CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006360
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein HSP 90-beta 
Protein Synonyms/Alias
 Heat shock 84 kDa; HSP 84; HSP84 
Gene Name
 Hsp90ab1 
Gene Synonyms/Alias
 Hsp84; Hspcb 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
36INTFYSNKEIFLRELacetylation[1]
53NASDALDKIRYESLTacetylation[1]
69PSKLDSGKELKIDIIacetylation[1]
107NNLGTIAKSGTKAFMubiquitination[2]
180EPIGRGTKVILHLKEubiquitination[2]
275KTKKIKEKYIDQEELubiquitination[2]
350LFENKKKKNNIKLYVacetylation[1]
354KKKKNNIKLYVRRVFacetylation[1]
624MGYMMAKKHLEINPDubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
Functional Description
 Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). 
Sequence Annotation
 MOTIF 720 724 TPR repeat-binding.
 BINDING 46 46 ATP (By similarity).
 BINDING 88 88 ATP (By similarity).
 BINDING 107 107 ATP (By similarity).
 BINDING 133 133 ATP; via amide nitrogen (By similarity).
 BINDING 392 392 ATP (By similarity).
 MOD_RES 226 226 Phosphoserine (By similarity).
 MOD_RES 255 255 Phosphoserine (By similarity).
 MOD_RES 261 261 Phosphoserine (By similarity).
 MOD_RES 275 275 N6-acetyllysine (By similarity).
 MOD_RES 284 284 N6-acetyllysine (By similarity).
 MOD_RES 297 297 Phosphothreonine (By similarity).
 MOD_RES 305 305 Phosphotyrosine (By similarity).
 MOD_RES 307 307 Phosphoserine (By similarity).
 MOD_RES 354 354 N6-acetyllysine (By similarity).
 MOD_RES 399 399 N6-acetyllysine; alternate (By
 MOD_RES 399 399 N6-malonyllysine; alternate (By
 MOD_RES 402 402 N6-acetyllysine (By similarity).
 MOD_RES 435 435 N6-acetyllysine (By similarity).
 MOD_RES 452 452 Phosphoserine; alternate (By similarity).
 MOD_RES 481 481 N6-acetyllysine (By similarity).
 MOD_RES 484 484 Phosphotyrosine (By similarity).
 MOD_RES 532 532 Phosphoserine (By similarity).
 MOD_RES 568 568 N6-acetyllysine (By similarity).
 MOD_RES 590 590 S-nitrosocysteine (By similarity).
 MOD_RES 624 624 N6-acetyllysine (By similarity).
 MOD_RES 718 718 Phosphoserine (By similarity).
 CARBOHYD 434 434 O-linked (GlcNAc...) (By similarity).
 CARBOHYD 452 452 O-linked (GlcNAc...); alternate (By  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Nucleotide-binding; Phosphoprotein; Reference proteome; S-nitrosylation; Stress response; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 724 AA 
Protein Sequence
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT 60
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG 120
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK 180
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE 240
DKEDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE 300
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV 360
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA 420
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ 480
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG 540
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA 600
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE 660
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP SAAVPDEIPP LEGDEDASRM 720
EEVD 724 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IDA:RGD.
 GO:0016323; C:basolateral plasma membrane; IDA:RGD.
 GO:0031526; C:brush border membrane; IDA:RGD.
 GO:0009986; C:cell surface; IDA:RGD.
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0016234; C:inclusion body; IDA:RGD.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0008180; C:signalosome; IEA:Compara.
 GO:0005524; F:ATP binding; IDA:RGD.
 GO:0002135; F:CTP binding; IDA:RGD.
 GO:0032564; F:dATP binding; IDA:RGD.
 GO:0005525; F:GTP binding; IDA:RGD.
 GO:0002134; F:UTP binding; IDA:RGD.
 GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
 GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
 GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
 GO:0001890; P:placenta development; IEA:Compara.
 GO:0045793; P:positive regulation of cell size; IMP:RGD.
 GO:0032092; P:positive regulation of protein binding; IMP:RGD.
 GO:0033160; P:positive regulation of protein import into nucleus, translocation; IMP:RGD.
 GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:RGD.
 GO:0006457; P:protein folding; TAS:RGD.
 GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IEA:Compara.
 GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IEA:Compara.
 GO:0009651; P:response to salt stress; IEP:RGD.
 GO:0006986; P:response to unfolded protein; TAS:RGD. 
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.