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P17302 (CXA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gap junction alpha-1 protein
Alternative name(s):
Connexin-43
Short name=Cx43
Gap junction 43 kDa heart protein
Gene names
Name:GJA1
Synonyms:GJAL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

A connexon is composed of a hexamer of connexins. Interacts (via C-terminus) with TJP1. Interacts (via C-terminus) with SRC (via SH3 domain). Interacts with UBQLN4 By similarity. Interacts with SGSM3. Interacts with KIAA1432/CIP150. Interacts with CNST and CSNK1D. Ref.16 Ref.17

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctiongap junction Ref.22.

Tissue specificity

Expressed in the heart and fetal cochlea. Ref.15

Post-translational modification

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. Ref.10 Ref.16 Ref.18

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. Ref.22

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.42

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.27

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.41

Sequence similarities

Belongs to the connexin family. Alpha-type (group II) subfamily.

Caution

Ref.23 reported a mutation Pro-364 linked to congenital heart diseases. Ref.12 later shown that it is an artifact.

Ref.15 reported 2 mutations (Phe-11 and Ala-24) linked to non-syndromic autosomal recessive deafness (DFNBG). These mutations have subsequently been shown (Ref.20) to involve the pseudogene of connexin-43 located on chromosome 5.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Gap junction
Membrane
   Coding sequence diversityPolymorphism
   DiseaseCataract
Disease mutation
   DomainTransmembrane
Transmembrane helix
   PTMDisulfide bond
Isopeptide bond
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP transport

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: Ensembl

atrial cardiac muscle cell action potential

Traceable author statement PubMed 23348765. Source: BHF-UCL

cell communication by electrical coupling

Inferred from direct assay PubMed 16790700PubMed 23348765. Source: BHF-UCL

cell-cell signaling

Traceable author statement Ref.23. Source: ProtInc

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

chronic inflammatory response

Inferred from electronic annotation. Source: Ensembl

endothelium development

Inferred from electronic annotation. Source: Ensembl

gap junction assembly

Traceable author statement PubMed 15709751. Source: UniProtKB

heart development

Traceable author statement Ref.23. Source: ProtInc

ion transmembrane transport

Traceable author statement Ref.1. Source: GOC

membrane organization

Traceable author statement. Source: Reactome

muscle contraction

Traceable author statement Ref.23. Source: ProtInc

negative regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

positive regulation of behavioral fear response

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell communication by chemical coupling

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of glomerular filtration

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

protein oligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

regulation of tight junction assembly

Inferred from electronic annotation. Source: Ensembl

response to fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from mutant phenotype PubMed 12761501. Source: GOC

transmembrane transport

Inferred from direct assay PubMed 16790700PubMed 23348765. Source: GOC

transport

Traceable author statement Ref.1. Source: ProtInc

vascular transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: BHF-UCL

Golgi membrane

Traceable author statement. Source: Reactome

Golgi-associated vesicle membrane

Traceable author statement. Source: Reactome

connexon complex

Traceable author statement PubMed 1850831. Source: ProtInc

early endosome

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

fascia adherens

Inferred from electronic annotation. Source: Ensembl

gap junction

Inferred from direct assay PubMed 23348765. Source: BHF-UCL

integral component of plasma membrane

Traceable author statement PubMed 15709751. Source: UniProtKB

intercalated disc

Inferred from direct assay PubMed 22889254. Source: BHF-UCL

lysosome

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from sequence or structural similarity. Source: BHF-UCL

mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

multivesicular body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functiongap junction channel activity

Inferred from direct assay PubMed 16790700PubMed 23348765. Source: BHF-UCL

ion transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 15709751. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 382381Gap junction alpha-1 protein
PRO_0000057801

Regions

Topological domain2 – 1312Cytoplasmic Potential
Transmembrane14 – 3623Helical; Potential
Topological domain37 – 7640Extracellular Potential
Transmembrane77 – 9923Helical; Potential
Topological domain100 – 15455Cytoplasmic Potential
Transmembrane155 – 17723Helical; Potential
Topological domain178 – 20831Extracellular Potential
Transmembrane209 – 23123Helical; Potential
Topological domain232 – 382151Cytoplasmic Potential

