ABCMdb

ABCC7 p.Arg1403Ala

None has been submitted yet.

Publications

PMID: 11022033 [PubMed] Gentzsch M et al: "Localization of sequences within the C-terminal domain of the cystic fibrosis transmembrane conductance regulator which impact maturation and stability."

No. Sentence Comment

40 F1413A/ L1414A/V1415A/I1416A/E1417A, 5Ј-GCTGGAATGCCAACAAGCTGC- GGCCGCAGCAGAGAACAAAGTGCGG-3Ј and 5Ј-CCGCACTTTGTTC- TCTGCTGCGGCCGCAGCTTGTTGGCATTCCAGC-3Ј; F1413A- /L1414A/V1415A/I1416A, 5Ј-GCTGGAATGCCAACAAGCTGCGGCCG- CAGAAGAGAACAAAGTGCGG-3Ј and 5Ј-CCGCACTTTGTTCTCTTC- TGCGGCCGCAGCTTGTTGGCATTCCAGC-3Ј; Q1411A/Q1412A, 5Ј-G- GATAGAAGCAATGCTGGAATGCGCAGCATTTTTGGTCATAGAAG-3 and 5Ј-CTTCTATGACCAAAAATGCTGCGCATTCCAGCATTGCTTCT- ATCC-3; F1413A/L1414A, 5Ј-GCTGGAATGCCAACAAGCTGCGGTCA- TAGAAGAGAACAAAGTGCG-3Ј and 5Ј-CGCACTTTGTTCTCTTCTA- TGACCGCAGCTTGTTGGCATTCCAGC-3Ј; L1414A/V1415A, 5Ј-GCT- GGAATGCCAACAATTTGCGGCCATAGAAGAGAACAAAGTGCGG-3Ј and 5Ј-CCGCACTTTGTTCTCTTCTATGGCCGCAAATTGTTGGCATT- CCAGC-3Ј; V1415A/I1416A, 5Ј-GGAATGCCAACAATTTTTGGCCGCA- GAAGAGAACAAAGTGCGGCAG-3Ј and 5Ј-CTGCCGCACTTTGTTCT- CTTCTGCGGCCAAAAATTGTTGGCATTCC-3Ј; E1417A/E1418A, 5Ј- GCCAACAATTTTTGGTCATAGCAGCGAACAAAGTGCGGCAGTAC- G-3Ј and 5Ј-CGTACTGCCGCACTTTGTTCGCTGCTATGACCAAAAA- TTGTTGGC-3Ј; F1413A, 5Ј-GCAATGCTGGAATGCCAACAAGCTTTG- GTCATAGAAGAGAAC-3Ј and 5Ј-GTTCTCTTCTATGACCAAAGCTT- GTTGGCATTCCAGCATTGC-3Ј; L1414A, 5Ј-GCTGGAATGCCAACAA- TTTGCGGTCATAGAAGAGAACAAAGTGCG-3Ј and 5Ј-CGCACTTTG- TTCTCTTCTATGACCGCAAATTGTTGGCATTCCAGC-3Ј; V1415A, 5Ј- GGAATGCCAACAATTTTTGGCCATAGAAGAGAACAAAGTGCGGC- AG-3Ј and 5Ј-CTGCCGCACTTTGTTCTCTTCTATGGCCAAAAATTGT- TGGCATTCC-3Ј; I1416A, 5Ј-GGAATGCCAACAATTTTTGGTCGCAG- AAGAGAACAAAGTGCGGCAG-3Ј and 5Ј-CTGCCGCACTTTGTTCTC- TTCTGCGACCAAAAATTGTTGGCATTCC-3Ј; E1417A, 5Ј-GCCAACA- ATTTTTGGTCATAGCAGAGAACAAAGTGCGGCAGTACG-3Ј and 5Ј- CGTACTGCCGCACTTTGTTCTCTGCTATGACCAAAAATTGTTGGC- 3Ј; C1400A/E1401A/H1402A/R1403A/I1404A, 5Ј-GCACAGTAATTCTC- GCTGCAGCCGCGGCAGAAGCAATGCTGGAATGCC-3Ј and 5Ј-GGC- ATTCCAGCATTGCTTCTGCCGCGGCTGCAGCGAGAATTACTGTG- C-3Ј; ⌬1400-1404: 5Ј-GCATTTGCTGATTGCACAGTAATTCTCGAAG- CAATGCTGGAATGCC-3Ј and 5Ј-GGCATTCCAGCATTGCTTCGAGA- ATTACTGTGCAATCAGCAAATGC-3Ј; C1400A/E1401A, 5Ј-GATTGC- ACAGTAATTCTCGCTGCACACAGGATAGAAGCAATGC-3Ј and 5Ј-G- CATTGCTTCTATCCTGTGTGCAGCGAGAATTACTGTGCAATC-3Ј; H1402A/R1403A, 5Ј-CAGTAATTCTCTGTGAAGCCGCGATAGAAGC- AATGCTGGAATGCC-3Ј and 5Ј-GGCATTCCAGCATTGCTTCTATCG- CGGCTTCACAGAGAATTAC TG-3Ј; I1404A/E1405A, 5Ј-CTCTGTGA- ACACAGGGCAGCAGCAATGCTGGAATGCCAAC-3Ј and 5Ј-GTTGGC- ATTCCAGCATTGCTGCTGCCCTGTGTTCACAGAG-3Ј, Q1390A/A- 1391A/F1392A/A1393A/D1394A, 5Ј-GAAGAACTCTAAAAGCAGCAG- CTGCTGCTTGCACAGTAATTCTC-3Ј and 5Ј-GAGAATTACTGTGCA- AGCAGCAGCTGCTGCTTTTAGAGTTCTTC-3Ј. Login to comment

