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. 2010 Jun 15;21(12):1945–1954. doi: 10.1091/mbc.E10-02-0116

Table 1.

KATP channel subunits-associated chaperone proteinsa

Accession no. (NCBI) Protein name Sequence coverage (%) Unique spectra Total spectra
fSUR1 only
    Q09427 SUR1 46 143 588
    Q61743 Kir6.2 11 4 4
    Q76G10 Hsp40 26 7 9
    P19378 Hsc70 57 43 72
    P46633 Hsp90α 29 20 26
    P11499 Hsp90β 39 30 43
    O54981 HOP 16 6 6
    Q8K3H8 Calnexin 13 7 10
fSUR1 + Kir6.2
    Q09427 SUR1 48 126 377
    Q61743 Kir6.2 21 10 18
Q76G10 Hsp40 37 9 12
    P19378 Hsc70 61 33 57
    P46633 Hsp90α 26 19 25
    P11499 Hsp90β 34 24 35
    O54981 HOP 7 3 3
    Q8K3H8 Calnexin 13 7 8
HA-Kir6.2 only
    Q09427 SUR1 8 7 9
    Q61743 Kir6.2 30 22 100
    Q76G10 Hsp40 29 6 10
    P19378 Hsc70 57 42 95
    P46633 Hsp90α 17 9 13
    P11499 Hsp90β 23 13 18
    O54981 HOP 0 0 0
    Q8K3H8 Calnexin 0 0 0

a In total, 10 proteomics experiments were performed: three in INS-1 cells infected with fSUR1 virus only, five in INS-1 cells infected with fSUR1 and Kir6.2 viruses, and two in INS-1 cells infected with HA-Kir6.2 virus only. The fSUR1 or HA-Kir6.2 protein complexes in INS-1 cell lysates were affinity purified using FLAG- or HA-antibody–conjugated agarose beads and subjected to mass spectrometry analyses as described in Materials and Methods. Results from three proteomic experiments representing each condition are shown. Note Hsp40, Hsc70, and Hsp90α and -β are present in all experiments. The protein HOP is found in only a subset of experiments overexpressing fSUR1 alone or fSUR1 plus Kir6.2 (6 of 8 experiments), so is the protein calnexin (5 of 8 experiments); neither proteins showed up in cells overexpressing HA-Kir6.2 only. NCBI, National Center for Biotechnology Information.