Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  ATP synthase subunit f, mitochondrial  

UniProtKB / Swiss-Prot ID :  ATPK_MOUSE

Gene Name (Synonyms) : 
Atp5j2  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Mitochondrion. Mitochondrion inner membrane; Single-pass membrane protein (Potential). 

Protein 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. Minor subunit located with subunit a in the membrane. 

Transmembrane Topology (topPTM) : ATPK_MOUSE 

Protein Sequence MASLVPLKEKKLMEVKLGELPSWIMMRDFTPSGIAGAFRRGYDRYYNKYINVRKGSISGISMVLAAYVVF...
Predicted Secondary Structure CCCCCCCCCCEEEEEEECCHHHHHHHHCCCCCHHHHHHHHHHHHHHHEEEEEEECCCHHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
16N6-acetyllysineLMEVKLGEL
EEEEEECCH
37.15Phosphositeplus
Link-
30PhosphothreonineMRDFTPSGI
HHCCCCCHH
22.34Phosphositeplus
Link-
32PhosphoserineDFTPSGIAG
CCCCCHHHH
39.51Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures