UniProt ID | TXTP_HUMAN | |
---|---|---|
UniProt AC | P53007 | |
Protein Name | Tricarboxylate transport protein, mitochondrial | |
Gene Name | SLC25A1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 311 | |
Subcellular Localization |
Mitochondrion inner membrane Multi-pass membrane protein. |
|
Protein Description | Involved in citrate-H(+)/malate exchange. Important for the bioenergetics of hepatic cells as it provides a carbon source for fatty acid and sterol biosyntheses, and NAD(+) for the glycolytic pathway.. | |
Protein Sequence | MPAPRAPRALAAAAPASGKAKLTHPGKAILAGGLAGGIEICITFPTEYVKTQLQLDERSHPPRYRGIGDCVRQTVRSHGVLGLYRGLSSLLYGSIPKAAVRFGMFEFLSNHMRDAQGRLDSTRGLLCGLGAGVAEAVVVVCPMETIKVKFIHDQTSPNPKYRGFFHGVREIVREQGLKGTYQGLTATVLKQGSNQAIRFFVMTSLRNWYRGDNPNKPMNPLITGVFGAIAGAASVFGNTPLDVIKTRMQGLEAHKYRNTWDCGLQILKKEGLKAFYKGTVPRLGRVCLDVAIVFVIYDEVVKLLNKVWKTD | |
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 |
---|---|---|---|---|---|
17 | Phosphorylation | LAAAAPASGKAKLTH HHHHCCCCCCCCCCC | 39.50 | 29396449 | |
19 | Ubiquitination | AAAPASGKAKLTHPG HHCCCCCCCCCCCCC | 39.59 | - | |
21 | Acetylation | APASGKAKLTHPGKA CCCCCCCCCCCCCCC | 58.36 | 25953088 | |
21 | Ubiquitination | APASGKAKLTHPGKA CCCCCCCCCCCCCCC | 58.36 | - | |
48 | Phosphorylation | CITFPTEYVKTQLQL EEECCHHHHHHHHHH | 15.10 | 26074081 | |
51 | Phosphorylation | FPTEYVKTQLQLDER CCHHHHHHHHHHCCC | 25.19 | 26074081 | |
65 | Methylation | RSHPPRYRGIGDCVR CCCCCCCCCHHHHHH | 31.37 | 115917061 | |
70 | S-nitrosylation | RYRGIGDCVRQTVRS CCCCHHHHHHHHHHH | 1.98 | 24105792 | |
74 | Phosphorylation | IGDCVRQTVRSHGVL HHHHHHHHHHHCCHH | 13.81 | 27080861 | |
88 | Phosphorylation | LGLYRGLSSLLYGSI HHHHHHHHHHHHCCC | 23.05 | 28152594 | |
89 | Phosphorylation | GLYRGLSSLLYGSIP HHHHHHHHHHHCCCC | 27.69 | 28152594 | |
92 | Phosphorylation | RGLSSLLYGSIPKAA HHHHHHHHCCCCHHH | 17.70 | 28152594 | |
94 | Phosphorylation | LSSLLYGSIPKAAVR HHHHHHCCCCHHHHH | 23.35 | 28152594 | |
97 | Acetylation | LLYGSIPKAAVRFGM HHHCCCCHHHHHHHH | 47.51 | 19608861 | |
97 | Ubiquitination | LLYGSIPKAAVRFGM HHHCCCCHHHHHHHH | 47.51 | 21890473 | |
121 | Phosphorylation | DAQGRLDSTRGLLCG HHCCCCCCCHHHHHH | 25.29 | 22210691 | |
122 | Phosphorylation | AQGRLDSTRGLLCGL HCCCCCCCHHHHHHC | 28.55 | 22210691 | |
149 | Acetylation | PMETIKVKFIHDQTS CCCEEEEEEECCCCC | 33.33 | 25825284 | |
149 | Ubiquitination | PMETIKVKFIHDQTS CCCEEEEEEECCCCC | 33.33 | - | |
155 | Phosphorylation | VKFIHDQTSPNPKYR EEEECCCCCCCHHHC | 52.81 | 30266825 | |
156 | Phosphorylation | KFIHDQTSPNPKYRG EEECCCCCCCHHHCC | 19.63 | 30266825 | |
