UniProt ID | THG1_HUMAN | |
---|---|---|
UniProt AC | Q9NWX6 | |
Protein Name | Probable tRNA(His) guanylyltransferase | |
Gene Name | THG1L | |
Organism | Homo sapiens (Human). | |
Sequence Length | 298 | |
Subcellular Localization | Cytoplasm . Found near the nuclear membrane. | |
Protein Description | Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis.. | |
Protein Sequence | MWGACKVKVHDSLATISITLRRYLRLGATMAKSKFEYVRDFEADDTCLAHCWVVVRLDGRNFHRFAEKHNFAKPNDSRALQLMTKCAQTVMEELEDIVIAYGQSDEYSFVFKRKTNWFKRRASKFMTHVASQFASSYVFYWRDYFEDQPLLYPPGFDGRVVVYPSNQTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQGRLQGTLAADKNEILFSEFNINYNNELPMYRKGTVLIWQKVDEVMTKEIKLPTEMEGKKMAVTRTRTKPVPLHCDIIGDAFWKEHPEILDEDS | |
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 |
---|---|---|---|---|---|
33 | O-linked_Glycosylation | LGATMAKSKFEYVRD HCCEEECCCCEECCC | 32.79 | 30379171 | |
34 | Acetylation | GATMAKSKFEYVRDF CCEEECCCCEECCCC | 41.32 | 25953088 | |
68 | Acetylation | NFHRFAEKHNFAKPN CHHHHHHHCCCCCCC | 40.18 | 19608861 | |
73 | Ubiquitination | AEKHNFAKPNDSRAL HHHCCCCCCCHHHHH | 39.97 | - | |
114 | Acetylation | YSFVFKRKTNWFKRR CEEEEECCCCHHHHH | 46.96 | 7377641 | |
119 | Ubiquitination | KRKTNWFKRRASKFM ECCCCHHHHHHHHHH | 32.37 | 21890473 | |
119 | Acetylation | KRKTNWFKRRASKFM ECCCCHHHHHHHHHH | 32.37 | 7377651 | |
170 | Ubiquitination | YPSNQTLKDYLSWRQ ECCCCCHHHHHHHHH | 47.95 | - | |
174 | Phosphorylation | QTLKDYLSWRQADCH CCHHHHHHHHHCCCH | 17.62 | 24719451 | |
222 | Phosphorylation | DKNEILFSEFNINYN CCCCEEEEEECCCCC | 37.52 | 20068231 | |
228 | Phosphorylation | FSEFNINYNNELPMY EEEECCCCCCCCCCC | 18.63 | 20068231 | |
235 | Phosphorylation | YNNELPMYRKGTVLI CCCCCCCCCCCEEEE | 13.77 | 20068231 | |
237 | Malonylation | NELPMYRKGTVLIWQ CCCCCCCCCEEEEEE | 41.25 | 26320211 | |
239 | Phosphorylation | LPMYRKGTVLIWQKV CCCCCCCEEEEEEEH | 18.38 | - | |
251 | Phosphorylation | QKVDEVMTKEIKLPT EEHHHHHHCCCCCCC | 30.60 | - | |
252 | Ubiquitination | KVDEVMTKEIKLPTE EHHHHHHCCCCCCCC | 39.07 | 21890473 | |
263 | Acetylation | LPTEMEGKKMAVTRT CCCCCCCCEEEEEEC | 26.52 | 23749302 | |
263 | 2-Hydroxyisobutyrylation | LPTEMEGKKMAVTRT CCCCCCCCEEEEEEC | 26.52 | - | |
264 | Acetylation | PTEMEGKKMAVTRTR CCCCCCCEEEEEECC | 42.84 | 7339661 |
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 THG1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of THG1_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 THG1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ELMD1_HUMAN | ELMOD1 | physical | 16189514 | |
AASD1_HUMAN | AARSD1 | physical | 22863883 | |
DPP9_HUMAN | DPP9 | physical | 22863883 | |
EF2K_HUMAN | EEF2K | physical | 22863883 | |
METH_HUMAN | MTR | physical | 22863883 | |
RAGP1_HUMAN | RANGAP1 | physical | 22863883 | |
SH3G1_HUMAN | SH3GL1 | physical | 22863883 | |
SHLB1_HUMAN | SH3GLB1 | physical | 22863883 | |
TPRKB_HUMAN | TPRKB | physical | 22863883 | |
THG1_HUMAN | THG1L | physical | 25416956 | |
THG1_HUMAN | THG1L | physical | 21516116 |
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-68, AND MASS SPECTROMETRY. |