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P13569 (CFTR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 195. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystic fibrosis transmembrane conductance regulator

Short name=CFTR
Alternative name(s):
ATP-binding cassette sub-family C member 7
Channel conductance-controlling ATPase
EC=3.6.3.49
cAMP-dependent chloride channel
Gene names
Name:CFTR
Synonyms:ABCC7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1480 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. Can inhibit the chloride channel activity of ANO1. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation. Ref.20

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts with SLC26A3, SLC26A6 and SHANK2 By similarity. Interacts with SLC9A3R1, MYO6 and GOPC. Interacts with SLC4A7 through SLC9A3R1. Found in a complex with MYO5B and RAB11A. Interacts with ANO1. Interacts with SLC26A8. Ref.10 Ref.11 Ref.13 Ref.17 Ref.20 Ref.22

Subcellular location

Early endosome membrane; Multi-pass membrane protein. Cell membrane. Note: In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia (Ref.21). Ref.18 Ref.20 Ref.21

Tissue specificity

Expressed in the respiratory airway, including bronchial epithelium, and in the female reproductive tract, including oviduct (at protein level). Ref.21

Domain

The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, SLC9A3R1/EBP50 complex.

Post-translational modification

Phosphorylated; activates the channel. It is not clear whether PKC phosphorylation itself activates the channel or permits activation by phosphorylation at PKA sites. Phosphorylated by AMPK. Ref.6 Ref.8 Ref.12 Ref.16 Ref.23

Ubiquitinated, leading to its degradation in the lysosome. Deubiquitination by USP10 in early endosomes, enhances its endocytic recycling. Ubiquitinated by RNF185 during ER stress. Ref.18 Ref.23 Ref.24

Involvement in disease

Cystic fibrosis (CF) [MIM:219700]: A common generalized disorder of the exocrine glands which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes. It is the most common genetic disease in Caucasians, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.78

Congenital bilateral absence of the vas deferens (CBAVD) [MIM:277180]: Important cause of sterility in men and could represent an incomplete form of cystic fibrosis, as the majority of men suffering from cystic fibrosis lack the vas deferens.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.48 Ref.49 Ref.62 Ref.76 Ref.77

Sequence similarities

Belongs to the ABC transporter superfamily. ABCC family. CFTR transporter (TC 3.A.1.202) subfamily. [View classification]

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell membrane
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Chloride
Nucleotide-binding
   Molecular functionChloride channel
Hydrolase
Ion channel
   PTMGlycoprotein
Isopeptide bond
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

chloride transmembrane transport

Inferred from direct assay Ref.20. Source: GOC

cholesterol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

cholesterol transport

Inferred from electronic annotation. Source: Ensembl

intracellular pH elevation

Inferred from sequence or structural similarity. Source: UniProtKB

iodide transport

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

membrane hyperpolarization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

positive regulation of voltage-gated chloride channel activity

Inferred from direct assay PubMed 22006324. Source: UniProt

respiratory gaseous exchange

Traceable author statement PubMed 9875854. Source: ProtInc

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

sperm capacitation

Inferred from sequence or structural similarity. Source: UniProtKB

transepithelial chloride transport

Inferred from electronic annotation. Source: Ensembl

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement PubMed 10581360PubMed 7541313. Source: ProtInc

vasodilation

Inferred from electronic annotation. Source: Ensembl

water transport

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 12801959Ref.13. Source: UniProtKB

basolateral plasma membrane

Non-traceable author statement Ref.10. Source: UniProtKB

cell surface

Inferred from direct assay PubMed 20658517. Source: UniProtKB

chloride channel complex

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from direct assay Ref.18. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microvillus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.20. Source: UniProtKB

protein complex

Inferred from direct assay Ref.17. Source: UniProtKB

   Molecular_functionATP binding

Traceable author statement Ref.1. Source: ProtInc

ATP-binding and phosphorylation-dependent chloride channel activity

Traceable author statement PubMed 10581360. Source: ProtInc

PDZ domain binding

Inferred from direct assay Ref.10. Source: UniProtKB

bicarbonate transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

channel-conductance-controlling ATPase activity

Non-traceable author statement Ref.10. Source: UniProtKB

chloride channel activity

Inferred from direct assay Ref.20. Source: UniProtKB

chloride channel inhibitor activity

Inferred from direct assay Ref.20. Source: UniProtKB

chloride transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10Ref.13PubMed 20658517Ref.20PubMed 9792704. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P13569-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P13569-2)

The sequence of this isoform differs from the canonical sequence as follows:
     404-464: Missing.
Note: Exon skipping favored by a high number of TG repeats and a low number of T repeats at the intron-exon boundary. Causes congenital bilateral absence of the vas deferens (CBAVD).
Isoform 3 (identifier: P13569-3)

The sequence of this isoform differs from the canonical sequence as follows:
     589-605: SCVCKLMANKTRILVTS → RRRCSCLLDRNKKTIF
     606-1480: Missing.
Note: Alternative acceptor site favored by mutation in an exonic splicing enhancer (ESE). Causes cystic fibrosis (CF).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14801480Cystic fibrosis transmembrane conductance regulator
PRO_0000093419

Regions

Topological domain1 – 8080Cytoplasmic Potential
Transmembrane81 – 10323Helical; Name=1; Potential
Topological domain104 – 11714Extracellular Potential
Transmembrane118 – 13821Helical; Name=2; Potential
Topological domain139 – 19456Cytoplasmic Potential
Transmembrane195 – 21521Helical; Name=3; Potential
Topological domain216 – 2205Extracellular Potential
Transmembrane221 – 24121Helical; Name=4; Potential
Topological domain242 – 30766Cytoplasmic Potential
Transmembrane308 – 32821Helical; Name=5; Potential
Topological domain329 – 3302Extracellular Potential
Transmembrane331 – 35020Helical; Name=6; Potential
Topological domain351 – 859509Cytoplasmic Potential
Transmembrane860 – 88021Helical; Name=7; Potential
Topological domain881 – 91131Extracellular Potential
Transmembrane912 – 93221Helical; Name=8; Potential
Topological domain933 – 99058Cytoplasmic Potential
Transmembrane991 – 101121Helical; Name=9; Potential
Topological domain1012 – 10132Extracellular Potential
Transmembrane1014 – 103421Helical; Name=10; Potential
Topological domain1035 – 110268Cytoplasmic Potential
Transmembrane1103 – 112321Helical; Name=11; Potential
Topological domain1124 – 11285Extracellular Potential
Transmembrane1129 – 114921Helical; Name=12; Potential
Topological domain1150 – 1480331Cytoplasmic Potential
Domain81 – 365285ABC transmembrane type-1 1
Domain423 – 646224ABC transporter 1
Domain859 – 1155297ABC transmembrane type-1 2
Domain1210 – 1443234ABC transporter 2
Nucleotide binding458 – 4658ATP 1 Potential
Nucleotide binding1244 – 12518ATP 2 Potential
Motif1478 – 14803PDZ-binding

