ATG13_YEAST - dbPTM
ATG13_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG13_YEAST
UniProt AC Q06628
Protein Name Autophagy-related protein 13
Gene Name ATG13
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 738
Subcellular Localization Cytoplasm . Preautophagosomal structure .
Protein Description Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Required for autophosphorylation of ATG1 at 'Thr-226' and its dimerization. May also be involved in the regulation of autophagy through SNF1. Involved in ATG9 and ATG23 cycling through the pre-autophagosomal structure. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase..
Protein Sequence MVAEEDIEKQVLQLIDSFFLKTTLLICSTESSRYQSSTENIFLFDDTWFEDHSELVSELPEIISKWSHYDGRKELPPLVVETYLDLRQLNSSHLVRLKDHEGHLWNVCKGTKKQEIVMERWLIELDNSSPTFKSYSEDETDVNELSKQLVLLFRYLLTLIQLLPTTELYQLLIKSYNGPQNEGSSNPITSTGPLVSIRTCVLDGSKPILSKGRIGLSKPIINTYSNALNESNLPAHLDQKKITPVWTKFGLLRVSVSYRRDWKFEINNTNDELFSARHASVSHNSQGPQNQPEQEGQSDQDIGKRQPQFQQQQQPQQQQQQQQQQQRQHQVQTQQQRQIPDRRSLSLSPCTRANSFEPQSWQKKVYPISRPVQPFKVGSIGSQSASRNPSNSSFFNQPPVHRPSMSSNYGPQMNIEGTSVGSTSKYSSSFGNIRRHSSVKTTENAEKVSKAVKSPLQPQESQEDLMDFVKLLEEKPDLTIKKTSGNNPPNINISDSLIRYQNLKPSNDLLSEDLSVSLSMDPNHTYHRGRSDSHSPLPSISPSMHYGSLNSRMSQGANASHLIARGGGNSSTSALNSRRNSLDKSSNKQGMSGLPPIFGGESTSYHHDNKIQKYNQLGVEEDDDDENDRLLNQMGNSATKFKSSISPRSIDSISSSFIKSRIPIRQPYHYSQPTTAPFQAQAKFHKPANKLIDNGNRSNSNNNNHNGNDAVGVMHNDEDDQDDDLVFFMSDMNLSKEG
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
248AcetylationKITPVWTKFGLLRVS
CCCCHHHCCCEEEEE		23.0224489116
280PhosphorylationLFSARHASVSHNSQG
HHEEEEECCCCCCCC		20.3022890988
282PhosphorylationSARHASVSHNSQGPQ
EEEEECCCCCCCCCC		17.9222890988
285PhosphorylationHASVSHNSQGPQNQP
EECCCCCCCCCCCCC		30.9622890988
298PhosphorylationQPEQEGQSDQDIGKR
CCCCCCCCHHHHHHH		48.3628889911
344PhosphorylationRQIPDRRSLSLSPCT
HCCCCCCCCCCCCCC		24.1728889911
346PhosphorylationIPDRRSLSLSPCTRA
CCCCCCCCCCCCCCC		28.2222369663
348PhosphorylationDRRSLSLSPCTRANS
CCCCCCCCCCCCCCC		17.9822369663
351PhosphorylationSLSLSPCTRANSFEP
CCCCCCCCCCCCCCC		35.8822369663
355PhosphorylationSPCTRANSFEPQSWQ
CCCCCCCCCCCCCCC		29.9622369663
360PhosphorylationANSFEPQSWQKKVYP
CCCCCCCCCCCCEEE		42.0422369663
379PhosphorylationVQPFKVGSIGSQSAS
CCCEEECCCCCCCCC		27.1122369663
382PhosphorylationFKVGSIGSQSASRNP
EEECCCCCCCCCCCC		21.2022369663
384PhosphorylationVGSIGSQSASRNPSN
ECCCCCCCCCCCCCC		29.8822369663
386PhosphorylationSIGSQSASRNPSNSS
CCCCCCCCCCCCCCC		37.5322369663
390PhosphorylationQSASRNPSNSSFFNQ
CCCCCCCCCCCCCCC		53.5528889911
392PhosphorylationASRNPSNSSFFNQPP
CCCCCCCCCCCCCCC		32.6228889911
406PhosphorylationPVHRPSMSSNYGPQM
CCCCCCCCCCCCCCC		21.5519779198
418PhosphorylationPQMNIEGTSVGSTSK
CCCEEECCCCCCCCC		13.8819779198
419PhosphorylationQMNIEGTSVGSTSKY
CCEEECCCCCCCCCC		35.0228889911
426PhosphorylationSVGSTSKYSSSFGNI
CCCCCCCCCCCCCCC		17.3521440633
427PhosphorylationVGSTSKYSSSFGNIR
CCCCCCCCCCCCCCC		24.2019823750
428PhosphorylationGSTSKYSSSFGNIRR
CCCCCCCCCCCCCCC		26.9622369663
429PhosphorylationSTSKYSSSFGNIRRH
CCCCCCCCCCCCCCC		31.0922369663
437PhosphorylationFGNIRRHSSVKTTEN
CCCCCCCCCCCCCCC		34.7119823750
438PhosphorylationGNIRRHSSVKTTENA
CCCCCCCCCCCCCCH		22.8519684113
441PhosphorylationRRHSSVKTTENAEKV
CCCCCCCCCCCHHHH		36.8724961812
442PhosphorylationRHSSVKTTENAEKVS
CCCCCCCCCCHHHHH		22.8624961812
454PhosphorylationKVSKAVKSPLQPQES
HHHHHHHCCCCCCCC		25.0128152593
461PhosphorylationSPLQPQESQEDLMDF
CCCCCCCCHHHHHHH		33.3522369663
483PhosphorylationPDLTIKKTSGNNPPN
CCCEEEECCCCCCCC		36.5419779198
484PhosphorylationDLTIKKTSGNNPPNI
CCEEEECCCCCCCCC		48.6925752575
494PhosphorylationNPPNINISDSLIRYQ
CCCCCCCCHHHHHHC		19.3622369663
496PhosphorylationPNINISDSLIRYQNL
CCCCCCHHHHHHCCC		20.9322369663
515PhosphorylationDLLSEDLSVSLSMDP
CCCCCCCCEEECCCC		23.2127017623
517PhosphorylationLSEDLSVSLSMDPNH
CCCCCCEEECCCCCC		16.0227017623
519PhosphorylationEDLSVSLSMDPNHTY
CCCCEEECCCCCCCC		17.4027017623
531PhosphorylationHTYHRGRSDSHSPLP
CCCCCCCCCCCCCCC		46.4128889911
533PhosphorylationYHRGRSDSHSPLPSI
CCCCCCCCCCCCCCC		27.4128889911
535PhosphorylationRGRSDSHSPLPSISP
CCCCCCCCCCCCCCH		31.8919684113
539PhosphorylationDSHSPLPSISPSMHY
CCCCCCCCCCHHHCC		43.3025752575
541PhosphorylationHSPLPSISPSMHYGS
CCCCCCCCHHHCCCC		18.4325752575
543PhosphorylationPLPSISPSMHYGSLN
CCCCCCHHHCCCCCH		16.0528889911
546PhosphorylationSISPSMHYGSLNSRM
CCCHHHCCCCCHHHH		10.3619779198
548PhosphorylationSPSMHYGSLNSRMSQ
CHHHCCCCCHHHHCC		19.7428889911
551PhosphorylationMHYGSLNSRMSQGAN
HCCCCCHHHHCCCCC		34.3519779198
