| UniProt ID | TRM6_YEAST | |
|---|---|---|
| UniProt AC | P41814 | |
| Protein Name | tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6 | |
| Gene Name | GCD10 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 478 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. [PubMed: 10779558] | |
| Protein Sequence | MNALTTIDFNQHVIVRLPSKNYKIVELKPNTSVSLGKFGAFEVNDIIGYPFGLTFEIYYDGEEVSSDENRDSKPKNKIPIGKVRLLSQEIKDVNNDKDDGQSEPPLSIKEKSVSLELSSIDSSATNQNLVNMGSKAQELTVEEIEKMKQESLSSKEIIDKIIKSHKSFHNKTVYSQEKYVNRKKQKFAKYFTVEYLSSSNLLQFLIDKGDIQRVLDMSQESMGMLLNLANIQSEGNYLCMDETGGLLVYFLLERMFGGDNESKSKGKVIVIHENEHANLDLLKFANYSEKFIKEHVHTISLLDFFEPPTLQEIQSRFTPLPKEEARALKGGKKNSYYRKLRWYNTQWQILELTGEFLYDGLVMATTLHLPTLVPKLAEKIHGSRPIVCYGQFKETLLELAHTLYSDLRFLAPSILETRCRPYQSIRGKLHPLMTMKGGGGYLMWCHRVIPAPEPVSENATAADSSEKLAEHGAKKQKI | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 23 | Acetylation | RLPSKNYKIVELKPN ECCCCCEEEEEECCC | 50.06 | 24489116 | |
| 87 | Phosphorylation | IGKVRLLSQEIKDVN CHHHHHHCHHHHHHC | 30.29 | 22369663 | |
| 102 | Phosphorylation | NDKDDGQSEPPLSIK CCCCCCCCCCCCCCH | 58.56 | 24961812 | |
| 112 | Phosphorylation | PLSIKEKSVSLELSS CCCCHHEEEEEEEEC | 20.31 | 22369663 | |
| 114 | Phosphorylation | SIKEKSVSLELSSID CCHHEEEEEEEECCC | 24.18 | 22369663 | |
| 118 | Phosphorylation | KSVSLELSSIDSSAT EEEEEEEECCCCCCC | 18.84 | 22369663 | |
| 119 | Phosphorylation | SVSLELSSIDSSATN EEEEEEECCCCCCCC | 42.93 | 22369663 | |
| 122 | Phosphorylation | LELSSIDSSATNQNL EEEECCCCCCCCHHH | 21.87 | 22369663 | |
| 123 | Phosphorylation | ELSSIDSSATNQNLV EEECCCCCCCCHHHC | 35.05 | 22369663 | |
| 125 | Phosphorylation | SSIDSSATNQNLVNM ECCCCCCCCHHHCCC | 39.01 | 22369663 | |
| 134 | Phosphorylation | QNLVNMGSKAQELTV HHHCCCCHHHHCCCH | 17.66 | 22369663 | |
| 146 | Acetylation | LTVEEIEKMKQESLS CCHHHHHHHHHHCCC | 57.99 | 24489116 | |
| 151 | Phosphorylation | IEKMKQESLSSKEII HHHHHHHCCCCHHHH | 30.93 | 28889911 | |
| 153 | Phosphorylation | KMKQESLSSKEIIDK HHHHHCCCCHHHHHH | 48.95 | 30377154 | |
| 154 | Phosphorylation | MKQESLSSKEIIDKI HHHHCCCCHHHHHHH | 39.33 | 28889911 | |
| 160 | Acetylation | SSKEIIDKIIKSHKS CCHHHHHHHHHHCHH | 35.60 | 24489116 | |
| 166 | Acetylation | DKIIKSHKSFHNKTV HHHHHHCHHHCCCCC | 63.01 | 25381059 | |
| 167 | Phosphorylation | KIIKSHKSFHNKTVY HHHHHCHHHCCCCCC | 26.72 | 30377154 | |
| 171 | Acetylation | SHKSFHNKTVYSQEK HCHHHCCCCCCCHHH | 30.69 | 22865919 | |
| 172 | Phosphorylation | HKSFHNKTVYSQEKY CHHHCCCCCCCHHHH | 29.96 | 23749301 | |
| 174 | Phosphorylation | SFHNKTVYSQEKYVN HHCCCCCCCHHHHHH | 15.18 | 28889911 | |
| 175 | Phosphorylation | FHNKTVYSQEKYVNR HCCCCCCCHHHHHHH | 27.77 | 25752575 | |
| 178 | Acetylation | KTVYSQEKYVNRKKQ CCCCCHHHHHHHHHH | 47.03 | 25381059 | |
| 190 | Phosphorylation | KKQKFAKYFTVEYLS HHHHHHHHHHHEECC | 10.89 | 19823750 | |
| 192 | Phosphorylation | QKFAKYFTVEYLSSS HHHHHHHHHEECCCC | 14.88 | 19823750 | |
| 195 | Phosphorylation | AKYFTVEYLSSSNLL HHHHHHEECCCCCHH | 13.93 | 19823750 | |
| 197 | Phosphorylation | YFTVEYLSSSNLLQF HHHHEECCCCCHHHH | 30.71 | 19823750 | |
| 198 | Phosphorylation | FTVEYLSSSNLLQFL HHHEECCCCCHHHHH | 22.20 | 19823750 | |
| 199 | Phosphorylation | TVEYLSSSNLLQFLI HHEECCCCCHHHHHH | 28.28 | 19823750 | |
| 428 | Acetylation | PYQSIRGKLHPLMTM CCHHHCCEEECEEEE | 33.50 | 25381059 | |
| 436 | Methylation | LHPLMTMKGGGGYLM EECEEEEECCCEEEE | 45.28 | 20137074 | |
| 456 | Phosphorylation | IPAPEPVSENATAAD EECCCCCCCCCCCCC | 35.53 | 22369663 | |
| 460 | Phosphorylation | EPVSENATAADSSEK CCCCCCCCCCCHHHH | 33.68 | 22369663 | |
| 464 | Phosphorylation | ENATAADSSEKLAEH CCCCCCCHHHHHHHC | 35.35 | 22369663 | |
| 465 | Phosphorylation | NATAADSSEKLAEHG CCCCCCHHHHHHHCH | 39.02 | 22369663 | |
| 467 | Acetylation | TAADSSEKLAEHGAK CCCCHHHHHHHCHHH | 55.75 | 24489116 | |
| 474 | Acetylation | KLAEHGAKKQKI--- HHHHCHHHHCCC--- | 61.40 | 25381059 |
| 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 TRM6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRM6_YEAST !! | ||||||
* 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 TRM6_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; TYR-174 ANDSER-175, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASSSPECTROMETRY. | |