Amino acid modifications

Modified residue2911Phosphothreonine Ref.19
Modified residue5491Phosphoserine Ref.19
Modified residue6601Phosphoserine; by PKA Ref.6 Ref.8 Ref.23
Modified residue6861Phosphoserine; by PKC Ref.6 Ref.23
Modified residue7001Phosphoserine; by PKA Ref.6 Ref.8 Ref.23
Modified residue7121Phosphoserine; by PKA Ref.8 Ref.23
Modified residue7171Phosphothreonine Ref.23
Modified residue7371Phosphoserine; by PKA Ref.6 Ref.8 Ref.23
Modified residue7531Phosphoserine; by PKA Ref.8
Modified residue7681Phosphoserine; by PKA Ref.6 Ref.8
Modified residue7901Phosphoserine; by PKC Ref.6
Modified residue7951Phosphoserine; by PKA Ref.6 Ref.8 Ref.23
Modified residue8131Phosphoserine; by PKA Ref.6 Ref.8
Modified residue14441Phosphoserine Ref.23
Modified residue14561Phosphoserine Ref.23
Lipidation5241S-palmitoyl cysteine Ref.23
Lipidation13951S-palmitoyl cysteine Ref.23
Glycosylation8941N-linked (GlcNAc...) Ref.7
Glycosylation9001N-linked (GlcNAc...) Ref.7
Cross-link688Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

