| UniProt ID | CDC37_YEAST | |
|---|---|---|
| UniProt AC | P06101 | |
| Protein Name | Hsp90 co-chaperone Cdc37 | |
| Gene Name | CDC37 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 506 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Involved in both the HOG and the PKC MAP kinase signaling cascade necessary for adaptation to stress conditions due to high osmolarity or cell wall perturbation.. | |
| Protein Sequence | MAIDYSKWDKIELSDDSDVEVHPNVDKKSFIKWKQQSIHEQRFKRNQDIKNLETQVDMYSHLNKRVDRILSNLPESSLTDLPAVTKFLNANFDKMEKSKGENVDPEIATYNEMVEDLFEQLAKDLDKEGKDSKSPSLIRDAILKHRAKIDSVTVEAKKKLDELYKEKNAHISSEDIHTGFDSSFMNKQKGGAKPLEATPSEALSSAAESNILNKLAKSSVPQTFIDFKDDPMKLAKETEEFGKISINEYSKSQKFLLEHLPIISEQQKDALMMKAFEYQLHGDDKMTLQVIHQSELMAYIKEIYDMKKIPYLNPMELSNVINMFFEKVIFNKDKPMGKESFLRSVQEKFLHIQKRSKILQQEEMDESNAEGVETIQLKSLDDSTELEVNLPDFNSKDPEEMKKVKVFKTLIPEKMQEAIMTKNLDNINKVFEDIPIEEAEKLLEVFNDIDIIGIKAILENEKDFQSLKDQYEQDHEDATMENLSLNDRDGGGDNHEEVKHTADTVD | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 14 | Phosphorylation | KWDKIELSDDSDVEV HCCCEECCCCCCCEE | 26.95 | 25521595 | |
| 17 | Phosphorylation | KIELSDDSDVEVHPN CEECCCCCCCEECCC | 48.85 | 22369663 | |
| 27 | Acetylation | EVHPNVDKKSFIKWK EECCCCCHHHHHHHH | 46.14 | 24489116 | |
| 37 | Phosphorylation | FIKWKQQSIHEQRFK HHHHHHHHHHHHHHH | 24.34 | 30377154 | |
| 64 | Acetylation | DMYSHLNKRVDRILS HHHHHHHHHHHHHHH | 61.22 | 24489116 | |
| 71 | Phosphorylation | KRVDRILSNLPESSL HHHHHHHHCCCCCCC | 33.67 | 22369663 | |
| 76 | Phosphorylation | ILSNLPESSLTDLPA HHHCCCCCCCCCHHH | 28.80 | 30377154 | |
| 77 | Phosphorylation | LSNLPESSLTDLPAV HHCCCCCCCCCHHHH | 33.36 | 30377154 | |
| 86 | Ubiquitination | TDLPAVTKFLNANFD CCHHHHHHHHHCCHH | 41.05 | 24961812 | |
| 94 | Acetylation | FLNANFDKMEKSKGE HHHCCHHHHHHCCCC | 44.83 | 24489116 | |
| 134 | Phosphorylation | KEGKDSKSPSLIRDA HCCCCCCCHHHHHHH | 24.55 | 21440633 | |
| 136 | Phosphorylation | GKDSKSPSLIRDAIL CCCCCCHHHHHHHHH | 43.44 | 21440633 | |
| 158 | 2-Hydroxyisobutyrylation | SVTVEAKKKLDELYK EEEHHHHHHHHHHHH | 66.66 | - | |
| 172 | Phosphorylation | KEKNAHISSEDIHTG HHHCCCCCHHHHHCC | 20.15 | 22369663 | |
| 173 | Phosphorylation | EKNAHISSEDIHTGF HHCCCCCHHHHHCCC | 38.39 | 22369663 | |
| 178 | Phosphorylation | ISSEDIHTGFDSSFM CCHHHHHCCCCHHHH | 39.62 | 22369663 | |
| 182 | Phosphorylation | DIHTGFDSSFMNKQK HHHCCCCHHHHCCCC | 24.18 | 22369663 | |
| 183 | Phosphorylation | IHTGFDSSFMNKQKG HHCCCCHHHHCCCCC | 30.29 | 22369663 | |
| 187 | Acetylation | FDSSFMNKQKGGAKP CCHHHHCCCCCCCCC | 41.41 | 24489116 | |
| 198 | Phosphorylation | GAKPLEATPSEALSS CCCCCCCCHHHHHHH | 20.26 | 22369663 | |
| 200 | Phosphorylation | KPLEATPSEALSSAA CCCCCCHHHHHHHHH | 31.02 | 23749301 | |
| 204 | Phosphorylation | ATPSEALSSAAESNI CCHHHHHHHHHHHHH | 25.61 | 22369663 | |
