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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATPBy similarity
Binding sitei93 – 931ATPBy similarity
Binding sitei112 – 1121ATPBy similarity
Binding sitei138 – 1381ATP; via amide nitrogenBy similarity
Binding sitei376 – 3761ATPBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 694693Heat shock protein HSP 90-alphaBy similarityPRO_0000409818Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphothreonine; by PRKDC1 Publication
Modified residuei7 – 71Phosphothreonine; by PRKDC1 Publication
Modified residuei58 – 581N6-acetyllysineBy similarity
Modified residuei84 – 841N6-acetyllysineBy similarity
Modified residuei231 – 2311PhosphoserineBy similarity
Modified residuei249 – 2491PhosphoserineBy similarity
Modified residuei289 – 2891PhosphotyrosineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity
Modified residuei419 – 4191N6-acetyllysineBy similarity
Modified residuei429 – 4291PhosphoserineBy similarity
Modified residuei434 – 4341N6-acetyllysineBy similarity
Modified residuei452 – 4521PhosphoserineBy similarity
Modified residuei465 – 4651N6-acetyllysineBy similarity
Modified residuei468 – 4681PhosphotyrosineBy similarity
Modified residuei547 – 5471N6-acetyllysineBy similarity
Modified residuei560 – 5601S-nitrosocysteineBy similarity
Modified residuei603 – 6031PhosphoserineBy similarity

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

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 AHSA1, FNIP1, 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. May interact with NWD1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000001106.

Structurei

3D structure databases

ProteinModelPortaliP30946.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni644 – 69451Required for homodimerizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi690 – 6945TPR repeat-binding

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.

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: September 7, 2016
This is version 113 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.