Natural variations

Alternative sequence404 – 46461Missing in isoform 2.
VSP_022123
Alternative sequence589 – 60517SCVCK…ILVTS → RRRCSCLLDRNKKTIF in isoform 3.
VSP_022124
Alternative sequence606 – 1480875Missing in isoform 3.
VSP_022125
Natural variant131S → F in CF. Ref.72
VAR_000101
Natural variant311R → C. Ref.40
Corresponds to variant rs1800073 [ dbSNP | Ensembl ].
VAR_000102
Natural variant311R → L in CF. Ref.52
VAR_000103
Natural variant421S → F in CF. Ref.56
VAR_000104
Natural variant441D → G in CF.
VAR_000105
Natural variant441D → V.
Corresponds to variant rs1800074 [ dbSNP | Ensembl ].
VAR_000106
Natural variant501S → Y in CBAVD. Ref.62
VAR_000107
Natural variant571W → G in CF. Ref.50
VAR_000108
Natural variant671P → L in CF.
VAR_000109
Natural variant741R → W in CF.
Corresponds to variant rs115545701 [ dbSNP | Ensembl ].
VAR_000110
Natural variant751R → Q.
Corresponds to variant rs1800076 [ dbSNP | Ensembl ].
VAR_000111
Natural variant851G → E in CF. Ref.66
VAR_000112
Natural variant871F → L in CF. Ref.47
VAR_000113
Natural variant911G → R in CF.
VAR_000114
Natural variant921E → K in CF. Ref.34 Ref.37
VAR_000115
Natural variant981Q → R in CF. Ref.54
VAR_000116
Natural variant1051I → S in CF.
VAR_000117
Natural variant1091Y → C in CF. Ref.45
VAR_000118
Natural variant1101D → H in CF.
VAR_000119
Natural variant1111P → L in CBAVD. Ref.77
VAR_000120
Natural variant1171R → C in CF. Ref.34
VAR_000121
Natural variant1171R → H in CF and CBAVD. Ref.66
VAR_000122
Natural variant1171R → L in CF. Ref.56
VAR_000123
Natural variant1171R → P in CF. Ref.73
VAR_000124
Natural variant1201A → T in CF. Ref.46
VAR_000125
Natural variant1381L → P.
Corresponds to variant rs1800078 [ dbSNP | Ensembl ].
VAR_009895
Natural variant1391H → R in CF. Ref.56
VAR_000126
Natural variant1411A → D in CF. Ref.64
VAR_000127
Natural variant1481I → T in CF.
Corresponds to variant rs35516286 [ dbSNP | Ensembl ].
VAR_000128
Natural variant1491G → R in CBAVD. Ref.48
VAR_000129
Natural variant1701R → H.
Corresponds to variant rs1800079 [ dbSNP | Ensembl ].
VAR_009896
Natural variant1781G → R in CF.
VAR_000130
Natural variant1821S → G.
Corresponds to variant rs1800080 [ dbSNP | Ensembl ].
VAR_009897
Natural variant1921Missing in CF. Ref.73
VAR_000131
Natural variant1931E → K in CBAVD and CF. Ref.48 Ref.50
VAR_000132
Natural variant1991H → Q in CF.
VAR_000133
Natural variant1991H → Y in CF. Ref.42
VAR_000134
Natural variant2051P → S in CF. Ref.38
VAR_000135
Natural variant2061L → W in CF. Ref.51
VAR_000136
Natural variant2251C → R in CF.
VAR_000137
Natural variant2441M → K in CBAVD. Ref.77
VAR_000138
Natural variant2581R → G in CBAVD. Ref.48
Corresponds to variant rs191456345 [ dbSNP | Ensembl ].
VAR_000139
Natural variant2871N → Y in CF. Ref.66
VAR_000140
Natural variant2971R → Q in CF.
VAR_000141
Natural variant3011Y → C in CF.
Corresponds to variant rs150691494 [ dbSNP | Ensembl ].
VAR_000142
Natural variant3071S → N in CF.
VAR_000143
Natural variant3111F → L in CF.
VAR_000144
Natural variant3111Missing in CF. Ref.67
VAR_000145
Natural variant3141G → E in CF.
VAR_000146
Natural variant3141G → R in CF. Ref.58
VAR_000147
Natural variant3221V → M.
Corresponds to variant rs1800085 [ dbSNP | Ensembl ].
VAR_009898
Natural variant3341R → W in CF; mild.
Corresponds to variant rs121909011 [ dbSNP | Ensembl ].
VAR_000148
Natural variant3361I → K in CF.
VAR_000150
Natural variant3381T → I in CF; mild; isolated hypotonic dehydration. Ref.55 Ref.72
VAR_000151
Natural variant3461L → P in CF; dominant mutation but mild phenotype. Ref.41
VAR_000152
Natural variant3471R → H in CF.
VAR_000153
Natural variant3471R → L in CF.
VAR_000154
Natural variant3471R → P in CF; MILD.
VAR_000155
Natural variant3511T → S.
Corresponds to variant rs1800086 [ dbSNP | Ensembl ].
VAR_009899
Natural variant3521R → Q in CF.
VAR_000156
Natural variant3531Q → H.
Corresponds to variant rs1800087 [ dbSNP | Ensembl ].
VAR_009900
Natural variant359 – 3602QT → KK in CF.
VAR_000158
Natural variant3591Q → K in CF.
VAR_000157
Natural variant3701K → KNK in CF.
VAR_000159
Natural variant4551A → E in CF. Ref.66
VAR_000160
Natural variant4561V → F in CF.
VAR_000161
Natural variant4581G → V in CF.
VAR_000162
Natural variant4671L → F.
Corresponds to variant rs1800089 [ dbSNP | Ensembl ].
VAR_000163
Natural variant4701V → M. Ref.1 Ref.2 Ref.3 Ref.76 Ref.79
Corresponds to variant rs213950 [ dbSNP | Ensembl ].
VAR_000164
Natural variant4801G → C in CF.
VAR_000165
Natural variant4921S → F in CF.
VAR_000166
Natural variant5041E → Q in CF.
VAR_000167
Natural variant5061I → M.
Corresponds to variant rs1800092 [ dbSNP | Ensembl ].
VAR_009901
Natural variant5061I → V.
VAR_000168
Natural variant5071I → V.
Corresponds to variant rs1800091 [ dbSNP | Ensembl ].
VAR_000169
Natural variant5071Missing in CF.
VAR_000170
Natural variant5081F → C.
Corresponds to variant rs1800093 [ dbSNP | Ensembl ].
VAR_000172
Natural variant5081Missing in CF and CBAVD; most common mutation; 72% of the population; CFTR fails to be properly delivered to plasma membrane.
VAR_000171
Natural variant5131D → G in CBAVD. Ref.76
VAR_000173
Natural variant5201V → F in CF. Ref.31
Corresponds to variant rs77646904 [ dbSNP | Ensembl ].
VAR_000174
Natural variant5321K → E.
Corresponds to variant rs35032490 [ dbSNP | Ensembl ].
VAR_048150
Natural variant5441G → V in CBAVD. Ref.77
VAR_000175
Natural variant5491S → I in CF.
VAR_000177
Natural variant5491S → N in CF.
VAR_000176
Natural variant5491S → R in CF.
VAR_000178
Natural variant5511G → D in CF. Ref.66
VAR_000179
Natural variant5511G → S in CF.
VAR_000180
Natural variant5531R → Q in CF.
VAR_000181
Natural variant5581L → S in CF.
VAR_000182
Natural variant5591A → T in CF.
VAR_000183
Natural variant5601R → K in CF.
VAR_000184
Natural variant5601R → S in CF. Ref.71
VAR_000185
Natural variant5601R → T in CF.
VAR_000186
Natural variant5621V → I.
Corresponds to variant rs1800097 [ dbSNP | Ensembl ].
VAR_000187
Natural variant5621V → L in CF. Ref.61
Corresponds to variant rs1800097 [ dbSNP | Ensembl ].
VAR_000188
Natural variant5631Y → N in CF.
VAR_000189
Natural variant5691Y → C in CF. Ref.59
VAR_000190
Natural variant5691Y → D in CF. Ref.71
VAR_000191
Natural variant5691Y → H in CF.
VAR_000192
Natural variant5711L → S in CF.
VAR_000193
Natural variant5721D → N in CF. Ref.53
VAR_000194
Natural variant5741P → H in CF.
VAR_000195
Natural variant5761G → A.
Corresponds to variant rs1800098 [ dbSNP | Ensembl ].
VAR_000196
Natural variant5791D → G in CF. Ref.50 Ref.78
VAR_000197
Natural variant6011I → F in CF.
VAR_000198
Natural variant6051S → F.
Corresponds to variant rs766874 [ dbSNP | Ensembl ].
VAR_048151
Natural variant6101L → S in CF.
VAR_000199
Natural variant6131A → T in CF.
Corresponds to variant rs201978662 [ dbSNP | Ensembl ].
VAR_000200
Natural variant6141D → G in CF.
Corresponds to variant rs201124247 [ dbSNP | Ensembl ].
VAR_000201
Natural variant6181I → T in CF.
VAR_000202
Natural variant6191L → S in CF. Ref.42
VAR_000203
Natural variant6201H → P in CF.
VAR_000204
Natural variant6201H → Q in CF.
VAR_000205
Natural variant6221G → D in oligospermia.
VAR_000206
Natural variant6281G → R in CF.
VAR_000207
Natural variant6331L → P in CF.
VAR_000208
Natural variant6481D → V in CF.
VAR_000209
Natural variant6511D → N in CF.
VAR_000210
Natural variant6541S → G.
Corresponds to variant rs1800099 [ dbSNP | Ensembl ].
VAR_009902
Natural variant6651T → S in CF. Ref.57
VAR_000211
Natural variant6681R → C.
Corresponds to variant rs1800100 [ dbSNP | Ensembl ].
VAR_000212
Natural variant6931F → L.
Corresponds to variant rs1800101 [ dbSNP | Ensembl ].
VAR_000213
Natural variant7541V → M in CF.
Corresponds to variant rs150157202 [ dbSNP | Ensembl ].
VAR_000214
Natural variant7661R → M in CBAVD.
VAR_000215
Natural variant7921R → G in CBAVD.
VAR_000216
Natural variant8001A → G in CBAVD. Ref.48
VAR_000217
Natural variant8071I → M in CBAVD.
Corresponds to variant rs1800103 [ dbSNP | Ensembl ].
VAR_000218
Natural variant8221E → K in CF.
VAR_000219
Natural variant8261E → K in thoracic sarcoidosis.
VAR_000220
Natural variant8661C → Y in CF.
VAR_000221
Natural variant9031Y → H.
Corresponds to variant rs1800106 [ dbSNP | Ensembl ].
VAR_009903
Natural variant9091S → I.
Corresponds to variant rs1800107 [ dbSNP | Ensembl ].
VAR_009904
Natural variant9121S → L. Ref.40
Corresponds to variant rs121909034 [ dbSNP | Ensembl ].
VAR_000222
Natural variant9131Y → C in CF.
VAR_000223
Natural variant9171Y → C in CF.
VAR_000224
Natural variant9491H → Y in CF. Ref.40
VAR_000225
Natural variant9521M → I in CF.
VAR_000226
Natural variant9671L → S.
Corresponds to variant rs1800110 [ dbSNP | Ensembl ].
VAR_009905
Natural variant9971L → F in CF.
Corresponds to variant rs1800111 [ dbSNP | Ensembl ].
VAR_000227
Natural variant10051I → R in CF. Ref.42
VAR_000228
Natural variant10061A → E in CF. Ref.56
VAR_000229
Natural variant10131P → L in CF. Ref.68
VAR_000230
Natural variant10281M → I in CF. Ref.68
VAR_000231
Natural variant10521F → V in CF. Ref.36
VAR_000232
Natural variant10611G → R in CF. Ref.36 Ref.60
Corresponds to variant rs142394380 [ dbSNP | Ensembl ].
VAR_000233
Natural variant10651L → P in CF. Ref.40
VAR_000234
Natural variant10651L → R in CF. Ref.74
VAR_000235
Natural variant10661R → C in CF. Ref.65
VAR_000236
Natural variant10661R → H in CF.
VAR_000237
Natural variant10661R → L in CF. Ref.36
VAR_000238
Natural variant10671A → T in CF.
VAR_000239
Natural variant10671A → V.
Corresponds to variant rs1800114 [ dbSNP | Ensembl ].
VAR_000240
Natural variant10701R → P in CF. Ref.66
VAR_000242
Natural variant10701R → Q in CF. Ref.36
VAR_000241
Natural variant10701R → W in CBAVD.
Corresponds to variant rs202179988 [ dbSNP | Ensembl ].
VAR_011564
Natural variant10711Q → P in CF. Ref.40
VAR_000243
Natural variant10721P → L in CF.
VAR_000244
Natural variant10771L → P in CF.
VAR_000245
Natural variant10851H → R in CF. Ref.36
VAR_000246
Natural variant10981W → R in CF. Ref.52
VAR_000247
Natural variant11011M → K in CF. Ref.35
Corresponds to variant rs36210737 [ dbSNP | Ensembl ].
VAR_000248
Natural variant11011M → R in CF. Ref.36
VAR_011565
Natural variant11371M → V in CF.
VAR_000249
Natural variant11401Missing in CF. Ref.63
VAR_000250
Natural variant11521D → H in CF.
VAR_000251
Natural variant11621R → L.
Corresponds to variant rs1800120 [ dbSNP | Ensembl ].
VAR_000252
Natural variant12201T → I. Ref.40
Corresponds to variant rs1800123 [ dbSNP | Ensembl ].
VAR_000253
Natural variant12341I → V in CF.
VAR_000254
Natural variant12351S → R in CF.
Corresponds to variant rs34911792 [ dbSNP | Ensembl ].
VAR_000255
Natural variant12441G → E in CF.
VAR_000256
Natural variant12491G → E in CF. Ref.43
VAR_000257
Natural variant12511S → N in CF.
VAR_000258
Natural variant12551S → P in CF. Ref.33
VAR_000259
Natural variant12701D → N in CF.
Corresponds to variant rs11971167 [ dbSNP | Ensembl ].
VAR_000260
Natural variant12821W → R in CF.
VAR_000261
Natural variant12831R → M in CF. Ref.32
VAR_000262
Natural variant12861F → S in CF.
VAR_000263
Natural variant12911Q → H in CF. Ref.31
VAR_000264
Natural variant12911Q → R in CF. Ref.42
VAR_000265
Natural variant13031N → H in CF.
VAR_000266
Natural variant13031N → K in CF. Ref.66
Corresponds to variant rs80034486 [ dbSNP | Ensembl ].
VAR_000267
Natural variant13491G → D in CF.
VAR_000268
Natural variant13641A → V in CBAVD. Ref.77
VAR_000269
Natural variant13971V → E in CF. Ref.44
VAR_000270
Natural variant14531R → W. Ref.3
Corresponds to variant rs4148725 [ dbSNP | Ensembl ].
VAR_048152