Amino acid modifications

Modified residue2471Phosphotyrosine By similarity
Modified residue2551Phosphoserine Ref.18 Ref.21
Modified residue2621Phosphoserine Ref.10 Ref.18
Modified residue2711S-nitrosocysteine By similarity
Modified residue3061Phosphoserine Ref.21
Modified residue3141Phosphoserine Ref.21
Modified residue3251Phosphoserine; by CK1 Ref.16
Modified residue3281Phosphoserine; by CK1 Ref.16
Modified residue3301Phosphoserine; by CK1 Ref.16
Modified residue3441Phosphoserine Ref.21
Modified residue3651Phosphoserine By similarity
Modified residue3681Phosphoserine; by PKC/PRKCG By similarity
Modified residue3691Phosphoserine By similarity
Modified residue3731Phosphoserine By similarity
Disulfide bond54 ↔ 192 Ref.9
Disulfide bond187 ↔ 198 Ref.9
Cross-link144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.22
Cross-link237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.22

Natural variations

Natural variant21G → V in ODDD. Ref.37
VAR_058990
Natural variant71L → V in ODDD. Ref.38
VAR_058991
Natural variant111L → P in ODDD. Ref.35 Ref.39
VAR_058992
Natural variant171Y → S in ODDD. Ref.20
VAR_015747
Natural variant181S → P in ODDD. Ref.20
VAR_015748
Natural variant211G → R in ODDD. Ref.20
VAR_015749
Natural variant221G → E in ODDD. Ref.20
VAR_015750
Natural variant231K → T in ODDD. Ref.20
VAR_015751
Natural variant271S → P in ODDD. Ref.27
VAR_038356
Natural variant311I → M in ODDD. Ref.27
VAR_038357
Natural variant401A → V in ODDD. Ref.20 Ref.27 Ref.33 Ref.38
VAR_015752
Natural variant41 – 444Missing in ODDD.
VAR_070439
Natural variant411V → 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. Ref.32
VAR_058993
Natural variant471D → H in ODDD. Ref.42
VAR_071009
Natural variant491Q → K in ODDD. Ref.20
VAR_015753
Natural variant491Q → P in ODDD. Ref.38
VAR_058994
Natural variant491Q → QQ in ODDD. Ref.38
VAR_058995
Natural variant521F → FF in ODDD. Ref.20
VAR_015754
Natural variant591P → H in ODDD. Ref.30
VAR_058996
Natural variant691S → Y in ODDD. Ref.27
VAR_038358
Natural variant761R → H in HSS; overlapping features with oculodentodigital dysplasia. Ref.26
VAR_058997
Natural variant761R → S in ODDD. Ref.20
VAR_015755
Natural variant861S → Y in ODDD; de novo mutation found in a sporadic case. Ref.42
VAR_071010
Natural variant901L → V in ODDD. Ref.20
VAR_015756
Natural variant951H → R in ODDD. Ref.29
VAR_058998
Natural variant961V → A in ODDD. Ref.38
VAR_058999
Natural variant961V → E in ODDD. Ref.34
VAR_059000
Natural variant961V → M in ODDD. Ref.25
Corresponds to variant rs28931601 [ dbSNP | Ensembl ].
VAR_059001
Natural variant981Y → C in ODDD. Ref.20
VAR_015757
Natural variant1021K → N in ODDD. Ref.20
VAR_015758
Natural variant1061L → P in ODDD. Ref.38
VAR_059002
Natural variant1061L → R in ODDD. Ref.42
VAR_071011
Natural variant1101E → D in ODDD. Ref.33
VAR_059003
Natural variant1131L → P in ODDD. Ref.27 Ref.34
VAR_038359
Natural variant1241D → E.
Corresponds to variant rs2228966 [ dbSNP | Ensembl ].
VAR_014094
Natural variant1301I → T in ODDD. Ref.20
VAR_015759
Natural variant1341K → E in ODDD. Ref.20
VAR_015760
Natural variant1341K → N in ODDD. Ref.27
VAR_038360
Natural variant1381G → R in ODDD. Ref.20
VAR_015761
Natural variant1431G → S in SDTY3. Ref.27
Corresponds to variant rs28931600 [ dbSNP | Ensembl ].
VAR_038361
Natural variant1471M → T in ODDD. Ref.33
VAR_059004
Natural variant1481R → Q. Ref.27
Corresponds to variant rs2228960 [ dbSNP | Ensembl ].
VAR_014095
Natural variant1541T → A in ODDD. Ref.36 Ref.38
VAR_059005
Natural variant1541T → N in ODDD. Ref.34
VAR_059006
Natural variant1681A → T.
Corresponds to variant rs2228961 [ dbSNP | Ensembl ].
VAR_014096
Natural variant1691Missing in ODDD. Ref.33
VAR_059007
Natural variant1851Y → H.
Corresponds to variant rs2228962 [ dbSNP | Ensembl ].
VAR_014097
Natural variant1941H → 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. Ref.28
VAR_059008
Natural variant2011S → F in ODDD. Ref.38
VAR_059009
Natural variant2021R → C.
Corresponds to variant rs2228964 [ dbSNP | Ensembl ].
VAR_014098
Natural variant2021R → H in ODDD. Ref.20 Ref.27 Ref.38
VAR_015762
Natural variant2041T → M.
Corresponds to variant rs2228965 [ dbSNP | Ensembl ].
VAR_014099
Natural variant2061K → R in ODDD. Ref.40
VAR_070440
Natural variant2161V → L in ODDD. Ref.20
VAR_015763
Natural variant2201S → Y in ODDD. Ref.34
VAR_059010
Natural variant2391R → Q in CMDR. Ref.41
VAR_070441
Natural variant2391R → W in congenital heart malformations. Ref.31
Corresponds to variant rs2227887 [ dbSNP | Ensembl ].
VAR_014100
Natural variant2511S → T in congenital heart malformations. Ref.31
VAR_059011
Natural variant2531A → P in congenital heart malformations. Ref.31
VAR_059012
Natural variant2531A → V. Ref.20
Corresponds to variant rs17653265 [ dbSNP | Ensembl ].
VAR_015764
Natural variant2831P → L in congenital heart malformations. Ref.31
Corresponds to variant rs2228974 [ dbSNP | Ensembl ].
VAR_014101
Natural variant2901T → N in congenital heart malformations. Ref.31
Corresponds to variant rs2227881 [ dbSNP | Ensembl ].
VAR_014102
Natural variant3261T → A. Ref.23
VAR_059013
Natural variant3521E → G in heart malformations. Ref.23
VAR_059014
Natural variant3621R → Q in HLHS1 and AVSD3; associated with Gln-376 in one individual with atrioventricular septal defect; abolishes phosphorylation by PKA and PKC. Ref.24
Corresponds to variant rs2227885 [ dbSNP | Ensembl ].
VAR_032924
Natural variant3641S → P in heart malformations; shows abnormalities in the regulation of cell-cell communication as compared with cells expressing normal GJA1. Ref.23
VAR_059015
Natural variant3651S → N in heart malformations. Ref.23
VAR_059016
Natural variant3731S → G. Ref.23
VAR_059017
Natural variant3761R → Q in HLHS1 and AVSD3; associated with Gln-362 in one individual with atrioventricular septal defect; abolishes phosphorylation by PKA and PKC. Ref.24
VAR_032925

Secondary structure

....... 382
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17302 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7DDDAD8040284176

FASTA38243,008
        10         20         30         40         50         60 
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG 

        70         80         90        100        110        120 
CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG 

       130        140        150        160        170        180 
VNVDMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSIFEVAFL LIQWYIYGFS 

       190        200        210        220        230        240 
LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV 

       250        260        270        280        290        300 
KGKSDPYHAT SGALSPAKDC GSQKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN 

       310        320        330        340        350        360 
YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD NQNSKKLAAG HELQPLAIVD 

       370        380 
QRPSSRASSR ASSRPRPDDL EI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization and functional expression of the human cardiac gap junction channel."
Fishman G.I., Spray D.C., Leinwand L.A.
J. Cell Biol. 111:589-598(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart muscle.
[2]"The human connexin gene family of gap junction proteins: distinct chromosomal locations but similar structures."
Fishman G.I., Eddy R.L., Shows T.B., Rosenthal L., Leinwand L.A.
Genomics 10:250-256(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Sporadic cases of dilated cardiomyopathies associated with atrioventricular conduction defects are not linked to mutation within the connexins 40 and 43 genes."
Haefliger J.-A., Goy J.J., Waeber G.
Eur. Heart J. 20:1843-1843(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
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.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[6]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[9]"Intercellular calcium signaling via gap junction in connexin-43-transfected cells."
Toyofuku T., Yabuki M., Otsu K., Kuzuya T., Hori M., Tada M.
J. Biol. Chem. 273:1519-1528(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[10]"Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cell-cell contact forming cardiomyocytes."
Doble B.W., Dang X., Ping P., Fandrich R.R., Nickel B.E., Jin Y., Cattini P.A., Kardami E.
J. Cell Sci. 117:507-514(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-262.
[11]"Connexin expression and turnover: implications for cardiac excitability."
Saffitz J.E., Laing J.G., Yamada K.A.
Circ. Res. 86:723-728(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Failure to detect connexin43 mutations in 38 cases of sporadic and familial heterotaxy."
Gebbia M., Towbin J.A., Casey B.
Circulation 94:1909-1912(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT HEART LATERALIZATION DEFECT ARE NOT DUE TO GJA1.
[13]"Absence of mutations in the regulatory domain of the gap junction protein connexin 43 in patients with visceroatrial heterotaxy."
Penman Splitt M., Tsai M.Y., Burn J., Goodship J.A.
Heart 77:369-370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT HEART LATERALIZATION DEFECT ARE NOT DUE TO GJA1.
[14]"Connexin43 gene mutations and heterotaxy."
Toth T., Hajdu J., Marton T., Nagy B., Papp Z.
Circulation 97:117-118(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT HEART LATERALIZATION DEFECT ARE NOT DUE TO GJA1.
[15]"Mutations in GJA1 (connexin 43) are associated with non-syndromic autosomal recessive deafness."
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.
Hum. Mol. Genet. 10:2945-2951(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH NON-SYNDROMIC AUTOSOMAL RECESSIVE DEAFNESS, TISSUE SPECIFICITY.
[16]"Casein kinase 1 regulates connexin-43 gap junction assembly."
Cooper C.D., Lampe P.D.
J. Biol. Chem. 277:44962-44968(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-325; SER-328 AND SER-330 BY CSNK1D/CK1, INTERACTION WITH CSNK1D.
[17]"Molecular cloning and functional analysis of a novel Cx43 partner protein CIP150."