PMID: 12084728 [PubMed] Milewski MI et al: "Aggregation of misfolded proteins can be a selective process dependent upon peptide composition."

No. Sentence Comment

90 Only 25% (52/208) of cells expressing GFP fusion protein bearing single H1402A substitution and 27% (41/153) of R1403A mutants showed intracellular protein accumulation, whereas the corresponding number for the wild type sequence was 91% (132/145). Login to comment
93 Cells expressing the double mutant H1402A,R1403A showed no aggregation at all (0/108). Login to comment
97 However, the introduction of the ⌬ag deletion or the H1402A,R1403A double mutation significantly decreased the amount of the fusion protein in the insoluble fraction to approximately 31 and 36%, respectively. Login to comment
108 B-E, the effect of different mutations within the ag region, including ⌬ag (B), V1397E (C), T1396A (D), and double mutation H1402A,R1403A (E) on the aggregation of C terminus of CFTR fused to GFP (shown in green) in transiently transfected human airway epithelial (IB3-1) cells. Login to comment
120 Additionally, the double mutation H1402A,R1403A prevented aggregation of HA-tagged CFTR C terminus (Fig. 2E). Login to comment
146 E, lack of aggregation of HA-CFTR 1370-1480 construct carrying the H1402A and R1403A mutations. Login to comment
160 Similarly, the non-aggregating GFP-CFTR 1370-1480 H1402A,R1403A construct was included in giant aggregates formed by HA-CFTR 1370-1480 (Fig. 4D). Login to comment
195 C, colocalization of the aggregating GFP-CFTR 1370-1480 construct (green) and the non-aggregating HA-CFTR 1370-1480 H1402A,R1403A construct (red) in giant aggregates. Login to comment
196 D, co-localization of the non-aggregating GFP-CFTR 1370-1480 H1402A,R1403A construct (green) with the aggregating HA-CFTR 1370-1480 construct (red) in giant aggregates. Login to comment

PMID: 20110677 [PubMed] Kloch M et al: "The H-loop in the second nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator is required for efficient chloride channel closing."

No. Sentence Comment

30 Mutations within the H-loop of NBD2, including the deletion of the entire ag region (Δ1395-1403) and the double alanine substitution H1402A, R1403A (HR→AA), were created in the CFTR-containing pBQ4.7 vector (a gift from J. Rommens and L.-C. Tsui) using the site-directed mutagenesis system "Transformer" (Becton Dickinson). Login to comment

PMID: 15642363 [PubMed] Milewski MI et al: "PDZ-binding motifs are unable to ensure correct polarized protein distribution in the absence of additional localization signals."

No. Sentence Comment

25 Also, the introduction of the H1402A and R1403A mutations, reducing the aggregation rate of the CFTR C-terminus, was previously described [9]. Login to comment
64 A diagram illustrating the structure and subcellular localization of the GFP fusion proteins containing either the full-length CFTR protein or its C-terminal fragment (a.a. 1370-1480) with two alanine substitutions (H1402A and R1403A), eliminating the aggregation of the CFTR C-terminus. Login to comment
93 (B) Apical localization of the GFP-CFTR 1370-1480 H1402A, R1403A fusion protein containing the C-terminal M-K-D-T-R-L> motif. Login to comment
94 (C) Predominant cytoplasmic distribution of the GFP-CFTR 1370-1480 H1402A, R1403A fusion protein containing the extended Q-K-E-TC-L> PDZ-binding motif of LET23. Login to comment