Experimental info

Sequence conflict6201H → N in AAA35680. Ref.1
Sequence conflict8331F → L in AAA35680. Ref.1

Secondary structure

.................................................................................................... 1480
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 15, 2007. Version 3.
Checksum: 8D082AA2E768C065

FASTA1,480168,142
        10         20         30         40         50         60 
MQRSPLEKAS VVSKLFFSWT RPILRKGYRQ RLELSDIYQI PSVDSADNLS EKLEREWDRE 

        70         80         90        100        110        120 
LASKKNPKLI NALRRCFFWR FMFYGIFLYL GEVTKAVQPL LLGRIIASYD PDNKEERSIA 

       130        140        150        160        170        180 
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL 

       190        200        210        220        230        240 
VSLLSNNLNK FDEGLALAHF VWIAPLQVAL LMGLIWELLQ ASAFCGLGFL IVLALFQAGL 

       250        260        270        280        290        300 
GRMMMKYRDQ RAGKISERLV ITSEMIENIQ SVKAYCWEEA MEKMIENLRQ TELKLTRKAA 

       310        320        330        340        350        360 
YVRYFNSSAF FFSGFFVVFL SVLPYALIKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT 

       370        380        390        400        410        420 
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGELFE KAKQNNNNRK 

       430        440        450        460        470        480 
TSNGDDSLFF SNFSLLGTPV LKDINFKIER GQLLAVAGST GAGKTSLLMV IMGELEPSEG 

       490        500        510        520        530        540 
KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEDI SKFAEKDNIV 

       550        560        570        580        590        600 
LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR 

       610        620        630        640        650        660 
ILVTSKMEHL KKADKILILH EGSSYFYGTF SELQNLQPDF SSKLMGCDSF DQFSAERRNS 

       670        680        690        700        710        720 
ILTETLHRFS LEGDAPVSWT ETKKQSFKQT GEFGEKRKNS ILNPINSIRK FSIVQKTPLQ 

       730        740        750        760        770        780 
MNGIEEDSDE PLERRLSLVP DSEQGEAILP RISVISTGPT LQARRRQSVL NLMTHSVNQG 

       790        800        810        820        830        840 
QNIHRKTTAS TRKVSLAPQA NLTELDIYSR RLSQETGLEI SEEINEEDLK ECFFDDMESI 

       850        860        870        880        890        900 
PAVTTWNTYL RYITVHKSLI FVLIWCLVIF LAEVAASLVV LWLLGNTPLQ DKGNSTHSRN 

       910        920        930        940        950        960 
NSYAVIITST SSYYVFYIYV GVADTLLAMG FFRGLPLVHT LITVSKILHH KMLHSVLQAP 

       970        980        990       1000       1010       1020 
MSTLNTLKAG GILNRFSKDI AILDDLLPLT IFDFIQLLLI VIGAIAVVAV LQPYIFVATV 

      1030       1040       1050       1060       1070       1080 
PVIVAFIMLR AYFLQTSQQL KQLESEGRSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK 

      1090       1100       1110       1120       1130       1140 
ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGRVG IILTLAMNIM 

      1150       1160       1170       1180       1190       1200 
STLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEGKPTKSTK PYKNGQLSKV MIIENSHVKK 

      1210       1220       1230       1240       1250       1260 
DDIWPSGGQM TVKDLTAKYT EGGNAILENI SFSISPGQRV GLLGRTGSGK STLLSAFLRL 

      1270       1280       1290       1300       1310       1320 
LNTEGEIQID GVSWDSITLQ QWRKAFGVIP QKVFIFSGTF RKNLDPYEQW SDQEIWKVAD 

      1330       1340       1350       1360       1370       1380 
EVGLRSVIEQ FPGKLDFVLV DGGCVLSHGH KQLMCLARSV LSKAKILLLD EPSAHLDPVT 

      1390       1400       1410       1420       1430       1440 
YQIIRRTLKQ AFADCTVILC EHRIEAMLEC QQFLVIEENK VRQYDSIQKL LNERSLFRQA 

      1450       1460       1470       1480 
ISPSDRVKLF PHRNSSKCKS KPQIAALKEE TEEEVQDTRL 

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Isoform 2 [UniParc].

Checksum: 898B37C8C61CC24A
Show »

FASTA1,419161,596
Isoform 3 [UniParc].

Checksum: 6059582EE8505353
Show »

