8FZQ

Dehosphorylated, ATP-bound human cystic fibrosis transmembrane conductance regulator (CFTR)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005254	molecular_function	chloride channel activity
A	0005260	molecular_function	intracellularly ATP-gated chloride channel activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005768	cellular_component	endosome
A	0005769	cellular_component	early endosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006695	biological_process	cholesterol biosynthetic process
A	0006811	biological_process	monoatomic ion transport
A	0006821	biological_process	chloride transport
A	0006904	biological_process	vesicle docking involved in exocytosis
A	0009986	cellular_component	cell surface
A	0010008	cellular_component	endosome membrane
A	0015106	molecular_function	bicarbonate transmembrane transporter activity
A	0015108	molecular_function	chloride transmembrane transporter activity
A	0015701	biological_process	bicarbonate transport
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0016853	molecular_function	isomerase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0017081	molecular_function	chloride channel regulator activity
A	0019869	molecular_function	chloride channel inhibitor activity
A	0019899	molecular_function	enzyme binding
A	0030165	molecular_function	PDZ domain binding
A	0030301	biological_process	cholesterol transport
A	0030660	cellular_component	Golgi-associated vesicle membrane
A	0030669	cellular_component	clathrin-coated endocytic vesicle membrane
A	0031901	cellular_component	early endosome membrane
A	0032991	cellular_component	protein-containing complex
A	0034220	biological_process	monoatomic ion transmembrane transport
A	0034707	cellular_component	chloride channel complex
A	0034976	biological_process	response to endoplasmic reticulum stress
A	0035377	biological_process	transepithelial water transport
A	0035774	biological_process	positive regulation of insulin secretion involved in cellular response to glucose stimulus
A	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
A	0043225	molecular_function	ATPase-coupled inorganic anion transmembrane transporter activity
A	0045921	biological_process	positive regulation of exocytosis
A	0048240	biological_process	sperm capacitation
A	0050891	biological_process	multicellular organismal-level water homeostasis
A	0051087	molecular_function	protein-folding chaperone binding
A	0051454	biological_process	intracellular pH elevation
A	0051649	biological_process	establishment of localization in cell
A	0055037	cellular_component	recycling endosome
A	0055038	cellular_component	recycling endosome membrane
A	0055085	biological_process	transmembrane transport
A	0060081	biological_process	membrane hyperpolarization
A	0070175	biological_process	positive regulation of enamel mineralization
A	0071320	biological_process	cellular response to cAMP
A	0097186	biological_process	amelogenesis
A	0106138	molecular_function	Sec61 translocon complex binding
A	0140359	molecular_function	ABC-type transporter activity
A	1902161	biological_process	positive regulation of cyclic nucleotide-gated ion channel activity
A	1902476	biological_process	chloride transmembrane transport
A	1902943	biological_process	positive regulation of voltage-gated chloride channel activity
A	1904322	biological_process	cellular response to forskolin

Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV

Chain	Residue	Details
A	LEU548-VAL562

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	76
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	MET1-PHE77

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	TRANSMEM: Helical; Name=1 => ECO:0000269|Ref.55

Chain	Residue	Details
A	PHE78-GLN98

---

site_id	SWS_FT_FI3
Number of Residues	99
Details	TOPO_DOM: Extracellular => ECO:0000269|Ref.55

Chain	Residue	Details
A	PRO99-TYR122
A	GLU217-SER222
A	LEU320-THR339
A	VAL880-ILE918
A	GLN1012-PRO1013
A	ILE1117-GLY1130

---

site_id	SWS_FT_FI4
Number of Residues	23
Details	TRANSMEM: Helical; Name=2 => ECO:0000269|Ref.55

Chain	Residue	Details
A	LEU123-HIS146

---

site_id	SWS_FT_FI5
Number of Residues	1039
Details	TOPO_DOM: Cytoplasmic => ECO:0000269|Ref.55

Chain	Residue	Details
A	HIS147-LEU195
A	MET244-LYS298
A	GLN359-SER858
A	THR940-THR990
A	GLN1035-THR1095
A	ASP1152-LEU1480

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	TRANSMEM: Helical; Name=3 => ECO:0000269|Ref.55

