| UniProt ID | GBLP_YEAST | |
|---|---|---|
| UniProt AC | P38011 | |
| Protein Name | Guanine nucleotide-binding protein subunit beta-like protein | |
| Gene Name | ASC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 319 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. [PubMed: 22096102 Located at the head of the 40S ribosomal subunit in the vicinity of the mRNA exit channel, RACK1 serves as a scaffold protein that can recruit other proteins to the ribosome. Involved in the negative regulation of translation of a specific subset of proteins] | |
| Protein Sequence | MASNEVLVLRGTLEGHNGWVTSLATSAGQPNLLLSASRDKTLISWKLTGDDQKFGVPVRSFKGHSHIVQDCTLTADGAYALSASWDKTLRLWDVATGETYQRFVGHKSDVMSVDIDKKASMIISGSRDKTIKVWTIKGQCLATLLGHNDWVSQVRVVPNEKADDDSVTIISAGNDKMVKAWNLNQFQIEADFIGHNSNINTLTASPDGTLIASAGKDGEIMLWNLAAKKAMYTLSAQDEVFSLAFSPNRYWLAAATATGIKVFSLDPQYLVDDLRPEFAGYSKAAEPHAVSLAWSADGQTLFAGYTDNVIRVWQVMTAN | |
| 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 | Acetylation | ------MASNEVLVL ------CCCCEEEEE | 22.51 | 22814378 | |
| 3 | Phosphorylation | -----MASNEVLVLR -----CCCCEEEEEE | 32.02 | 28152593 | |
| 40 | Succinylation | LLSASRDKTLISWKL EEEECCCCEEEEEEE | 44.09 | 23954790 | |
| 40 | 2-Hydroxyisobutyrylation | LLSASRDKTLISWKL EEEECCCCEEEEEEE | 44.09 | - | |
| 40 | Acetylation | LLSASRDKTLISWKL EEEECCCCEEEEEEE | 44.09 | 24489116 | |
| 41 | Phosphorylation | LSASRDKTLISWKLT EEECCCCEEEEEEEC | 33.34 | 22369663 | |
| 44 | Phosphorylation | SRDKTLISWKLTGDD CCCCEEEEEEECCCC | 22.67 | 22369663 | |
| 46 | Acetylation | DKTLISWKLTGDDQK CCEEEEEEECCCCCC | 29.40 | 24489116 | |
| 46 | Succinylation | DKTLISWKLTGDDQK CCEEEEEEECCCCCC | 29.40 | 23954790 | |
| 46 | Ubiquitination | DKTLISWKLTGDDQK CCEEEEEEECCCCCC | 29.40 | 23749301 | |
| 46 | 2-Hydroxyisobutyrylation | DKTLISWKLTGDDQK CCEEEEEEECCCCCC | 29.40 | - | |
| 48 | Phosphorylation | TLISWKLTGDDQKFG EEEEEEECCCCCCCC | 34.53 | 22369663 | |
| 53 | Acetylation | KLTGDDQKFGVPVRS EECCCCCCCCCEEEE | 51.59 | 24489116 | |
| 53 | Ubiquitination | KLTGDDQKFGVPVRS EECCCCCCCCCEEEE | 51.59 | 23749301 | |
| 53 | 2-Hydroxyisobutyrylation | KLTGDDQKFGVPVRS EECCCCCCCCCEEEE | 51.59 | - | |
| 60 | Phosphorylation | KFGVPVRSFKGHSHI CCCCEEEEECCCCCE | 31.38 | 20377248 | |
| 87 | Ubiquitination | ALSASWDKTLRLWDV EEEEECCCEEEEEEC | 43.11 | 23749301 | |
| 88 | Phosphorylation | LSASWDKTLRLWDVA EEEECCCEEEEEECC | 18.03 | 24961812 | |
| 96 | Phosphorylation | LRLWDVATGETYQRF EEEEECCCCCEEHHH | 35.08 | 17287358 | |
| 99 | Phosphorylation | WDVATGETYQRFVGH EECCCCCEEHHHCCC | 26.71 | 17287358 | |
| 107 | Succinylation | YQRFVGHKSDVMSVD EHHHCCCCCCCEEEE | 42.28 | 23954790 | |
| 107 | Acetylation | YQRFVGHKSDVMSVD EHHHCCCCCCCEEEE | 42.28 | 24489116 | |
| 107 | Ubiquitination | YQRFVGHKSDVMSVD EHHHCCCCCCCEEEE | 42.28 | 24961812 | |
| 108 | Phosphorylation | QRFVGHKSDVMSVDI HHHCCCCCCCEEEEC | 29.75 | 21440633 | |
| 112 | Phosphorylation | GHKSDVMSVDIDKKA CCCCCCEEEECCCCE | 19.25 | 21440633 | |
| 117 | 2-Hydroxyisobutyrylation | VMSVDIDKKASMIIS CEEEECCCCEEEEEE | 51.04 | - | |
