| UniProt ID | ATG1_YEAST | |
|---|---|---|
| UniProt AC | P53104 | |
| Protein Name | Serine/threonine-protein kinase ATG1 {ECO:0000305} | |
| Gene Name | ATG1 {ECO:0000303|PubMed:14536056} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 897 | |
| Subcellular Localization |
Cytoplasm. Preautophagosomal structure membrane Peripheral membrane protein. Formes punctate structures in starvation conditions only when ATG13 and ATG17 were both present. Localizes to both the isolation membrane (IM) and the vacuole-isolation mem |
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| Protein Description | Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Finally, ATG1 is also required for the maintenance of cell viability under starvation and for glycogen storage during stationary phase. Plays a role in genome stability through suppression of abnormal mitosis under starvation, and in regulation of filamentous growth.. | |
| Protein Sequence | MGDIKNKDHTTSVNHNLMASAGNYTAEKEIGKGSFATVYRGHLTSDKSQHVAIKEVSRAKLKNKKLLENLEIEIAILKKIKHPHIVGLIDCERTSTDFYLIMEYCALGDLTFLLKRRKELMENHPLLRTVFEKYPPPSENHNGLHRAFVLSYLQQLASALKFLRSKNLVHRDIKPQNLLLSTPLIGYHDSKSFHELGFVGIYNLPILKIADFGFARFLPNTSLAETLCGSPLYMAPEILNYQKYNAKADLWSVGTVVFEMCCGTPPFRASNHLELFKKIKRANDVITFPSYCNIEPELKELICSLLTFDPAQRIGFEEFFANKVVNEDLSSYELEDDLPELESKSKGIVESNMFVSEYLSKQPKSPNSNLAGHQSMADNPAELSDALKNSNILTAPAVKTDHTQAVDKKASNNKYHNSLVSDRSFEREYVVVEKKSVEVNSLADEVAQAGFNPNPIKHPTSTQNQNVLLNEQFSPNNQQYFQNQGENPRLLRATSSSSGGSDGSRRPSLVDRRLSISSLNPSNALSRALGIASTRLFGGANQQQQQQQITSSPPYSQTLLNSQLFHELTENIILRIDHLQHPETLKLDNTNIVSILESLAAKAFVVYSYAEVKFSQIVPLSTTLKGMANFENRRSMDSNAIAEEQDSDDAEEEDETLKKYKEDCLSTKTFGKGRTLSATSQLSATFNKLPRSEMILLCNEAIVLYMKALSILSKSMQVTSNWWYESQEKSCSLRVNVLVQWLREKFNECLEKADFLRLKINDLRFKHASEVAENQTLEEKGSSEEPVYLEKLLYDRALEISKMAAHMELKGENLYNCELAYATSLWMLETSLDDDDFTNAYGDYPFKTNIHLKSNDVEDKEKYHSVLDENDRIIIRKYIDSIANRLKILRQKMNHQN | |
| 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 | VNHNLMASAGNYTAE CCHHHHHHCCCEEEE | 23.81 | 28889911 | |
| 24 | Phosphorylation | LMASAGNYTAEKEIG HHHHCCCEEEEEEEC | 13.35 | 21551504 | |
| 25 | Phosphorylation | MASAGNYTAEKEIGK HHHCCCEEEEEEECC | 32.13 | 21551504 | |
| 34 | Phosphorylation | EKEIGKGSFATVYRG EEEECCCCEEEEEEC | 18.39 | 21460632 | |
| 129 | Phosphorylation | ENHPLLRTVFEKYPP HHCCHHHHHHHHCCC | 29.53 | 21460632 | |
| 181 | Phosphorylation | KPQNLLLSTPLIGYH CHHHEEECCCEEEEC | 28.13 | 28889911 | |
| 226 | Phosphorylation | PNTSLAETLCGSPLY CCCCHHHHHCCCCCC | 23.03 | 20953146 | |
| 230 | Phosphorylation | LAETLCGSPLYMAPE HHHHHCCCCCCCCHH | 15.67 | 28889911 | |
| 304 | Phosphorylation | ELKELICSLLTFDPA HHHHHHHHHCCCCHH | 21.30 | 21460632 | |
| 330 | Phosphorylation | KVVNEDLSSYELEDD HHHCCCHHHCCCCCC | 43.10 | 28889911 | |
| 345 | Phosphorylation | LPELESKSKGIVESN HHHHHHCCCCCHHCH | 45.45 | 21126336 | |
| 351 | Phosphorylation | KSKGIVESNMFVSEY CCCCCHHCHHHHHHH | 23.77 | 28889911 | |
| 356 | Phosphorylation | VESNMFVSEYLSKQP HHCHHHHHHHHHCCC | 14.84 | 20953146 | |
| 360 | Phosphorylation | MFVSEYLSKQPKSPN HHHHHHHHCCCCCCC | 28.48 | 24961812 | |
| 365 | Phosphorylation | YLSKQPKSPNSNLAG HHHCCCCCCCCCCCC | 35.68 | 22369663 | |
| 368 | Phosphorylation | KQPKSPNSNLAGHQS CCCCCCCCCCCCCHH | 36.28 | 22369663 | |
| 375 | Phosphorylation | SNLAGHQSMADNPAE CCCCCCHHHCCCHHH | 15.40 | 22369663 | |
| 384 | Phosphorylation | ADNPAELSDALKNSN CCCHHHHHHHHHHCC | 16.61 | 20953146 | |
| 390 | Phosphorylation | LSDALKNSNILTAPA HHHHHHHCCCCCCCC | 24.53 | 20953146 | |
| 418 | Phosphorylation | SNNKYHNSLVSDRSF HCCCCCCCCCCCCCC | 19.48 | 20953146 | |
| 421 | Phosphorylation | KYHNSLVSDRSFERE CCCCCCCCCCCCEEE | 32.38 | 24961812 | |
| 424 | Phosphorylation | NSLVSDRSFEREYVV CCCCCCCCCEEEEEE | 36.13 | 20953146 | |
| 436 | Phosphorylation | YVVVEKKSVEVNSLA EEEEEECCEEHHHHH | 34.28 | 20953146 | |
| 441 | Phosphorylation | KKSVEVNSLADEVAQ ECCEEHHHHHHHHHH | 30.06 | 20953146 | |
| 474 | Phosphorylation | VLLNEQFSPNNQQYF EEECCCCCCCHHHHH | 26.81 | 20953146 | |
| 496 | Phosphorylation | RLLRATSSSSGGSDG CEEECCCCCCCCCCC | 24.94 | 27017623 | |
| 497 | Phosphorylation | LLRATSSSSGGSDGS EEECCCCCCCCCCCC | 32.54 | 28889911 | |
| 498 | Phosphorylation | LRATSSSSGGSDGSR EECCCCCCCCCCCCC | 49.47 | 28889911 | |
| 501 | Phosphorylation | TSSSSGGSDGSRRPS CCCCCCCCCCCCCCH | 42.18 | 28889911 | |
| 504 | Phosphorylation | SSGGSDGSRRPSLVD CCCCCCCCCCCHHHC | 30.06 | 20953146 | |
| 508 | Phosphorylation | SDGSRRPSLVDRRLS CCCCCCCHHHCCCCC | 38.93 | 20953146 | |
| 515 | Phosphorylation | SLVDRRLSISSLNPS HHHCCCCCCHHCCHH | 20.72 | 22369663 | |
| 517 | Phosphorylation | VDRRLSISSLNPSNA HCCCCCCHHCCHHHH | 25.95 | 22369663 | |
| 518 | Phosphorylation | DRRLSISSLNPSNAL CCCCCCHHCCHHHHH | 30.42 | 22369663 | |
| 522 | Phosphorylation | SISSLNPSNALSRAL CCHHCCHHHHHHHHH | 33.39 | 22369663 | |
| 526 | Phosphorylation | LNPSNALSRALGIAS CCHHHHHHHHHHHHH | 17.07 | 22369663 | |
| 533 | Phosphorylation | SRALGIASTRLFGGA HHHHHHHHHHHCCCC | 16.49 | 21460632 | |
| 534 | Phosphorylation | RALGIASTRLFGGAN HHHHHHHHHHCCCCC | 23.52 | 30377154 | |
| 551 | Phosphorylation | QQQQQITSSPPYSQT HHHHHHHCCCCCHHH | 42.34 | 21460632 | |
| 552 | Phosphorylation | QQQQITSSPPYSQTL HHHHHHCCCCCHHHH | 22.65 | 21460632 | |
| 590 | Phosphorylation | ETLKLDNTNIVSILE CCCCCCCCCHHHHHH | 26.45 | 21460632 | |
| 594 | Phosphorylation | LDNTNIVSILESLAA CCCCCHHHHHHHHHH | 20.05 | 28889911 | |
| 598 | Phosphorylation | NIVSILESLAAKAFV CHHHHHHHHHHHHHE | 21.62 | 28889911 | |
| 621 | Phosphorylation | FSQIVPLSTTLKGMA HHHEEECCCCHHCHH | 17.18 | 21460632 | |
| 635 | Phosphorylation | ANFENRRSMDSNAIA HCCCCCCCCCHHHHH | 24.57 | 20953146 | |
| 638 | Phosphorylation | ENRRSMDSNAIAEEQ CCCCCCCHHHHHCCC | 21.37 | 20953146 | |
| 647 | Phosphorylation | AIAEEQDSDDAEEED HHHCCCCCCCHHHHH | 36.76 | 20953146 | |
| 656 | Phosphorylation | DAEEEDETLKKYKED CHHHHHHHHHHHHHH | 57.08 | 28889911 | |
| 666 | Phosphorylation | KYKEDCLSTKTFGKG HHHHHHHCCCCCCCC | 33.90 | 20953146 | |
| 667 | Phosphorylation | YKEDCLSTKTFGKGR HHHHHHCCCCCCCCC | 22.58 | 28889911 | |
| 675 | Phosphorylation | KTFGKGRTLSATSQL CCCCCCCEEECHHHH | 33.46 | 25752575 | |
| 677 | Phosphorylation | FGKGRTLSATSQLSA CCCCCEEECHHHHHH | 28.96 | 20953146 | |
| 679 | Phosphorylation | KGRTLSATSQLSATF CCCEEECHHHHHHHH | 17.40 | 20953146 | |
| 680 | Phosphorylation | GRTLSATSQLSATFN CCEEECHHHHHHHHC | 28.92 | 21460632 | |
| 683 | Phosphorylation | LSATSQLSATFNKLP EECHHHHHHHHCCCC | 20.02 | 19823750 | |
| 685 | Phosphorylation | ATSQLSATFNKLPRS CHHHHHHHHCCCCHH | 25.10 | 19779198 | |
| 726 | Phosphorylation | TSNWWYESQEKSCSL CCCCCHHCCCCHHHH | 28.13 | 28889911 | |
| 769 | Phosphorylation | DLRFKHASEVAENQT HHHHHCHHHHHCCCC | 32.12 | 21460632 | |
| 776 | Phosphorylation | SEVAENQTLEEKGSS HHHHCCCCHHHCCCC | 47.95 | 28889911 | |
| 782 | Phosphorylation | QTLEEKGSSEEPVYL CCHHHCCCCCCCCHH | 45.72 | 28889911 | |
| 783 | Phosphorylation | TLEEKGSSEEPVYLE CHHHCCCCCCCCHHH | 55.43 | 20953146 | |
| 801 | Phosphorylation | YDRALEISKMAAHME HHHHHHHHHHHHHCH | 13.65 | 28889911 | |
| 865 | Phosphorylation | EDKEKYHSVLDENDR CCHHHHHHHCCCCCC | 22.68 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 508 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| 515 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
* 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 ATG1_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-365; SER-390; SER-508;SER-515; SER-517; SER-647; SER-677; SER-683 AND SER-783, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASSSPECTROMETRY. | |