554PhosphorylationGSLNSRMSQGANASH
CCCHHHHCCCCCHHH		25.0922369663
560PhosphorylationMSQGANASHLIARGG
HCCCCCHHHEEECCC		20.7323749301
570PhosphorylationIARGGGNSSTSALNS
EECCCCCCHHHHHHH		37.9622369663
571PhosphorylationARGGGNSSTSALNSR
ECCCCCCHHHHHHHH		30.3122369663
572PhosphorylationRGGGNSSTSALNSRR
CCCCCCHHHHHHHHH		20.1722369663
573PhosphorylationGGGNSSTSALNSRRN
CCCCCHHHHHHHHHH		32.4822369663
577PhosphorylationSSTSALNSRRNSLDK
CHHHHHHHHHHHCCC		33.2022369663
581PhosphorylationALNSRRNSLDKSSNK
HHHHHHHHCCCCCCC		35.8123749301
602PhosphorylationPPIFGGESTSYHHDN
CCCCCCCCCCCCCCC		26.4021440633
603PhosphorylationPIFGGESTSYHHDNK
CCCCCCCCCCCCCCC		29.0628889911
604PhosphorylationIFGGESTSYHHDNKI
CCCCCCCCCCCCCCH		31.5721440633
605PhosphorylationFGGESTSYHHDNKIQ
CCCCCCCCCCCCCHH		11.8521440633
614PhosphorylationHDNKIQKYNQLGVEE
CCCCHHHHHHCCCCC		7.5522369663
637PhosphorylationLLNQMGNSATKFKSS
HHHHHHCHHHHHHHC		31.4222369663
639PhosphorylationNQMGNSATKFKSSIS
HHHHCHHHHHHHCCC		36.5122369663
643PhosphorylationNSATKFKSSISPRSI
CHHHHHHHCCCCHHH		35.7222369663
644PhosphorylationSATKFKSSISPRSID
HHHHHHHCCCCHHHH		27.8922369663
646PhosphorylationTKFKSSISPRSIDSI
HHHHHCCCCHHHHHC		19.0622369663
649PhosphorylationKSSISPRSIDSISSS
HHCCCCHHHHHCCHH		33.8522369663
652PhosphorylationISPRSIDSISSSFIK
CCCHHHHHCCHHHHH		23.7722890988
654PhosphorylationPRSIDSISSSFIKSR
CHHHHHCCHHHHHHC		24.7122890988
655PhosphorylationRSIDSISSSFIKSRI
HHHHHCCHHHHHHCC		27.8322890988
656PhosphorylationSIDSISSSFIKSRIP
HHHHCCHHHHHHCCC		24.9722369663
671PhosphorylationIRQPYHYSQPTTAPF
CCCCCCCCCCCCCCH		19.1721440633
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
344SPhosphorylationKinasePKA-FAMILY-GPS
344SPhosphorylationKinasePKA-Uniprot
348SPhosphorylationKinaseTORC1-Uniprot
437SPhosphorylationKinasePKA-FAMILY-GPS
437SPhosphorylationKinasePKA-Uniprot
437SPhosphorylationKinaseTORC1-Uniprot
438SPhosphorylationKinaseTORC1-Uniprot
496SPhosphorylationKinaseTORC1-Uniprot
535SPhosphorylationKinaseTORC1-Uniprot
541SPhosphorylationKinaseTORC1-Uniprot
581SPhosphorylationKinasePKA-FAMILY-GPS
581SPhosphorylationKinasePKA-Uniprot
646SPhosphorylationKinaseTORC1-Uniprot
649SPhosphorylationKinaseTORC1-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATG13_YEAST !!
