General Information of Target

Target ID LDTP05474
Target Name ATP synthase F(0) complex subunit C2, mitochondrial (ATP5MC2)
Gene Name ATP5MC2
Gene ID 517
Synonyms
ATP5G2; ATP synthase F(0) complex subunit C2, mitochondrial; ATP synthase lipid-binding protein; ATP synthase membrane subunit c locus 2; ATP synthase proteolipid P2; ATP synthase proton-transporting mitochondrial F(0) complex subunit C2; ATPase protein 9; ATPase subunit c
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MFACSKFVSTPSLVKSTSQLLSRPLSAVVLKRPEILTDESLSSLAVSCPLTSLVSSRSFQ
TSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGF
ALSEAMGLFCLMVAFLILFAM
Target Bioclass
Transporter and channel
Family
ATPase C chain family
Subcellular location
Mitochondrion membrane
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Uniprot ID
Q06055
Ensemble ID
ENST00000338662.6
HGNC ID
HGNC:842

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
IGROV1 SNV: p.E39D .
Ishikawa (Heraklio) 02 ER SNV: p.E39D .

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 1 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
DBIA
 Probe Info 
C48(1.05)  LDD1513  [1]
PAL-AfBPP Probe
Click To Hide/Show 2 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
C112
 Probe Info 
28.25  LDD1799  [2]
C278
 Probe Info 
56.49  LDD1948  [2]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0270  AC15 HEK-293T C48(1.05)  LDD1513  [1]
 LDCM0283  AC23 HEK-293T C48(1.06)  LDD1522  [1]
 LDCM0284  AC24 HEK-293T C48(1.07)  LDD1523  [1]
 LDCM0292  AC31 HEK-293T C48(1.28)  LDD1531  [1]
 LDCM0293  AC32 HEK-293T C48(0.91)  LDD1532  [1]
 LDCM0300  AC39 HEK-293T C48(1.04)  LDD1539  [1]
 LDCM0302  AC40 HEK-293T C48(0.97)  LDD1541  [1]
 LDCM0309  AC47 HEK-293T C48(0.91)  LDD1548  [1]
 LDCM0310  AC48 HEK-293T C48(1.05)  LDD1549  [1]
 LDCM0318  AC55 HEK-293T C48(0.99)  LDD1557  [1]
 LDCM0319  AC56 HEK-293T C48(1.07)  LDD1558  [1]
 LDCM0327  AC63 HEK-293T C48(1.21)  LDD1566  [1]
 LDCM0328  AC64 HEK-293T C48(1.02)  LDD1567  [1]
 LDCM0334  AC7 HEK-293T C48(1.12)  LDD1568  [1]
 LDCM0345  AC8 HEK-293T C48(1.09)  LDD1569  [1]
 LDCM0275  AKOS034007705 HEK-293T C48(0.97)  LDD1514  [1]
 LDCM0379  CL11 HEK-293T C48(1.23)  LDD1583  [1]
 LDCM0390  CL12 HEK-293T C48(1.15)  LDD1594  [1]
 LDCM0411  CL23 HEK-293T C48(1.32)  LDD1615  [1]
 LDCM0412  CL24 HEK-293T C48(1.03)  LDD1616  [1]
 LDCM0424  CL35 HEK-293T C48(1.15)  LDD1628  [1]
 LDCM0425  CL36 HEK-293T C48(1.07)  LDD1629  [1]
 LDCM0437  CL47 HEK-293T C48(1.23)  LDD1641  [1]
 LDCM0438  CL48 HEK-293T C48(1.20)  LDD1642  [1]
 LDCM0450  CL59 HEK-293T C48(1.35)  LDD1653  [1]
 LDCM0452  CL60 HEK-293T C48(1.25)  LDD1655  [1]
 LDCM0464  CL71 HEK-293T C48(1.46)  LDD1667  [1]
 LDCM0465  CL72 HEK-293T C48(1.16)  LDD1668  [1]
 LDCM0477  CL83 HEK-293T C48(1.15)  LDD1680  [1]
 LDCM0478  CL84 HEK-293T C48(1.21)  LDD1681  [1]
 LDCM0490  CL95 HEK-293T C48(1.11)  LDD1693  [1]
 LDCM0491  CL96 HEK-293T C48(1.26)  LDD1694  [1]

References

1 Accelerating multiplexed profiling of protein-ligand interactions: High-throughput plate-based reactive cysteine profiling with minimal input. Cell Chem Biol. 2024 Mar 21;31(3):565-576.e4. doi: 10.1016/j.chembiol.2023.11.015. Epub 2023 Dec 19.
Mass spectrometry data entry: PXD044402
2 Large-scale chemoproteomics expedites ligand discovery and predicts ligand behavior in cells. Science. 2024 Apr 26;384(6694):eadk5864. doi: 10.1126/science.adk5864. Epub 2024 Apr 26.
Mass spectrometry data entry: PXD041587