| UniProt ID | ECO1_YEAST | |
|---|---|---|
| UniProt AC | P43605 | |
| Protein Name | N-acetyltransferase ECO1 | |
| Gene Name | ECO1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 281 | |
| Subcellular Localization | Nucleus . Associated with chromatin. | |
| Protein Description | Required for establishment of sister chromatid cohesion during S phase but not for its further maintenance during G2 or M phases or for loading the cohesin complex onto DNA. Interacts with the three known alternate replication factor C (RFC) complexes, suggesting that these complexes have essential but redundant activity in cohesion establishment. Acts by acetylating the cohesin complex component SMC3. In vitro, possesses acetyltransferase activity where it can acetylate itself and components of the cohesin complex (MCD1, IRR1 and PDS5), but is unable to acetylate histones.. | |
| Protein Sequence | MKARKSQRKAGSKPNLIQSKLQVNNGSKSNKIVKCDKCEMSYSSTSIEDRAIHEKYHTLQLHGRKWSPNWGSIVYTERNHSRTVHLSRSTGTITPLNSSPLKKSSPSITHQEEKIVYVRPDKSNGEVRAMTEIMTLVNNELNAPHDENVIWNSTTEEKGKAFVYIRNDRAVGIIIIENLYGGNGKTSSRGRWMVYDSRRLVQNVYPDFKIGISRIWVCRTARKLGIATKLIDVARENIVYGEVIPRYQVAWSQPTDSGGKLASKYNGIMHKSGKLLLPVYI | |
| 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 |
|---|---|---|---|---|---|
| 98 | Phosphorylation | GTITPLNSSPLKKSS CCEECCCCCCCCCCC | 40.80 | 28889911 | |
| 99 | Phosphorylation | TITPLNSSPLKKSSP CEECCCCCCCCCCCC | 32.93 | 23749301 | |
| 164 | Phosphorylation | EKGKAFVYIRNDRAV CCCCEEEEEECCCEE | 6.42 | 21126336 | |
| 223 | Acetylation | WVCRTARKLGIATKL HHHHHHHHHCCHHHH | 48.91 | 11864574 |
| 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 ECO1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ECO1_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 ECO1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Eco1 is a novel acetyltransferase that can acetylate proteinsinvolved in cohesion."; Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H.,Nasmyth K.; Curr. Biol. 12:323-328(2002). Cited for: ACETYLATION AT LYS-223, ENZYME ACTIVITY, AND MUTAGENESIS OF GLY-211;222-ARG-LYS-223; GLY-225 AND ASP-232. | |