FASTA60469,230

References

« Hide 'large scale' references
[1]"Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA."
Riordan J.R., Rommens J.M., Kerem B., Alon N., Rozmahel R., Grzelczak Z., Zielenski J., Lok S., Plavsic N., Chou J.-L., Drumm M.L., Iannuzzi M.C., Collins F.S., Tsui L.-C.
Science 245:1066-1073(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-470.
[2]"Genomic DNA sequence of the cystic fibrosis transmembrane conductance regulator (CFTR) gene."
Zielenski J., Rozmahel R., Bozon D., Kerem B., Grzelczak Z., Riordan J.R., Rommens J., Tsui L.-C.
Genomics 10:214-228(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-470.
[3]Stacy R., Subramanian S., Deodato C., Burkhardt P., Song Y., Paddock M., Chang J., Zhou Y., Haugen E., Waring D., Chapman P., Hayden H., Levy R., Wu Z., Rouse G., James R., Phelps K., Olson M.V., Kaul R.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-470 AND TRP-1453.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Phosphorylation of the cystic fibrosis transmembrane conductance regulator."
Picciotto M.R., Cohn J.A., Bertuzzi G., Greenguard P., Nairn A.C.
J. Biol. Chem. 267:12742-12752(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-737; SER-768; SER-790; SER-795 AND SER-813.
[7]"Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion."
Chang X.-B., Hou Y.-X., Jensen T.J., Riordan J.R.
J. Biol. Chem. 269:18572-18575(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-894 AND ASN-900, TOPOLOGY.
[8]"Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry."
Neville D.C.A., Rozanas C.R., Rice E.M., Gruis D.B., Verkman A.S., Townsend R.R.
Protein Sci. 6:2436-2445(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-660; SER-700; SER-712; SER-737; SER-753; SER-768; SER-795 AND SER-813.
[9]"Splicing factors induce cystic fibrosis transmembrane regulator exon 9 skipping through a nonevolutionary conserved intronic element."
Pagani F., Buratti E., Stuani C., Romano M., Zuccato E., Niksic M., Giglio L., Faraguna D., Baralle F.E.
J. Biol. Chem. 275:21041-21047(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
[10]"A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression."
Cheng J., Moyer B.D., Milewski M., Loffing J., Ikeda M., Mickle J.E., Cutting G.R., Li M., Stanton B.A., Guggino W.B.
J. Biol. Chem. 277:3520-3529(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GOPC.
[11]"The cystic fibrosis transmembrane conductance regulator interacts with and regulates the activity of the HCO3- salvage transporter human Na+-HCO3-cotransport isoform 3."
Park M., Ko S.B.H., Choi J.Y., Muallem G., Thomas P.J., Pushkin A., Lee M.-S., Kim J.Y., Lee M.G., Muallem S., Kurtz I.
J. Biol. Chem. 277:50503-50509(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SC4A7 AND SLC9A3R1.
[12]"Physiological modulation of CFTR activity by AMP-activated protein kinase in polarized T84 cells."
Hallows K.R., Kobinger G.P., Wilson J.M., Witters L.A., Foskett J.K.
Am. J. Physiol. 284:C1297-C1308(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY AMPK.
[13]"Myosin VI regulates endocytosis of the cystic fibrosis transmembrane conductance regulator."
Swiatecka-Urban A., Boyd C., Coutermarsh B., Karlson K.H., Barnaby R., Aschenbrenner L., Langford G.M., Hasson T., Stanton B.A.
J. Biol. Chem. 279:38025-38031(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO6.
[14]"Cystic fibrosis transmembrane conductance regulator and the etiology and pathogenesis of cystic fibrosis."
McIntosh I., Cutting G.R.
FASEB J. 6:2775-2782(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[15]"Characterization of disease-associated mutations affecting an exonic splicing enhancer and two cryptic splice sites in exon 13 of the cystic fibrosis transmembrane conductance regulator gene."
Aznarez I., Chan E.M., Zielenski J., Blencowe B.J., Tsui L.-C.
Hum. Mol. Genet. 12:2031-2040(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 3).
[16]"Phosphorylation of protein kinase C sites in NBD1 and the R domain control CFTR channel activation by PKA."
Chappe V., Hinkson D.A., Zhu T., Chang X.B., Riordan J.R., Hanrahan J.W.
J. Physiol. (Lond.) 548:39-52(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHANNEL GATING REGULATION, PHOSPHORYLATION.
[17]"Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells."
Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S., Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E., Langford G.M., Fukuda M., Stanton B.A.
J. Biol. Chem. 282:23725-23736(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RAB11A AND MYO5B.
[18]"The deubiquitinating enzyme USP10 regulates the post-endocytic sorting of cystic fibrosis transmembrane conductance regulator in airway epithelial cells."
Bomberger J.M., Barnaby R.L., Stanton B.A.
J. Biol. Chem. 284:18778-18789(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, SUBCELLULAR LOCATION.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-291 AND SER-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"CFTR and TMEM16A are separate but functionally related Cl-channels."
Ousingsawat J., Kongsuphol P., Schreiber R., Kunzelmann K.
Cell. Physiol. Biochem. 28:715-724(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ANO1.
[21]"Epithelial sodium channels (ENaC) are uniformly distributed on motile cilia in the oviduct and the respiratory airways."
Enuka Y., Hanukoglu I., Edelheit O., Vaknine H., Hanukoglu A.
Histochem. Cell Biol. 137:339-353(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[22]"The testis anion transporter TAT1 (SLC26A8) physically and functionally interacts with the cystic fibrosis transmembrane conductance regulator channel: a potential role during sperm capacitation."
Rode B., Dirami T., Bakouh N., Rizk-Rabin M., Norez C., Lhuillier P., Lores P., Jollivet M., Melin P., Zvetkova I., Bienvenu T., Becq F., Planelles G., Edelman A., Gacon G., Toure A.
Hum. Mol. Genet. 21:1287-1298(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC26A8.
[23]"Purification of CFTR for mass spectrometry analysis: identification of palmitoylation and other post-translational modifications."
McClure M., Delucas L.J., Wilson L., Ray M., Rowe S.M., Wu X., Dai Q., Hong J.S., Sorscher E.J., Kappes J.C., Barnes S.
Protein Eng. Des. Sel. 25:7-14(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-712; THR-717; SER-737; SER-795; SER-1444 AND SER-1456, UBIQUITINATION AT LYS-688, PALMITOYLATION AT CYS-524 AND CYS-1395, IDENTIFICATION BY MASS SPECTROMETRY.
[24]"RNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)."
El Khouri E., Le Pavec G., Toledano M.B., Delaunay-Moisan A.
J. Biol. Chem. 288:31177-31191(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY RNF185.
[25]"A model for the nucleotide-binding domains of ABC transporters based on the large domain of aspartate aminotransferase."
Hoedemaeker F.J., Davidson A.R., Rose D.R.
Proteins 30:275-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 425-638.
[26]"Structural basis of the Na+/H+ exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator."
Karthikeyan S., Leung T., Ladias J.A.A.
J. Biol. Chem. 276:19683-19686(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1476-1480 IN COMPLEX WITH SLC9A3R1.
[27]"Mutations and sequence variations detected in the cystic fibrosis transmembrane conductance regulator (CFTR) gene: a report from the Cystic Fibrosis Genetic Analysis Consortium."
Tsui L.-C.
Hum. Mutat. 1:197-203(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[28]"A cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator protein."
Cutting G.R., Kasch L.M., Rosenstein B.J., Zielenski J., Tsui L.-C., Antonarakis S.E., Kazazian H.H. Jr.
Nature 346:366-369(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF.
[29]"Identification of mutations in regions corresponding to the two putative nucleotide (ATP)-binding folds of the cystic fibrosis gene."
