ATG1_SCHPO - dbPTM
ATG1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG1_SCHPO
UniProt AC Q9Y7T4
Protein Name Serine/threonine-protein kinase atg1 {ECO:0000312|PomBase:SPCC63.08c}
Gene Name atg1 {ECO:0000312|PomBase:SPCC63.08c}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 830
Subcellular Localization Cytoplasm. Preautophagosomal structure membrane
Peripheral membrane protein.
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 (By similarity). Autophagy functions to supply nitrogen and is activated when cells cannot access exogenous nitrogen, thus ensuring that they can adapt and subsequently propagate. Finally, atg13 is also required for glycogen storage during stationary phase and has a role in meiosis and sporulation..
Protein Sequence MNLQTSTNQTIGPYVIRSEIGRGSFAIVYKGKHTETNRVISIKSVLTKKLTKKLLENLESEISILKEIRHVHVVELIDCIKAGRFIHLVMEYCSLGDLSYFIRKREKFNSIPSLAWINIDHPPVYKAGLNETLVRHFTQQLASALQFLRSRSLIHRDVKPQNLLLQPPPTAAYLEEHPQFVGSPKLPMLKLADFGFARYLQTSSMAETLCGSPLYMAPEILRYEKYDAKADLWSVGAVLYEMAVGKPPFKAPNHVELLRRIQKAKDVIKFPEEAFIHPDIKTLICALLKQNPADRIDYDGFFSSIVVTTPLDDASTLTGSDIQDAVKEINIPSSSPAYITDFFPKSNPGAPAPPGGLLRQAFQAQGSSIQPSEITGRRVPHRYAQDGNTLPYTPVFPPESAPAASIFPPRLTSKQPIPMASPAKLTSDTSNKSSAYVVVDHHPIISSTQLSNESLTHEQSINGNSPSPNEGVFQGSFSPESAPVNNHAFPHTSRMQIPYMKPNAFPSNPTYIASTPVTQLRRAFEQATAHVPQSGGGARNKSALERALNVANARLNEVVVDGMTDNGNTSLPTKESNLDNNVNIIQPSLPDTGKRLLDVLESIAMKSNSVYHLAEVKLAQIIPSLSDEMKPGDTLLDRPLTPFSLVMLAKESYVLYERDIELLQVAFDGVAAFWANSEERASPDCQQAIEWFRQRYSESLEKSQFLREIIISQSAAHSLPTTKPVSASQLIYHRALDLSRNAATSELSGNDAQACLQNYRLAAHLLESLLESNFSTPDGANDSNNSVTIRNLIALITKRQELLQSKQIQANVANKVTESVAKITLAPNLA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
333PhosphorylationVKEINIPSSSPAYIT
HHHCCCCCCCCCEEE
39.3824763107
334PhosphorylationKEINIPSSSPAYITD
HHCCCCCCCCCEEEC
34.6825720772
335PhosphorylationEINIPSSSPAYITDF
HCCCCCCCCCEEECC
20.2125720772
338PhosphorylationIPSSSPAYITDFFPK
CCCCCCCEEECCCCC
14.0325720772
340PhosphorylationSSSPAYITDFFPKSN
CCCCCEEECCCCCCC
17.6829996109
346PhosphorylationITDFFPKSNPGAPAP
EECCCCCCCCCCCCC
48.7928889911
367PhosphorylationQAFQAQGSSIQPSEI
HHHHHCCCCCCHHHC
16.5225720772
368PhosphorylationAFQAQGSSIQPSEIT
HHHHCCCCCCHHHCC
31.8725720772
400PhosphorylationTPVFPPESAPAASIF
CCCCCCCCCCHHHCC
45.3829996109
427PhosphorylationASPAKLTSDTSNKSS
CCCCCCCCCCCCCCC
49.6927738172
534PhosphorylationATAHVPQSGGGARNK
HHCCCCCCCCCCCCH
33.0829996109

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 ATG1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATG1_SCHPO !!

Disease-associated PTM Sites based on SAP

* 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_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YKW3_SCHPObop1genetic
22681890
CCH1_SCHPOcch1genetic
22681890
YOI5_SCHPOSPBC1778.05cgenetic
22681890
YKZ2_SCHPOSPAC15E1.02cgenetic
22681890
YNU4_SCHPOSPBC28E12.04genetic
22681890
PYP1_SCHPOpyp1genetic
22681890
ALY1_SCHPOSPBC839.02genetic
22681890
NUP60_SCHPOnup60genetic
22681890
YFH9_SCHPOSPAC23A1.09genetic
22681890
YAI8_SCHPOSPAC24B11.08cgenetic
22681890
MGR2_SCHPOmgr2genetic
22681890
RAD55_SCHPOrad55genetic
22681890
UBP11_SCHPOubp11genetic
22681890
YDH1_SCHPOSPAC6G9.01cgenetic
22681890
YIQ4_SCHPOSPAC824.04genetic
22681890
YGRG_SCHPOSPBC365.16genetic
22681890
YLO2_SCHPOtma23genetic
22681890
YLV1_SCHPOSPAC2H10.01genetic
22681890
GIT3_SCHPOgit3genetic
22681890
PPK4_SCHPOire1genetic
22681890
ATG11_SCHPOatg11genetic
22681890
TRX2_SCHPOtrx2genetic
22681890
UBC13_SCHPOubc13genetic
22681890
AP3D_SCHPOapl5genetic
22681890
SGF73_SCHPOsgf73genetic
22681890
PNK1_SCHPOpnk1genetic
22681890
RCF2_SCHPOSPAC1565.01genetic
22681890
ZFS1_SCHPOzfs1genetic
22681890
NU124_SCHPOnup124genetic
22681890
ATP14_SCHPOatp14genetic
22681890
PPZ_SCHPOpzh1genetic
22681890
ATP11_SCHPOatp11genetic
22681890
CAND1_SCHPOknd1genetic
22681890
EME1_SCHPOeme1genetic
22681890
YC84_SCHPOSPCC622.04genetic
22681890
ETFA_SCHPOetf1genetic
22681890
YCPE_SCHPOtrp663genetic
22681890
BUD23_SCHPObud23genetic
22681890
YA99_SCHPOSPAC13G6.09genetic
22681890
BLT1_SCHPOblt1genetic
22681890
YJC7_SCHPOSPCC736.07cgenetic
22681890
YLA3_SCHPOSPAC1527.03genetic
22681890
YOM1_SCHPOSPBPB7E8.01genetic
22681890
PRZ1_SCHPOprz1genetic
22681890
CSK1_SCHPOcsk1genetic
22681890
YLF8_SCHPOSPAC30C2.08genetic
22681890
YJE6_SCHPOSPCC1682.06genetic
22681890
ULP1_SCHPOulp1genetic
22681890
LYS12_SCHPOlys12genetic
22681890

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATG1_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346, AND MASSSPECTROMETRY.

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