| UniProt ID | IES1_YEAST | |
|---|---|---|
| UniProt AC | P43579 | |
| Protein Name | Ino eighty subunit 1 | |
| Gene Name | IES1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 692 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin-remodeling complex.. | |
| Protein Sequence | MGKRVYDPIHDTFQLREDNSDETKADSPMQSVKSGSQEEASPSSIQSETETVTTKSIPVIHEIEIDDKNDDDSTQSEEENTNILLNFEPSTVPEATGASTATGPVTTNTVRRKPKESNASKYNRHLKKPDGEPFNRKDIQFSFMQELLMDKRQIFTNVLKPLYKNSIVPINIDGDKLSINVTDKEYDARTFVFNDKLTFAQLYVLTIATSIKCSKILRDKLLLDQQVAFSTCVLALLVNIGRLNTTINFYLEMTSQLRTFHSVPVLQLHANDPKLLQDTPRLKSILKNLPWGNEQLSLMETYKKVDQNDGEVDTVNKFNIINMLFSICDNSGLIDKRFLSKYVEVESKAQEQDMVDEQNEVKETEAENEKQESKAAYATTLFDILDYSKYEPKDRSNILIWLLYIHLETNLSQEEVEESVRFFNGLEDGAPAGKFILRCTERSYDTDPEDELEFGANQRIKRREFMSKMEEGRKRERTNVTEVKKPSIGGDKSEEDGEGEDDKSEETVEETRSLLTPTPILESSSPMTLNRKKVTPQLPKVTPAAPTETEEEITSAAIIDKNDLNLTPLKKYNSSATVNKVDKLISLDLNKHVSENGKTQEEFLADLKKSQVPNRLKRRDIGLIKIFNEFEDIPVASVLGIRGKKRKKFKDNLLGFETDFMKNLGASKKVLLNKIERAEIDDEEATAMFKLE | |
| 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 |
|---|---|---|---|---|---|
| 20 | Phosphorylation | FQLREDNSDETKADS EECCCCCCCCCCCCC | 49.50 | 22369663 | |
| 23 | Phosphorylation | REDNSDETKADSPMQ CCCCCCCCCCCCCCC | 36.20 | 22369663 | |
| 27 | Phosphorylation | SDETKADSPMQSVKS CCCCCCCCCCCCCCC | 27.42 | 22369663 | |
| 31 | Phosphorylation | KADSPMQSVKSGSQE CCCCCCCCCCCCCCC | 25.84 | 22369663 | |
| 34 | Phosphorylation | SPMQSVKSGSQEEAS CCCCCCCCCCCCCCC | 41.33 | 22369663 | |
| 36 | Phosphorylation | MQSVKSGSQEEASPS CCCCCCCCCCCCCCC | 41.32 | 22369663 | |
| 41 | Phosphorylation | SGSQEEASPSSIQSE CCCCCCCCCCCCCCC | 28.70 | 20377248 | |
| 43 | Phosphorylation | SQEEASPSSIQSETE CCCCCCCCCCCCCCE | 37.26 | 20377248 | |
| 44 | Phosphorylation | QEEASPSSIQSETET CCCCCCCCCCCCCEE | 28.21 | 20377248 | |
| 47 | Phosphorylation | ASPSSIQSETETVTT CCCCCCCCCCEEEEC | 44.83 | 20377248 | |
| 49 | Phosphorylation | PSSIQSETETVTTKS CCCCCCCCEEEECCC | 42.05 | 22369663 | |
| 51 | Phosphorylation | SIQSETETVTTKSIP CCCCCCEEEECCCCC | 30.49 | 20377248 | |
| 53 | Phosphorylation | QSETETVTTKSIPVI CCCCEEEECCCCCEE | 35.61 | 22369663 | |
| 54 | Phosphorylation | SETETVTTKSIPVIH CCCEEEECCCCCEEE | 20.61 | 22369663 | |
| 443 | Phosphorylation | ILRCTERSYDTDPED EEEECCCCCCCCCHH | 22.56 | 22369663 | |
| 444 | Phosphorylation | LRCTERSYDTDPEDE EEECCCCCCCCCHHH | 29.14 | 22369663 | |
| 446 | Phosphorylation | CTERSYDTDPEDELE ECCCCCCCCCHHHCC | 45.26 | 22369663 | |
| 481 | Phosphorylation | KRERTNVTEVKKPSI CCCCCCCCEECCCCC | 36.81 | 29136822 | |
