UniProt ID | EIF3I_YEAST | |
---|---|---|
UniProt AC | P40217 | |
Protein Name | Eukaryotic translation initiation factor 3 subunit I {ECO:0000255|HAMAP-Rule:MF_03008} | |
Gene Name | TIF34 {ECO:0000255|HAMAP-Rule:MF_03008} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 347 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.. | |
Protein Sequence | MKAIKLTGHERPLTQVKYNKEGDLLFSCSKDSSASVWYSLNGERLGTLDGHTGTIWSIDVDCFTKYCVTGSADYSIKLWDVSNGQCVATWKSPVPVKRVEFSPCGNYFLAILDNVMKNPGSINIYEIERDSATHELTKVSEEPIHKIITHEGLDAATVAGWSTKGKYIIAGHKDGKISKYDVSNNYEYVDSIDLHEKSISDMQFSPDLTYFITSSRDTNSFLVDVSTLQVLKKYETDCPLNTAVITPLKEFIILGGGQEAKDVTTTSANEGKFEARFYHKIFEEEIGRVQGHFGPLNTVAISPQGTSYASGGEDGFIRLHHFEKSYFDFKYDVEKAAEAKEHMQEAN | |
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 |
---|---|---|---|---|---|
65 | Ubiquitination | IDVDCFTKYCVTGSA EEEECEECEECCCCC | 19.19 | 17644757 | |
138 | Acetylation | SATHELTKVSEEPIH CCCCCCCCCCCCCCH | 57.28 | 24489116 | |
146 | Acetylation | VSEEPIHKIITHEGL CCCCCCHHHCCCCCC | 36.20 | 24489116 | |
173 | 2-Hydroxyisobutyrylation | KYIIAGHKDGKISKY CEEEEECCCCCEEEE | 68.22 | - | |
179 | Acetylation | HKDGKISKYDVSNNY CCCCCEEEEECCCCE | 49.28 | 24489116 | |
213 | Phosphorylation | PDLTYFITSSRDTNS CCEEEEEECCCCCCC | 15.68 | 27017623 | |
215 | Phosphorylation | LTYFITSSRDTNSFL EEEEEECCCCCCCEE | 26.06 | 27017623 | |
265 | Phosphorylation | QEAKDVTTTSANEGK CCCCCCEECCCCCCC | 20.71 | 27717283 | |
266 | Phosphorylation | EAKDVTTTSANEGKF CCCCCEECCCCCCCE | 19.24 | 27717283 | |
267 | Phosphorylation | AKDVTTTSANEGKFE CCCCEECCCCCCCEE | 27.31 | 23749301 | |
272 | Acetylation | TTSANEGKFEARFYH ECCCCCCCEEEEEEH | 33.58 | 24489116 | |
280 | Acetylation | FEARFYHKIFEEEIG EEEEEEHHHHHHHHH | 37.40 | 24489116 | |
302 | Phosphorylation | PLNTVAISPQGTSYA CCCEEEECCCCCCCC | 11.05 | 28889911 | |
325 | Phosphorylation | RLHHFEKSYFDFKYD EEEEEECCCCCEECH | 24.68 | 21440633 | |
330 | Acetylation | EKSYFDFKYDVEKAA ECCCCCEECHHHHHH | 42.24 | 24489116 | |
335 | Acetylation | DFKYDVEKAAEAKEH CEECHHHHHHHHHHH | 53.39 | 22865919 | |
335 | Ubiquitination | DFKYDVEKAAEAKEH CEECHHHHHHHHHHH | 53.39 | 23749301 |
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 EIF3I_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EIF3I_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 EIF3I_YEAST !! |
Kegg Drug | ||||||
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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-302, AND MASSSPECTROMETRY. |