ATPG_DROME - dbPTM
ATPG_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATPG_DROME
UniProt AC O01666
Protein Name ATP synthase subunit gamma, mitochondrial
Gene Name ATPsyngamma {ECO:0000312|FlyBase:FBgn0020235}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 297
Subcellular Localization Mitochondrion. Mitochondrion inner membrane
Peripheral membrane protein.
Protein Description 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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits..
Protein Sequence MMMQRTQLLLPLAMEATMLAQQQRGMATLKMISIRLKSVKNIQKITQSMKMVSAAKYARAERDLKAARPYGIGAQQFFEKTEIQPDEKAEPKKLLIAVTSDRGLCGAVHTGVARLIRGELAQDEANTKVFCVGDKSRAILSRLYGKNILMVANEVGRLPPTFLDASKIANEVLQTGYDYTEGKIVYNRFKSVVSYQCSTLPIFSGSTVEKSEKLAVYDSLDSDVVKSYLEFSLASLIFYTMKEGACSEQSSRMTAMDNASKNAGEMIDKLTLTFNRTRQAVITRELIEIISGAAALT
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
56AcetylationMKMVSAAKYARAERD
HHHHHHHHHHHHHHH
38.8821791702
88AcetylationTEIQPDEKAEPKKLL
CCCCCCCCCCCCEEE
66.4821791702
88UbiquitinationTEIQPDEKAEPKKLL
CCCCCCCCCCCCEEE
66.4831113955
128AcetylationAQDEANTKVFCVGDK
CCCCCCCEEEEECHH
32.8721791702

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ATPG_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATPG_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ATPG_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATPK_DROMECG4692physical
22036573
ACADM_DROMECG12262physical
22036573
CCD1P_DROMECyp12d1-pphysical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATPG_DROME

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Related Literatures of Post-Translational Modification

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