UniProt ID | ATP5H_RAT | |
---|---|---|
UniProt AC | P31399 | |
Protein Name | ATP synthase subunit d, mitochondrial | |
Gene Name | Atp5h | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 161 | |
Subcellular Localization | Mitochondrion. Mitochondrion inner membrane. | |
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(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.. | |
Protein Sequence | MAGRKLALKTIDWVSFVEIMPQNQKAIGNALKSWNETFHTRLASLSEKPPAIDWAYYRANVDKPGLVDDFKNKYNALKIPVPEDKYTALVDAEEKEDVKNCAQFVTGSQARVREYEKQLEKIKNMIPFDQMTIDDLNEVFPETKLDKRKYPYWPHQPIENL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAGRKLALK ------CCCCHHHHH | 26.88 | - | |
10 | Phosphorylation | GRKLALKTIDWVSFV CCHHHHHHCCEEEEE | 25.64 | 23991683 | |
15 | Phosphorylation | LKTIDWVSFVEIMPQ HHHCCEEEEEEECCC | 21.22 | 23991683 | |
32 | Acetylation | KAIGNALKSWNETFH HHHHHHHHHHHHHHH | 51.52 | 22902405 | |
33 | Phosphorylation | AIGNALKSWNETFHT HHHHHHHHHHHHHHH | 35.66 | 23991683 | |
44 | Phosphorylation | TFHTRLASLSEKPPA HHHHHHHHHCCCCCC | 36.70 | 23991683 | |
44 | O-linked_Glycosylation | TFHTRLASLSEKPPA HHHHHHHHHCCCCCC | 36.70 | 26446791 | |
46 | Phosphorylation | HTRLASLSEKPPAID HHHHHHHCCCCCCCC | 40.87 | 23991683 | |
48 | Acetylation | RLASLSEKPPAIDWA HHHHHCCCCCCCCEE | 53.58 | 22902405 | |
63 | Succinylation | YYRANVDKPGLVDDF EHHCCCCCCCCHHHH | 36.38 | 26843850 | |
63 | Acetylation | YYRANVDKPGLVDDF EHHCCCCCCCCHHHH | 36.38 | 22902405 | |
71 | Succinylation | PGLVDDFKNKYNALK CCCHHHHHHHCCCCC | 60.57 | 26843850 | |
71 | Acetylation | PGLVDDFKNKYNALK CCCHHHHHHHCCCCC | 60.57 | 22902405 | |
73 | Succinylation | LVDDFKNKYNALKIP CHHHHHHHCCCCCCC | 40.24 | 26843850 | |
73 | Acetylation | LVDDFKNKYNALKIP CHHHHHHHCCCCCCC | 40.24 | 22902405 | |
78 | Succinylation | KNKYNALKIPVPEDK HHHCCCCCCCCCCCC | 42.42 | - | |
78 | Acetylation | KNKYNALKIPVPEDK HHHCCCCCCCCCCCC | 42.42 | 22902405 | |
85 | Succinylation | KIPVPEDKYTALVDA CCCCCCCCCEEEECH | 42.72 | - | |
85 | Acetylation | KIPVPEDKYTALVDA CCCCCCCCCEEEECH | 42.72 | 22902405 | |
95 | Acetylation | ALVDAEEKEDVKNCA EEECHHHHHHHHHHH | 51.20 | 22902405 | |
95 | Succinylation | ALVDAEEKEDVKNCA EEECHHHHHHHHHHH | 51.20 | 26843850 | |
99 | Acetylation | AEEKEDVKNCAQFVT HHHHHHHHHHHHHHH | 59.64 | 22902405 | |
106 | Phosphorylation | KNCAQFVTGSQARVR HHHHHHHHHHHHHHH | 32.19 | 27097102 | |
108 | Phosphorylation | CAQFVTGSQARVREY HHHHHHHHHHHHHHH | 15.99 | 27097102 | |
117 | Acetylation | ARVREYEKQLEKIKN HHHHHHHHHHHHHHH | 60.32 | 25786129 | |
117 | Succinylation | ARVREYEKQLEKIKN HHHHHHHHHHHHHHH | 60.32 | 26843850 | |
121 | Acetylation | EYEKQLEKIKNMIPF HHHHHHHHHHHCCCC | 68.52 | 26302492 | |
123 | Acetylation | EKQLEKIKNMIPFDQ HHHHHHHHHCCCCCC | 52.08 | 22902405 | |
144 | Succinylation | NEVFPETKLDKRKYP HHHCCCCCCCCCCCC | 53.69 | - | |
144 | Acetylation | NEVFPETKLDKRKYP HHHCCCCCCCCCCCC | 53.69 | 22902405 | |
147 | Acetylation | FPETKLDKRKYPYWP CCCCCCCCCCCCCCC | 62.31 | 26302492 | |
149 | Acetylation | ETKLDKRKYPYWPHQ CCCCCCCCCCCCCCC | 57.21 | 22902405 | |
149 | Succinylation | ETKLDKRKYPYWPHQ CCCCCCCCCCCCCCC | 57.21 | 26843850 | |
152 | Phosphorylation | LDKRKYPYWPHQPIE CCCCCCCCCCCCCCC | 28.60 | - |
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 ATP5H_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATP5H_RAT !! |
* 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 ATP5H_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ATP5H_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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