Chain	Residue	Details
A	ALA196-TRP216

---

site_id	SWS_FT_FI7
Number of Residues	20
Details	TRANSMEM: Helical; Name=4 => ECO:0000269|Ref.55

Chain	Residue	Details
A	ALA223-MET243

---

site_id	SWS_FT_FI8
Number of Residues	20
Details	TRANSMEM: Helical; Name=5 => ECO:0000269|Ref.55

Chain	Residue	Details
A	ALA299-PHE319

---

site_id	SWS_FT_FI9
Number of Residues	18
Details	TRANSMEM: Helical; Name=6 => ECO:0000269|Ref.55

Chain	Residue	Details
A	ILE340-VAL358

---

site_id	SWS_FT_FI10
Number of Residues	20
Details	TRANSMEM: Helical; Name=7 => ECO:0000269|Ref.55

Chain	Residue	Details
A	LEU859-VAL879

---

site_id	SWS_FT_FI11
Number of Residues	20
Details	TRANSMEM: Discontinuously helical; Name=8 => ECO:0000269|Ref.55

Chain	Residue	Details
A	TYR919-HIS939

---

site_id	SWS_FT_FI12
Number of Residues	20
Details	TRANSMEM: Helical; Name=9 => ECO:0000269|Ref.55

Chain	Residue	Details
A	ILE991-LEU1011

---

site_id	SWS_FT_FI13
Number of Residues	20
Details	TRANSMEM: Helical; Name=10 => ECO:0000269|Ref.55

Chain	Residue	Details
A	TYR1014-LEU1034

---

site_id	SWS_FT_FI14
Number of Residues	20
Details	TRANSMEM: Helical; Name=11 => ECO:0000269|Ref.55

Chain	Residue	Details
A	LEU1096-PHE1116

---

site_id	SWS_FT_FI15
Number of Residues	20
Details	TRANSMEM: Helical; Name=12 => ECO:0000269|Ref.55

Chain	Residue	Details
A	ILE1131-ILE1151

---

site_id	SWS_FT_FI16
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15528182, ECO:0000269|PubMed:20150177, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG

Chain	Residue	Details
A	TRP401

---

site_id	SWS_FT_FI17
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:20150177, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG

Chain	Residue	Details
A	SER434

---

site_id	SWS_FT_FI18
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT

Chain	Residue	Details
A	GLY458

---

site_id	SWS_FT_FI19
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS

Chain	Residue	Details
A	GLN493

---

site_id	SWS_FT_FI20
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744|PDB:3GD7

Chain	Residue	Details
A	TYR1219

---

site_id	SWS_FT_FI21
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0007744|PDB:3GD7

Chain	Residue	Details
A	GLY1244

---

site_id	SWS_FT_FI22
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	SER549

---

site_id	SWS_FT_FI23
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:1377674, ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646

Chain	Residue	Details
A	SER660
A	SER700
A	SER737
A	SER795

---

site_id	SWS_FT_FI24
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:25330774

Chain	Residue	Details
A	SER670

---

site_id	SWS_FT_FI25
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:1377674, ECO:0000269|PubMed:22119790

Chain	Residue	Details
A	SER686

---

site_id	SWS_FT_FI26
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646

Chain	Residue	Details
A	SER712

---

site_id	SWS_FT_FI27
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:22119790

Chain	Residue	Details
A	THR717

---

site_id	SWS_FT_FI28
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646

Chain	Residue	Details
A	UNK753

---

site_id	SWS_FT_FI29
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:1377674, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646

Chain	Residue	Details
A	UNK768
A	SER813

---

site_id	SWS_FT_FI30
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:1377674

Chain	Residue	Details
A	SER790

---

site_id	SWS_FT_FI31
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:22119790

Chain	Residue	Details
A	SER1444
A	SER1456

---

site_id	SWS_FT_FI32
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:22119790

Chain	Residue	Details
A	CYS524
A	CYS1395

---

site_id	SWS_FT_FI33
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:7518437, ECO:0000305|PubMed:20008117

Chain	Residue	Details
A	ASN894
A	ASN900

---

site_id	SWS_FT_FI34
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22119790

Chain	Residue	Details
A	LYS688

---