| 487 | Phosphorylation | VTEVKKPSIGGDKSE CCEECCCCCCCCCCC | 42.62 | 17330950 | |
| 493 | Phosphorylation | PSIGGDKSEEDGEGE CCCCCCCCCCCCCCC | 51.46 | 17330950 | |
| 504 | Phosphorylation | GEGEDDKSEETVEET CCCCCCCCCHHHHHH | 47.89 | 17330950 | |
| 507 | Phosphorylation | EDDKSEETVEETRSL CCCCCCHHHHHHHHH | 29.21 | 17563356 | |
| 511 | Phosphorylation | SEETVEETRSLLTPT CCHHHHHHHHHCCCC | 16.44 | 19795423 | |
| 513 | Phosphorylation | ETVEETRSLLTPTPI HHHHHHHHHCCCCCC | 34.84 | 22369663 | |
| 516 | Phosphorylation | EETRSLLTPTPILES HHHHHHCCCCCCCCC | 30.34 | 22369663 | |
| 518 | Phosphorylation | TRSLLTPTPILESSS HHHHCCCCCCCCCCC | 20.09 | 22369663 | |
| 523 | Phosphorylation | TPTPILESSSPMTLN CCCCCCCCCCCCCCC | 32.44 | 23749301 | |
| 524 | Phosphorylation | PTPILESSSPMTLNR CCCCCCCCCCCCCCC | 29.14 | 22369663 | |
| 525 | Phosphorylation | TPILESSSPMTLNRK CCCCCCCCCCCCCCC | 28.15 | 22369663 | |
| 528 | Phosphorylation | LESSSPMTLNRKKVT CCCCCCCCCCCCCCC | 25.02 | 22369663 | |
| 535 | Phosphorylation | TLNRKKVTPQLPKVT CCCCCCCCCCCCCCC | 17.75 | 22369663 | |
| 547 | Phosphorylation | KVTPAAPTETEEEIT CCCCCCCCCCHHHHH | 51.30 | 24961812 | |
| 549 | Phosphorylation | TPAAPTETEEEITSA CCCCCCCCHHHHHHH | 51.69 | 24961812 | |
| 554 | Phosphorylation | TETEEEITSAAIIDK CCCHHHHHHHEEECC | 18.65 | 24961812 | |
| 555 | Phosphorylation | ETEEEITSAAIIDKN CCHHHHHHHEEECCC | 22.74 | 24961812 | |
| 567 | Phosphorylation | DKNDLNLTPLKKYNS CCCCCCCCCCCCCCC | 26.04 | 22369663 | |
| 571 | Acetylation | LNLTPLKKYNSSATV CCCCCCCCCCCCCCC | 58.30 | 25381059 | |
| 572 | Phosphorylation | NLTPLKKYNSSATVN CCCCCCCCCCCCCCC | 20.77 | 21440633 | |
| 574 | Phosphorylation | TPLKKYNSSATVNKV CCCCCCCCCCCCCCC | 20.47 | 21440633 | |
| 575 | Phosphorylation | PLKKYNSSATVNKVD CCCCCCCCCCCCCCC | 25.07 | 25752575 | |
| 577 | Phosphorylation | KKYNSSATVNKVDKL CCCCCCCCCCCCCHH | 26.93 | 21440633 | |
| 580 | Acetylation | NSSATVNKVDKLISL CCCCCCCCCCHHHHC | 47.69 | 22865919 | |
| 583 | Acetylation | ATVNKVDKLISLDLN CCCCCCCHHHHCCCH | 51.19 | 24489116 | |
| 674 | Acetylation | SKKVLLNKIERAEID CHHHHHHHHHHHCCC | 46.01 | 24489116 |
| 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 IES1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IES1_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 IES1_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-34; SER-36; SER-47;SER-443; THR-446; THR-516; THR-567 AND SER-574, 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-27; SER-493; SER-504 ANDTHR-507, AND MASS SPECTROMETRY. | |