UniProt ID | KAD3_HUMAN | |
---|---|---|
UniProt AC | Q9UIJ7 | |
Protein Name | GTP:AMP phosphotransferase AK3, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03169} | |
Gene Name | AK3 {ECO:0000255|HAMAP-Rule:MF_03169} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 227 | |
Subcellular Localization | Mitochondrion matrix . | |
Protein Description | Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.. | |
Protein Sequence | MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFIDQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVIKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQTKPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP | |
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 |
---|---|---|---|---|---|
4 | Phosphorylation | ----MGASARLLRAV ----CCHHHHHHHHH | 14.27 | 24719451 | |
18 | Phosphorylation | VIMGAPGSGKGTVSS HHHCCCCCCCCCCCC | 35.95 | 28857561 | |
20 | Succinylation | MGAPGSGKGTVSSRI HCCCCCCCCCCCCCE | 53.78 | 23954790 | |
20 | Succinylation | MGAPGSGKGTVSSRI HCCCCCCCCCCCCCE | 53.78 | - | |
20 | Acetylation | MGAPGSGKGTVSSRI HCCCCCCCCCCCCCE | 53.78 | 2402139 | |
20 | Malonylation | MGAPGSGKGTVSSRI HCCCCCCCCCCCCCE | 53.78 | 26320211 | |
22 | Phosphorylation | APGSGKGTVSSRITT CCCCCCCCCCCCEEC | 22.24 | 28857561 | |
24 | Phosphorylation | GSGKGTVSSRITTHF CCCCCCCCCCEECCE | 17.46 | 28857561 | |
25 | Phosphorylation | SGKGTVSSRITTHFE CCCCCCCCCEECCEE | 24.30 | 24719451 | |
34 | Acetylation | ITTHFELKHLSSGDL EECCEEEECCCCCCH | 34.99 | 25825284 | |
34 | Malonylation | ITTHFELKHLSSGDL EECCEEEECCCCCCH | 34.99 | 26320211 | |
37 | Phosphorylation | HFELKHLSSGDLLRD CEEEECCCCCCHHHH | 31.81 | 28450419 | |
38 | Phosphorylation | FELKHLSSGDLLRDN EEEECCCCCCHHHHC | 42.56 | 30108239 | |
48 | Methylation | LLRDNMLRGTEIGVL HHHHCCCCCCHHHHH | 38.94 | - | |
57 | Acetylation | TEIGVLAKAFIDQGK CHHHHHHHHHHHCCC | 39.40 | 25953088 | |
57 | Succinylation | TEIGVLAKAFIDQGK CHHHHHHHHHHHCCC | 39.40 | - | |
57 | Succinylation | TEIGVLAKAFIDQGK CHHHHHHHHHHHCCC | 39.40 | - | |
64 | Malonylation | KAFIDQGKLIPDDVM HHHHHCCCCCCHHHH | 37.30 | 26320211 | |
64 | Succinylation | KAFIDQGKLIPDDVM HHHHHCCCCCCHHHH | 37.30 | - | |
64 | Acetylation | KAFIDQGKLIPDDVM HHHHHCCCCCCHHHH | 37.30 | - | |
64 | Succinylation | KAFIDQGKLIPDDVM HHHHHCCCCCCHHHH | 37.30 | - | |
72 | Phosphorylation | LIPDDVMTRLALHEL CCCHHHHHHHHHHHH | 23.52 | 20068231 | |
80 | Succinylation | RLALHELKNLTQYSW HHHHHHHHHHHHHHH | 47.10 | - | |
80 | Acetylation | RLALHELKNLTQYSW HHHHHHHHHHHHHHH | 47.10 | - | |
80 | Succinylation | RLALHELKNLTQYSW HHHHHHHHHHHHHHH | 47.10 | - | |
85 | Phosphorylation | ELKNLTQYSWLLDGF HHHHHHHHHHHHHCC | 9.14 | 20562437 | |
138 | Phosphorylation | HPASGRVYNIEFNPP ECCCCCEEEEEECCC | 14.73 | 21406692 | |
147 | Phosphorylation | IEFNPPKTVGIDDLT EEECCCCCCCCCCCC | 29.73 | 21406692 | |
154 | Phosphorylation | TVGIDDLTGEPLIQR CCCCCCCCCCCCEEC | 46.63 | 21406692 | |
165 | Acetylation | LIQREDDKPETVIKR CEECCCCCCHHHHHH | 58.01 | 23954790 | |
174 | Malonylation | ETVIKRLKAYEDQTK HHHHHHHHHHCCCCH | 53.61 | 26320211 | |
174 | Succinylation | ETVIKRLKAYEDQTK HHHHHHHHHHCCCCH | 53.61 | - | |
174 | Succinylation | ETVIKRLKAYEDQTK HHHHHHHHHHCCCCH | 53.61 | - | |
174 | Acetylation | ETVIKRLKAYEDQTK HHHHHHHHHHCCCCH | 53.61 | - | |
176 | Phosphorylation | VIKRLKAYEDQTKPV HHHHHHHHCCCCHHH | 20.60 | 29496907 | |
181 | Ubiquitination | KAYEDQTKPVLEYYQ HHHCCCCHHHHHHHH | 27.74 | - | |
181 | Acetylation | KAYEDQTKPVLEYYQ HHHCCCCHHHHHHHH | 27.74 | 20167786 | |
181 | Succinylation | KAYEDQTKPVLEYYQ HHHCCCCHHHHHHHH | 27.74 | 23954790 | |
181 | Malonylation | KAYEDQTKPVLEYYQ HHHCCCCHHHHHHHH | 27.74 | 26320211 | |
186 | Phosphorylation | QTKPVLEYYQKKGVL CCHHHHHHHHHHCCE | 13.67 | 119557 | |
189 | Succinylation | PVLEYYQKKGVLETF HHHHHHHHHCCEECC | 35.06 | - | |
189 | Succinylation | PVLEYYQKKGVLETF HHHHHHHHHCCEECC | 35.06 | 23954790 | |
189 | Acetylation | PVLEYYQKKGVLETF HHHHHHHHHCCEECC | 35.06 | 23236377 | |
190 | Acetylation | VLEYYQKKGVLETFS HHHHHHHHCCEECCC | 38.43 | 6271573 | |
197 | Phosphorylation | KGVLETFSGTETNKI HCCEECCCCCCCCCH | 52.83 | 110760127 | |
203 | Acetylation | FSGTETNKIWPYVYA CCCCCCCCHHHHHHH | 54.27 | - | |
207 | Phosphorylation | ETNKIWPYVYAFLQT CCCCHHHHHHHHHHC | 7.35 | 46161143 | |
209 | Phosphorylation | NKIWPYVYAFLQTKV CCHHHHHHHHHHCCC | 5.94 | 46161149 | |
220 | Phosphorylation | QTKVPQRSQKASVTP HCCCCCHHHCCCCCC | 30.68 | 26437602 | |
224 | Phosphorylation | PQRSQKASVTP---- CCHHHCCCCCC---- | 33.29 | 26437602 |
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 KAD3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KAD3_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 KAD3_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
DAPK3_HUMAN | DAPK3 | physical | 21988832 | |
CAF17_HUMAN | IBA57 | physical | 26186194 | |
HNRL2_HUMAN | HNRNPUL2 | physical | 26344197 | |
RS14_HUMAN | RPS14 | physical | 26344197 |
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-34, AND MASS SPECTROMETRY. |