Akiyama M., Ishida N., Ogawa T., Yogo K., Takeya T.
Biochem. Biophys. Res. Commun. 335:1264-1271(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIAA1432.
[18]"Cellular sublocalization of Cx43 and the establishment of functional coupling in IMR-32 neuroblastoma cells."
Arnold J.M., Phipps M.W., Chen J., Phipps J.
Mol. Carcinog. 42:159-169(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-255 AND SER-262.
[19]"A nonsense mutation in the first transmembrane domain of connexin 43 underlies autosomal recessive oculodentodigital syndrome."
Richardson R.J., Joss S., Tomkin S., Ahmed M., Sheridan E., Dixon M.J.
J. Med. Genet. 43:E37-E37(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ODDD-AR.
[20]"Connexin 43 (GJA1) mutations cause the pleiotropic phenotype of oculodentodigital dysplasia."
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.
Am. J. Hum. Genet. 72:408-418(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, VARIANT VAL-253.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-306; SER-314 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"The gap junction channel protein connexin 43 is covalently modified and regulated by SUMOylation."
Kjenseth A., Fykerud T.A., Sirnes S., Bruun J., Yohannes Z., Kolberg M., Omori Y., Rivedal E., Leithe E.
J. Biol. Chem. 287:15851-15861(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-144 AND LYS-237, SUBCELLULAR LOCATION.
[23]"Mutations of the connexin43 gap-junction gene in patients with heart malformations and defects of laterality."
Britz-Cunningham S.H., Shah M.M., Zuppan C.W., Fletcher W.H.
N. Engl. J. Med. 332:1323-1329(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HEART MALFORMATIONS GLY-352; PRO-364 AND ASN-365, VARIANTS ALA-326 AND GLY-373, CHARACTERIZATION OF VARIANT HEART MALFORMATIONS PRO-364.
[24]"Identification of connexin43 (alpha1) gap junction gene mutations in patients with hypoplastic left heart syndrome by denaturing gradient gel electrophoresis (DGGE)."
Dasgupta C., Martinez A.-M., Zuppan C.W., Shah M.M., Bailey L.L., Fletcher W.H.
Mutat. Res. 479:173-186(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLHS1 GLN-362 AND GLN-376, VARIANTS AVSD3 GLN-362 AND GLN-376, CHARACTERIZATION OF VARIANTS HLHS1 GLN-362 AND GLN-376.
[25]"Novel Connexin 43 (GJA1) mutation causes oculo-dento-digital dysplasia with curly hair."
Kjaer K.W., Hansen L., Eiberg H., Leicht P., Opitz J.M., Tommerup N.
Am. J. Med. Genet. A 127:152-157(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODDD MET-96.
[26]"A homozygous GJA1 gene mutation causes a Hallermann-Streiff/ODDD spectrum phenotype."
Pizzuti A., Flex E., Mingarelli R., Salpietro C., Zelante L., Dallapiccola B.
Hum. Mutat. 23:286-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HSS HIS-76.
[27]"Expression of Gja1 correlates with the phenotype observed in oculodentodigital syndrome/type III syndactyly."
Richardson R.R., Donnai D., Meire F., Dixon M.J.
J. Med. Genet. 41:60-67(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ODDD PRO-27; MET-31; VAL-40; TYR-69; PRO-113; ASN-134; GLN-148 AND HIS-202, VARIANT SDTY3 SER-143.
[28]"A novel GJA1 mutation causes oculodentodigital dysplasia without syndactyly."
Vitiello C., D'Adamo P., Gentile F., Vingolo E.M., Gasparini P., Banfi S.
Am. J. Med. Genet. A 133:58-60(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODDD PRO-194.
[29]"Letter to the editor: Novel GJA1 mutation in oculodentodigital dysplasia."
Honkaniemi J., Kalkkila J.P., Koivisto P., Kahara V., Latvala T., Simola K.
Am. J. Med. Genet. A 139:48-49(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODDD ARG-95.
[30]"A novel mutation in the GJA1 gene in a family with oculodentodigital dysplasia."
Vasconcellos J.P.C., Melo M.B., Schimiti R.B., Bressanim N.C., Costa F.F., Costa V.P.
Arch. Ophthalmol. 123:1422-1426(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODDD HIS-59.
[31]"Mutations of connexin43 in fetuses with congenital heart malformations."
Chen P., Xie L.-J., Huang G.-Y., Zhao X.-Q., Chang C.
