CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002557
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heat shock protein HSP 90-alpha 
Protein Synonyms/Alias
 Heat shock 86 kDa; HSP 86; HSP86; Renal carcinoma antigen NY-REN-38 
Gene Name
 HSP90AA1 
Gene Synonyms/Alias
 HSP90A; HSPC1; HSPCA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
180NSSDALDKIRYESLTubiquitination[1, 2, 3]
191ESLTDPSKLDSGKELubiquitination[2]
196PSKLDSGKELHINLIubiquitination[1, 2, 3, 4]
206HINLIPNKQDRTLTIubiquitination[2, 3, 5]
222DTGIGMTKADLINNLubiquitination[5]
234NNLGTIAKSGTKAFMubiquitination[1, 2, 3, 5]
307EPMGRGTKVILHLKEubiquitination[1, 5]
313TKVILHLKEDQTEYLubiquitination[5]
331RIKEIVKKHSQFIGYubiquitination[3, 4]
346PITLFVEKERDKEVSubiquitination[1, 2, 3, 4]
405KKKKIKEKYIDQEELubiquitination[1]
414IDQEELNKTKPIWTRubiquitination[1]
416QEELNKTKPIWTRNPubiquitination[1, 2, 4, 5]
436EEYGEFYKSLTNDWEubiquitination[3, 4, 5]
449WEDHLAVKHFSVEGQubiquitination[2]
484RKKKNNIKLYVRRVFubiquitination[1, 5]
529REMLQQSKILKVIRKubiquitination[1, 5]
541IRKNLVKKCLELFTEubiquitination[2, 3, 5]
558EDKENYKKFYEQFSKubiquitination[2, 3]
565KFYEQFSKNIKLGIHubiquitination[1, 2, 3, 4, 5]
568EQFSKNIKLGIHEDSubiquitination[2, 3, 5]
579HEDSQNRKKLSELLRubiquitination[2]
580EDSQNRKKLSELLRYubiquitination[2]
600GDEMVSLKDYCTRMKubiquitination[2, 5]
607KDYCTRMKENQKHIYubiquitination[2]
611TRMKENQKHIYYITGubiquitination[1, 2, 3, 4]
621YYITGETKDQVANSAubiquitination[2, 3, 4]
661QLKEFEGKTLVSVTKubiquitination[1, 2, 3]
668KTLVSVTKEGLELPEubiquitination[1, 4]
689KQEEKKTKFENLCKIubiquitination[1]
698ENLCKIMKDILEKKVubiquitination[2]
703IMKDILEKKVEKVVVubiquitination[2]
704MKDILEKKVEKVVVSubiquitination[2]
707ILEKKVEKVVVSNRLubiquitination[2]
737ANMERIMKAQALRDNubiquitination[1, 5]
753TMGYMAAKKHLEINPubiquitination[2, 4, 5]
754MGYMAAKKHLEINPDubiquitination[1, 2, 3]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
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. 
Sequence Annotation
 REGION 682 732 Required for homodimerization.
 MOTIF 728 732 TPR repeat-binding.
 BINDING 51 51 ATP.
 BINDING 93 93 ATP.
 BINDING 112 112 ATP (By similarity).
 BINDING 138 138 ATP; via amide nitrogen.
 BINDING 400 400 ATP (By similarity).
 MOD_RES 5 5 Phosphothreonine; by PRKDC.
 MOD_RES 7 7 Phosphothreonine; by PRKDC.
 MOD_RES 224 224 N6-acetyllysine.
 MOD_RES 231 231 Phosphoserine.
 MOD_RES 252 252 Phosphoserine.
 MOD_RES 263 263 Phosphoserine.
 MOD_RES 313 313 Phosphotyrosine (By similarity).
 MOD_RES 399 399 Phosphoserine.
 MOD_RES 410 410 N6-acetyllysine.
 MOD_RES 443 443 N6-acetyllysine.
 MOD_RES 458 458 N6-acetyllysine.
