| UniProt ID | NACA_YEAST | |
|---|---|---|
| UniProt AC | P38879 | |
| Protein Name | Nascent polypeptide-associated complex subunit alpha | |
| Gene Name | EGD2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 174 | |
| Subcellular Localization | Cytoplasm. Nucleus. Predominantly cytoplasmic, may also transiently localize to the nucleus. Nuclear import may occur via redundant pathways including one requiring the karyopherins PSE1 and KAP123, which also participate in nuclear import of ribosom | |
| Protein Description | Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD2 may also be involved in transcription regulation.. | |
| Protein Sequence | MSAIPENANVTVLNKNEKKARELIGKLGLKQIPGIIRVTFRKKDNQIYAIEKPEVFRSAGGNYVVFGEAKVDNFTQKLAAAQQQAQASGIMPSNEDVATKSPEDIQADMQAAAEGSVNAAAEEDDEEGEVDAGDLNKDDIELVVQQTNVSKNQAIKALKAHNGDLVNAIMSLSK | |
| 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 | ------MSAIPENAN ------CCCCCCCCC | 34.60 | 22814378 | |
| 2 | Phosphorylation | ------MSAIPENAN ------CCCCCCCCC | 34.60 | 24909858 | |
| 15 | Succinylation | ANVTVLNKNEKKARE CCCEECCCCHHHHHH | 63.42 | 23954790 | |
| 15 | Acetylation | ANVTVLNKNEKKARE CCCEECCCCHHHHHH | 63.42 | 22865919 | |
| 26 | 2-Hydroxyisobutyrylation | KARELIGKLGLKQIP HHHHHHHHHCHHCCC | 32.18 | - | |
| 26 | Acetylation | KARELIGKLGLKQIP HHHHHHHHHCHHCCC | 32.18 | 24489116 | |
| 30 | Acetylation | LIGKLGLKQIPGIIR HHHHHCHHCCCCEEE | 44.37 | 24489116 | |
| 30 | Ubiquitination | LIGKLGLKQIPGIIR HHHHHCHHCCCCEEE | 44.37 | 23749301 | |
| 43 | 2-Hydroxyisobutyrylation | IRVTFRKKDNQIYAI EEEEEECCCCEEEEE | 58.62 | - | |
| 48 | Phosphorylation | RKKDNQIYAIEKPEV ECCCCEEEEEECCEE | 7.55 | 30377154 | |
| 52 | Succinylation | NQIYAIEKPEVFRSA CEEEEEECCEEEECC | 40.12 | 23954790 | |
| 52 | Acetylation | NQIYAIEKPEVFRSA CEEEEEECCEEEECC | 40.12 | 24489116 | |
| 52 | Ubiquitination | NQIYAIEKPEVFRSA CEEEEEECCEEEECC | 40.12 | 22817900 | |
| 58 | Phosphorylation | EKPEVFRSAGGNYVV ECCEEEECCCCCEEE | 21.57 | 17287358 | |
| 63 | Phosphorylation | FRSAGGNYVVFGEAK EECCCCCEEEECEEE | 10.98 | 21082442 | |
| 70 | Acetylation | YVVFGEAKVDNFTQK EEEECEEEECCHHHH | 45.91 | 24489116 | |
| 75 | Phosphorylation | EAKVDNFTQKLAAAQ EEEECCHHHHHHHHH | 30.92 | 28889911 | |
| 77 | Acetylation | KVDNFTQKLAAAQQQ EECCHHHHHHHHHHH | 36.72 | 24489116 | |
| 88 | Phosphorylation | AQQQAQASGIMPSNE HHHHHHHCCCCCCCH | 19.44 | 24909858 | |
| 93 | Phosphorylation | QASGIMPSNEDVATK HHCCCCCCCHHHHCC | 35.16 | 22369663 | |
| 99 | Phosphorylation | PSNEDVATKSPEDIQ CCCHHHHCCCHHHHH | 31.72 | 24909858 | |
| 101 | Phosphorylation | NEDVATKSPEDIQAD CHHHHCCCHHHHHHH | 29.21 | 27214570 | |
| 116 | Phosphorylation | MQAAAEGSVNAAAEE HHHHHHCCCCCCHHC | 12.05 | 24909858 | |
| 151 | Ubiquitination | VQQTNVSKNQAIKAL EEECCCCHHHHHHHH | 49.12 | 22817900 | |
| 156 | Ubiquitination | VSKNQAIKALKAHNG CCHHHHHHHHHHCCC | 51.16 | 23749301 | |
| 156 | Acetylation | VSKNQAIKALKAHNG CCHHHHHHHHHHCCC | 51.16 | 22865919 | |
| 156 | 2-Hydroxyisobutyrylation | VSKNQAIKALKAHNG CCHHHHHHHHHHCCC | 51.16 | - | |
| 159 | Ubiquitination | NQAIKALKAHNGDLV HHHHHHHHHCCCHHH | 53.08 | 24961812 | |
| 171 | Phosphorylation | DLVNAIMSLSK---- HHHHHHHHHCC---- | 24.31 | 22369663 | |
| 173 | Phosphorylation | VNAIMSLSK------ HHHHHHHCC------ | 29.07 | 22369663 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NACA_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 NACA_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 THR-99 AND SER-101, AND MASSSPECTROMETRY. | |
| "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-58, AND MASSSPECTROMETRY. | |
