.485;
Yale Center for Mendelian Genomics;
Boyden L.M., Craiglow B.G., Zhou J., Hu R., Loring E.C., Morel K.D.,
Lauren C.T., Lifton R.P., Bilguvar K., Paller A.S., Choate K.A.;
"Dominant De Novo Mutations in GJA1 Cause Erythrokeratodermia
Variabilis et Progressiva, without Features of Oculodentodigital
Dysplasia.";
J. Invest. Dermatol. 135:1540-1547(2015).
[27]
VARIANTS HEART MALFORMATIONS GLY-352; PRO-364 AND ASN-365, VARIANTS
ALA-326 AND GLY-373, AND CHARACTERIZATION OF VARIANT HEART
MALFORMATIONS PRO-364.
PubMed=7715640; DOI=10.1056/NEJM199505183322002;
Britz-Cunningham S.H., Shah M.M., Zuppan C.W., Fletcher W.H.;
"Mutations of the connexin43 gap-junction gene in patients with heart
malformations and defects of laterality.";
N. Engl. J. Med. 332:1323-1329(1995).
[28]
VARIANTS HLHS1 GLN-362 AND GLN-376, VARIANTS AVSD3 GLN-362 AND
GLN-376, AND CHARACTERIZATION OF VARIANTS HLHS1 GLN-362 AND GLN-376.
PubMed=11470490; DOI=10.1016/S0027-5107(01)00160-9;
Dasgupta C., Martinez A.-M., Zuppan C.W., Shah M.M., Bailey L.L.,
Fletcher W.H.;
"Identification of connexin43 (alpha1) gap junction gene mutations in
patients with hypoplastic left heart syndrome by denaturing gradient
gel electrophoresis (DGGE).";
Mutat. Res. 479:173-186(2001).
[29]
VARIANT ODDD MET-96.
PubMed=15108203; DOI=10.1002/ajmg.a.20614;
Kjaer K.W., Hansen L., Eiberg H., Leicht P., Opitz J.M., Tommerup N.;
"Novel Connexin 43 (GJA1) mutation causes oculo-dento-digital
dysplasia with curly hair.";
Am. J. Med. Genet. A 127:152-157(2004).
[30]
VARIANT HSS HIS-76.
PubMed=14974090; DOI=10.1002/humu.9220;
Pizzuti A., Flex E., Mingarelli R., Salpietro C., Zelante L.,
Dallapiccola B.;
"A homozygous GJA1 gene mutation causes a Hallermann-Streiff/ODDD
spectrum phenotype.";
Hum. Mutat. 23:286-286(2004).
[31]
VARIANTS ODDD PRO-27; MET-31; VAL-40; TYR-69; PRO-113; ASN-134;
GLN-148 AND HIS-202, AND VARIANT SDTY3 SER-143.
PubMed=14729836; DOI=10.1136/jmg.2003.012005;
Richardson R.R., Donnai D., Meire F., Dixon M.J.;
"Expression of Gja1 correlates with the phenotype observed in
oculodentodigital syndrome/type III syndactyly.";
J. Med. Genet. 41:60-67(2004).
[32]
VARIANT ODDD PRO-194.
PubMed=15637728; DOI=10.1002/ajmg.a.30554;
Vitiello C., D'Adamo P., Gentile F., Vingolo E.M., Gasparini P.,
Banfi S.;
"A novel GJA1 mutation causes oculodentodigital dysplasia without
syndactyly.";
Am. J. Med. Genet. A 133:58-60(2005).
[33]
VARIANT ODDD ARG-95.
PubMed=16222672; DOI=10.1002/ajmg.a.30925;
Honkaniemi J., Kalkkila J.P., Koivisto P., Kahara V., Latvala T.,
Simola K.;
"Letter to the editor: Novel GJA1 mutation in oculodentodigital
dysplasia.";
Am. J. Med. Genet. A 139:48-49(2005).
[34]
VARIANT ODDD HIS-59.
PubMed=16219735; DOI=10.1001/archopht.123.10.1422;
Vasconcellos J.P.C., Melo M.B., Schimiti R.B., Bressanim N.C.,
Costa F.F., Costa V.P.;
"A novel mutation in the GJA1 gene in a family with oculodentodigital
dysplasia.";
Arch. Ophthalmol. 123:1422-1426(2005).
