SNA4_YEAST - dbPTM
SNA4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNA4_YEAST
UniProt AC Q07549
Protein Name Protein SNA4
Gene Name SNA4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 140
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MCCYCVCCTVSDFILYIVAFFFPPAAVLLRSGPCSSDFLLNVLLTLLGFLPGMLHAFYYITITSPLRNAEYVYYYQQGWVDSERNVPSNRPQNSQTPQNRPQQGSSARNVYPSVETPLLQGAAPHDNKQSLVESPPPYVP
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
2S-palmitoylation------MCCYCVCCT
------CCCCHHEEC		1.9716751107
3S-palmitoylation-----MCCYCVCCTV
-----CCCCHHEECH		2.5916751107
5S-palmitoylation---MCCYCVCCTVSD
---CCCCHHEECHHH		0.8716751107
7S-palmitoylation-MCCYCVCCTVSDFI
-CCCCHHEECHHHHH		1.1216751107
8S-palmitoylationMCCYCVCCTVSDFIL
CCCCHHEECHHHHHH		1.7816751107
116PhosphorylationNVYPSVETPLLQGAA
CCCCCCCCCCCCCCC		19.6527214570
128UbiquitinationGAAPHDNKQSLVESP
CCCCCCCCCCCCCCC		47.5223749301
130PhosphorylationAPHDNKQSLVESPPP
CCCCCCCCCCCCCCC		35.6728152593
134PhosphorylationNKQSLVESPPPYVP-
CCCCCCCCCCCCCC-		34.9219823750
138PhosphorylationLVESPPPYVP-----
CCCCCCCCCC-----		31.0019795423
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNA4_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 SNA4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATC2_YEASTPMC1physical
18467557
VPS35_YEASTVPS35physical
18467557
YBT1_YEASTYBT1physical
18467557
HXT1_YEASTHXT1physical
18467557
VATD_YEASTVMA8physical
18467557
GTR1_YEASTGTR1physical
18467557
MEH1_YEASTMEH1physical
18467557
VPS5_YEASTVPS5physical
18467557
VATH_YEASTVMA13physical
18467557
KES1_YEASTKES1physical
18467557
VATF_YEASTVMA7physical
18467557
PIB2_YEASTPIB2physical
18467557
VAC8_YEASTVAC8physical
18467557
GTR2_YEASTGTR2physical
18467557
RSP5_YEASTRSP5physical
19168755
ATC2_YEASTPMC1physical
22615397
HSP72_YEASTSSA2physical
22940862
HSC82_YEASTHSC82physical
22940862
ENO2_YEASTENO2physical
22940862
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
IF2A_YEASTSUI2genetic
27708008
KTHY_YEASTCDC8genetic
27708008
MED14_YEASTRGR1genetic
27708008
ROT1_YEASTROT1genetic
27708008
SGT1_YEASTSGT1genetic
27708008
MED4_YEASTMED4genetic
27708008
DYR_YEASTDFR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNA4_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-134, AND MASSSPECTROMETRY.

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