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 ATG13_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATG1_YEASTATG1physical
10688190
PSA5_YEASTPUP2physical
10688190
COG2_YEASTCOG2physical
10688190
SNAPN_YEASTSNN1physical
10688190
VAC8_YEASTVAC8physical
10888680
ATG17_YEASTATG17physical
15901835
VAC8_YEASTVAC8physical
15901835
ATG1_YEASTATG1genetic
9224892
BMT2_YEASTBMT2genetic
20093466
MRC1_YEASTMRC1genetic
20093466
ILV6_YEASTILV6genetic
20093466
PTP1_YEASTPTP1genetic
20093466
UBP1_YEASTUBP1genetic
20093466
WDR59_YEASTMTC5genetic
20093466
ENT5_YEASTENT5genetic
20093466
PAC11_YEASTPAC11genetic
20093466
AROC_YEASTARO2genetic
20093466
FYV4_YEASTFYV4genetic
20093466
GRE3_YEASTGRE3genetic
20093466
COX23_YEASTCOX23genetic
20093466
GPP1_YEASTGPP1genetic
20093466
GVP36_YEASTGVP36genetic
20093466
SOP4_YEASTSOP4genetic
20093466
LTHAD_YEASTSRY1genetic
20093466
PEX1_YEASTPEX1genetic
20093466
AMPL_YEASTAPE1genetic
20093466
MDM35_YEASTMDM35genetic
20093466
RL14A_YEASTRPL14Agenetic
20093466
MLP1_YEASTMLP1genetic
20093466
COX12_YEASTCOX12genetic
20093466
MDL1_YEASTMDL1genetic
20093466
ECM38_YEASTECM38genetic
20093466
VRP1_YEASTVRP1genetic
20093466
ERG2_YEASTERG2genetic
20093466
PMA2_YEASTPMA2genetic
20093466
YME1_YEASTYME1genetic
20093466
ATG1_YEASTATG1physical
21460632
ATG1_YEASTATG1physical
21712380
ATG17_YEASTATG17physical
21712380
ATG8_YEASTATG8genetic
21987634
ARPC3_YEASTARC18genetic
21987634
CYK2_YEASTHOF1genetic
21987634
KIME_YEASTERG12genetic
21987634
ATG1_YEASTATG1physical
22885598
ATG1_YEASTATG1genetic
23322149
CARP_YEASTPEP4genetic
23322149
ATG14_YEASTATG14genetic
24586198
ATG17_YEASTATG17genetic
24586198
ATG18_YEASTATG18genetic
24586198
ATG23_YEASTATG23genetic
24586198
ATG3_YEASTATG3genetic
24586198
ATG4_YEASTATG4genetic
24586198
ATG7_YEASTATG7genetic
24586198
ATG9_YEASTATG9genetic
24586198
CCZ1_YEASTCCZ1genetic
24586198
PHO80_YEASTPHO80genetic
24586198
BET1_YEASTBET1physical
23904270
CDC48_YEASTCDC48physical
23904270
FKS1_YEASTFKS1physical
23904270
PIL1_YEASTPIL1physical
23904270
SEC15_YEASTSEC15physical
23904270
COPG_YEASTSEC21physical
23904270
SNF7_YEASTSNF7physical
23904270
COPB_YEASTSEC26physical
23904270
SSO1_YEASTSSO1physical
23904270
VPS1_YEASTVPS1physical
23904270
ATG17_YEASTATG17physical
23904270
CASP_YEASTCOY1physical
23904270
ATC1_YEASTPMR1physical
23904270
TVP23_YEASTTVP23physical
23904270
SEC23_YEASTSEC23physical
23904270
VTI1_YEASTVTI1physical
23904270
ATG29_YEASTATG29physical
23904270
SFT2_YEASTSFT2physical
23904270
ATG11_YEASTATG11physical
23904270
ATG31_YEASTATG31physical
23904270
ATG1_YEASTATG1physical
23904270
ATG17_YEASTATG17physical
24793651
ATG1_YEASTATG1physical
24793651
ATG17_YEASTATG17physical
25998554
ATG9_YEASTATG9physical
25737544
HRR25_YEASTHRR25genetic
27708008
ATG17_YEASTATG17physical
27404361
ATG1_YEASTATG1physical
27404361
ATG17_YEASTATG17physical
29065154
ATG31_YEASTATG31physical
29065154
ATG29_YEASTATG29physical
29065154
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
ATG1_YEASTATG1physical
25737544
ATG17_YEASTATG17physical
25737544
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATG13_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-348; SER-355; SER-379;SER-382; SER-419; SER-429; SER-461; SER-484; SER-541; SER-548;SER-554; SER-571; SER-649 AND SER-656, 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-554, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-360, ANDMASS SPECTROMETRY.
"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-428 AND SER-649, ANDMASS SPECTROMETRY.

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