[35]
VARIANTS CONGENITAL HEART MALFORMATIONS TRP-239; THR-251; PRO-253;
LEU-283 AND ASN-290.
PubMed=15978203;
Chen P., Xie L.-J., Huang G.-Y., Zhao X.-Q., Chang C.;
"Mutations of connexin43 in fetuses with congenital heart
malformations.";
Chin. Med. J. 118:971-976(2005).
[36]
VARIANT LEU-41.
PubMed=15757815;
Kellermayer R., Keller M., Ratajczak P., Richardson E., Harangi F.,
Merei E., Melegh B., Kosztolanyi G., Richard G.;
"Bigenic connexin mutations in a patient with hidrotic ectodermal
dysplasia.";
Eur. J. Dermatol. 15:75-79(2005).
[37]
VARIANTS ODDD VAL-40; ASP-110; THR-147 AND PHE-169 DEL.
PubMed=16378922; DOI=10.1016/j.ejmg.2005.05.003;
Debeer P., Van Esch H., Huysmans C., Pijkels E., De Smet L.,
Van de Ven W., Devriendt K., Fryns J.-P.;
"Novel GJA1 mutations in patients with oculo-dento-digital dysplasia
(ODDD).";
Eur. J. Med. Genet. 48:377-387(2005).
[38]
VARIANTS ODDD GLU-96; PRO-113; ASN-154 AND TYR-220.
PubMed=16813608; DOI=10.1111/j.1399-0004.2006.00631.x;
Wiest T., Herrmann O., Stoegbauer F., Grasshoff U., Enders H.,
Koch M.J., Grond-Ginsbach C., Schwaninger M.;
"Clinical and genetic variability of oculodentodigital dysplasia.";
Clin. Genet. 70:71-72(2006).
[39]
VARIANT ODDD PRO-11.
PubMed=16709485;
Kelly S.C., Ratajczak P., Keller M., Purcell S.M., Griffin T.,
Richard G.;
"A novel GJA 1 mutation in oculo-dento-digital dysplasia with curly
hair and hyperkeratosis.";
Eur. J. Dermatol. 16:241-245(2006).
[40]
VARIANT ODDD ALA-154.
PubMed=17509830; DOI=10.1016/j.ijom.2007.03.004;
van Es R.J.J., Wittebol-Post D., Beemer F.A.;
"Oculodentodigital dysplasia with mandibular retrognathism and absence
of syndactyly: a case report with a novel mutation in the connexin 43
gene.";
Int. J. Oral Maxillofac. Surg. 36:858-860(2007).
[41]
VARIANT ODDD VAL-2.
PubMed=18161618; DOI=10.1080/13816810701538620;
de la Parra D.R., Zenteno J.C.;
"A new GJA1 (connexin 43) mutation causing oculodentodigital dysplasia
associated to uncommon features.";
Ophthalmic Genet. 28:198-202(2007).
[42]
VARIANTS ODDD VAL-7; VAL-40; PRO-49; GLN-49 INS; ALA-96; PRO-106;
ALA-154; PHE-201 AND HIS-202.
PubMed=19338053; DOI=10.1002/humu.20958;
Paznekas W.A., Karczeski B., Vermeer S., Lowry R.B., Delatycki M.,
Laurence F., Koivisto P.A., Van Maldergem L., Boyadjiev S.A.,
Bodurtha J.N., Jabs E.W.;
"GJA1 mutations, variants, and connexin 43 dysfunction as it relates
to the oculodentodigital dysplasia phenotype.";
Hum. Mutat. 30:724-733(2009).
[43]
VARIANTS ODDD PRO-11 AND 41-VAL--ALA-44 DEL.
PubMed=21670345; DOI=10.1001/archophthalmol.2011.113;
Gabriel L.A., Sachdeva R., Marcotty A., Rockwood E.J., Traboulsi E.I.;
"Oculodentodigital dysplasia: new ocular findings and a novel connexin
43 mutation.";
Arch. Ophthalmol. 129:781-784(2011).
[44]
VARIANT ODDD ARG-206.
PubMed=23550541; DOI=10.1111/cge.12158;
Brice G., Ostergaard P., Jeffery S., Gordon K., Mortimer P.S.,
Mansour S.;
"A novel mutation in GJA1 causing oculodentodigital syndrome and
primary lymphoedema in a three generation family.";
Clin. Genet. 84:378-381(2013).