| 117 | Acetylation | VMSVDIDKKASMIIS CEEEECCCCEEEEEE | 51.04 | 24489116 | |
| 117 | Succinylation | VMSVDIDKKASMIIS CEEEECCCCEEEEEE | 51.04 | 23954790 | |
| 117 | Ubiquitination | VMSVDIDKKASMIIS CEEEECCCCEEEEEE | 51.04 | 23749301 | |
| 118 | Ubiquitination | MSVDIDKKASMIISG EEEECCCCEEEEEEC | 41.78 | 23749301 | |
| 118 | 2-Hydroxyisobutyrylation | MSVDIDKKASMIISG EEEECCCCEEEEEEC | 41.78 | - | |
| 118 | Acetylation | MSVDIDKKASMIISG EEEECCCCEEEEEEC | 41.78 | 24489116 | |
| 120 | Phosphorylation | VDIDKKASMIISGSR EECCCCEEEEEECCC | 21.28 | 22369663 | |
| 124 | Phosphorylation | KKASMIISGSRDKTI CCEEEEEECCCCCEE | 21.57 | 22369663 | |
| 126 | Phosphorylation | ASMIISGSRDKTIKV EEEEEECCCCCEEEE | 30.43 | 22369663 | |
| 129 | Acetylation | IISGSRDKTIKVWTI EEECCCCCEEEEEEE | 51.55 | 25381059 | |
| 129 | Ubiquitination | IISGSRDKTIKVWTI EEECCCCCEEEEEEE | 51.55 | 22817900 | |
| 132 | Ubiquitination | GSRDKTIKVWTIKGQ CCCCCEEEEEEECCH | 36.63 | 23749301 | |
| 132 | Acetylation | GSRDKTIKVWTIKGQ CCCCCEEEEEEECCH | 36.63 | 24489116 | |
| 132 | 2-Hydroxyisobutyrylation | GSRDKTIKVWTIKGQ CCCCCEEEEEEECCH | 36.63 | - | |
| 137 | Acetylation | TIKVWTIKGQCLATL EEEEEEECCHHHHHH | 35.24 | 24489116 | |
| 137 | Ubiquitination | TIKVWTIKGQCLATL EEEEEEECCHHHHHH | 35.24 | 23749301 | |
| 152 | Phosphorylation | LGHNDWVSQVRVVPN HCCCCCEEEEEECCC | 20.78 | 21440633 | |
| 161 | Acetylation | VRVVPNEKADDDSVT EEECCCCCCCCCCEE | 64.85 | 24489116 | |
| 161 | Succinylation | VRVVPNEKADDDSVT EEECCCCCCCCCCEE | 64.85 | 23954790 | |
| 161 | Ubiquitination | VRVVPNEKADDDSVT EEECCCCCCCCCCEE | 64.85 | 23749301 | |
| 166 | Phosphorylation | NEKADDDSVTIISAG CCCCCCCCEEEEEEC | 28.31 | 22369663 | |
| 168 | Phosphorylation | KADDDSVTIISAGND CCCCCCEEEEEECCC | 19.28 | 22369663 | |
| 171 | Phosphorylation | DDSVTIISAGNDKMV CCCEEEEEECCCCEE | 26.69 | 22369663 | |
| 176 | Acetylation | IISAGNDKMVKAWNL EEEECCCCEEEEEEC | 49.98 | 24489116 | |
| 176 | Ubiquitination | IISAGNDKMVKAWNL EEEECCCCEEEEEEC | 49.98 | 23749301 | |
| 228 | Ubiquitination | MLWNLAAKKAMYTLS EEEEHHHHHHHHEEC | 35.14 | 22817900 | |
| 228 | Acetylation | MLWNLAAKKAMYTLS EEEEHHHHHHHHEEC | 35.14 | 24489116 | |
| 228 | Succinylation | MLWNLAAKKAMYTLS EEEEHHHHHHHHEEC | 35.14 | 23954790 | |
| 229 | Ubiquitination | LWNLAAKKAMYTLSA EEEHHHHHHHHEECC | 33.39 | 23749301 | |
| 229 | Acetylation | LWNLAAKKAMYTLSA EEEHHHHHHHHEECC | 33.39 | 24489116 | |
| 264 | Phosphorylation | ATGIKVFSLDPQYLV CCCCEEEEECHHHHH | 34.55 | 21440633 | |
| 281 | Phosphorylation | LRPEFAGYSKAAEPH CCHHHCCCCCCCCCC | 11.99 | 21440633 | |
| 283 | Ubiquitination | PEFAGYSKAAEPHAV HHHCCCCCCCCCCEE | 43.03 | 17644757 |
| 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 GBLP_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GBLP_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 GBLP_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-166 AND THR-168, ANDMASS 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-166 AND THR-168, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96 AND THR-99, AND MASSSPECTROMETRY. | |