Chin. Med. J. 118:971-976(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CONGENITAL HEART MALFORMATIONS TRP-239; THR-251; PRO-253; LEU-283 AND ASN-290.
[32]"Bigenic connexin mutations in a patient with hidrotic ectodermal dysplasia."
Kellermayer R., Keller M., Ratajczak P., Richardson E., Harangi F., Merei E., Melegh B., Kosztolanyi G., Richard G.
Eur. J. Dermatol. 15:75-79(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-41.
[33]"Novel GJA1 mutations in patients with oculo-dento-digital dysplasia (ODDD)."
Debeer P., Van Esch H., Huysmans C., Pijkels E., De Smet L., Van de Ven W., Devriendt K., Fryns J.-P.
Eur. J. Med. Genet. 48:377-387(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ODDD VAL-40; ASP-110; THR-147 AND PHE-169 DEL.
[34]"Clinical and genetic variability of oculodentodigital dysplasia."
Wiest T., Herrmann O., Stoegbauer F., Grasshoff U., Enders H., Koch M.J., Grond-Ginsbach C., Schwaninger M.
Clin. Genet. 70:71-72(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ODDD GLU-96; PRO-113; ASN-154 AND TYR-220.
[35]"A novel GJA 1 mutation in oculo-dento-digital dysplasia with curly hair and hyperkeratosis."
Kelly S.C., Ratajczak P., Keller M., Purcell S.M., Griffin T., Richard G.
Eur. J. Dermatol. 16:241-245(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODDD PRO-11.
[36]"Oculodentodigital dysplasia with mandibular retrognathism and absence of syndactyly: a case report with a novel mutation in the connexin 43 gene."
van Es R.J.J., Wittebol-Post D., Beemer F.A.
Int. J. Oral Maxillofac. Surg. 36:858-860(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODDD ALA-154.
[37]"A new GJA1 (connexin 43) mutation causing oculodentodigital dysplasia associated to uncommon features."
de la Parra D.R., Zenteno J.C.
Ophthalmic Genet. 28:198-202(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODDD VAL-2.
[38]"GJA1 mutations, variants, and connexin 43 dysfunction as it relates to the oculodentodigital dysplasia phenotype."
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.
Hum. Mutat. 30:724-733(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ODDD VAL-7; VAL-40; PRO-49; GLN-49 INS; ALA-96; PRO-106; ALA-154; PHE-201 AND HIS-202.
[39]"Oculodentodigital dysplasia: new ocular findings and a novel connexin 43 mutation."
Gabriel L.A., Sachdeva R., Marcotty A., Rockwood E.J., Traboulsi E.I.
Arch. Ophthalmol. 129:781-784(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ODDD PRO-11 AND 41-VAL--ALA-44 DEL.
[40]"A novel mutation in GJA1 causing oculodentodigital syndrome and primary lymphoedema in a three generation family."
Brice G., Ostergaard P., Jeffery S., Gordon K., Mortimer P.S., Mansour S.
Clin. Genet. 84:378-381(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ODDD ARG-206.
[41]"A novel autosomal recessive GJA1 missense mutation linked to Craniometaphyseal dysplasia."
Hu Y., Chen I.P., de Almeida S., Tiziani V., Do Amaral C.M., Gowrishankar K., Passos-Bueno M.R., Reichenberger E.J.
PLoS ONE 8:E73576-E73576(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMDR GLN-239.
[42]"Three novel GJA1 missense substitutions resulting in oculo-dento-digital dysplasia (ODDD) - further extension of the mutational spectrum."
Jamsheer A., Sowinska-Seidler A., Socha M., Stembalska A., Kiraly-Borri C., Latos-Bielenska A.
Gene 539:157-161(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ODDD HIS-47; TYR-86 AND ARG-106.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52947 mRNA. Translation: CAA37122.1.
M65188 mRNA. Translation: AAA52131.1.
AF151980 Genomic DNA. Translation: AAD37802.2.
CR541660 mRNA. Translation: CAG46461.1.
AK312324 mRNA. Translation: BAG35246.1.
AL139098 Genomic DNA. Translation: CAI20002.1.
CH471051 Genomic DNA. Translation: EAW48178.1.
BC026329 mRNA. Translation: AAH26329.1.
CCDSCCDS5123.1.
PIRA35853.
RefSeqNP_000156.1. NM_000165.4.
UniGeneHs.74471.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LL2NMR-A234-259[»]
ProteinModelPortalP17302.
SMRP17302. Positions 3-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108964. 19 interactions.
IntActP17302. 3 interactions.
MINTMINT-147603.
STRING9606.ENSP00000282561.

