| UniProt ID | IF5A1_YEAST | |
|---|---|---|
| UniProt AC | P23301 | |
| Protein Name | Eukaryotic translation initiation factor 5A-1 | |
| Gene Name | HYP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 157 | |
| Subcellular Localization | Cytoplasm . Concentrates in the perinuclear region. | |
| Protein Description | mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Essential for polarized growth, a process necessary for G1/S transition. May mediate large range of effects of the polyamine spermidine in the cell.. | |
| Protein Sequence | MSDEEHTFETADAGSSATYPMQCSALRKNGFVVIKSRPCKIVDMSTSKTGKHGHAKVHLVAIDIFTGKKLEDLSPSTHNMEVPVVKRNEYQLLDIDDGFLSLMNMDGDTKDDVKAPEGELGDSLQTAFDEGKDLMVTIISAMGEEAAISFKEAARTD | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSDEEHTFE ------CCCCCCEEC | 54.45 | 22369663 | |
| 2 | Acetylation | ------MSDEEHTFE ------CCCCCCEEC | 54.45 | 8243648 | |
| 7 | Phosphorylation | -MSDEEHTFETADAG -CCCCCCEECCCCCC | 26.84 | 22369663 | |
| 10 | Phosphorylation | DEEHTFETADAGSSA CCCCEECCCCCCCCC | 26.16 | 22369663 | |
| 15 | Phosphorylation | FETADAGSSATYPMQ ECCCCCCCCCCCCEE | 20.65 | 22369663 | |
| 16 | Phosphorylation | ETADAGSSATYPMQC CCCCCCCCCCCCEEC | 24.58 | 22890988 | |
| 18 | Phosphorylation | ADAGSSATYPMQCSA CCCCCCCCCCEECCH | 30.06 | 22890988 | |
| 19 | Phosphorylation | DAGSSATYPMQCSAL CCCCCCCCCEECCHH | 9.09 | 22890988 | |
| 24 | Phosphorylation | ATYPMQCSALRKNGF CCCCEECCHHCCCCE | 17.28 | 22890988 | |
| 28 | Ubiquitination | MQCSALRKNGFVVIK EECCHHCCCCEEEEE | 63.37 | 23749301 | |
| 35 | Ubiquitination | KNGFVVIKSRPCKIV CCCEEEEECCCEEEE | 28.89 | 23749301 | |
| 35 | Acetylation | KNGFVVIKSRPCKIV CCCEEEEECCCEEEE | 28.89 | 24489116 | |
| 40 | Acetylation | VIKSRPCKIVDMSTS EEECCCEEEEECCCC | 48.74 | 24489116 | |
| 40 | Ubiquitination | VIKSRPCKIVDMSTS EEECCCEEEEECCCC | 48.74 | 23749301 | |
| 45 | Phosphorylation | PCKIVDMSTSKTGKH CEEEEECCCCCCCCC | 25.68 | 22369663 | |
| 46 | Phosphorylation | CKIVDMSTSKTGKHG EEEEECCCCCCCCCC | 27.83 | 22369663 | |
| 47 | Phosphorylation | KIVDMSTSKTGKHGH EEEECCCCCCCCCCC | 22.40 | 22369663 | |
| 51 | Other | MSTSKTGKHGHAKVH CCCCCCCCCCCCEEE | 52.20 | 19120453 | |
| 51 | Hypusine | MSTSKTGKHGHAKVH CCCCCCCCCCCCEEE | 52.20 | - | |
| 56 | Ubiquitination | TGKHGHAKVHLVAID CCCCCCCEEEEEEEE | 25.23 | 17644757 | |
| 68 | Acetylation | AIDIFTGKKLEDLSP EEECCCCCCHHHCCC | 51.64 | 24489116 | |
| 68 | Ubiquitination | AIDIFTGKKLEDLSP EEECCCCCCHHHCCC | 51.64 | 22106047 | |
| 69 | Ubiquitination | IDIFTGKKLEDLSPS EECCCCCCHHHCCCC | 59.46 | 24961812 | |
| 69 | Acetylation | IDIFTGKKLEDLSPS EECCCCCCHHHCCCC | 59.46 | 24489116 | |
| 74 | Phosphorylation | GKKLEDLSPSTHNME CCCHHHCCCCCCCCE | 29.18 | 22369663 | |
| 76 | Phosphorylation | KLEDLSPSTHNMEVP CHHHCCCCCCCCEEE | 38.63 | 20377248 | |
| 77 | Phosphorylation | LEDLSPSTHNMEVPV HHHCCCCCCCCEEEE | 22.21 | 22369663 | |
| 86 | Ubiquitination | NMEVPVVKRNEYQLL CCEEEEEECCEEEEE | 50.14 | 24961812 | |
| 86 | Acetylation | NMEVPVVKRNEYQLL CCEEEEEECCEEEEE | 50.14 | 24489116 | |
| 114 | Acetylation | GDTKDDVKAPEGELG CCCHHHCCCCCCCCH | 66.28 | 22865919 | |
| 123 | Phosphorylation | PEGELGDSLQTAFDE CCCCCHHHHHHHHHC | 22.15 | 22369663 | |
| 126 | Phosphorylation | ELGDSLQTAFDEGKD CCHHHHHHHHHCCHH | 34.29 | 22369663 | |
| 149 | Phosphorylation | MGEEAAISFKEAART CCHHHHHHHHHHHCC | 26.07 | 27214570 |
| 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 IF5A1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IF5A1_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 IF5A1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Determination and mutational analysis of the phosphorylation site inthe hypusine-containing protein Hyp2p."; Klier H., Woehl T., Eckerskorn C., Magdolen V., Lottspeich F.; FEBS Lett. 334:360-364(1993). Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2, AND PHOSPHORYLATION ATSER-2. | |
| 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-2; SER-15; SER-74 ANDSER-149, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-74, AND MASSSPECTROMETRY. | |
| "Translation initiation factor eIF-5A, the hypusine-containingprotein, is phosphorylated on serine in Saccharomyces cerevisiae."; Kang H.A., Schwelberger H.G., Hershey J.W.B.; J. Biol. Chem. 268:14750-14756(1993). Cited for: PHOSPHORYLATION AT SER-2. | |
| "Determination and mutational analysis of the phosphorylation site inthe hypusine-containing protein Hyp2p."; Klier H., Woehl T., Eckerskorn C., Magdolen V., Lottspeich F.; FEBS Lett. 334:360-364(1993). Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2, AND PHOSPHORYLATION ATSER-2. | |
