SNA2_YEAST - dbPTM
SNA2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNA2_YEAST
UniProt AC P56508
Protein Name Protein SNA2
Gene Name SNA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 79
Subcellular Localization Membrane
Multi-pass membrane protein. Lipid droplet. Localized to punctate structures and lipid particles in the cytoplasm.
Protein Description
Protein Sequence MHARDWFLVFIAIFIPPLAVWLKRGFFTKDLLINFLLFLLGFFPGLIHALYVISCHPYEENEARYSHLSSSDDNYGSLA
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
65PhosphorylationYEENEARYSHLSSSD
CCCCHHHHHCCCCCC		13.9022890988
66PhosphorylationEENEARYSHLSSSDD
CCCHHHHHCCCCCCC		16.6422890988
69PhosphorylationEARYSHLSSSDDNYG
HHHHHCCCCCCCCCC		23.5222369663
70PhosphorylationARYSHLSSSDDNYGS
HHHHCCCCCCCCCCC		44.1122369663
71PhosphorylationRYSHLSSSDDNYGSL
HHHCCCCCCCCCCCC		45.6822369663
75PhosphorylationLSSSDDNYGSLA---
CCCCCCCCCCCC---		18.3222890988
77PhosphorylationSSDDNYGSLA-----
CCCCCCCCCC-----		15.6822890988
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 SNA2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNA2_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 SNA2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP71_YEASTSSA1physical
22940862
SNA3_YEASTSNA3genetic
26303201
SNA4_YEASTSNA4genetic
26303201
SLX5_YEASTSLX5genetic
27708008
WHI5_YEASTWHI5genetic
27708008
RU2A_YEASTLEA1genetic
27708008
ALG14_YEASTALG14genetic
27708008
MOB2_YEASTMOB2genetic
27708008
NEP1_YEASTEMG1genetic
27708008
ORC1_YEASTORC1genetic
27708008
MVD1_YEASTMVD1genetic
27708008
NOG2_YEASTNOG2genetic
27708008
PP2C3_YEASTPTC3genetic
27708008
ADH4_YEASTADH4genetic
27708008
OPI1_YEASTOPI1genetic
27708008
YHY2_YEASTYHR182Wgenetic
27708008
CTK1_YEASTCTK1genetic
27708008
TDA1_YEASTTDA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNA2_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-69; SER-70; SER-71 ANDSER-77, 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 SER-71, AND MASSSPECTROMETRY.

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