[45]
VARIANT CMDR GLN-239.
PubMed=23951358; DOI=10.1371/journal.pone.0073576;
Hu Y., Chen I.P., de Almeida S., Tiziani V., Do Amaral C.M.,
Gowrishankar K., Passos-Bueno M.R., Reichenberger E.J.;
"A novel autosomal recessive GJA1 missense mutation linked to
Craniometaphyseal dysplasia.";
PLoS ONE 8:E73576-E73576(2013).
[46]
VARIANTS ODDD HIS-47; TYR-86 AND ARG-106.
PubMed=24508941; DOI=10.1016/j.gene.2014.01.066;
Jamsheer A., Sowinska-Seidler A., Socha M., Stembalska A.,
Kiraly-Borri C., Latos-Bielenska A.;
"Three novel GJA1 missense substitutions resulting in oculo-dento-
digital dysplasia (ODDD) - further extension of the mutational
spectrum.";
Gene 539:157-161(2014).
[47]
VARIANT ODDD ILE-11.
PubMed=28258662; DOI=10.1111/odi.12663;
Porntaveetus T., Srichomthong C., Ohazama A., Suphapeetiporn K.,
Shotelersuk V.;
"A novel GJA1 mutation in oculodentodigitaldysplasia with extensive
loss of enamel.";
Oral Dis. 0:0-0(2017).
-!- FUNCTION: Gap junction protein that acts as a regulator of bladder
capacity. A gap junction consists of a cluster of closely packed
pairs of transmembrane channels, the connexons, through which
materials of low MW diffuse from one cell to a neighboring cell.
May play a critical role in the physiology of hearing by
participating in the recycling of potassium to the cochlear
endolymph. 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 cell
growth inhibition through the regulation of NOV expression and
localization. Plays an essential role in gap junction
communication in the ventricles (By similarity).
{ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:P23242}.
-!- SUBUNIT: A connexon is composed of a hexamer of connexins.
Interacts (via C-terminus) with TJP1 (By similarity). Interacts
(via C-terminus) with SRC (via SH3 domain) (By similarity).
Interacts (not ubiquitinated) with UBQLN4 (via UBA domain) (By
similarity). Interacts with SGSM3 and CNST (By similarity).
Interacts with RIC1/CIP150. Interacts with CSNK1D. Interacts with
NOV (PubMed:15181016, PubMed:15213231). Interacts with TMEM65 (By
similarity). {ECO:0000250|UniProtKB:P23242,
ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:15181016,
ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:16112082}.
-!- INTERACTION:
O43889-2:CREB3; NbExp=3; IntAct=EBI-1103439, EBI-625022;
Q02487-1:DSC2; NbExp=2; IntAct=EBI-1103439, EBI-6900677;
Q07157:TJP1; NbExp=3; IntAct=EBI-1103439, EBI-79553;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22411987};
Multi-pass membrane protein {ECO:0000255}. Cell junction, gap
junction {ECO:0000269|PubMed:22411987}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated
disk (ICD) in cardiomyocytes and the proper localization at ICD is
dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}.
-!- TISSUE SPECIFICITY: Expressed in the heart and fetal cochlea.
{ECO:0000269|PubMed:11741837}.
-!- 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).
{ECO:0000250|UniProtKB:P08050, ECO:0000250|UniProtKB:Q6TYA7,
ECO:0000269|PubMed:12270943, ECO:0000269|PubMed:14702389,
ECO:0000269|PubMed:15605363}.
-!- 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.
-!- 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:12457340,
ECO:0000269|PubMed:14729836, ECO:0000269|PubMed:15108203,
ECO:0000269|PubMed:15637728, ECO:0000269|PubMed:16219735,
ECO:0000269|PubMed:16222672, ECO:0000269|PubMed:16378922,
ECO:0000269|PubMed:16709485, ECO:0000269|PubMed:16813608,
ECO:0000269|PubMed:16816024, ECO:0000269|PubMed:17509830,
ECO:0000269|PubMed:18161618, ECO:0000269|PubMed:19338053,
ECO:0000269|PubMed:21670345, ECO:0000269|PubMed:23550541,
ECO:0000269|PubMed:24508941, ECO:0000269|PubMed:28258662}.
Note=The disease is caused by mutations 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
mutations 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
mutations 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 is
caused by mutations 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. Mental retardation is present in a
minority of cases. {ECO:0000269|PubMed:14974090}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Atrioventricular septal defect 3 (AVSD3) [MIM:600309]: A
congenital heart malformation characterized by a common
atrioventricular junction coexisting with deficient
atrioventricular septation. The complete form involves
underdevelopment of the lower part of the atrial septum and the
upper part of the ventricular septum; the valve itself is also
shared. A less severe form, known as ostium primum atrial septal
defect, is characterized by separate atrioventricular valvar
orifices despite a common junction. {ECO:0000269|PubMed:11470490}.
Note=The disease is caused by mutations 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 mutations affecting the gene represented in this entry.
-!- DISEASE: Erythrokeratodermia variabilis (EKV) [MIM:133200]: A
genodermatosis characterized by the appearance of two independent
skin lesions: transient figurate erythematous patches 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
mutations 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 mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
subfamily. {ECO:0000305}.
-!- CAUTION: PubMed:7715640 reported a mutation Pro-364 linked to
congenital heart diseases. PubMed:8873667 later shown that it is
an artifact. {ECO:0000305}.
-!- CAUTION: PubMed:11741837 reported 2 mutations (Phe-11 and Ala-24)
linked to non-syndromic autosomal recessive deafness (DFNBG).
These mutations have subsequently been shown (PubMed:12457340) to
involve the pseudogene of connexin-43 located on chromosome 5.
{ECO:0000305|PubMed:12457340}.
-----------------------------------------------------------------------
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EMBL; X52947; CAA37122.1; -; mRNA.
EMBL; M65188; AAA52131.1; -; mRNA.
EMBL; AF151980; AAD37802.2; -; Genomic_DNA.
EMBL; CR541660; CAG46461.1; -; mRNA.
EMBL; AK312324; BAG35246.1; -; mRNA.
EMBL; AL139098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48178.1; -; Genomic_DNA.
EMBL; BC026329; AAH26329.1; -; mRNA.
CCDS; CCDS5123.1; -.
PIR; A35853; A35853.
RefSeq; NP_000156.1; NM_000165.4.
UniGene; Hs.700699; -.
UniGene; Hs.74471; -.
PDB; 2LL2; NMR; -; A=234-259.
PDBsum; 2LL2; -.
ProteinModelPortal; P17302; -.
SMR; P17302; -.
BioGrid; 108964; 60.
IntAct; P17302; 14.
MINT; MINT-147603; -.
STRING; 9606.ENSP00000282561; -.
DrugBank; DB01136; Carvedilol.
iPTMnet; P17302; -.
PhosphoSitePlus; P17302; -.
BioMuta; GJA1; -.
DMDM; 117706; -.
EPD; P17302; -.
MaxQB; P17302; -.
PaxDb; P17302; -.
PeptideAtlas; P17302; -.
PRIDE; P17302; -.
TopDownProteomics; P17302; -.
DNASU; 2697; -.
Ensembl; ENST00000282561; ENSP00000282561; ENSG00000152661.
GeneID; 2697; -.
KEGG; hsa:2697; -.
UCSC; uc003pyr.4; human.
CTD; 2697; -.
DisGeNET; 2697; -.
EuPathDB; HostDB:ENSG00000152661.7; -.
GeneCards; GJA1; -.
HGNC; HGNC:4274; GJA1.
HPA; CAB010753; -.
HPA; HPA035097; -.
MalaCards; GJA1; -.
MIM; 104100; phenotype.
MIM; 121014; gene.
MIM; 133200; phenotype.
MIM; 164200; phenotype.
MIM; 186100; phenotype.
MIM; 218400; phenotype.
MIM; 234100; phenotype.
MIM; 241550; phenotype.
MIM; 257850; phenotype.
MIM; 600309; phenotype.
neXtProt; NX_P17302; -.
OpenTargets; ENSG00000152661; -.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
Orphanet; 1522; Craniometaphyseal dysplasia.
Orphanet; 2248; Hypoplastic left heart syndrome.
Orphanet; 2710; Oculodentodigital dysplasia.
Orphanet; 93404; Syndactyly type 3.