| 205 | Phosphorylation | TPSEALSSAAESNIL CHHHHHHHHHHHHHH | 32.14 | 23749301 | |
| 209 | Phosphorylation | ALSSAAESNILNKLA HHHHHHHHHHHHHHH | 25.17 | 23749301 | |
| 214 | Acetylation | AESNILNKLAKSSVP HHHHHHHHHHHCCCC | 46.51 | 24489116 | |
| 228 | Acetylation | PQTFIDFKDDPMKLA CCCCCCCCCCHHHHH | 58.43 | 24489116 | |
| 243 | Acetylation | KETEEFGKISINEYS HHHHHHCCCCHHHCC | 38.30 | 24489116 | |
| 254 | Acetylation | NEYSKSQKFLLEHLP HHCCHHHHHHHHHCC | 45.10 | 24489116 | |
| 294 | Phosphorylation | TLQVIHQSELMAYIK EEEEEEHHHHHHHHH | 20.66 | 21551504 | |
| 299 | Phosphorylation | HQSELMAYIKEIYDM EHHHHHHHHHHHHHC | 9.88 | 21551504 | |
| 348 | Acetylation | FLRSVQEKFLHIQKR HHHHHHHHHHHHHHH | 35.81 | 24489116 | |
| 356 | Phosphorylation | FLHIQKRSKILQQEE HHHHHHHHHHHHHHH | 30.96 | 19779198 | |
| 364 | Oxidation | KILQQEEMDESNAEG HHHHHHHHCCCCCCC | 7.34 | 15665377 | |
| 367 | Phosphorylation | QQEEMDESNAEGVET HHHHHCCCCCCCCEE | 36.76 | 22369663 | |
| 374 | Phosphorylation | SNAEGVETIQLKSLD CCCCCCEEEEEEECC | 16.18 | 22369663 | |
| 408 | Acetylation | MKKVKVFKTLIPEKM HHHHHHHHHHCCHHH | 45.46 | 24489116 | |
| 414 | Acetylation | FKTLIPEKMQEAIMT HHHHCCHHHHHHHHC | 40.29 | 24489116 | |
| 422 | Acetylation | MQEAIMTKNLDNINK HHHHHHCCCHHHHHH | 37.83 | 24489116 | |
| 462 | Ubiquitination | KAILENEKDFQSLKD HHHHHCHHHHHHHHH | 75.36 | 24961812 | |
| 462 | Acetylation | KAILENEKDFQSLKD HHHHHCHHHHHHHHH | 75.36 | 24489116 | |
| 462 | Succinylation | KAILENEKDFQSLKD HHHHHCHHHHHHHHH | 75.36 | 23954790 | |
| 466 | Phosphorylation | ENEKDFQSLKDQYEQ HCHHHHHHHHHHHHH | 37.06 | 24909858 | |
| 471 | Phosphorylation | FQSLKDQYEQDHEDA HHHHHHHHHHHHHHC | 26.20 | 22369663 | |
| 479 | Phosphorylation | EQDHEDATMENLSLN HHHHHHCCHHHCCCC | 37.02 | 22369663 | |
| 484 | Phosphorylation | DATMENLSLNDRDGG HCCHHHCCCCCCCCC | 36.39 | 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 CDC37_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 14 | S | Phosphorylation |
| 17220467 |
* 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 CDC37_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-14; SER-17; SER-367;SER-466 AND SER-484, 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-14 AND SER-17, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-17, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-17, AND MASSSPECTROMETRY. | |
| "Cdc37p is required for stress-induced high-osmolarity glycerol andprotein kinase C mitogen-activated protein kinase pathwayfunctionality by interaction with Hog1p and Slt2p (Mpk1p)."; Hawle P., Horst D., Bebelman J.-P., Yang X.X., Siderius M.,van der Vies S.M.; Eukaryot. Cell 6:521-532(2007). Cited for: FUNCTION, INTERACTION WITH HOG1; HSP90 AND SLT2, PHOSPHORYLATION ATSER-14, AND MUTAGENESIS OF SER-14. | |
| "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-367, AND MASSSPECTROMETRY. | |