Chemistry

DrugBankDB01136. Carvedilol.
GuidetoPHARMACOLOGY728.

PTM databases

PhosphoSiteP17302.

Polymorphism databases

DMDM117706.

Proteomic databases

MaxQBP17302.
PaxDbP17302.
PeptideAtlasP17302.
PRIDEP17302.

Protocols and materials databases

DNASU2697.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282561; ENSP00000282561; ENSG00000152661.
GeneID2697.
KEGGhsa:2697.
UCSCuc003pyr.3. human.

Organism-specific databases

CTD2697.
GeneCardsGC06P121756.
HGNCHGNC:4274. GJA1.
HPACAB010753.
MIM121014. gene.
164200. phenotype.
186100. phenotype.
218400. phenotype.
234100. phenotype.
241550. phenotype.
257850. phenotype.
600309. phenotype.
neXtProtNX_P17302.
Orphanet90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
1522. Craniometaphyseal dysplasia.
2248. Hypoplastic left heart syndrome.
2710. Oculodentodigital dysplasia.
93404. Syndactyly type 3.
PharmGKBPA28685.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45368.
HOGENOMHOG000231127.
HOVERGENHBG009576.
InParanoidP17302.
KOK07372.
OMAGANVDMH.
OrthoDBEOG7P2XSS.
PhylomeDBP17302.
TreeFamTF329606.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
SignaLinkP17302.

Gene expression databases

ArrayExpressP17302.
BgeeP17302.
CleanExHS_GJA1.
GenevestigatorP17302.

Family and domain databases

InterProIPR000500. Connexin.
IPR002261. Connexin43.
IPR013124. Connexin43_C.
IPR019570. Connexin_CCC.
IPR017990. Connexin_CS.
IPR013092. Connexin_N.
[Graphical view]
PANTHERPTHR11984. PTHR11984. 1 hit.
PfamPF00029. Connexin. 1 hit.
PF03508. Connexin43. 1 hit.
PF10582. Connexin_CCC. 1 hit.
[Graphical view]
PRINTSPR00206. CONNEXIN.
PR01132. CONNEXINA1.
SMARTSM00037. CNX. 1 hit.
SM01089. Connexin_CCC. 1 hit.
[Graphical view]
PROSITEPS00407. CONNEXINS_1. 1 hit.
PS00408. CONNEXINS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGJA1. human.
GeneWikiGJA1.
GenomeRNAi2697.
NextBio10668.
PROP17302.
SOURCESearch...

Entry information

Entry nameCXA1_HUMAN
AccessionPrimary (citable) accession number: P17302
Secondary accession number(s): B2R5U9, Q6FHU1, Q9Y5I8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 180 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM