UniProt ID | AGK_HUMAN | |
---|---|---|
UniProt AC | Q53H12 | |
Protein Name | Acylglycerol kinase, mitochondrial {ECO:0000303|PubMed:15939762} | |
Gene Name | AGK {ECO:0000303|PubMed:15939762, ECO:0000312|HGNC:HGNC:21869} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 422 | |
Subcellular Localization |
Mitochondrion inner membrane Peripheral membrane protein . Mitochondrion intermembrane space . Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane (PubMed:28712724). It is unclear whether the N-terminal h |
|
Protein Description | Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. [PubMed: 15939762 Does not phosphorylate sphingosine] | |
Protein Sequence | MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ | |
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 |
---|---|---|---|---|---|
6 | Ubiquitination | --MTVFFKTLRNHWK --CCEEHHHHHHHHC | 34.87 | 21890473 | |
6 (in isoform 2) | Ubiquitination | - | 34.87 | 21890473 | |
6 | Acetylation | --MTVFFKTLRNHWK --CCEEHHHHHHHHC | 34.87 | 19608861 | |
72 | Glutathionylation | VFLNPAACKGKARTL EEECHHHHCCHHHHH | 6.93 | 22555962 | |
107 (in isoform 1) | Ubiquitination | - | 35.75 | 21890473 | |
107 | Ubiquitination | TDYEGQAKKLLELME ECCHHHHHHHHHHHH | 35.75 | 21906983 | |
157 | Phosphorylation | GFIPLGETSSLSHTL EEEECCCCCCCCEEE | 23.09 | 27732954 | |
158 | Phosphorylation | FIPLGETSSLSHTLF EEECCCCCCCCEEEE | 25.61 | 27732954 | |
159 | Phosphorylation | IPLGETSSLSHTLFA EECCCCCCCCEEEEE | 41.11 | 27732954 | |
161 | Phosphorylation | LGETSSLSHTLFAES CCCCCCCCEEEEECC | 19.17 | 27732954 | |
163 | Phosphorylation | ETSSLSHTLFAESGN CCCCCCEEEEECCCC | 21.86 | 27732954 | |
168 | Phosphorylation | SHTLFAESGNKVQHI CEEEEECCCCEEEEE | 44.21 | 30108239 | |
184 | Ubiquitination | DATLAIVKGETVPLD ECEEEEECCCEEECE | 44.94 | - | |
196 | Ubiquitination | PLDVLQIKGEKEQPV ECEEEEECCCCCCCE | 48.32 | - | |
199 (in isoform 1) | Ubiquitination | - | 71.02 | 21890473 | |
199 | Ubiquitination | VLQIKGEKEQPVFAM EEEECCCCCCCEEEE | 71.02 | 21906983 | |
223 (in isoform 1) | Ubiquitination | - | 42.67 | 21890473 | |
223 | Ubiquitination | DAGVKVSKYWYLGPL HCCCEEEEEEEECCC | 42.67 | 21890473 | |
226 | Phosphorylation | VKVSKYWYLGPLKIK CEEEEEEEECCCEEH | 9.93 | 7178993 | |
231 | Acetylation | YWYLGPLKIKAAHFF EEEECCCEEHHHHHH | 45.34 | 7825219 | |
233 | Acetylation | YLGPLKIKAAHFFST EECCCEEHHHHHHHH | 37.62 | 7825229 | |
285 | Phosphorylation | RILRRLASYWAQPQD HHHHHHHHHHCCCHH | 26.29 | 28122231 | |
286 | Phosphorylation | ILRRLASYWAQPQDA HHHHHHHHHCCCHHH | 10.12 | 28122231 | |
295 | Phosphorylation | AQPQDALSQEVSPEV CCCHHHHCCCCCHHH | 26.47 | 28122231 | |
325 | Phosphorylation | RNNQLDPTSKEDFLN CCCCCCCCCHHHHHH | 52.69 | 20068231 | |
326 | Phosphorylation | NNQLDPTSKEDFLNI CCCCCCCCHHHHHHE | 39.16 | 20068231 | |
327 | Ubiquitination | NQLDPTSKEDFLNIC CCCCCCCHHHHHHEE | 64.87 | 2190698 | |
327 (in isoform 1) | Ubiquitination | - | 64.87 | 21890473 | |
334 | Glutathionylation | KEDFLNICIEPDTIS HHHHHHEECCCCCCC | 2.54 | 22555962 | |
347 | Phosphorylation | ISKGDFITIGSRKVR CCCCCEEEECCEECC | 21.19 | 27080861 | |
350 | Phosphorylation | GDFITIGSRKVRNPK CCEEEECCEECCCCC | 25.69 | 30266825 | |
408 | Glutathionylation | PRKLQFFCDPRKREQ CCCCHHHCCHHHHHH | 8.11 | 22555962 | |
418 | Phosphorylation | RKREQMLTSPTQ--- HHHHHHCCCCCC--- | 27.58 | 29759185 | |
419 | Phosphorylation | KREQMLTSPTQ---- HHHHHCCCCCC---- | 23.22 | 20068231 | |
421 | Phosphorylation | EQMLTSPTQ------ HHHCCCCCC------ | 46.83 | 20068231 |
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 AGK_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AGK_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 AGK_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
T10B_HUMAN | TIMM10B | physical | 28514442 | |
TIM10_HUMAN | TIMM10 | physical | 28514442 | |
TIM29_HUMAN | C19orf52 | physical | 28514442 | |
AT12A_HUMAN | ATP12A | physical | 28514442 | |
RAB18_HUMAN | RAB18 | physical | 28514442 |
loading...
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-6, AND MASS SPECTROMETRY. |