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Overview

Uniprot IDO02705
Protein NameHeat shock protein HSP 90-alpha
Gene NameHSP90AA1
OrganismSus scrofa

Kla Sites from experimental identification

Position Flanking peptide
112 NNLGTIAKSGTKAFM
185 EPMGRGTKVILHLKE
191 TKVILHLKEDQTEYL
209 RIKEIVKKHSQFIGY
284 KKKKIKEKYIDQEEL
293 IDQEELNKTKPIWTR
363 RKKKNNIKLYVRRVF
408 REMLQQSKILKVIRK
420 IRKNLVKKCLELFTE
437 EDKENYKKFYEQFSK
444 KFYEQFSKNIKLGIH
447 EQFSKNIKLGIHEDS
459 EDSQNRKKLSELLRY
490 TRMKENQKHIYYITG
500 YYITGETKDQVANSA
540 QLKEFEGKTLVSVTK
547 KTLVSVTKEGLELPE
559 LPEDEEEKKKQEEKK
566 KKKQEEKKTKFENLC
568 KQEEKKTKFENLCKI
574 TKFENLCKIMKDILE
577 ENLCKIMKDILEKKV
58 NSSDALDKIRYESLT
586 ILEKKVEKVVVSNRL
616 ANMERIMKAQALRDN
633 MGYMAAKKHLEINPD
658 AEADKNDKSVKDLVI
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 SDDEAEEKED 250 KEEEKEKEEK 260 ESEDKPEIED 270 VGSDEEEEEK 280 KDGDKKKKKK 290 IKEKYIDQEE 300 LNKTKPIWTR 310 NPDDITNEEY 320 GEFYKSLTND 330 WEDHLAVKHF 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 HIYYITGETK 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 EDDPTADDSS 720 AAVTEEMPPL 730 EGDDDTSRME EVD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
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:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032991 protein-containing complex
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:0030235 nitric-oxide synthase regulator activity
Molecular Function GO:0030911 TPR domain binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0002218 activation of innate immune response
Biological Process GO:0034605 cellular response to heat
Biological Process GO:0098586 cellular response to virus
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:0045429 positive regulation of nitric oxide biosynthetic process
Biological Process GO:0006457 protein folding
Biological Process GO:0050821 protein stabilization
Biological Process GO:0042981 regulation of apoptotic process
Biological Process GO:0046677 response to antibiotic
Biological Process GO:0009409 response to cold
Biological Process GO:0009408 response to heat

Reference

[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.