Kerem B.-S., Zielenski J., Markiewicz D., Bozon D., Gazit E., Yahav J., Kennedy D., Riordan J.R., Collins F.S., Rommens J.M., Tsui L.-C.
Proc. Natl. Acad. Sci. U.S.A. 87:8447-8451(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF.
[30]"Detection of three rare frameshift mutations in the cystic fibrosis gene in an African-American (CF444delA), an Italian (CF2522insC), and a Soviet (CF3821delT)."
White M.B., Krueger L.J., Holsclaw D.S. Jr., Gerrard B.C., Stewart C., Quittell L., Dolganov G., Baranov V., Ivaschenko T., Kapronov N.I., Sebastio G., Castiglione O., Dean M.
Genomics 10:266-269(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF.
[31]"Three novel mutations in the cystic fibrosis gene detected by chemical cleavage: analysis of variant splicing and a nonsense mutation."
Jones C.T., McIntosh I., Keston M., Ferguson A., Brock D.J.H.
Hum. Mol. Genet. 1:11-17(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF PHE-520 AND HIS-1291.
[32]"A new missense mutation (R1283M) in exon 20 of the cystic fibrosis transmembrane conductance regulator gene."
Cheadle J.P., Meredith A.L., Al-Jader L.N.
Hum. Mol. Genet. 1:123-125(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF MET-1283.
[33]"A serine to proline substitution (S1255P) in the second nucleotide binding fold of the cystic fibrosis gene."
Lissens W., Bonduelle M., Malfroot A., Dab I., Liebaers I.
Hum. Mol. Genet. 1:441-442(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF PRO-1255.
[34]"Detection of novel and rare mutations in exon 4 of the cystic fibrosis gene by SSCP."
Shackleton S., Beards F., Harris A.
Hum. Mol. Genet. 1:439-440(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF LYS-92 AND CYS-117.
[35]"Identification of the M1101K mutation in the cystic fibrosis transmembrane conductance regulator (CFTR) gene and complete detection of cystic fibrosis mutations in the Hutterite population."
Zielenski J., Fugiwara T.M., Markiewicz D., Paradis A.J., Anacleto A.I., Richards B., Schwartz R.H., Klinger K.W., Tsui L.-C., Morgan K.
Am. J. Hum. Genet. 52:609-615(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF LYS-1101.
[36]"Identification of eight novel mutations in a collaborative analysis of a part of the second transmembrane domain of the CFTR gene."
Mercier B., Lissens W., Novelli G., Kalaydjieva L., De Arce M., Kapranov N., Klain N.C., Lenoir G., Chauveau P., Lenaerts C., Rault G., Cashman S., Sangiuolo F., Audrezet M.-P., Dallapiccola B., Guillermit H., Bonduelle M., Liebaers I. expand/collapse author list , Quere I., Verlingue C., Ferec C.
Genomics 16:296-297(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF VAL-1052; ARG-1061; LEU-1066; GLN-1070; ARG-1085 AND ARG-1101.
[37]"A new missense mutation (E92K) in the first transmembrane domain of the CFTR gene causes a benign cystic fibrosis phenotype."
Nunes V., Chillon M., Doerk T., Tuemmler B., Casals T., Estivill X.
Hum. Mol. Genet. 2:79-80(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF LYS-92.
[38]"Identification of a new missense mutation (P205S) in the first transmembrane domain of the CFTR gene associated with a mild cystic fibrosis phenotype."
Chillon M., Casals T., Nunes V., Gimenez J., Ruiz E.P., Estivill X.
Hum. Mol. Genet. 2:1741-1742(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF SER-205.
[39]"Screening of 62 mutations in a cohort of cystic fibrosis patients from north eastern Italy: their incidence and clinical features of defined genotypes."
Gasparini P., Marigo C., Bisceglia G., Nicolis E., Zelante L., Bombieri C., Borgo G., Pignatti P.F., Cabrini G.
Hum. Mutat. 2:389-394(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF.
[40]"Identification of eight mutations and three sequence variations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene."
Ghaneb N., Costes B., Girodon E., Martin J., Fanen P., Goossens M.
Genomics 21:434-436(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-31 AND ILE-1220, VARIANTS CF LEU-912; TYR-949; PRO-1065 AND PRO-1071.
[41]"Novel cystic fibrosis mutation associated with mild disease in Cypriot patients."
Boteva K., Papageorgiou E., Georgiou C., Angastiniotis M., Middleton L.T., Constantinou-Deltas C.D.
Hum. Genet. 93:529-532(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF PRO-346.
[42]"Detection of more than 50 different CFTR mutations in a large group of German cystic fibrosis patients."
Doerk T., Mekus F., Schmidt K., Bosshammer J., Fislage R., Heuer T., Dziadek V., Neumann T., Kaelin N., Wulbrand U., Wulf B., von der Hardt H., Maass G., Tuemmler B.
Hum. Genet. 94:533-542(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF TYR-199; SER-619; ARG-1005 AND ARG-1291.
[43]"A new missense mutation G1249E in exon 20 of the cystic fibrosis transmembrane conductance regulator (CFTR) gene."
Greil I., Wagner K., Rosenkranz W.
Hum. Hered. 44:238-240(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF GLU-1249.
[44]"Identification of two new mutations (711 +3A-->G and V1397E) in CF chromosomes of Albanian and Macedonian origin."
Petreska L., Koceva S., Gordova-Muratovska A., Nestorov R., Efremov G.D.
Hum. Mol. Genet. 3:999-1000(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF GLU-1397.
[45]"A novel cystic fibrosis mutation, Y109C, in the first transmembrane domain of CFTR."
Schaedel C., Kristoffersson A.-C., Kornfaelt R., Holmberg L.
Hum. Mol. Genet. 3:1001-1002(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF CYS-109.
[46]"Analysis of the CFTR gene in the Spanish population: SSCP-screening for 60 known mutations and identification of four new mutations (Q30X, A120T, 1812-1 G-->A, and 3667del4)."
Chillon M., Casals T., Gimenez J., Nunes V., Estivill X.
Hum. Mutat. 3:223-230(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF THR-120.
[47]"A missense mutation (F87L) in exon 3 of the cystic fibrosis transmembrane conductance regulator gene."
Bienvenu T., Petitpretz P., Beldjord C., Kaplan J.C.
Hum. Mutat. 3:395-396(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF LEU-87.
[48]"Is congenital bilateral absence of vas deferens a primary form of cystic fibrosis? Analyses of the CFTR gene in 67 patients."
Mercier B., Verlingue C., Lissens W., Silber S.J., Novelli G., Bonduelle M., Audrezet M.-P., Ferec C.
Am. J. Hum. Genet. 56:272-277(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBAVD ARG-149; LYS-193; GLY-258 AND GLY-800.
[49]"Structural analysis of CFTR gene in congenital bilateral absence of vas deferens."
Jezequel P., Dorval I., Fergelot P., Chauvel B., Le Treut A., Le Gall J.-Y., Le Lannou D., Blayau M.
Clin. Chem. 41:833-835(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBAVD.
[50]"Search for mutations in pancreatic sufficient cystic fibrosis Italian patients: detection of 90% of molecular defects and identification of three novel mutations."
Brancolini V., Cremonesi L., Belloni E., Pappalardo E., Bordoni R., Seia M., Russo S., Padoan R., Giunta A., Ferrari M.
Hum. Genet. 96:312-318(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF GLY-57; LYS-193 AND GLY-579.
[51]"Four adult patients with the missense mutation L206W and a mild cystic fibrosis phenotype."
Desgeorges M., Rodier M., Piot M., Demaille J., Claustres M.
Hum. Genet. 96:717-720(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF TRP-206.
[52]"Identification of six mutations (R31L, 441delA, 681delC, 1461ins4, W1089R, E1104X) in the cystic fibrosis transmembrane conductance regulator (CFTR) gene."
Zielenski J., Markiewicz D., Chen H.S., Schappert K.T., Seller A., Durie P., Corey M., Tsui L.-C.
Hum. Mutat. 5:43-47(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF LEU-31 AND ARG-1098.
[53]"Complete screening of mutations in the coding sequence of the CFTR gene in a sample of CF patients from Russia: identification of three novel alleles."
Verlingue C., Kapranov N.I., Mercier B., Ginter E.K., Petrova N.V., Audrezet M.P., Ferec C.
Hum. Mutat. 5:205-209(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF ASN-572.
[54]"Novel missense mutation in the first transmembrane segment of the CFTR gene (Q98R) identified in a male adult."
Romey M.-C., Desgeorges M., Ray P., Godard P., Demaille J., Claustres M.
Hum. Mutat. 6:190-191(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF ARG-98.
[55]"A specific cystic fibrosis mutation (T338I) associated with the phenotype of isolated hypotonic dehydration."
Leoni G.B., Pitzalis S., Podda R., Zanda M., Silvetti M., Caocci L., Cao A., Rosatelli M.C.
J. Pediatr. 127:281-283(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF ILE-338.
[56]"Identification of six novel CFTR mutations in a sample of Italian cystic fibrosis patients."
Ferec C., Novelli G., Verlingue C., Quere I., Dallapiccola B., Audrezet M.P., Mercier B.
Mol. Cell. Probes 9:135-137(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF PHE-42; LEU-117; ARG-139 AND GLU-1006.
[57]"Distribution of CFTR mutations in cystic fibrosis patients of Tunisian origin: identification of two novel mutations."
Messaoud T., Verlingue C., Denamur E., Pascaud O., Quere I., Fattoum S., Elion J., Ferec C.
Eur. J. Hum. Genet. 4:20-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF SER-665.
[58]"Novel missense mutation (G314R) in a cystic fibrosis patient with hepatic failure."
Nasr S.Z., Strong T.V., Mansoura M.K., Dawson D.C., Collins F.S.
Hum. Mutat. 7:151-154(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF ARG-314.
[59]"A novel mutation in exon 12 (Y569C) of the CFTR gene identified in a patient of Croatian origin."
Petreska L., Plaseska D., Koseva S., Stavljenic-Rukavina A., Efremov G.D.
Hum. Mutat. 7:374-375(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF CYS-569.
[60]"Identification of three novel mutations in the cystic fibrosis transmembrane conductance regulator gene in Argentinian CF patients."
Bienvenu T., Chertkoff L., Beldjord C., Segal E., Carniglia L., Barreiro C., Kaplan J.-C.
Hum. Mutat. 7:376-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF ARG-1061.
[61]"Mutation characterization of CFTR gene in 206 Northern Irish CF families: thirty mutations, including two novel, account for approximately 94% of CF chromosomes."
Hughes D.J., Hill A.J.M., Macek M. Jr., Redmond A.O., Nevin N.C., Graham C.A.
Hum. Mutat. 8:340-347(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF LEU-562.
[62]"Identification of two mutations (S50Y and 4173delC) in the CFTR gene from patients with congenital bilateral absence of vas deferens (CBAVD)."
Zielenski J., Patrizio P., Markiewicz D., Asch R.H., Tsui L.-C.
Hum. Mutat. 9:183-184(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CBAVD TYR-50.
[63]"Identification of four novel mutations in the cystic fibrosis transmembrane conductance regulator gene: E664X, 2113delA, 306delTAGA, and delta M1140."
Clavel C., Pennaforte F., Pigeon F., Verlingue C., Birembaut P., Ferec C.
Hum. Mutat. 9:368-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF MET-1140 DEL.
[64]"Novel mutation (A141D) in exon 4 of the CFTR gene identified in an Algerian patient."
Gouya L., Pascaud O., Munck A., Elion J., Denamur E.
Hum. Mutat. 10:86-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF ASP-141.
[65]"Missense mutation R1066C in the second transmembrane domain of CFTR causes a severe cystic fibrosis phenotype: study of 19 heterozygous and 2 homozygous patients."
Casals T., Pacheco P., Barreto C., Gimenez J., Ramos M.D., Pereira S., Pinheiro J.A., Cobos N., Curvelo A., Vazquez C., Rocha H., Seculi J.L., Perez E., Dapena J., Carrilho E., Duarte A., Palacio A.M., Nunes V., Lavinha J., Estivill X.
Hum. Mutat. 10:387-392(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF CYS-1066.
[66]"Cystic fibrosis mutation frequencies in upstate New York."
Shrimpton A.E., Borowitz D., Swender P.
Hum. Mutat. 10:436-442(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF GLU-85; HIS-117; TYR-287; GLU-455; ASP-551; PRO-1070 AND LYS-1303.
[67]"Cystic fibrosis transmembrane-conductance regulator mutations among African Americans."
Friedman K.J., Leigh M.W., Czarnecki P., Feldman G.L.
Am. J. Hum. Genet. 62:195-196(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF PHE-311 DEL.
[68]"Analysis of the CFTR gene in Turkish cystic fibrosis patients: identification of three novel mutations (3172delAC, P1013L and M1028I)."
Onay T., Topaloglu O., Zielenski J., Gokgoz N., Kayserili H., Camcioglu Y., Cokugras H., Akcakaya N., Apak M., Tsui L.-C., Kirdar B.
Hum. Genet. 102:224-230(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF LEU-1013 AND ILE-1028.
[69]"Complete mutational screening of the CFTR gene in 120 patients with pulmonary disease."
Bombieri C., Benetazzo M., Saccomani A., Belpinati F., Gile L.S., Luisetti M., Pignatti P.F.
Hum. Genet. 103:718-722(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF.
[70]"Characterization of 19 disease-associated missense mutations in the regulatory domain of the cystic fibrosis transmembrane conductance regulator."
Vankeerberghen A., Wei L., Jaspers M., Cassiman J.-J., Nilius B., Cuppens H.
Hum. Mol. Genet. 7:1761-1769(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF.
[71]"Detection of five novel mutations of the cystic fibrosis transmembrane regulator (CFTR) gene in Pakistani patients with cystic fibrosis: Y569D, Q98X, 296+12(T>C), 1161delC and 621+2(T>C)."
Malone G., Haworth A., Schwarz M.J., Cuppens H., Super M.
Hum. Mutat. 11:152-157(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF SER-560 AND ASP-569.
[72]"Identification of a novel mutation (S13F) in the CFTR gene in a CF patient of Sardinian origin."
Leoni G.B., Pitzalis S., Tonelli R., Cao A.
Hum. Mutat. 11:337-337(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF PHE-13 AND ILE-338.
[73]"Identification of three novel mutations in the CFTR gene, R117P, deltaD192, and 3121+1G-->A in four French patients."
Feldmann D., Sardet A., Cougoureux E., Plouvier E., Fontaine J.-L., Tournier G., Aymard P.
Hum. Mutat. Suppl. 1:S78-S80(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CF PRO-117 AND ASP-192 DEL.
[74]"Paternal origin of a de novo novel CFTR mutation (L1065R) causing cystic fibrosis."
Casals T., Ramos M.D., Gimenez J., Nadal M., Nunes V., Estivill X.
Hum. Mutat. Suppl. 1:S99-S102(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF ARG-1065.
[75]"A 2-amino acid insertion mutation (1243insACAAAA) in exon 7 of the CFTR gene."
Shackleton S., Harris A.
Hum. Mutat. Suppl. 1:S156-S157(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF ASN-LYS-370 INS.
[76]"A novel missense mutation D513G in exon 10 of the cystic fibrosis transmembrane conductance regulator (CFTR) gene identified in a French CBAVD patient."
Bienvenu T., Bousquet S., Vidaud D., Hubert D., Francoual C., Beldjord C., Kaplan J.-C.
Hum. Mutat. 12:213-214(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CBAVD GLY-513, VARIANT MET-470.
[77]"Genetic findings in congenital bilateral aplasia of vas deferens patients and identification of six novel mutations."
de Meeus A., Guittard C., Desgeorges M., Carles S., Demaille J., Claustres M.
Hum. Mutat. 12:480-480(1998)
Cited for: VARIANTS CBAVD LEU-111; LYS-244; VAL-544 AND VAL-1364.
[78]"Identification of a D579G homozygote cystic fibrosis patient with pancreatic sufficiency and minor lung involvement."
Picci L., Cameran M., Olante P., Zacchello F., Scarpa M.
Hum. Mutat. 13:173-173(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CF GLY-579.
[79]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-470.
+Additional computationally mapped references.

