ATG19_YEAST - dbPTM
ATG19_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG19_YEAST
UniProt AC P35193
Protein Name Autophagy-related protein 19
Gene Name ATG19
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 415
Subcellular Localization Preautophagosomal structure membrane
Peripheral membrane protein . Also found in other perivacuolar punctate structures.
Protein Description Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole. Involved in the organization of the preautophagosomal structure (PAS). ATG19 association with cargo protein is required to localize ATG11 to the PAS. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates, and is essential for the survival of cells subjected to severe ER stress. Plays also a role in regulation of filamentous growth..
Protein Sequence MNNSKTNQQMNTSMGYPLTVYDECNKFQLIVPTLDANIMLWCIGQLSLLNDSNGCKHLFWQPNDKSNVRILLNNYDYGHLFKYLQCQRKCSVYIGEGTLKKYNLTISTSFDNFLDLTPSEEKESLCREDAHEDPVSPKAGSEEEISPNSTSNVVVSRECLDNFMKQLLKLEESLNKLELEQKVTNKEPNHRISGTIDIPEDRSELVNFFTELKTVKQLEDVFQRYHDYERLSQECDSKTEIASDHSKKETKIEVEPPNERSLQITMNQRDNSLYFQLFNNTNSVLAGNCKLKFTDAGDKPTTQIIDMGPHEIGIKEYKEYRYFPYALDLEAGSTIEIENQYGEVIFLGKYGSSPMINLRPPSRLSAESLQASQEPFYSFQIDTLPELDDSSIISTSISLSYDGDDNEKALTWEEL
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
13PhosphorylationTNQQMNTSMGYPLTV
HHHHCCCCCCCCEEE		12.7627017623
21PhosphorylationMGYPLTVYDECNKFQ
CCCCEEEEECCCCEE		10.7827017623
56UbiquitinationLNDSNGCKHLFWQPN
HCCCCCCCCEEECCC		44.7517644757
65UbiquitinationLFWQPNDKSNVRILL
EEECCCCCCCEEEEE		51.0417644757
82UbiquitinationYDYGHLFKYLQCQRK
CCHHHHHHHHHCCCC		51.9517644757
89UbiquitinationKYLQCQRKCSVYIGE
HHHHCCCCCEEEECC		12.6517644757
100UbiquitinationYIGEGTLKKYNLTIS
EECCCCEEEEEEEEE		53.7217644757
101UbiquitinationIGEGTLKKYNLTIST
ECCCCEEEEEEEEEE		42.3517644757
122UbiquitinationDLTPSEEKESLCRED
CCCCHHHHHHHHCCC		48.8517644757
124PhosphorylationTPSEEKESLCREDAH
CCHHHHHHHHCCCCC		43.7821440633
136PhosphorylationDAHEDPVSPKAGSEE
CCCCCCCCCCCCCCC		26.5219823750
138UbiquitinationHEDPVSPKAGSEEEI
CCCCCCCCCCCCCCC		58.8517644757
141PhosphorylationPVSPKAGSEEEISPN
CCCCCCCCCCCCCCC		46.8525752575
146PhosphorylationAGSEEEISPNSTSNV
CCCCCCCCCCCCCCE		22.7021440633
165UbiquitinationECLDNFMKQLLKLEE
HHHHHHHHHHHHHHH		33.3917644757
169UbiquitinationNFMKQLLKLEESLNK
HHHHHHHHHHHHHHH		63.5517644757
173PhosphorylationQLLKLEESLNKLELE
HHHHHHHHHHHHHHH		28.0630377154
176UbiquitinationKLEESLNKLELEQKV
HHHHHHHHHHHHHHH		48.9417644757
182UbiquitinationNKLELEQKVTNKEPN
HHHHHHHHHCCCCCC		41.4717644757
193PhosphorylationKEPNHRISGTIDIPE
CCCCCCEEEEEECCC		29.8230377154
213UbiquitinationVNFFTELKTVKQLED
HHHHHHHHHHHHHHH		45.0716186126
216UbiquitinationFTELKTVKQLEDVFQ
HHHHHHHHHHHHHHH		55.1623749301
232PhosphorylationYHDYERLSQECDSKT
HHCHHHHHHHCCCCC		30.1028889911
237PhosphorylationRLSQECDSKTEIASD
HHHHHCCCCCCCCCC		53.8125005228
238UbiquitinationLSQECDSKTEIASDH
HHHHCCCCCCCCCCC		36.6123749301
239PhosphorylationSQECDSKTEIASDHS
HHHCCCCCCCCCCCC		36.2519823750
243PhosphorylationDSKTEIASDHSKKET
CCCCCCCCCCCCCCC		41.3316186126
246PhosphorylationTEIASDHSKKETKIE
CCCCCCCCCCCCEEE		50.8719823750
250PhosphorylationSDHSKKETKIEVEPP
CCCCCCCCEEEECCC		46.3228889911
290UbiquitinationSVLAGNCKLKFTDAG
CEECCCEEEEECCCC		59.7317644757
292UbiquitinationLAGNCKLKFTDAGDK
ECCCEEEEECCCCCC		31.5417644757
299UbiquitinationKFTDAGDKPTTQIID
EECCCCCCCCEEEEE		43.2617644757
315UbiquitinationGPHEIGIKEYKEYRY
CCCCCCCCCCHHCCC		50.1817644757
318UbiquitinationEIGIKEYKEYRYFPY
CCCCCCCHHCCCCCE		49.7317644757
349UbiquitinationGEVIFLGKYGSSPMI
EEEEEEEECCCCCCC		48.8917644757
411PhosphorylationDDNEKALTWEEL---
CCCCEEECCEEC---		35.3722369663
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 ATG19_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
213Kubiquitylation

16186126
216Kubiquitylation

16186126
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 ATG19_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AMPL_YEASTAPE1physical
12479808
MAN1_YEASTAMS1physical
12479808
ATG11_YEASTATG11physical
15659643
ATG8_YEASTATG8physical
19021777
ATG8_YEASTATG8physical
19619494
ATG11_YEASTATG11physical
19619494
ATG34_YEASTATG34genetic
20639194
MAN1_YEASTAMS1physical
20659891
ATG8_YEASTATG8physical
20615880
DNPEP_YEASTAPE4physical
21343297
AMPL_YEASTAPE1physical
21343297
MAN1_YEASTAMS1physical
21343297
ATG21_YEASTATG21genetic
24586198
ATG29_YEASTATG29genetic
24586198
ATG32_YEASTATG32genetic
24586198
ATG33_YEASTATG33genetic
24586198
CCZ1_YEASTCCZ1genetic
24586198
PHO80_YEASTPHO80genetic
24586198
REG1_YEASTREG1genetic
24586198
SNF1_YEASTSNF1genetic
24586198
SNX4_YEASTSNX4genetic
24586198
TEP1_YEASTTEP1genetic
24586198
TLG2_YEASTTLG2genetic
24586198
BECN1_YEASTVPS30genetic
24586198
ATG11_YEASTATG11physical
25287303
AMPL_YEASTAPE1physical
25287303
ATG8_YEASTATG8physical
24705553
HSP72_YEASTSSA2physical
26166702
AMPL_YEASTAPE1physical
26166702
SSB1_YEASTSSB1physical
26166702
HSC82_YEASTHSC82physical
26166702
EF2_YEASTEFT2physical
26166702
ATG19_YEASTATG19physical
26166702
KPYK1_YEASTCDC19physical
26166702
PABP_YEASTPAB1physical
26166702
HSP77_YEASTSSC1physical
26166702
PFKA2_YEASTPFK2physical
26166702
PEX19_YEASTPEX19genetic
27708008
TAPT1_YEASTEMP65genetic
27708008
STF2_YEASTSTF2genetic
27708008
SNF6_YEASTSNF6genetic
27708008
YRA2_YEASTYRA2genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
COA4_YEASTCOA4genetic
27708008
BUL2_YEASTBUL2genetic
27708008
COX7_YEASTCOX7genetic
27708008
SCS7_YEASTSCS7genetic
27708008
VAM3_YEASTVAM3genetic
27708008
PMA2_YEASTPMA2genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
ATG5_YEASTATG5physical
27879200
ATG12_YEASTATG12physical
27879200
ATG16_YEASTATG16physical
27879200
ATG8_YEASTATG8physical
27879200
ATG8_YEASTATG8physical
27402840
MAN1_YEASTAMS1physical
27266708
AMPL_YEASTAPE1physical
27266708
ATG11_YEASTATG11physical
24968893
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATG19_YEAST

loading...

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-136, AND MASSSPECTROMETRY.
"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-136, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-243 ANDSER-246, AND MASS 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 THR-411, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory