Table 1 Proteomic analysis of GFP-RCP immunoprecipitates.

From: Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion

Protein

Accession number

IP:GFP

IP:GFP-RCP

  

Number of peptides (unique)

Percentage covered (%)

Number of peptides (unique)

Percentage covered (%)

Ubiquitin

P62988

4 (3)

50

Rab11B

Q15907

53 (8)

40

Heat shock cognate 71 kDa

P11142

1 (1)

3

43 (16)

32

Rab6A

P20340

18 (5)

25

α-actinin 4

O43707

32 (16)

23

Rab11-FIP1 (RCP)

Q6WKZ4

60 (17)

16

Clathrin heavy chain 1

Q00610

27 (15)

13

Rab11-FIP5

Q9BXF6

11 (5)

13

Rab14

P61106

6 (2)

13

5'-nucleotidase

P21589

1 (1)

2

9 (5)

13

Myoferlin

Q9NZM1

34 (20)

12

Aminopeptidase N

P15144

21 (9)

12

Ephrin type-A receptor 2 (EphA2)

P29317

18 (9)

12

Peroxisomal multifunctional enzyme type 2

P51659

11 (5)

10

Desmoglein 2

Q14126

8 (6)

10

Myeloid-associated differentiation marker

Q96S97

8 (2)

10

Heat shock 70 kDa protein 1

P08107

3 (3)

10

β1 integrin

P05556

1 (1)

1

17 (5)

9

EGFR

P00533

17 (7)

8

Neurabin 2

Q96SB3

7 (6)

8

4F2 cell-surface antigen heavy chain

P08195

3 (3)

8

  1. Immunoprecipitates generated in Fig. 1a were analysed by MALDI-TOF mass spectrometry. Proteins that were significantly more abundant in GFP-RCP (IP:GFP-RCP) than GFP (IP:GFP) immunoprecipitates are listed. The number of peptides identified by mass spectrometry and the percentage of these proteins covered by the identified peptides are indicated.