Web resources

CFTR

Cystic fibrosis mutation db

Wikipedia

CFTR entry

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28668 mRNA. Translation: AAA35680.1.
M55131 expand/collapse EMBL AC list , M55106, M55107, M55108, M55110, M55111, M55112, M55113, M55114, M55115, M55116, M55117, M55118, M55119, M55120, M55121, M55122, M55123, M55124, M55125, M55126, M55127, M55128, M55129, M55130 Genomic DNA. Translation: AAC13657.1.
DQ354388 Genomic DNA. Translation: ABC79050.1.
DQ354389 Genomic DNA. Translation: ABC79052.1.
DQ354390 Genomic DNA. Translation: ABC79054.1.
DQ354391 Genomic DNA. Translation: ABC79056.1.
DQ356258 Genomic DNA. Translation: ABC87055.1.
DQ356259 Genomic DNA. Translation: ABC87057.1.
DQ356261 Genomic DNA. Translation: ABC87061.1.
DQ356262 Genomic DNA. Translation: ABC87063.1.
DQ356263 Genomic DNA. Translation: ABC87065.1.
DQ356264 Genomic DNA. Translation: ABC87067.1.
DQ388128 Genomic DNA. Translation: ABD72183.1.
DQ388129 Genomic DNA. Translation: ABD72185.1.
DQ388131 Genomic DNA. Translation: ABD72189.1.
DQ388132 Genomic DNA. Translation: ABD72191.1.
DQ388133 Genomic DNA. Translation: ABD72193.1.
DQ388134 Genomic DNA. Translation: ABD72195.1.
DQ388135 Genomic DNA. Translation: ABD72197.1.
DQ388138 Genomic DNA. Translation: ABD72203.1.
DQ388139 Genomic DNA. Translation: ABD72205.1.
DQ388140 Genomic DNA. Translation: ABD72207.1.
DQ388141 Genomic DNA. Translation: ABD72209.1.
DQ388142 Genomic DNA. Translation: ABD72211.1.
DQ388143 Genomic DNA. Translation: ABD72213.1.
DQ388145 Genomic DNA. Translation: ABD72217.1.
AC000061 Genomic DNA. No translation available.
AC000111 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24353.1.
M65196 Genomic DNA. Translation: AAA51979.1.
M65197 Genomic DNA. Translation: AAA51980.1.
CCDSCCDS5773.1. [P13569-1]
PIRDVHUCF. A39069.
RefSeqNP_000483.3. NM_000492.3. [P13569-1]
UniGeneHs.489786.
Hs.621460.
Hs.661104.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NBDmodel-A425-638[»]
1XMIX-ray2.25A/B/C/D/E389-678[»]
1XMJX-ray2.30A389-677[»]
2BBOX-ray2.55A389-678[»]
2BBSX-ray2.05A/B389-677[»]
2BBTX-ray2.30A/B389-678[»]
2LOBNMR-B1473-1480[»]
2PZEX-ray1.70A/B387-646[»]
2PZFX-ray2.00A/B387-646[»]
2PZGX-ray1.80A/B375-646[»]
3GD7X-ray2.70A/B/C/D1193-1427[»]
3ISWX-ray2.80C5-20[»]
DisProtDP00012.
ProteinModelPortalP13569.
SMRP13569. Positions 87-738, 860-1470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107506. 274 interactions.
DIPDIP-32788N.
IntActP13569. 138 interactions.
MINTMINT-148539.
STRING9606.ENSP00000003084.

Chemistry

BindingDBP13569.
ChEMBLCHEMBL4051.
DrugBankDB00887. Bumetanide.
DB01016. Glibenclamide.
GuidetoPHARMACOLOGY707.

Protein family/group databases

TCDB3.A.1.202.1. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteP13569.

Polymorphism databases

DMDM147744553.

Proteomic databases

PaxDbP13569.
PRIDEP13569.

Protocols and materials databases

DNASU1080.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000003084; ENSP00000003084; ENSG00000001626. [P13569-1]
ENST00000454343; ENSP00000403677; ENSG00000001626. [P13569-2]
GeneID1080.
KEGGhsa:1080.
UCSCuc003vjd.3. human. [P13569-1]

Organism-specific databases

CTD1080.
GeneCardsGC07P117119.
GeneReviewsCFTR.
HGNCHGNC:1884. CFTR.
HPACAB001951.
HPA021939.
MIM219700. phenotype.
277180. phenotype.
602421. gene.
neXtProtNX_P13569.
Orphanet48. Congenital bilateral absence of vas deferens.
586. Cystic fibrosis.
676. Hereditary chronic pancreatitis.
60033. Idiopathic bronchiectasis.
217034. Male infertility with normal virilization due to meiosis defect.
PharmGKBPA109.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1132.
HOVERGENHBG004169.
InParanoidP13569.
KOK05031.
OMATLAMNIM.
OrthoDBEOG7C2R0B.
PhylomeDBP13569.
TreeFamTF105200.

Enzyme and pathway databases

BioCycMetaCyc:HS00075-MONOMER.
BRENDA3.6.3.49. 2681.
ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP13569.
BgeeP13569.
CleanExHS_CFTR.
GenevestigatorP13569.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR005291. cAMP_cl_channel.
IPR025837. CFTR_reg_dom.
IPR009147. CysFib_conduc_TM.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
PF14396. CFTR_R. 1 hit.
[Graphical view]
PRINTSPR01851. CYSFIBREGLTR.
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 2 hits.
TIGRFAMsTIGR01271. CFTR_protein. 1 hit.
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13569.
GenomeRNAi1080.
NextBio4500.
PROP13569.
SOURCESearch...

Entry information

Entry nameCFTR_HUMAN
AccessionPrimary (citable) accession number: P13569
Secondary accession number(s): Q20BG8 expand/collapse secondary AC list , Q20BH2, Q2I0A1, Q2I102
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 195 of the entry and version 3 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 7

Human chromosome 7: entries, gene names and cross-references to MIM