| Tag | Content |
|---|
| CPLM ID | CPLM-006297 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Hsp70/Hsp90 co-chaperone CNS1 |
Protein Synonyms/Alias | Cyclophilin seven suppressor 1; STI1 stress-inducible protein homolog |
Gene Name | CNS1 |
Gene Synonyms/Alias | YBR155W; YBR1205 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 87 | HEIAENFKKQGNELY | acetylation | [1] | | 163 | KCYYRTSKAFFQLNK | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Co-chaperone that binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). Stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. Involved in only a subset of Hsp90 functions. |
Sequence Annotation | REPEAT 83 116 TPR 1.
REPEAT 121 154 TPR 2.
REPEAT 155 189 TPR 3. |
Keyword | Chaperone; Complete proteome; Cytoplasm; Reference proteome; Repeat; TPR repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 385 AA |
Protein Sequence | MSSVNANGGY TKPQKYVPGP GDPELPPQLS EFKDKTSDEI LKEMNRMPFF MTKLDETDGA 60
GGENVELEAL KALAYEGEPH EIAENFKKQG NELYKAKRFK DARELYSKGL AVECEDKSIN 120
ESLYANRAAC ELELKNYRRC IEDCSKALTI NPKNVKCYYR TSKAFFQLNK LEEAKSAATF 180
ANQRIDPENK SILNMLSVID RKEQELKAKE EKQQREAQER ENKKIMLESA MTLRNITNIK 240
THSPVELLNE GKIRLEDPMD FESQLIYPAL IMYPTQDEFD FVGEVSELTT VQELVDLVLE 300
GPQERFKKEG KENFTPKKVL VFMETKAGGL IKAGKKLTFH DILKKESPDV PLFDNALKIY 360
IVPKVESEGW ISKWDKQKAL ERRSV 385 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |