UniProt Accession

 HS90B_MOUSE; P11499; O89078; Q3UIQ7 

Genbank Protein ID

 M36829; M18186; AK146809; AC163677; U89426; S46109 

Genbank Nucleotide ID

 AAA37866.1; AAA37865.1; BAE27449.1; AAC36532.1; AAB23704.1 

Protein Name

 Heat shock protein HSP 90-beta 

Protein Synonyms/Alias

 Heat shock 84 kDa; HSP 84; HSP84; Tumor-specific transplantation 84 kDa antigen; TSTA 

Gene Name

 Hsp90ab1 

Gene Synonyms/Alias

 Hsp84; Hsp84-1; Hspcb 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
53	NASDALDKIRYESLT	ubiquitination	[1]
64	ESLTDPSKLDSGKEL	ubiquitination	[1]
69	PSKLDSGKELKIDII	ubiquitination	[1]
72	LDSGKELKIDIIPNP	ubiquitination	[1]
95	DTGIGMTKADLINNL	ubiquitination	[1]
107	NNLGTIAKSGTKAFM	ubiquitination	[1]
180	EPIGRGTKVILHLKE	ubiquitination	[1]
186	TKVILHLKEDQTEYL	ubiquitination	[1]
204	RVKEVVKKHSQFIGY	acetylation	[2, 3]
204	RVKEVVKKHSQFIGY	succinylation	[3]
204	RVKEVVKKHSQFIGY	ubiquitination	[1]
219	PITLYLEKEREKEIS	acetylation	[2, 3]
219	PITLYLEKEREKEIS	succinylation	[3]
219	PITLYLEKEREKEIS	ubiquitination	[1]
237	AEEEKGEKEEEDKED	ubiquitination	[1]
275	KTKKIKEKYIDQEEL	ubiquitination	[1]
284	IDQEELNKTKPIWTR	ubiquitination	[1]
286	QEELNKTKPIWTRNP	ubiquitination	[1]
306	EEYGEFYKSLTNDWE	ubiquitination	[1]
347	PFDLFENKKKKNNIK	ubiquitination	[1]
354	KKKKNNIKLYVRRVF	ubiquitination	[1]
399	REMLQQSKILKVIRK	ubiquitination	[1]
411	IRKNIVKKCLELFSE	ubiquitination	[1]
428	EDKENYKKFYEAFSK	ubiquitination	[1]
435	KFYEAFSKNLKLGIH	ubiquitination	[1]
438	EAFSKNLKLGIHEDS	ubiquitination	[1]
481	SRMKETQKSIYYITG	ubiquitination	[1]
491	YYITGESKEQVANSA	ubiquitination	[1]
531	QLKEFDGKSLVSVTK	acetylation	[3]
531	QLKEFDGKSLVSVTK	succinylation	[3]
531	QLKEFDGKSLVSVTK	ubiquitination	[1]
538	KSLVSVTKEGLELPE	acetylation	[2, 4]
538	KSLVSVTKEGLELPE	ubiquitination	[1]
550	LPEDEEEKKKMEESK	acetylation	[5]
551	PEDEEEKKKMEESKA	acetylation	[5]
559	KMEESKAKFENLCKL	acetylation	[2, 3, 5]
559	KMEESKAKFENLCKL	succinylation	[3]
559	KMEESKAKFENLCKL	ubiquitination	[1]
565	AKFENLCKLMKEILD	acetylation	[2]
565	AKFENLCKLMKEILD	ubiquitination	[1]
568	ENLCKLMKEILDKKV	acetylation	[2, 3, 4]
568	ENLCKLMKEILDKKV	succinylation	[3]
574	MKEILDKKVEKVTIS	ubiquitination	[1]
577	ILDKKVEKVTISNRL	acetylation	[2, 3]
577	ILDKKVEKVTISNRL	succinylation	[3]
607	ANMERIMKAQALRDN	ubiquitination	[1]
623	TMGYMMAKKHLEINP	acetylation	[2]
623	TMGYMMAKKHLEINP	ubiquitination	[1]
624	MGYMMAKKHLEINPD	acetylation	[2, 3]
624	MGYMMAKKHLEINPD	ubiquitination	[1]
646	RQKAEADKNDKAVKD	acetylation	[5]
649	AEADKNDKAVKDLVV	acetylation	[5]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 

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.
 MOD_RES 255 255 Phosphoserine.
 MOD_RES 261 261 Phosphoserine.
 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.
 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.
 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...).
 CARBOHYD 452 452 O-linked (GlcNAc...); alternate.  

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

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; IEA:Compara.
 GO:0016234; C:inclusion body; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0008180; C:signalosome; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0002135; F:CTP binding; IEA:Compara.
 GO:0032564; F:dATP binding; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:Compara.
 GO:0030235; F:nitric-oxide synthase regulator activity; ISS:UniProtKB.
 GO:0030911; F:TPR domain binding; ISS:UniProtKB.
 GO:0002134; F:UTP binding; IEA:Compara.
 GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
 GO:0071407; P:cellular response to organic cyclic compound; IEA:Compara.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
 GO:0001890; P:placenta development; IMP:MGI.
 GO:0045793; P:positive regulation of cell size; IEA:Compara.
 GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
 GO:0032092; P:positive regulation of protein binding; IEA:Compara.
 GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Compara.
 GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro.
 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; 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.