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Overview

Uniprot IDP82995
Protein NameHeat shock protein HSP 90-alpha
Gene NameHsp90aa1
OrganismRattus norvegicus

Kla Sites from experimental identification

Position Flanking peptide
112 NNLGTIAKSGTKAFM
209 RIKEIVKKHSQFIGY
284 KKKKIKEKYIDQEEL
293 IDQEELNKTKPIWTR
408 REMLQQSKILKVIRK
437 EDKENYKKFYEQFSK
447 EQFSKNIKLGIHEDS
459 EDSQNRKKLSELLRY
540 QLKEFEGKTLVSVTK
568 KQEEKKTKFENLCKI
577 ENLCKIMKDILEKKV
58 NSSDALDKIRYESLT
586 ILEKKVEKVVVSNRL
632 TMGYMAAKKHLEINP
633 MGYMAAKKHLEINPD
69 ESLTDPSKLDSGKEL
74 PSKLDSGKELHINLI
84 HINLIPNKQDRTLTI

Function

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 which is essential for its chaperone 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. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response

Protein Sequence

10 MPEETQTQDQ 20 PMEEEEVETF 30 AFQAEIAQLM 40 SLIINTFYSN 50 KEIFLRELIS 60 NSSDALDKIR 70 YESLTDPSKL 80 DSGKELHINL 90 IPNKQDRTLT 100 IVDTGIGMTK 110 ADLINNLGTI 120 AKSGTKAFME 130 ALQAGADISM 140 IGQFGVGFYS 150 AYLVAEKVTV 160 ITKHNDDEQY 170 AWESSAGGSF 180 TVRTDTGEPM 190 GRGTKVILHL 200 KEDQTEYLEE 210 RRIKEIVKKH 220 SQFIGYPITL 230 FVEKERDKEV 240 SDDEAEEKEE 250 KEEEKEKEEK 260 ESDDKPEIED 270 VGSDEEEEEK 280 KDGDKKKKKK 290 IKEKYIDQEE 300 LNKTKPIWTR 310 NPDDITNEEY 320 GEFYKSLTND 330 WEEHLAVKHF 340 SVEGQLEFRA 350 LLFVPRRAPF 360 DLFENRKKKN 370 NIKLYVRRVF 380 IMDNCEELIP 390 EYLNFIRGVV 400 DSEDLPLNIS 410 REMLQQSKIL 420 KVIRKNLVKK 430 CLELFTELAE 440 DKENYKKFYE 450 QFSKNIKLGI 460 HEDSQNRKKL 470 SELLRYYTSA 480 SGDEMVSLKD 490 YCTRMKENQK 500 HIYFITGETK 510 DQVANSAFVE 520 RLRKHGLEVI 530 YMIEPIDEYC 540 VQQLKEFEGK 550 TLVSVTKEGL 560 ELPEDEEEKK 570 KQEEKKTKFE 580 NLCKIMKDIL 590 EKKVEKVVVS 600 NRLVTSPCCI 610 VTSTYGWTAN 620 MERIMKAQAL 630 RDNSTMGYMA 640 AKKHLEINPD 650 HSIIETLRQK 660 AEADKNDKSV 670 KDLVILLYET 680 ALLSSGFSLE 690 DPQTHANRIY 700 RMIKLGLGID 710 EDDPTVDDTS 720 AAVTEEMPPL 730 EGDDDTSRME EVD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0042470 melanosome
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0043209 myelin sheath
Cellular Component GO:0043025 neuronal cell body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0101031 protein folding chaperone complex
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0036126 sperm flagellum
Cellular Component GO:0097226 sperm mitochondrial sheath
Cellular Component GO:0097524 sperm plasma membrane
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0140662 ATP-dependent protein folding chaperone
Molecular Function GO:0002135 CTP binding
Molecular Function GO:0032564 dATP binding
Molecular Function GO:0097718 disordered domain specific binding
Molecular Function GO:0070182 DNA polymerase binding
Molecular Function GO:0140767 enzyme-substrate adaptor activity
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0051020 GTPase binding
Molecular Function GO:0042826 histone deacetylase binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0030235 nitric-oxide synthase regulator activity
Molecular Function GO:0140597 protein carrier chaperone
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0019903 protein phosphatase binding
Molecular Function GO:1990782 protein tyrosine kinase binding
Molecular Function GO:0051022 Rho GDP-dissociation inhibitor binding
Molecular Function GO:0097110 scaffold protein binding
Molecular Function GO:0017098 sulfonylurea receptor binding
Molecular Function GO:0048156 tau protein binding
Molecular Function GO:0030911 TPR domain binding
Molecular Function GO:0044325 transmembrane transporter binding
Molecular Function GO:0031625 ubiquitin protein ligase binding
Molecular Function GO:0051082 unfolded protein binding
Molecular Function GO:0002134 UTP binding
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:0010659 cardiac muscle cell apoptotic process
Biological Process GO:0034605 cellular response to heat
Biological Process GO:0098586 cellular response to virus
Biological Process GO:0061684 chaperone-mediated autophagy
Biological Process GO:0051131 chaperone-mediated protein complex assembly
Biological Process GO:1902988 neurofibrillary tangle assembly
Biological Process GO:0001764 neuron migration
Biological Process GO:0060452 positive regulation of cardiac muscle contraction
Biological Process GO:0045793 positive regulation of cell size
Biological Process GO:0002230 positive regulation of defense response to virus by host
Biological Process GO:0032728 positive regulation of interferon-beta production
Biological Process GO:0010592 positive regulation of lamellipodium assembly
Biological Process GO:0045429 positive regulation of nitric oxide biosynthetic process
Biological Process GO:0045732 positive regulation of protein catabolic process
Biological Process GO:0042307 positive regulation of protein import into nucleus
Biological Process GO:0032273 positive regulation of protein polymerization
Biological Process GO:0006457 protein folding
Biological Process GO:0030150 protein import into mitochondrial matrix
Biological Process GO:0050821 protein stabilization
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:0099072 regulation of postsynaptic membrane neurotransmitter receptor levels
Biological Process GO:0061635 regulation of protein complex stability
Biological Process GO:0032880 regulation of protein localization
Biological Process GO:0031396 regulation of protein ubiquitination
Biological Process GO:0046677 response to antibiotic
Biological Process GO:0042220 response to cocaine
Biological Process GO:0009409 response to cold
Biological Process GO:0043627 response to estrogen
Biological Process GO:0009408 response to heat
Biological Process GO:0009651 response to salt stress
Biological Process GO:0009410 response to xenobiotic stimulus
Biological Process GO:0003009 skeletal muscle contraction
Biological Process GO:1905323 telomerase holoenzyme complex assembly
Biological Process GO:0007004 telomere maintenance via telomerase
Cellular Component GO:0016324 apical plasma membrane
Cellular Component GO:0044295 axonal growth cone
Cellular Component GO:0016323 basolateral plasma membrane
Cellular Component GO:0031526 brush border membrane
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0044294 dendritic growth cone
Cellular Component GO:0031012 extracellular matrix
Cellular Component GO:0043202 lysosomal lumen
Cellular Component GO:0005765 lysosomal membrane

Reference

[1] Yao Y, Bade R, Li G, Zhang A, Zhao H et al.. Global-Scale Profiling of Differential Expressed Lysine-Lactylated Proteins in the Cerebral Endothelium of Cerebral Ischemia-Reperfusion Injury Rats.. Cell Mol Neurobiol 43(5):1989-2004. 2023 Jul. PMID: 36030297.

[2] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.

[3] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.