| UniProt ID | EIF3B_YEAST | |
|---|---|---|
| UniProt AC | P06103 | |
| Protein Name | Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001} | |
| Gene Name | PRT1 {ECO:0000255|HAMAP-Rule:MF_03001} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 763 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | RNA-binding 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 | MKNFLPRTLKNIYELYFNNISVHSIVSRNTQLKRSKIIQMTTETFEDIKLEDIPVDDIDFSDLEEQYKVTEEFNFDQYIVVNGAPVIPSAKVPVLKKALTSLFSKAGKVVNMEFPIDEATGKTKGFLFVECGSMNDAKKIIKSFHGKRLDLKHRLFLYTMKDVERYNSDDFDTEFREPDMPTFVPSSSLKSWLMDDKVRDQFVLQDDVKTSVFWNSMFNEEDSLVESRENWSTNYVRFSPKGTYLFSYHQQGVTAWGGPNFDRLRRFYHPDVRNSSVSPNEKYLVTFSTEPIIVEEDNEFSPFTKKNEGHQLCIWDIASGLLMATFPVIKSPYLKWPLVRWSYNDKYCARMVGDSLIVHDATKNFMPLEAKALKPSGIRDFSFAPEGVKLQPFRNGDEPSVLLAYWTPETNNSACTATIAEVPRGRVLKTVNLVQVSNVTLHWQNQAEFLCFNVERHTKSGKTQFSNLQICRLTERDIPVEKVELKDSVFEFGWEPHGNRFVTISVHEVADMNYAIPANTIRFYAPETKEKTDVIKRWSLVKEIPKTFANTVSWSPAGRFVVVGALVGPNMRRSDLQFYDMDYPGEKNINDNNDVSASLKDVAHPTYSAATNITWDPSGRYVTAWSSSLKHKVEHGYKIFNIAGNLVKEDIIAGFKNFAWRPRPASILSNAERKKVRKNLREWSAQFEEQDAMEADTAMRDLILHQRELLKQWTEYREKIGQEMEKSMNFKIFDVQPEDASDDFTTIEEIVEEVLEETKEKVE | |
| 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 |
|---|---|---|---|---|---|
| 61 | Phosphorylation | PVDDIDFSDLEEQYK CCCCCCHHHHHHHHC | 37.22 | 22369663 | |
| 67 | Phosphorylation | FSDLEEQYKVTEEFN HHHHHHHHCCCCCCC | 15.65 | 28889911 | |
| 100 | Phosphorylation | PVLKKALTSLFSKAG HHHHHHHHHHHHHCC | 28.39 | 29136822 | |
| 101 | Phosphorylation | VLKKALTSLFSKAGK HHHHHHHHHHHHCCC | 28.41 | 30377154 | |
| 122 | Acetylation | PIDEATGKTKGFLFV CCCCCCCCCCCEEEE | 42.58 | 24489116 | |
| 152 | Acetylation | HGKRLDLKHRLFLYT CCCCCCCHHHEEEEE | 26.75 | 25381059 | |
| 161 | Acetylation | RLFLYTMKDVERYNS HEEEEEHHHHHHHCC | 51.31 | 24489116 | |
| 161 | Succinylation | RLFLYTMKDVERYNS HEEEEEHHHHHHHCC | 51.31 | 23954790 | |
| 168 | Phosphorylation | KDVERYNSDDFDTEF HHHHHHCCCCCCCCC | 29.62 | 17563356 | |
| 187 | Phosphorylation | MPTFVPSSSLKSWLM CCCCCCCHHHHHHHC | 33.35 | 27821475 | |
| 188 | Phosphorylation | PTFVPSSSLKSWLMD CCCCCCHHHHHHHCC | 44.12 | 20377248 | |
| 197 | Acetylation | KSWLMDDKVRDQFVL HHHHCCCHHHCCEEC | 34.60 | 24489116 | |
| 197 | Ubiquitination | KSWLMDDKVRDQFVL HHHHCCCHHHCCEEC | 34.60 | 23749301 | |
| 335 | Acetylation | VIKSPYLKWPLVRWS CCCCCCCCCCEECCC | 40.70 | 24489116 | |
| 346 | Acetylation | VRWSYNDKYCARMVG ECCCCCCHHHHHHHC | 38.29 | 24489116 | |
| 363 | Acetylation | LIVHDATKNFMPLEA EEEEECCCCCCCCCC | 50.32 | 24489116 | |
| 371 | Acetylation | NFMPLEAKALKPSGI CCCCCCCCCCCCCCC | 44.89 | 24489116 | |
| 389 | Acetylation | SFAPEGVKLQPFRNG CCCCCCCCCCCCCCC | 52.87 | 24489116 | |
| 482 | Acetylation | ERDIPVEKVELKDSV CCCCCCEEEEECCCE | 41.04 | 24489116 | |
| 486 | Acetylation | PVEKVELKDSVFEFG CCEEEEECCCEEEEE | 34.16 | 24489116 | |
| 539 | Phosphorylation | TDVIKRWSLVKEIPK CCHHHHHHHHHHCCC | 27.58 | 21440633 | |
| 542 | Acetylation | IKRWSLVKEIPKTFA HHHHHHHHHCCCCCC | 56.04 | 24489116 | |
| 546 | Acetylation | SLVKEIPKTFANTVS HHHHHCCCCCCCCCC | 63.03 | 24489116 | |
| 587 | Ubiquitination | DMDYPGEKNINDNND CCCCCCCCCCCCCCC | 69.87 | 23749301 | |
| 630 | Acetylation | TAWSSSLKHKVEHGY EECCHHHHHHHHHCC | 43.24 | 24489116 | |
| 638 | Acetylation | HKVEHGYKIFNIAGN HHHHHCCEEEEEECC | 45.47 | 22865919 | |
| 666 | Phosphorylation | AWRPRPASILSNAER CCCCCCHHHHCHHHH | 27.09 | 25704821 | |
| 669 | Phosphorylation | PRPASILSNAERKKV CCCHHHHCHHHHHHH | 32.12 | 28889911 | |
| 711 | Acetylation | LHQRELLKQWTEYRE HHHHHHHHHHHHHHH | 57.31 | 24489116 | |
| 726 | Ubiquitination | KIGQEMEKSMNFKIF HHHHHHHHHCCEEEE | 54.41 | 23749301 | |
| 726 | Acetylation | KIGQEMEKSMNFKIF HHHHHHHHHCCEEEE | 54.41 | 24489116 |
| 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 EIF3B_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EIF3B_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 EIF3B_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-61; SER-168 AND SER-669,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-168, AND MASSSPECTROMETRY. | |
