SNA3_YEAST - dbPTM
SNA3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNA3_YEAST
UniProt AC P14359
Protein Name Protein SNA3
Gene Name SNA3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 133
Subcellular Localization Membrane
Multi-pass membrane protein. Late endosome membrane
Multi-pass membrane protein. Vacuole lumen. Cytoplasmic vesicle membrane
Multi-pass membrane protein . Sorted via late endosomes to the vacuolar lumen in a ubiquitin-independent manner.
Protein Description
Protein Sequence MDRDHINDHDHRMSYSINKDDLLLMVLAVFIPPVAVWKRKGMFNRDTLLNLLLFLLLFFPAIIHACYVVYETSSERSYDLSRRHATAPAVDRDLEAHPAEESQAQPPAYDEDDEAGADVPLMDNKQQLSSGRT
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
86PhosphorylationDLSRRHATAPAVDRD
CCHHHCCCCCHHCCC
27.3517563356
125UbiquitinationDVPLMDNKQQLSSGR
CCCCCCCCHHHHCCC
34.8523749301

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 SNA3_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 SNA3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSP5_YEASTRSP5physical
17182850
RSP5_YEASTRSP5physical
17645729
PDR12_YEASTPDR12physical
18467557
UBX2_YEASTUBX2physical
18467557
LCB1_YEASTLCB1physical
18467557
MEH1_YEASTMEH1physical
18467557
ENG2_YEASTACF2physical
18467557
VATH_YEASTVMA13physical
18467557
KES1_YEASTKES1physical
18467557
LOA1_YEASTLOA1physical
18467557
YIM1_YEASTYIM1physical
18467557
TGL1_YEASTTGL1physical
18467557
MGLL_YEASTYJU3physical
18467557
COPG_YEASTSEC21physical
18467557
ERG27_YEASTERG27physical
18467557
SNA3_YEASTSNA3physical
18467557
VPS35_YEASTVPS35physical
18467557
YCY0_YEASTYCR090Cgenetic
20093466
WDR59_YEASTMTC5genetic
20093466
EAF1_YEASTEAF1genetic
20093466
YFF2_YEASTYFL052Wgenetic
20093466
VAM7_YEASTVAM7genetic
20093466
RME1_YEASTRME1genetic
20093466
THIK_YEASTPOT1genetic
20093466
ATG32_YEASTATG32genetic
20093466
OCA2_YEASTOCA2genetic
20093466
YP089_YEASTYPR089Wgenetic
20093466
PDR12_YEASTPDR12physical
22615397
HSP71_YEASTSSA1physical
22940862
UBI4P_YEASTUBI4physical
23936628
SNA4_YEASTSNA4genetic
26303201
RSP5_YEASTRSP5physical
25942624
GPR1_YEASTGPR1genetic
27708008
UBC13_YEASTUBC13genetic
27708008
YFF2_YEASTYFL052Wgenetic
27708008
EFM4_YEASTEFM4genetic
27708008
ATG32_YEASTATG32genetic
27708008
PUB1_YEASTPUB1genetic
27708008
RAS2_YEASTRAS2genetic
27708008
THI22_YEASTTHI22genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNA3_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-86, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-125, AND MASSSPECTROMETRY.

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