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Protein

Heat shock protein HSP 90-alpha

Gene

HSP90AA1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei51ATPBy similarity1
Binding sitei93ATPBy similarity1
Binding sitei112ATPBy similarity1
Binding sitei138ATP; via amide nitrogenBy similarity1
Binding sitei376ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein HSP 90-alpha
Gene namesi
Name:HSP90AA1
Synonyms:HSPCA
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00004098182 – 694Heat shock protein HSP 90-alphaBy similarityAdd BLAST693

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5Phosphothreonine; by PRKDC1 Publication1
Modified residuei7Phosphothreonine; by PRKDC1 Publication1
Modified residuei58N6-acetyllysineBy similarity1
Modified residuei84N6-acetyllysineBy similarity1
Modified residuei231PhosphoserineBy similarity1
Modified residuei249PhosphoserineBy similarity1
Modified residuei289PhosphotyrosineBy similarity1
Modified residuei375PhosphoserineBy similarity1
Modified residuei419N6-acetyllysineBy similarity1
Modified residuei429PhosphoserineBy similarity1
Modified residuei434N6-acetyllysineBy similarity1
Modified residuei452PhosphoserineBy similarity1
Modified residuei465N6-acetyllysineBy similarity1
Modified residuei468PhosphotyrosineBy similarity1
Modified residuei547N6-acetyllysineBy similarity1
Modified residuei560S-nitrosocysteineBy similarity1
Modified residuei603PhosphoserineBy similarity1

Post-translational modificationi

ISGylated.By similarity
S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PRIDEiP30946.

PTM databases

iPTMnetiP30946.

Interactioni

Subunit structurei

Homodimer (By similarity). Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C or STIP1 (PubMed:9195923). Interacts with HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8. Interacts with KSR1. Interacts with co-chaperone CDC37 (via C-terminus); the interaction inhibits HSP90AA1 ATPase activity. May interact with NWD1. Interacts with FNIP1 and FNIP2; the interaction inhibits HSP90AA1 ATPase activity. Interacts with AHSA1; the interaction activates HSP90AA1 ATPase activity. Interacts with FLCN in the presence of FNIP1. Interacts with HSP70, STIP1 and PTGES3 (By similarity).By similarity1 Publication

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000001106.

Structurei

3D structure databases

ProteinModelPortaliP30946.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni261 – 694Interaction with FLCN and FNIP1By similarityAdd BLAST434
Regioni261 – 582Interaction with FNIP2By similarityAdd BLAST322
Regioni644 – 694Required for homodimerizationBy similarityAdd BLAST51

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi685 – 694TPR repeat-bindingBy similarity10

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiKOG0020. Eukaryota.
COG0326. LUCA.
HOGENOMiHOG000031988.
InParanoidiP30946.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS
60 70 80 90 100
NSSDALDKIR YESLTDPSKL DSGKELHINL IPNKQDRTLT IVDTGIGMTK
110 120 130 140 150
ADLINNLGTI AKSGTKAFME ALQAGADISM IGQFGVGFYS AYLVAEKVTV
160 170 180 190 200
ITKHNDDEQY AWESSAGGSF TVRTDAGEPM GRGTKVVLHL KEDQTEYLEE
210 220 230 240 250
RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAKQPDD KPEIEDVGSD
260 270 280 290 300
EEEEEKKDGD IDQEELNKTK PIWTRNPDDI TNEEYGEFYK SLTNDWEDHL
310 320 330 340 350
AVKHFSVEGQ LEFRALLFVP RRAPFDLFEN RKKKNNIKLY VRRVFIMDNC
360 370 380 390 400
EELIPEYLNF IRGVVDSEDL PLNISREMLQ QSKILKVIRK NLVKKCLELF
410 420 430 440 450
TELAEDKENY KKFYEQFSKN IKLGIHEDSQ NRKKLSELLR YYTSASGDEM
460 470 480 490 500
VSLKDYCTRM KENQKHIYYI TGETKDQVAN SAFVERLRKH GLEVIYMIEP
510 520 530 540 550
IDEYCVQQLK EFEGKTLVSV TKEGLELTKF ENLCKIMKDI LEKKVEKVVV
560 570 580 590 600
SNRLVTSPCC IVTSTYGWTA NMERIMKAQA LRDNSTMGYM AAKKHLEVNP
610 620 630 640 650
DHSIIETLRQ KAEADKNDKS VKDLVILLYE TALLSSGFSL EDPQTHANRI
660 670 680 690
YRMIKLGLGI DEDDPTADDT AAAVTEEMPP LEGDDDTSRM EEVD
Length:694
Mass (Da):79,733
Last modified:June 28, 2011 - v2
Checksum:iB080801B6C141D05
GO

Sequence databases

PIRiA34461.

Cross-referencesi

Sequence databases

PIRiA34461.

3D structure databases

ProteinModelPortaliP30946.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000001106.

PTM databases

iPTMnetiP30946.

Proteomic databases

PRIDEiP30946.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0020. Eukaryota.
COG0326. LUCA.
HOGENOMiHOG000031988.
InParanoidiP30946.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90. 1 hit.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHS90A_RABIT
AccessioniPrimary (citable) accession number: P30946
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: June 28, 2011
Last modified: November 30, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.