UniProt ID | HSP30_YEAST | |
---|---|---|
UniProt AC | P25619 | |
Protein Name | 30 kDa heat shock protein | |
Gene Name | HSP30 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 332 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
Protein Description | Probably cooperates with other heat shock proteins in the translocation of polypeptides through membranes. It may counteract the altering effect of heat shock on the plasma membrane.. | |
Protein Sequence | MNDTLSSFLNRNEALGLNPPHGLDMHITKRGSDWLWAVFAVFGFILLCYVVMFFIAENKGSRLTRYALAPAFLITFFEFFAFFTYASDLGWTGVQAEFNHVKVSKSITGEVPGIRQIFYSKYIAWFLSWPCLLFLIELAASTTGENDDISALDMVHSLLIQIVGTLFWVVSLLVGSLIKSTYKWGYYTIGAVAMLVTQGVICQRQFFNLKTRGFNALMLCTCMVIVWLYFICWGLSDGGNRIQPDGEAIFYGVLDLCVFAIYPCYLLIAVSRDGKLPRLSLTGGFSHHHATDDVEDAAPETKEAVPESPRASGETAIHEPEPEAEQAVEDTA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
105 | 2-Hydroxyisobutyrylation | FNHVKVSKSITGEVP CCEEEEHHHHCCCCC | 49.19 | - | |
210 | 2-Hydroxyisobutyrylation | QRQFFNLKTRGFNAL HHHHCCCCCCCHHHH | 36.96 | - | |
291 | Phosphorylation | GFSHHHATDDVEDAA CCCCCCCCCCHHHCC | 28.51 | 30377154 | |
301 | Phosphorylation | VEDAAPETKEAVPES HHHCCHHHHHCCCCC | 32.88 | 28889911 | |
302 | Ubiquitination | EDAAPETKEAVPESP HHCCHHHHHCCCCCC | 41.85 | 23749301 | |
308 | Phosphorylation | TKEAVPESPRASGET HHHCCCCCCCCCCCC | 17.39 | 22369663 | |
312 | Phosphorylation | VPESPRASGETAIHE CCCCCCCCCCCCCCC | 38.14 | 22369663 | |
315 | Phosphorylation | SPRASGETAIHEPEP CCCCCCCCCCCCCCC | 34.14 | 22369663 | |
331 | Phosphorylation | AEQAVEDTA------ HHHHHHHCC------ | 22.29 | 22369663 |
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 HSP30_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HSP30_YEAST !! |
* 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 HSP30_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-308; THR-315 ANDTHR-331, AND MASS SPECTROMETRY. | |
"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-308 AND SER-312, ANDMASS SPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASSSPECTROMETRY. | |
"A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-331, AND MASSSPECTROMETRY. |