160 | 2-Hydroxyisobutyrylation | DQTSPNPKYRGFFHG CCCCCCHHHCCHHHH | 54.97 | - | |
160 | Acetylation | DQTSPNPKYRGFFHG CCCCCCHHHCCHHHH | 54.97 | 19608861 | |
160 | Ubiquitination | DQTSPNPKYRGFFHG CCCCCCHHHCCHHHH | 54.97 | 21890473 | |
178 | Methylation | IVREQGLKGTYQGLT HHHHCCCCCEECCEE | 56.91 | 2418839 | |
178 | Malonylation | IVREQGLKGTYQGLT HHHHCCCCCEECCEE | 56.91 | 26320211 | |
178 | Ubiquitination | IVREQGLKGTYQGLT HHHHCCCCCEECCEE | 56.91 | 21890473 | |
187 | Phosphorylation | TYQGLTATVLKQGSN EECCEEEEEECCCCC | 22.57 | 27080861 | |
190 | Ubiquitination | GLTATVLKQGSNQAI CEEEEEECCCCCHHH | 48.56 | 21890473 | |
190 | Malonylation | GLTATVLKQGSNQAI CEEEEEECCCCCHHH | 48.56 | 26320211 | |
204 | Phosphorylation | IRFFVMTSLRNWYRG HHHHHHHHHHHHHCC | 13.77 | 22210691 | |
255 | Acetylation | MQGLEAHKYRNTWDC HCHHHHHHCCCCHHH | 53.61 | 25825284 | |
255 | Malonylation | MQGLEAHKYRNTWDC HCHHHHHHCCCCHHH | 53.61 | 26320211 | |
255 | Ubiquitination | MQGLEAHKYRNTWDC HCHHHHHHCCCCHHH | 53.61 | 19608861 | |
255 | 2-Hydroxyisobutyrylation | MQGLEAHKYRNTWDC HCHHHHHHCCCCHHH | 53.61 | - | |
256 | Phosphorylation | QGLEAHKYRNTWDCG CHHHHHHCCCCHHHH | 10.14 | 20068231 | |
268 | 2-Hydroxyisobutyrylation | DCGLQILKKEGLKAF HHHCHHHHHHCCHHH | 50.86 | - | |
268 | Malonylation | DCGLQILKKEGLKAF HHHCHHHHHHCCHHH | 50.86 | 26320211 | |
268 | Acetylation | DCGLQILKKEGLKAF HHHCHHHHHHCCHHH | 50.86 | 25038526 | |
276 | Phosphorylation | KEGLKAFYKGTVPRL HHCCHHHHCCCCCCH | 17.23 | 22817900 | |
277 | Malonylation | EGLKAFYKGTVPRLG HCCHHHHCCCCCCHH | 41.47 | 26320211 | |
277 | Acetylation | EGLKAFYKGTVPRLG HCCHHHHCCCCCCHH | 41.47 | 25825284 | |
277 | Succinylation | EGLKAFYKGTVPRLG HCCHHHHCCCCCCHH | 41.47 | 23954790 | |
297 | Phosphorylation | VAIVFVIYDEVVKLL EEHHHHHHHHHHHHH | 10.76 | 19835603 | |
306 | Ubiquitination | EVVKLLNKVWKTD-- HHHHHHHHHHCCC-- | 49.82 | - | |
306 | Acetylation | EVVKLLNKVWKTD-- HHHHHHHHHHCCC-- | 49.82 | 25825284 |
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 TXTP_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TXTP_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 TXTP_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MIC60_HUMAN | IMMT | physical | 26344197 | |
RL9_HUMAN | RPL9 | physical | 26344197 | |
RS26_HUMAN | RPS26 | physical | 26344197 | |
RS4X_HUMAN | RPS4X | physical | 26344197 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
OMIM Disease | ||||||
615182 | Combined D-2- and L-2-hydroxyglutaric aciduria (D2L2AD) | |||||
Kegg Drug | ||||||
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-97; LYS-160 AND LYS-255, ANDMASS SPECTROMETRY. |