CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004299
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent molecular chaperone HSC82 
Protein Synonyms/Alias
 82 kDa heat shock cognate protein; Heat shock protein Hsp90 constitutive isoform 
Gene Name
 HSC82 
Gene Synonyms/Alias
 YMR186W; YM8010.16 
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
54YQALSDPKQLETEPDacetylation[1]
54YQALSDPKQLETEPDubiquitination[2]
69LFIRITPKPEEKVLEubiquitination[2]
73ITPKPEEKVLEIRDSacetylation[1]
73ITPKPEEKVLEIRDSubiquitination[2]
249VDEEEEEKKPKTKKVacetylation[1]
249VDEEEEEKKPKTKKVubiquitination[2]
250DEEEEEKKPKTKKVKubiquitination[2]
257KPKTKKVKEEVQELEacetylation[1]
268QELEELNKTKPLWTRacetylation[1]
395IRKNIVKKLIEAFNEacetylation[1]
412EDSEQFDKFYSAFAKubiquitination[2]
419KFYSAFAKNIKLGVHacetylation[1]
490FLDALKAKNFEVLFLubiquitination[3]
551EPLTKALKDILGDQVacetylation[1]
560ILGDQVEKVVVSYKLacetylation[1]
566EKVVVSYKLLDAPAAubiquitination[3]
633DEGGAQDKTVKDLTNubiquitination[3]
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]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures. 
Sequence Annotation
 REPEAT 221 225 1.
 REPEAT 226 230 2.
 REPEAT 232 236 3.
 REPEAT 246 250 4.
 REGION 221 259 4 X 5 AA repeats of [DE]-[DE]-[DE]-K-K;
 MOTIF 701 705 TPR repeat-binding.
 BINDING 37 37 ATP (By similarity).
 BINDING 79 79 ATP (By similarity).
 BINDING 98 98 ATP (By similarity).
 BINDING 124 124 ATP; via amide nitrogen (By similarity).
 BINDING 376 376 ATP (By similarity).
 MOD_RES 653 653 Phosphoserine.  
Keyword
 ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Stress response. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 705 AA 
Protein Sequence
MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL SDPKQLETEP 60
DLFIRITPKP EEKVLEIRDS GIGMTKAELI NNLGTIAKSG TKAFMEALSA GADVSMIGQF 120
GVGFYSLFLV ADRVQVISKN NEDEQYIWES NAGGSFTVTL DEVNERIGRG TVLRLFLKDD 180
QLEYLEEKRI KEVIKRHSEF VAYPIQLLVT KEVEKEVPIP EEEKKDEEKK DEDDKKPKLE 240
EVDEEEEEKK PKTKKVKEEV QELEELNKTK PLWTRNPSDI TQEEYNAFYK SISNDWEDPL 300
YVKHFSVEGQ LEFRAILFIP KRAPFDLFES KKKKNNIKLY VRRVFITDEA EDLIPEWLSF 360
VKGVVDSEDL PLNLSREMLQ QNKIMKVIRK NIVKKLIEAF NEIAEDSEQF DKFYSAFAKN 420
IKLGVHEDTQ NRAALAKLLR YNSTKSVDEL TSLTDYVTRM PEHQKNIYYI TGESLKAVEK 480
SPFLDALKAK NFEVLFLTDP IDEYAFTQLK EFEGKTLVDI TKDFELEETD EEKAEREKEI 540
KEYEPLTKAL KDILGDQVEK VVVSYKLLDA PAAIRTGQFG WSANMERIMK AQALRDSSMS 600
SYMSSKKTFE ISPKSPIIKE LKKRVDEGGA QDKTVKDLTN LLFETALLTS GFSLEEPTSF 660
ASRINRLISL GLNIDEDEET ETAPEASTEA PVEEVPADTE MEEVD 705 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042623; F:ATPase activity, coupled; ISS:SGD.
 GO:0051082; F:unfolded protein binding; IDA:SGD.
 GO:0006458; P:'de novo' protein folding; ISS:SGD.
 GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
 GO:0043248; P:proteasome assembly; IMP:SGD.
 GO:0042026; P:protein refolding; ISS:SGD.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0000723; P:telomere maintenance; IMP:SGD. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR019805; Heat_shock_protein_90_CS.
 IPR001404; Hsp90.
 IPR020575; Hsp90_N.
 IPR020568; Ribosomal_S5_D2-typ_fold. 
Pfam
 PF02518; HATPase_c
 PF00183; HSP90 
SMART
 SM00387; HATPase_c 
PROSITE
 PS00298; HSP90 
PRINTS
 PR00775; HEATSHOCK90.