| UniProt ID | ELG1_YEAST | |
|---|---|---|
| UniProt AC | Q12050 | |
| Protein Name | Telomere length regulation protein ELG1 | |
| Gene Name | ELG1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 791 | |
| Subcellular Localization | Nucleus . Chromosome, telomere . | |
| Protein Description | Involved in the negative control of telomere length and in telomeric silencing through a replication-mediated pathway. May have a role in Okazaki fragment maturation. Required for S-phase progression. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair.. | |
| Protein Sequence | MKRHVSLSDILTGNKRKVRRQDALQITIDDENDTESGTFDARTAKHDDSSVIFLNHSVVKPIEAVSTNHKSAKEFLMTKRTKEKCDDDDDDLIVISDKSPKSETNCSKIALSQEHEDDISIISTSRIKSSLLNERASKIKNFLKHETTDTFKRLNSISKLNEIEPPLPLHQSIFPVGDKELSDRSVDIPLPFRTIPPLNHNFLPSDYESLKDKNSASCIPVRYQAPVLLGTNIKRNTTLTWPQLFKPVTLKQVLIEPKLKLRIKNWIETSFHTLEKPTLRNRLLNRINPNKQQGSGDELANFIVPDLEEDENLRPDFYRNGEANSSLSEFVPLMILHGNSIGKKTLIQTIMREIAGDDNSYQIYEVNSNMNRSKKDLLDILLDFTTTHYVKDSSKRKSDYGLVLFNDVDVLFKEHDRGYWAMISKLCEFSRRPLVLTCKDLSLVPSELIALASEQNSLFHTKKISTSTVYAFLTKYLKSLEIEVCDDWLRDVVKQNNADIRKCLMHLQFWCVDTEADLISSKNRLPVLTSTLGSSVKDISQLTDLLSINDVIGQATLNRSMVRQEIDSTTMTPEKVNTFQDQNLDDEMKLKFDYVIDYKLHLNDPNRQPLLPFELNIYQHIQEQLEARYSYVREANHRLDNEYLVNRFKKMTESTLNFLASRIPKYDHLQSARRTRNSKKISDILNQFKGIYNDETLNENAEIDLLSATTQQIKAEINPFVFEIAKSDANVKNENKQIFELHSENVSERRYKDLVYQLSQEGVLKNVWFNADPSIVVRKWEHLHSGFSKNK | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MKRHVSLSDILTG --CCCCCCHHHHHCC | 18.94 | 22369663 | |
| 8 | Phosphorylation | MKRHVSLSDILTGNK CCCCCCHHHHHCCCC | 18.33 | 22369663 | |
| 38 | Phosphorylation | ENDTESGTFDARTAK CCCCCCCEEECEECC | 27.85 | 25371407 | |
| 96 | Phosphorylation | DDDLIVISDKSPKSE CCCEEEECCCCCCCC | 28.26 | 30377154 | |
| 99 | Phosphorylation | LIVISDKSPKSETNC EEEECCCCCCCCCCC | 42.42 | 27017623 | |
| 112 | Phosphorylation | NCSKIALSQEHEDDI CCCCCCCCCCCCCCC | 25.22 | 28889911 | |
| 129 | Phosphorylation | ISTSRIKSSLLNERA EEHHHHHHHHHHHHH | 24.69 | 30377154 | |
| 223 | Phosphorylation | ASCIPVRYQAPVLLG CCCCEEEECCCEEEC | 14.84 | 27214570 | |
| 231 | Phosphorylation | QAPVLLGTNIKRNTT CCCEEECCCCCCCCC | 33.47 | 27214570 | |
| 360 | Phosphorylation | EIAGDDNSYQIYEVN HHHCCCCCEEEEECC | 25.96 | 30377154 | |
| 364 | Phosphorylation | DDNSYQIYEVNSNMN CCCCEEEEECCCCCC | 9.78 | 30377154 | |
| 368 | Phosphorylation | YQIYEVNSNMNRSKK EEEEECCCCCCCCHH | 42.50 | 30377154 | |
| 465 | Phosphorylation | LFHTKKISTSTVYAF CCCCCCCCHHHHHHH | 25.78 | 27017623 | |
| 529 | Phosphorylation | KNRLPVLTSTLGSSV CCCCCHHHHCCCCCC | 21.65 | 19823750 | |
| 530 | Phosphorylation | NRLPVLTSTLGSSVK CCCCHHHHCCCCCCC | 19.92 | 19823750 | |
| 531 | Phosphorylation | RLPVLTSTLGSSVKD CCCHHHHCCCCCCCC | 29.87 | 19823750 | |
| 534 | Phosphorylation | VLTSTLGSSVKDISQ HHHHCCCCCCCCHHH | 34.76 | 19823750 | |
| 535 | Phosphorylation | LTSTLGSSVKDISQL HHHCCCCCCCCHHHH | 31.24 | 19823750 | |
| 682 | Phosphorylation | TRNSKKISDILNQFK HCCHHHHHHHHHHHC | 27.72 | 21440633 | |
| 779 | Acetylation | DPSIVVRKWEHLHSG CHHHHHCCHHHHHCC | 45.37 | 22865919 |
| 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 ELG1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ELG1_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 ELG1_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-112, 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-6, AND MASSSPECTROMETRY. | |
