AMPL_YEAST - dbPTM
AMPL_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPL_YEAST
UniProt AC P14904
Protein Name Vacuolar aminopeptidase 1 {ECO:0000303|PubMed:17329814}
Gene Name APE1 {ECO:0000303|PubMed:2689224}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 514
Subcellular Localization Vacuole . Transported to the vacuole by the cytosol-to-vacuole targeting (Cvt) pathway.
Protein Description Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative growth conditions and by a similar but larger double-membrane structure termed the autophagosome under nitrogen starvation conditions. The Cvt vesicle or the autophagosome fuses with the vacuolar membrane and release its content in the vacuolar lumen. In the vacuole, prApe1 is processed into mature aminopeptidase 1 (mApe1)..
Protein Sequence MEEQREILEQLKKTLQMLTVEPSKNNQIANEEKEKKENENSWCILEHNYEDIAQEFIDFIYKNPTTYHVVSFFAELLDKHNFKYLSEKSNWQDSIGEDGGKFYTIRNGTNLSAFILGKNWRAEKGVGVIGSHVDALTVKLKPVSFKDTAEGYGRIAVAPYGGTLNELWLDRDLGIGGRLLYKKKGTNEIKSALVDSTPLPVCRIPSLAPHFGKPAEGPFDKEDQTIPVIGFPTPDEEGNEPPTDDEKKSPLFGKHCIHLLRYVAKLAGVEVSELIQMDLDLFDVQKGTIGGIGKHFLFAPRLDDRLCSFAAMIALICYAKDVNTEESDLFSTVTLYDNEEIGSLTRQGAKGGLLESVVERSSSAFTKKPVDLHTVWANSIILSADVNHLYNPNFPEVYLKNHFPVPNVGITLSLDPNGHMATDVVGTALVEELARRNGDKVQYFQIKNNSRSGGTIGPSLASQTGARTIDLGIAQLSMHSIRAATGSKDVGLGVKFFNGFFKHWRSVYDEFGEL
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
24UbiquitinationMLTVEPSKNNQIANE
HHCCCCCCCCCCCCC		71.3024961812
88AcetylationNFKYLSEKSNWQDSI
CCHHHCCCCCCCCCC		45.7924489116
107N-linked_GlycosylationGKFYTIRNGTNLSAF
CEEEEEECCCCEEEE		58.76-
110N-linked_GlycosylationYTIRNGTNLSAFILG
EEEECCCCEEEEEEC		33.14-
124UbiquitinationGKNWRAEKGVGVIGS
CCCCCCCCCCEEECC		58.8924961812
146AcetylationKLKPVSFKDTAEGYG
EEEECCCCCCCCCCC		46.8124489116
213AcetylationSLAPHFGKPAEGPFD
CCCCCCCCCCCCCCC		39.8622865919
294AcetylationGTIGGIGKHFLFAPR
CCCCCCCHHHEECCC		29.3024489116
356PhosphorylationAKGGLLESVVERSSS
CCCCHHHHHHHHCCC		31.2828889911
440AcetylationLARRNGDKVQYFQIK
HHHHCCCCCEEEEEE		32.4124489116
4472-HydroxyisobutyrylationKVQYFQIKNNSRSGG
CCEEEEEECCCCCCC		39.01-
448N-linked_GlycosylationVQYFQIKNNSRSGGT
CEEEEEECCCCCCCC		54.03-
452PhosphorylationQIKNNSRSGGTIGPS
EEECCCCCCCCCCHH		41.2028889911
4882-HydroxyisobutyrylationIRAATGSKDVGLGVK
HHHHHCCCCCCCCHH		58.75-
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 AMPL_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMPL_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 AMPL_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATG19_YEASTATG19physical
11805837
MAN1_YEASTAMS1physical
11805837
YFD4_YEASTYFL034Wphysical
11805837
BIK1_YEASTBIK1physical
11805837
CYPH_YEASTCPR1physical
11805837
H2B1_YEASTHTB1physical
11805837
H3_YEASTHHT1physical
11805837
VATE_YEASTVMA4physical
11805837
DLD3_YEASTDLD3physical
11805837
AMPL_YEASTAPE1physical
10688190
ATG19_YEASTATG19physical
10688190
ATG19_YEASTATG19physical
12479808
ATG19_YEASTATG19physical
11430817
AMPL_YEASTAPE1physical
11283351
ATG19_YEASTATG19physical
11283351
AMPL_YEASTAPE1physical
18719252
SSB1_YEASTSSB1physical
19536198
AMPL_YEASTAPE1physical
19343713
MNN10_YEASTMNN10genetic
20093466
YOR1_YEASTYOR1genetic
20093466
LRP1_YEASTLRP1genetic
20093466
VRP1_YEASTVRP1genetic
20093466
EIS1_YEASTEIS1genetic
20093466
ATG13_YEASTATG13genetic
20093466
ATG19_YEASTATG19physical
20639194
ATG19_YEASTATG19physical
20659891
ATG19_YEASTATG19physical
21343297
ATG19_YEASTATG19physical
22123825
ATG11_YEASTATG11physical
22123825
ATG8_YEASTATG8physical
22123825
ATG19_YEASTATG19physical
24705553
ATG34_YEASTATG34physical
24705553
AMPL_YEASTAPE1physical
26208681
ATG8_YEASTATG8genetic
27708008
XRN1_YEASTXRN1genetic
27708008
YOR1_YEASTYOR1genetic
27708008
LRP1_YEASTLRP1genetic
27708008
VRP1_YEASTVRP1genetic
27708008
AMPL_YEASTAPE1physical
28027291
AMPL_YEASTAPE1physical
27266708
AMPL_YEASTAPE1physical
27320913
ATG19_YEASTATG19physical
27320913
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMPL_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-356 AND SER-452, ANDMASS SPECTROMETRY.

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