UniProt ID | AT5F1_HUMAN | |
---|---|---|
UniProt AC | P24539 | |
Protein Name | ATP synthase F(0) complex subunit B1, mitochondrial | |
Gene Name | ATP5F1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 256 | |
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 | MLSRVVLSAAATAAPSLKNAAFLGPGVLQATRTFHTGQPHLVPVPPLPEYGGKVRYGLIPEEFFQFLYPKTGVTGPYVLGTGLILYALSKEIYVISAETFTALSVLGVMVYGIKKYGPFVADFADKLNEQKLAQLEEAKQASIQHIQNAIDTEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLYRVYKEVKNRLDYHISVQNMMRRKEQEHMINWVEKHVVQSISTQQEKETIAKCIADLKLLAKKAQAQPVM | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
18 | Ubiquitination | ATAAPSLKNAAFLGP HHHCHHCCCHHHCCC | 49.21 | - | |
31 | Phosphorylation | GPGVLQATRTFHTGQ CCCCHHHHEEEECCC | 19.79 | - | |
53 | Acetylation | PLPEYGGKVRYGLIP CCCCCCCEEECEECC | 21.12 | 30584097 | |
53 | Ubiquitination | PLPEYGGKVRYGLIP CCCCCCCEEECEECC | 21.12 | - | |
71 | Phosphorylation | FQFLYPKTGVTGPYV HHHHCCCCCCCCCCH | 32.17 | 25219547 | |
74 | Phosphorylation | LYPKTGVTGPYVLGT HCCCCCCCCCCHHHH | 33.51 | 25219547 | |
77 | Phosphorylation | KTGVTGPYVLGTGLI CCCCCCCCHHHHHHH | 15.06 | 25219547 | |
81 | Phosphorylation | TGPYVLGTGLILYAL CCCCHHHHHHHHHHH | 25.34 | 25219547 | |
86 | Phosphorylation | LGTGLILYALSKEIY HHHHHHHHHHCCCEE | 9.86 | 25219547 | |
89 | Phosphorylation | GLILYALSKEIYVIS HHHHHHHCCCEEEEE | 21.77 | 25219547 | |
115 | Acetylation | VMVYGIKKYGPFVAD HHHHHHHHHCCHHHH | 54.22 | 25038526 | |
116 | Phosphorylation | MVYGIKKYGPFVADF HHHHHHHHCCHHHHH | 25.65 | 21406692 | |
126 | Acetylation | FVADFADKLNEQKLA HHHHHHHHHCHHHHH | 50.19 | 25038526 | |
126 | Ubiquitination | FVADFADKLNEQKLA HHHHHHHHHCHHHHH | 50.19 | 21906983 | |
131 | Ubiquitination | ADKLNEQKLAQLEEA HHHHCHHHHHHHHHH | 39.34 | - | |
131 | Succinylation | ADKLNEQKLAQLEEA HHHHCHHHHHHHHHH | 39.34 | 23954790 | |
131 | 2-Hydroxyisobutyrylation | ADKLNEQKLAQLEEA HHHHCHHHHHHHHHH | 39.34 | - | |
131 | Acetylation | ADKLNEQKLAQLEEA HHHHCHHHHHHHHHH | 39.34 | 23236377 | |
131 | Succinylation | ADKLNEQKLAQLEEA HHHHCHHHHHHHHHH | 39.34 | - | |
139 | Acetylation | LAQLEEAKQASIQHI HHHHHHHHHHHHHHH | 50.07 | 27452117 | |
139 | Ubiquitination | LAQLEEAKQASIQHI HHHHHHHHHHHHHHH | 50.07 | 21906983 | |
142 | Phosphorylation | LEEAKQASIQHIQNA HHHHHHHHHHHHHHH | 21.93 | 20860994 | |
152 | Phosphorylation | HIQNAIDTEKSQQAL HHHHHHCCHHHHHHH | 38.92 | 21406692 | |
154 | Acetylation | QNAIDTEKSQQALVQ HHHHCCHHHHHHHHH | 56.51 | 23954790 | |
154 | 2-Hydroxyisobutyrylation | QNAIDTEKSQQALVQ HHHHCCHHHHHHHHH | 56.51 | - | |
154 | Ubiquitination | QNAIDTEKSQQALVQ HHHHCCHHHHHHHHH | 56.51 | 21906983 | |
154 | Malonylation | QNAIDTEKSQQALVQ HHHHCCHHHHHHHHH | 56.51 | 26320211 | |
155 | Phosphorylation | NAIDTEKSQQALVQK HHHCCHHHHHHHHHH | 22.69 | 26437602 | |
162 | 2-Hydroxyisobutyrylation | SQQALVQKRHYLFDV HHHHHHHHHHHHHHH | 33.39 | - | |
162 | Acetylation | SQQALVQKRHYLFDV HHHHHHHHHHHHHHH | 33.39 | 23236377 | |
162 | Ubiquitination | SQQALVQKRHYLFDV HHHHHHHHHHHHHHH | 33.39 | 21906983 | |
165 | Phosphorylation | ALVQKRHYLFDVQRN HHHHHHHHHHHHHHC | 17.07 | 28152594 | |
187 | Phosphorylation | VTYRERLYRVYKEVK HHHHHHHHHHHHHHH | 12.31 | 29496907 | |
190 | Phosphorylation | RERLYRVYKEVKNRL HHHHHHHHHHHHHHH | 7.76 | 29496907 | |
199 | Phosphorylation | EVKNRLDYHISVQNM HHHHHHHHHHHHHHH | 12.97 | 23403867 | |
206 | Sulfoxidation | YHISVQNMMRRKEQE HHHHHHHHHHHHHHH | 0.93 | 28183972 | |
207 | Sulfoxidation | HISVQNMMRRKEQEH HHHHHHHHHHHHHHH | 5.00 | 28183972 | |
210 | 2-Hydroxyisobutyrylation | VQNMMRRKEQEHMIN HHHHHHHHHHHHHHH | 54.08 | - | |
210 | Ubiquitination | VQNMMRRKEQEHMIN HHHHHHHHHHHHHHH | 54.08 | - | |
221 | Ubiquitination | HMINWVEKHVVQSIS HHHHHHHHHHHHHCC | 31.89 | 19608861 | |
221 | Acetylation | HMINWVEKHVVQSIS HHHHHHHHHHHHHCC | 31.89 | 19608861 | |
226 | Phosphorylation | VEKHVVQSISTQQEK HHHHHHHHCCCHHHH | 13.59 | 25159151 | |
228 | Phosphorylation | KHVVQSISTQQEKET HHHHHHCCCHHHHHH | 25.97 | 25159151 | |
229 | Phosphorylation | HVVQSISTQQEKETI HHHHHCCCHHHHHHH | 32.38 | 25159151 | |
233 | Ubiquitination | SISTQQEKETIAKCI HCCCHHHHHHHHHHH | 56.68 | 19608861 | |
233 | Malonylation | SISTQQEKETIAKCI HCCCHHHHHHHHHHH | 56.68 | 26320211 | |
233 | Acetylation | SISTQQEKETIAKCI HCCCHHHHHHHHHHH | 56.68 | 19608861 | |
235 | Phosphorylation | STQQEKETIAKCIAD CCHHHHHHHHHHHHH | 36.98 | 24641631 | |
238 | Ubiquitination | QEKETIAKCIADLKL HHHHHHHHHHHHHHH | 23.48 | 19608861 | |
238 | Acetylation | QEKETIAKCIADLKL HHHHHHHHHHHHHHH | 23.48 | 25825284 | |
244 | Ubiquitination | AKCIADLKLLAKKAQ HHHHHHHHHHHHHHH | 41.84 | - | |
244 | Acetylation | AKCIADLKLLAKKAQ HHHHHHHHHHHHHHH | 41.84 | 25953088 | |
244 | Succinylation | AKCIADLKLLAKKAQ HHHHHHHHHHHHHHH | 41.84 | 23954790 | |
248 | Acetylation | ADLKLLAKKAQAQPV HHHHHHHHHHHCCCC | 48.92 | 6567955 |
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 AT5F1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AT5F1_HUMAN !! |
* 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 AT5F1_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-233, AND MASSSPECTROMETRY. |