| UniProt ID | EIF3C_YEAST | |
|---|---|---|
| UniProt AC | P32497 | |
| Protein Name | Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002} | |
| Gene Name | NIP1 {ECO:0000255|HAMAP-Rule:MF_03002} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 812 | |
| Subcellular Localization | Cytoplasm . Mainly cytoplasmic. | |
| 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 | MSRFFSSNYEYDVASSSSEEDLLSSSEEDLLSSSSSESELDQESDDSFFNESESESEADVDSDDSDAKPYGPDWFKKSEFRKQGGGSNKFLKSSNYDSSDEESDEEDGKKVVKSAKEKLLDEMQDVYNKISQAENSDDWLTISNEFDLISRLLVRAQQQNWGTPNIFIKVVAQVEDAVNNTQQADLKNKAVARAYNTTKQRVKKVSRENEDSMAKFRNDPESFDKEPTADLDISANGFTISSSQGNDQAVQEDFFTRLQTIIDSRGKKTVNQQSLISTLEELLTVAEKPYEFIMAYLTLIPSRFDASANLSYQPIDQWKSSFNDISKLLSILDQTIDTYQVNEFADPIDFIEDEPKEDSDGVKRILGSIFSFVERLDDEFMKSLLNIDPHSSDYLIRLRDEQSIYNLILRTQLYFEATLKDEHDLERALTRPFVKRLDHIYYKSENLIKIMETAAWNIIPAQFKSKFTSKDQLDSADYVDNLIDGLSTILSKQNNIAVQKRAILYNIYYTALNKDFQTAKDMLLTSQVQTNINQFDSSLQILFNRVVVQLGLSAFKLCLIEECHQILNDLLSSSHLREILGQQSLHRISLNSSNNASADERARQCLPYHQHINLDLIDVVFLTCSLLIEIPRMTAFYSGIKVKRIPYSPKSIRRSLEHYDKLSFQGPPETLRDYVLFAAKSMQKGNWRDSVKYLREIKSWALLPNMETVLNSLTERVQVESLKTYFFSFKRFYSSFSVAKLAELFDLPENKVVEVLQSVIAELEIPAKLNDEKTIFVVEKGDEITKLEEAMVKLNKEYKIAKERLNPPSNRR | |
| 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 |
|---|---|---|---|---|---|
| 89 | Acetylation | KQGGGSNKFLKSSNY HCCCCCCCCHHHCCC | 54.49 | 25381059 | |
| 93 | Phosphorylation | GSNKFLKSSNYDSSD CCCCCHHHCCCCCCC | 26.43 | 22890988 | |
| 94 | Phosphorylation | SNKFLKSSNYDSSDE CCCCHHHCCCCCCCC | 37.51 | 22890988 | |
| 96 | Phosphorylation | KFLKSSNYDSSDEES CCHHHCCCCCCCCCC | 21.10 | 22890988 | |
| 98 | Phosphorylation | LKSSNYDSSDEESDE HHHCCCCCCCCCCCH | 29.36 | 25521595 | |
| 99 | Phosphorylation | KSSNYDSSDEESDEE HHCCCCCCCCCCCHH | 46.25 | 25521595 | |
| 103 | Phosphorylation | YDSSDEESDEEDGKK CCCCCCCCCHHHHHH | 48.55 | 25521595 | |
| 118 | Acetylation | VVKSAKEKLLDEMQD HHHHHHHHHHHHHHH | 54.35 | 24489116 | |
| 118 | Ubiquitination | VVKSAKEKLLDEMQD HHHHHHHHHHHHHHH | 54.35 | 15699485 | |
| 129 | Ubiquitination | EMQDVYNKISQAENS HHHHHHHHHHHCCCC | 26.50 | 15699485 | |
| 136 | Phosphorylation | KISQAENSDDWLTIS HHHHCCCCCCCEECC | 28.58 | 28889911 | |
| 169 | Ubiquitination | GTPNIFIKVVAQVED CCCCEEEEEHHHHHH | 21.65 | 17644757 | |
| 187 | Ubiquitination | NTQQADLKNKAVARA HCHHHHHHHHHHHHH | 57.88 | 23749301 | |
| 187 | Acetylation | NTQQADLKNKAVARA HCHHHHHHHHHHHHH | 57.88 | 24489116 | |
| 228 | Phosphorylation | ESFDKEPTADLDISA HHCCCCCCCCEEEEC | 33.62 | 27214570 | |
| 243 | Phosphorylation | NGFTISSSQGNDQAV CCEEEECCCCCCHHH | 35.00 | 27214570 | |
| 382 | Ubiquitination | RLDDEFMKSLLNIDP HCCHHHHHHHHCCCC | 43.18 | 17644757 | |
| 443 | Acetylation | RLDHIYYKSENLIKI HCHHHEECCHHHHHH | 34.03 | 24489116 | |
| 500 | Succinylation | QNNIAVQKRAILYNI CCCHHHHHHHHHHHH | 36.88 | 23954790 | |
| 500 | Ubiquitination | QNNIAVQKRAILYNI CCCHHHHHHHHHHHH | 36.88 | 23749301 | |
| 514 | Methylation | IYYTALNKDFQTAKD HHHHHHCCCHHHHHH | 61.85 | 20137074 | |
| 589 | Phosphorylation | QQSLHRISLNSSNNA CCCCEEEECCCCCCC | 22.81 | 28889911 | |
| 592 | Phosphorylation | LHRISLNSSNNASAD CEEEECCCCCCCCHH | 39.47 | 28889911 | |
| 597 | Phosphorylation | LNSSNNASADERARQ CCCCCCCCHHHHHHH | 38.07 | 28889911 | |
| 647 | Phosphorylation | IKVKRIPYSPKSIRR CEEEECCCCHHHHHH | 34.92 | 21440633 | |
| 648 | Phosphorylation | KVKRIPYSPKSIRRS EEEECCCCHHHHHHH | 22.09 | 21440633 | |
| 661 | Acetylation | RSLEHYDKLSFQGPP HHHHHHHHHCCCCCC | 38.57 | 24489116 | |
| 661 | Ubiquitination | RSLEHYDKLSFQGPP HHHHHHHHHCCCCCC | 38.57 | 24961812 | |
| 692 | Ubiquitination | GNWRDSVKYLREIKS CCHHHHHHHHHHHHH | 42.38 | 23749301 | |
| 698 | Ubiquitination | VKYLREIKSWALLPN HHHHHHHHHHHHCCC | 34.88 | 15699485 | |
| 740 | Ubiquitination | YSSFSVAKLAELFDL HHHCCHHHHHHHCCC | 46.18 | 15699485 | |
| 751 | Ubiquitination | LFDLPENKVVEVLQS HCCCCCCHHHHHHHH | 46.10 | 15699485 | |
| 768 | Ubiquitination | AELEIPAKLNDEKTI HHCCCCCCCCCCCEE | 42.33 | 15699485 | |
| 773 | Ubiquitination | PAKLNDEKTIFVVEK CCCCCCCCEEEEEEC | 50.19 | 15699485 | |
| 809 | Phosphorylation | KERLNPPSNRR---- HHHCCCCCCCC---- | 44.20 | 17287358 |
| 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 EIF3C_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EIF3C_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 EIF3C_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-98; SER-99 AND SER-103,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-98; SER-99 AND SER-103,AND MASS 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 SER-809, AND MASSSPECTROMETRY. | |
| "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-98; SER-99 AND SER-103,AND MASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-99 AND SER-103,AND MASS SPECTROMETRY. | |
