ATG22_YEAST - dbPTM
ATG22_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATG22_YEAST
UniProt AC P25568
Protein Name Autophagy-related protein 22
Gene Name ATG22
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 528
Subcellular Localization Vacuole membrane
Multi-pass membrane protein . Vacuole and punctate structures.
Protein Description Vacuolar effluxer which mediate the efflux of leucine and other amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation..
Protein Sequence MSYGTINDMNESVTNYRIKKAQNNIKGWYAYSFSSEPFVVSAVSTYIPLLLQQFASINGVKVHDHSIPCLSETGSDSDKCVLGLFNNRIFVDTSSFALYVFSLSVLFQTIIVISVSGIVDLWGSVKFKGRILVWFGIVGALSTVAISKLNDTQIYSLAGLYIVANGCFGVINVVGNSLLPIFVKDSLKCQSQGAYEPDKVDSLTTVISGRGASLGYSSALIVQIVSMFLVASKKGSKQDVQVAVLFVGIWWFVWQLPMIWLIDDVTIPIRVDDSTLASARSPYPGEQDALGQLNWKNYLSYGWVSLFESFKHARLLKDVMIFLIAWFIISDSITTINSTAVLFSKAELHMSTLNLIMISVLTVVNAMLGAFMIPQFLATKFRWTSSQTLMYIIIWASFIPFYGILGFFFNAFGLKHKFEMFLLAIWYGLSLGGLSAVSRSVFSLIVPPGKESTFFSMFSITDKGSSILGPFLVGLLTDKTHNIRYSFYFFFLLLMLSLPVLNCLDVKRGRREAEELSQVLPESERRLD
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
2Phosphorylation------MSYGTINDM
------CCCCCCCCC		32.0628132839
3Phosphorylation-----MSYGTINDMN
-----CCCCCCCCCC		19.5928132839
12PhosphorylationTINDMNESVTNYRIK
CCCCCCHHHHHHHHH		29.2728132839
14PhosphorylationNDMNESVTNYRIKKA
CCCCHHHHHHHHHHH		35.4928889911
16PhosphorylationMNESVTNYRIKKAQN
CCHHHHHHHHHHHHH		12.3528132839
274PhosphorylationIPIRVDDSTLASARS
EEEEECCCCHHCCCC		22.3628889911
278PhosphorylationVDDSTLASARSPYPG
ECCCCHHCCCCCCCC		27.5928889911
281PhosphorylationSTLASARSPYPGEQD
CCHHCCCCCCCCCCC		28.6227017623
283PhosphorylationLASARSPYPGEQDAL
HHCCCCCCCCCCCCC		25.7228889911
523PhosphorylationLSQVLPESERRLD--
HHHHCCHHHHCCC--		34.1727214570
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 ATG22_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATG22_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 ATG22_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHO88_YEASTPHO88physical
16093310
ATG5_YEASTATG5genetic
24586198
AP2A_YEASTAPL3genetic
27708008
ALG3_YEASTALG3genetic
27708008
RL4A_YEASTRPL4Agenetic
27708008
YBY9_YEASTYBR139Wgenetic
27708008
GDT1_YEASTGDT1genetic
27708008
PST1_YEASTPST1genetic
27708008
SAC3_YEASTSAC3genetic
27708008
PMP3_YEASTPMP3genetic
27708008
SGPL_YEASTDPL1genetic
27708008
SLT2_YEASTSLT2genetic
27708008
VPS51_YEASTVPS51genetic
27708008
UBP15_YEASTUBP15genetic
27708008
ESBP6_YEASTESBP6genetic
27708008
LIPA_YEASTLIP5genetic
27708008
PALA_YEASTRIM20genetic
27708008
YO365_YEASTYOR365Cgenetic
27708008
RQC2_YEASTTAE2genetic
27708008
PMA2_YEASTPMA2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATG22_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-278, AND MASSSPECTROMETRY.

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