 MOD_RES 489 489 N6-acetyllysine.
 MOD_RES 492 492 Phosphotyrosine (By similarity).
 MOD_RES 576 576 N6-acetyllysine.
 MOD_RES 585 585 N6-acetyllysine.
 MOD_RES 598 598 S-nitrosocysteine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Reference proteome; S-nitrosylation; Stress response; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 732 AA 
Protein Sequence
MPPCSGGDGS TPPGPSLRDR DCPAQSAEYP RDRLDPRPGS PSEASSPPFL RSRAPVNWYQ 60
EKAQVFLWHL MVSGSTTLLC LWKQPFHVSA FPVTASLAFR QSQGAGQHLY KDLQPFILLR 120
LLMPEETQTQ DQPMEEEEVE TFAFQAEIAQ LMSLIINTFY SNKEIFLREL ISNSSDALDK 180
IRYESLTDPS KLDSGKELHI NLIPNKQDRT LTIVDTGIGM TKADLINNLG TIAKSGTKAF 240
MEALQAGADI SMIGQFGVGF YSAYLVAEKV TVITKHNDDE QYAWESSAGG SFTVRTDTGE 300
PMGRGTKVIL HLKEDQTEYL EERRIKEIVK KHSQFIGYPI TLFVEKERDK EVSDDEAEEK 360
EDKEEEKEKE EKESEDKPEI EDVGSDEEEE KKDGDKKKKK KIKEKYIDQE ELNKTKPIWT 420
RNPDDITNEE YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFVPRRAP FDLFENRKKK 480
NNIKLYVRRV FIMDNCEELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNLVK 540
KCLELFTELA EDKENYKKFY EQFSKNIKLG IHEDSQNRKK LSELLRYYTS ASGDEMVSLK 600
DYCTRMKENQ KHIYYITGET KDQVANSAFV ERLRKHGLEV IYMIEPIDEY CVQQLKEFEG 660
KTLVSVTKEG LELPEDEEEK KKQEEKKTKF ENLCKIMKDI LEKKVEKVVV SNRLVTSPCC 720
IVTSTYGWTA NMERIMKAQA LRDNSTMGYM AAKKHLEINP DHSIIETLRQ KAEADKNDKS 780
VKDLVILLYE TALLSSGFSL EDPQTHANRI YRMIKLGLGI DEDDPTADDT SAAVTEEMPP 840
LEGDDDTSRM EEVD 854 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:Compara.
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0031526; C:brush border membrane; IEA:Compara.
 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005829; C:cytosol; NAS:UniProtKB.
 GO:0031012; C:extracellular matrix; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0005524; F:ATP binding; TAS:UniProtKB.
 GO:0016887; F:ATPase activity; IDA:UniProtKB.
 GO:0002135; F:CTP binding; IEA:Compara.
 GO:0032564; F:dATP binding; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:Compara.
 GO:0003729; F:mRNA binding; IEA:Compara.
 GO:0030235; F:nitric-oxide synthase regulator activity; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
 GO:0030911; F:TPR domain binding; IDA:UniProtKB.
 GO:0002134; F:UTP binding; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Compara.
 GO:0051131; P:chaperone-mediated protein complex assembly; IDA:BHF-UCL.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0046209; P:nitric oxide metabolic process; TAS:Reactome.
 GO:0060452; P:positive regulation of cardiac muscle contraction; IEA:Compara.
 GO:0045793; P:positive regulation of cell size; IEA:Compara.
 GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Compara.
 GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
 GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Compara.
 GO:0045040; P:protein import into mitochondrial outer membrane; IDA:BHF-UCL.
 GO:0042026; P:protein refolding; TAS:UniProtKB.
 GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
 GO:0043627; P:response to estrogen stimulus; IEA:Compara.
 GO:0009408; P:response to heat; IEA:Compara.
 GO:0009651; P:response to salt stress; IEA:Compara.
 GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
 GO:0003009; P:skeletal muscle contraction; IEA:Compara. 
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.