PharmGKB; PA28685; -.
eggNOG; ENOG410IF97; Eukaryota.
eggNOG; ENOG4110JTW; LUCA.
GeneTree; ENSGT00840000129674; -.
HOGENOM; HOG000231127; -.
HOVERGEN; HBG009576; -.
InParanoid; P17302; -.
KO; K07372; -.
OMA; GANVDMH; -.
OrthoDB; EOG091G0FKH; -.
PhylomeDB; P17302; -.
TreeFam; TF329606; -.
Reactome; R-HSA-190704; Oligomerization of connexins into connexons.
Reactome; R-HSA-190827; Transport of connexins along the secretory pathway.
Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
Reactome; R-HSA-190861; Gap junction assembly.
Reactome; R-HSA-190873; Gap junction degradation.
Reactome; R-HSA-191647; c-src mediated regulation of Cx43 function and closure of gap junctions.
Reactome; R-HSA-196025; Formation of annular gap junctions.
SignaLink; P17302; -.
SIGNOR; P17302; -.
ChiTaRS; GJA1; human.
GeneWiki; GJA1; -.
GenomeRNAi; 2697; -.
PRO; PR:P17302; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000152661; -.
CleanEx; HS_GJA1; -.
Genevisible; P17302; HS.
GO; GO:0005922; C:connexin complex; ISS:BHF-UCL.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005921; C:gap junction; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB.
GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:AgBase.
GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0071253; F:connexin binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0005243; F:gap junction channel activity; IDA:BHF-UCL.
GO; GO:0086075; F:gap junction channel activity involved in cardiac conduction electrical coupling; NAS:BHF-UCL.
GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; IDA:BHF-UCL.
GO; GO:0015075; F:ion transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; IDA:BHF-UCL.
GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
GO; GO:0015867; P:ATP transport; IEA:Ensembl.
GO; GO:0086014; P:atrial cardiac muscle cell action potential; TAS:BHF-UCL.
GO; GO:0010644; P:cell communication by electrical coupling; IDA:BHF-UCL.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; NAS:BHF-UCL.
GO; GO:0007267; P:cell-cell signaling; IDA:BHF-UCL.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl.
GO; GO:0046697; P:decidualization; IEA:Ensembl.
GO; GO:0003158; P:endothelium development; IEA:Ensembl.
GO; GO:1905867; P:epididymis development; IEA:Ensembl.
GO; GO:0016264; P:gap junction assembly; TAS:UniProtKB.
GO; GO:0007507; P:heart development; TAS:ProtInc.
GO; GO:0034220; P:ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
GO; GO:2000987; P:positive regulation of behavioral fear response; IEA:Ensembl.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:0010652; P:positive regulation of cell communication by chemical coupling; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0003104; P:positive regulation of glomerular filtration; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0051259; P:protein oligomerization; IEA:Ensembl.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0009268; P:response to pH; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
GO; GO:0006810; P:transport; TAS:ProtInc.
GO; GO:0010232; P:vascular transport; IEA:Ensembl.
Gene3D; 1.20.5.1130; -; 1.
InterPro; IPR035091; Alpha_helix_domain.
InterPro; IPR000500; Connexin.
InterPro; IPR002261; Connexin43.
InterPro; IPR013124; Connexin43_C.
InterPro; IPR034634; Connexin_C.
InterPro; IPR019570; Connexin_CCC.
InterPro; IPR017990; Connexin_CS.
InterPro; IPR013092; Connexin_N.
PANTHER; PTHR11984; PTHR11984; 1.
PANTHER; PTHR11984:SF70; PTHR11984:SF70; 1.
Pfam; PF00029; Connexin; 1.
Pfam; PF03508; Connexin43; 1.
PRINTS; PR00206; CONNEXIN.
PRINTS; PR01132; CONNEXINA1.
SMART; SM00037; CNX; 1.
SMART; SM01089; Connexin_CCC; 1.
SUPFAM; SSF118220; SSF118220; 1.
PROSITE; PS00407; CONNEXINS_1; 1.
PROSITE; PS00408; CONNEXINS_2; 1.
1: Evidence at protein level;
3D-structure; Cataract; Cell junction; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond;
Endoplasmic reticulum; Gap junction; Hypotrichosis; Isopeptide bond;
Membrane; Palmoplantar keratoderma; Phosphoprotein; Polymorphism;
Reference proteome; S-nitrosylation; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 382 Gap junction alpha-1 protein.
/FTId=PRO_0000057801.
TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.
TRANSMEM 14 36 Helical. {ECO:0000255}.
TOPO_DOM 37 76 Extracellular. {ECO:0000255}.
TRANSMEM 77 99 Helical. {ECO:0000255}.
TOPO_DOM 100 154 Cytoplasmic. {ECO:0000255}.
TRANSMEM 155 177 Helical. {ECO:0000255}.
TOPO_DOM 178 208 Extracellular. {ECO:0000255}.
TRANSMEM 209 231 Helical. {ECO:0000255}.
TOPO_DOM 232 382 Cytoplasmic. {ECO:0000255}.
REGION 244 382 Interaction with NOV.
{ECO:0000250|UniProtKB:P08050}.
REGION 264 382 Interaction with UBQLN4.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:P08050}.
MOD_RES 247 247 Phosphotyrosine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:15605363}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000269|PubMed:14702389,
ECO:0000269|PubMed:15605363}.
MOD_RES 271 271 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 275 275 Phosphothreonine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 306 306 Phosphoserine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 325 325 Phosphoserine; by CK1.
{ECO:0000269|PubMed:12270943}.
MOD_RES 326 326 Phosphothreonine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 328 328 Phosphoserine; by CK1.
{ECO:0000269|PubMed:12270943}.
MOD_RES 330 330 Phosphoserine; by CK1.
{ECO:0000269|PubMed:12270943}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 368 368 Phosphoserine; by PKC/PRKCG and
PKC/PRKCD.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:P23242}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:P08050}.
DISULFID 54 192 {ECO:0000269|PubMed:9430691}.
DISULFID 187 198 {ECO:0000269|PubMed:9430691}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:22411987}.
CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:22411987}.
VARIANT 2 2 G -> V (in ODDD).
{ECO:0000269|PubMed:18161618}.
/FTId=VAR_058990.
VARIANT 7 7 L -> V (in ODDD).
{ECO:0000269|PubMed:19338053}.
/FTId=VAR_058991.
VARIANT 8 8 G -> V (in PPKCA1; can form functional
gap junctions; results in enhanced
hemichannel activity that causes
increased cell death; dbSNP:rs864309644).
{ECO:0000269|PubMed:25168385}.
/FTId=VAR_075754.
VARIANT 11 11 L -> I (in ODDD).
{ECO:0000269|PubMed:28258662}.
/FTId=VAR_078238.
VARIANT 11 11 L -> P (in ODDD; dbSNP:rs121912969).
{ECO:0000269|PubMed:16709485,
ECO:0000269|PubMed:21670345}.
/FTId=VAR_058992.
VARIANT 17 17 Y -> S (in ODDD; dbSNP:rs104893961).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015747.
VARIANT 18 18 S -> P (in ODDD; dbSNP:rs104893962).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015748.
VARIANT 21 21 G -> R (in ODDD; dbSNP:rs104893963).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015749.
VARIANT 22 22 G -> E (in ODDD; dbSNP:rs104893964).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015750.
VARIANT 23 23 K -> T (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015751.
VARIANT 27 27 S -> P (in ODDD).
{ECO:0000269|PubMed:14729836}.
/FTId=VAR_038356.
VARIANT 31 31 I -> M (in ODDD).
{ECO:0000269|PubMed:14729836}.
/FTId=VAR_038357.
VARIANT 40 40 A -> V (in ODDD).
{ECO:0000269|PubMed:12457340,
ECO:0000269|PubMed:14729836,
ECO:0000269|PubMed:16378922,
ECO:0000269|PubMed:19338053}.
/FTId=VAR_015752.
VARIANT 41 44 Missing (in ODDD).
{ECO:0000269|PubMed:21670345}.
/FTId=VAR_070439.
VARIANT 41 41 V -> L (found in a patient with hidrotic
ectodermal dysplasia, abortive features
of oculodentodigital dysplasia and
extensive hyperkeratosis of the skin;
unknown pathological significance; the
patient also carries GJB2 variant H-127).
{ECO:0000269|PubMed:15757815}.
/FTId=VAR_058993.
VARIANT 44 44 A -> V (in EKV; does not localize to
intercellular junctions but is retained
in the cytoplasm; dbSNP:rs794729675).
{ECO:0000269|PubMed:25398053}.
/FTId=VAR_075755.
VARIANT 47 47 D -> H (in ODDD).
{ECO:0000269|PubMed:24508941}.
/FTId=VAR_071009.
VARIANT 49 49 Q -> K (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015753.
VARIANT 49 49 Q -> P (in ODDD).
{ECO:0000269|PubMed:19338053}.
/FTId=VAR_058994.
VARIANT 49 49 Q -> QQ (in ODDD).
{ECO:0000269|PubMed:19338053}.
/FTId=VAR_058995.
VARIANT 52 52 F -> FF (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015754.
VARIANT 59 59 P -> H (in ODDD).
{ECO:0000269|PubMed:16219735}.
/FTId=VAR_058996.
VARIANT 69 69 S -> Y (in ODDD).
{ECO:0000269|PubMed:14729836}.
/FTId=VAR_038358.
VARIANT 76 76 R -> H (in HSS; overlapping features with
oculodentodigital dysplasia;
dbSNP:rs267606844).
{ECO:0000269|PubMed:14974090}.
/FTId=VAR_058997.
VARIANT 76 76 R -> S (in ODDD; dbSNP:rs267606845).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015755.
VARIANT 86 86 S -> Y (in ODDD; de novo mutation found
in a sporadic case).
{ECO:0000269|PubMed:24508941}.
/FTId=VAR_071010.
VARIANT 90 90 L -> V (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015756.
VARIANT 95 95 H -> R (in ODDD).
{ECO:0000269|PubMed:16222672}.
/FTId=VAR_058998.
VARIANT 96 96 V -> A (in ODDD).
{ECO:0000269|PubMed:19338053}.
/FTId=VAR_058999.
VARIANT 96 96 V -> E (in ODDD).
{ECO:0000269|PubMed:16813608}.
/FTId=VAR_059000.
VARIANT 96 96 V -> M (in ODDD; dbSNP:rs28931601).
{ECO:0000269|PubMed:15108203}.
/FTId=VAR_059001.
VARIANT 98 98 Y -> C (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015757.
VARIANT 102 102 K -> N (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015758.
VARIANT 106 106 L -> P (in ODDD).
{ECO:0000269|PubMed:19338053}.
/FTId=VAR_059002.
VARIANT 106 106 L -> R (in ODDD).
{ECO:0000269|PubMed:24508941}.
/FTId=VAR_071011.
VARIANT 110 110 E -> D (in ODDD).
{ECO:0000269|PubMed:16378922}.
/FTId=VAR_059003.
VARIANT 113 113 L -> P (in ODDD).
{ECO:0000269|PubMed:14729836,
ECO:0000269|PubMed:16813608}.
/FTId=VAR_038359.
VARIANT 130 130 I -> T (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015759.
VARIANT 134 134 K -> E (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015760.
VARIANT 134 134 K -> N (in ODDD).
{ECO:0000269|PubMed:14729836}.
/FTId=VAR_038360.
VARIANT 138 138 G -> R (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015761.
VARIANT 143 143 G -> S (in SDTY3; dbSNP:rs28931600).
{ECO:0000269|PubMed:14729836}.
/FTId=VAR_038361.
VARIANT 147 147 M -> T (in ODDD).
{ECO:0000269|PubMed:16378922}.
/FTId=VAR_059004.
VARIANT 148 148 R -> Q. {ECO:0000269|PubMed:14729836}.
/FTId=VAR_014095.
VARIANT 154 154 T -> A (in ODDD).
{ECO:0000269|PubMed:17509830,
ECO:0000269|PubMed:19338053}.
/FTId=VAR_059005.
VARIANT 154 154 T -> N (in ODDD).
{ECO:0000269|PubMed:16813608}.
/FTId=VAR_059006.
VARIANT 168 168 A -> T (in dbSNP:rs2228961).
/FTId=VAR_014096.
VARIANT 169 169 Missing (in ODDD).
{ECO:0000269|PubMed:16378922}.
/FTId=VAR_059007.
VARIANT 194 194 H -> P (in ODDD; atypical form of ODDD
characterized by the predominance of the
ocular involvement and by the absence of
hand and/or foot syndactyly and absence
of any neurologic signs;
dbSNP:rs104893966).
{ECO:0000269|PubMed:15637728}.
/FTId=VAR_059008.
VARIANT 201 201 S -> F (in ODDD).
{ECO:0000269|PubMed:19338053}.
/FTId=VAR_059009.
VARIANT 202 202 R -> H (in ODDD; dbSNP:rs750294638).
{ECO:0000269|PubMed:12457340,
ECO:0000269|PubMed:14729836,
ECO:0000269|PubMed:19338053}.
/FTId=VAR_015762.
VARIANT 206 206 K -> R (in ODDD; dbSNP:rs397518464).
{ECO:0000269|PubMed:23550541}.
/FTId=VAR_070440.
VARIANT 216 216 V -> L (in ODDD).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015763.
VARIANT 220 220 S -> Y (in ODDD).
{ECO:0000269|PubMed:16813608}.
/FTId=VAR_059010.
VARIANT 227 227 E -> D (in EKV; does not localize to
intercellular junctions but is retained
in the cytoplasm; dbSNP:rs875989815).
{ECO:0000269|PubMed:25398053}.
/FTId=VAR_075756.
VARIANT 239 239 R -> Q (in CMDR; dbSNP:rs764670582).
{ECO:0000269|PubMed:23951358}.
/FTId=VAR_070441.
VARIANT 239 239 R -> W (in congenital heart
malformations).
{ECO:0000269|PubMed:15978203}.
/FTId=VAR_014100.
VARIANT 251 251 S -> T (in congenital heart
malformations).
{ECO:0000269|PubMed:15978203}.
/FTId=VAR_059011.
VARIANT 253 253 A -> P (in congenital heart
malformations).
{ECO:0000269|PubMed:15978203}.
/FTId=VAR_059012.
VARIANT 253 253 A -> V (in dbSNP:rs17653265).
{ECO:0000269|PubMed:12457340}.
/FTId=VAR_015764.
VARIANT 283 283 P -> L (in congenital heart
malformations).
{ECO:0000269|PubMed:15978203}.
/FTId=VAR_014101.
VARIANT 290 290 T -> N (in congenital heart
malformations).
{ECO:0000269|PubMed:15978203}.
/FTId=VAR_014102.
VARIANT 326 326 T -> A. {ECO:0000269|PubMed:7715640}.
/FTId=VAR_059013.
VARIANT 352 352 E -> G (in heart malformations).
{ECO:0000269|PubMed:7715640}.
/FTId=VAR_059014.
VARIANT 362 362 R -> Q (in HLHS1 and AVSD3; unknown
pathological significance; associated
with Gln-376 in one individual with
atrioventricular septal defect; abolishes
phosphorylation by PKA and PKC;
dbSNP:rs2227885).
{ECO:0000269|PubMed:11470490}.
/FTId=VAR_032924.
VARIANT 364 364 S -> P (in heart malformations; shows
abnormalities in the regulation of cell-
cell communication as compared with cells
expressing normal GJA1).
{ECO:0000269|PubMed:7715640}.
/FTId=VAR_059015.
VARIANT 365 365 S -> N (in heart malformations).
{ECO:0000269|PubMed:7715640}.
/FTId=VAR_059016.
VARIANT 373 373 S -> G. {ECO:0000269|PubMed:7715640}.
/FTId=VAR_059017.
VARIANT 376 376 R -> Q (in HLHS1 and AVSD3; unknown
pathological significance; associated
with Gln-362 in one individual with
atrioventricular septal defect; abolishes
phosphorylation by PKA and PKC;
dbSNP:rs104893965).
{ECO:0000269|PubMed:11470490}.
/FTId=VAR_032925.
HELIX 240 242 {ECO:0000244|PDB:2LL2}.
HELIX 246 253 {ECO:0000244|PDB:2LL2}.
HELIX 255 257 {ECO:0000244|PDB:2LL2}.
SEQUENCE 382 AA; 43008 MW; 7DDDAD8040284176 CRC64;
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG
CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG
VNVDMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSIFEVAFL LIQWYIYGFS
LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV
KGKSDPYHAT SGALSPAKDC GSQKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN
YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD NQNSKKLAAG HELQPLAIVD
QRPSSRASSR ASSRPRPDDL EI


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