OSW5_YEAST - dbPTM
OSW5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSW5_YEAST
UniProt AC P40219
Protein Name Outer spore wall protein 5
Gene Name OSW5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 148
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Involved in spore wall assembly..
Protein Sequence MVSTATFFFFVYLTLFVVIGFFSSLFIIPLLGISFVFAIGVVSFGFCSNMSFKMAQLIYVRADAFLKKVLDKMALQTQPAQLQEPQEPLSTLRPVSNPTIPSPLRQTARPSKFVTEEDVIFEPVSAQSAIARSLETTANKAGNKFQLS
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
90PhosphorylationQEPQEPLSTLRPVSN
CCCCCCHHHCCCCCC
35.7921440633
91PhosphorylationEPQEPLSTLRPVSNP
CCCCCHHHCCCCCCC
34.1723607784
96PhosphorylationLSTLRPVSNPTIPSP
HHHCCCCCCCCCCCC
39.5125521595
99PhosphorylationLRPVSNPTIPSPLRQ
CCCCCCCCCCCCCCC
50.1721440633
102PhosphorylationVSNPTIPSPLRQTAR
CCCCCCCCCCCCCCC
32.4925521595

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 OSW5_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSW5_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 OSW5_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEC66_YEASTSEC66genetic
19325107
HOP2_YEASTHOP2genetic
19325107
PRPD_YEASTPDH1physical
21748599
OM14_YEASTOM14physical
21748599
ATPG_YEASTATP3physical
21748599
PEX8_YEASTPEX8physical
21748599
TOM22_YEASTTOM22physical
21748599
IML2_YEASTIML2physical
21748599
HFD1_YEASTHFD1physical
21748599
AYR1_YEASTAYR1physical
21748599
FMP52_YEASTFMP52physical
21748599
GSF2_YEASTGSF2physical
21748599
DPM1_YEASTDPM1physical
21748599
DIC1_YEASTDIC1physical
21748599
DAP1_YEASTDAP1physical
21748599
YTP1_YEASTYTP1physical
21748599
PEX19_YEASTPEX19physical
21748599
DSL1_YEASTDSL1physical
21748599
HAC1_YEASTHAC1genetic
23891562
OST5_YEASTOST5genetic
23891562
MCES_YEASTABD1genetic
27708008
FAD1_YEASTFAD1genetic
27708008
SEC7_YEASTSEC7genetic
27708008
NUP57_YEASTNUP57genetic
27708008
COAD_YEASTCAB4genetic
27708008
CWC16_YEASTYJU2genetic
27708008
TF2B_YEASTSUA7genetic
27708008
HAP5_YEASTHAP5genetic
27708008
PSB6_YEASTPRE7genetic
27708008
SC61G_YEASTSSS1genetic
27708008
PGTB1_YEASTCDC43genetic
27708008
CDC3_YEASTCDC3genetic
27708008
YCQ6_YEASTYCR016Wgenetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
BFA1_YEASTBFA1genetic
27708008
CTK1_YEASTCTK1genetic
27708008
ELO3_YEASTELO3genetic
27708008
SEI1_YEASTFLD1genetic
27708008
TDA5_YEASTTDA5genetic
27708008
RCF2_YEASTRCF2genetic
27708008
SRO7_YEASTSRO7genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSW5_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-102, AND MASSSPECTROMETRY.
"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 SER-102, AND MASSSPECTROMETRY.

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