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P07901 (HS90A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock protein HSP 90-alpha
Alternative name(s):
Heat shock 86 kDa
Short name=HSP 86
Short name=HSP86
Tumor-specific transplantation 86 kDa antigen
Short name=TSTA
Gene names
Name:Hsp90aa1
Synonyms:Hsp86, Hsp86-1, Hspca
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length733 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. HAMAP-Rule MF_00505

Subunit structure

Homodimer. 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. 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 By similarity. Ref.5 Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasm. Melanosome By similarity. Cell membrane By similarity Ref.11.

Domain

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1 By similarity. HAMAP-Rule MF_00505

Post-translational modification

ISGylated. Ref.13

S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1 By similarity. HAMAP-Rule MF_00505

Sequence similarities

Belongs to the heat shock protein 90 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCell membrane
Cytoplasm
Membrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchaperone-mediated protein complex assembly

Inferred from electronic annotation. Source: Ensembl

nitric oxide biosynthetic process

Traceable author statement PubMed 12855682. Source: UniProtKB

positive regulation of cytotoxic T cell differentiation

Traceable author statement PubMed 12855682. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay PubMed 12855682. Source: UniProtKB

protein import into mitochondrial outer membrane

Inferred from electronic annotation. Source: Ensembl

protein refolding

Traceable author statement PubMed 12855682. Source: UniProtKB

regulation of catalytic activity

Inferred from direct assay PubMed 12855682. Source: GOC

response to unfolded protein

Traceable author statement PubMed 12855682. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17908927. Source: MGI

cytosol

Traceable author statement PubMed 12855682. Source: UniProtKB

intracellular

Inferred from direct assay PubMed 9122205. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: GOC

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from electronic annotation. Source: Ensembl

TPR domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

nitric-oxide synthase regulator activity

Inferred from direct assay PubMed 12855682. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12855682. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 12885400. Source: MGI

unfolded protein binding

Traceable author statement PubMed 12855682. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Akt1P317506EBI-78930,EBI-298707
Itgb1bp2Q9R0005EBI-78930,EBI-7922331

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 733732Heat shock protein HSP 90-alpha HAMAP-Rule MF_00505
PRO_0000062912

Regions

Region683 – 73351Required for homodimerization By similarity
Motif729 – 7335TPR repeat-binding HAMAP-Rule MF_00505

Sites

Binding site511ATP By similarity
Binding site931ATP By similarity
Binding site1121ATP By similarity
Binding site1381ATP; via amide nitrogen By similarity
Binding site4011ATP By similarity

Amino acid modifications

Modified residue51Phosphothreonine; by PRKDC HAMAP-Rule MF_00505
Modified residue71Phosphothreonine; by PRKDC HAMAP-Rule MF_00505
Modified residue581N6-acetyllysine Ref.19
Modified residue841N6-acetyllysine Ref.19
Modified residue2311Phosphoserine By similarity
Modified residue2521Phosphoserine By similarity
Modified residue2631Phosphoserine Ref.15 Ref.17 Ref.18
Modified residue3141Phosphotyrosine Ref.16
Modified residue4001Phosphoserine By similarity
Modified residue4441N6-acetyllysine By similarity
Modified residue4591N6-acetyllysine By similarity
Modified residue4901N6-acetyllysine By similarity
Modified residue4931Phosphotyrosine Ref.14
Modified residue5861N6-acetyllysine By similarity
Modified residue5991S-nitrosocysteine By similarity

Experimental info

Sequence conflict71T → A in AAA37868. Ref.6
Sequence conflict242 – 2454Missing in AAA37868. Ref.6
Sequence conflict3561R → K in AAA37868. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P07901 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: D92B8FD38A463B4E

FASTA73384,788
        10         20         30         40         50         60 
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR 

        70         80         90        100        110        120 
YESLTDPSKL DSGKELHINL IPSKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME 

       130        140        150        160        170        180 
ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM 

       190        200        210        220        230        240 
GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE 

       250        260        270        280        290        300 
KEEEKEKEEK ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR 

       310        320        330        340        350        360 
NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF DLFENRKKKN 

       370        380        390        400        410        420 
NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK 

       430        440        450        460        470        480 
CLELFTELAE DKENYKKFYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSA SGDEMVSLKD 

       490        500        510        520        530        540 
YCTRMKENQK HIYFITGETK DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK 

       550        560        570        580        590        600 
TLVSVTKEGL ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI 

       610        620        630        640        650        660 
VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK AEADKNDKSV 

       670        680        690        700        710        720 
KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID EDDPTVDDTS AAVTEEMPPL 

       730 
EGDDDTSRME EVD 

« Hide

References

« Hide 'large scale' references
[1]"Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome assignments, and evolutionary origins."
Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.
J. Biol. Chem. 264:5343-5351(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Mapping of the mouse 86-kDa heat-shock protein expressed gene (Hsp86-1) on chromosome 12 and related genes on chromosomes 3, 4, 9, and 11."
Moore S.K., Appella E., Villar C.J., Kozak C.A.
Genomics 10:1019-1029(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Retina.
[4]"A mouse tumor-specific transplantation antigen is a heat shock-related protein."
Ullrich S.J., Robinson E.A., Law L.W., Willingham M., Appella E.
Proc. Natl. Acad. Sci. U.S.A. 83:3121-3125(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31.
[5]"The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo."
Minami Y., Kimura Y., Kawasaki H., Suzuki K., Yahara I.
Mol. Cell. Biol. 14:1459-1464(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12, HOMODIMERIZATION.
[6]"Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens."
Hoffmann T., Hovemann B.
Gene 74:491-501(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-356.
[7]Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 47-58; 61-69; 75-84; 88-112; 154-173; 186-201; 210-224; 285-356; 369-401; 448-457; 491-511; 515-535; 548-561; 569-574; 593-632 AND 634-648.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[8]"High constitutive transcription of HSP86 gene in murine embryonal carcinoma cells."
Legagneux V., Mezger V., Quelard C., Barnier J.V., Bensaude O., Morange M.
Differentiation 41:42-48(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 460-733.
[9]"Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4; PPID; PPP5C OR STIP1.
[10]"Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus."
Galigniana M.D., Radanyi C., Renoir J.-M., Housley P.R., Pratt W.B.
J. Biol. Chem. 276:14884-14889(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND FKBP4.
[11]"A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins."
Davies T.H., Ning Y.M., Sanchez E.R.
J. Biol. Chem. 277:4597-4600(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A HETEROMULTIMERIC COMPLEX WITH NR3C1 AND FKBP4 OR FKBP5, SUBCELLULAR LOCATION.
[12]"The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues."
Lees-Miller S.P., Anderson C.W.
J. Biol. Chem. 264:17275-17280(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PRKDC AT THR-5 AND THR-7.
[13]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[14]"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Mast cell.
[15]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[16]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[17]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[18]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-84, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04633 mRNA. Translation: AAA53068.1.
M57673 Genomic DNA. Translation: AAA37867.1.
BC046614 mRNA. Translation: AAH46614.1.
M36830 mRNA. Translation: AAA37868.1.
X16857 mRNA. Translation: CAA34748.1.
CCDSCCDS26172.1.
PIRHHMS86. B32848.
RefSeqNP_034610.1. NM_010480.5.
UniGeneMm.1843.
Mm.315997.
Mm.341186.
Mm.440626.
Mm.486334.

3D structure databases

ProteinModelPortalP07901.
SMRP07901. Positions 11-700.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200455. 18 interactions.
DIPDIP-30975N.
IntActP07901. 25 interactions.
MINTMINT-152660.

Chemistry

BindingDBP07901.
ChEMBLCHEMBL4197.

PTM databases

PhosphoSiteP07901.

2D gel databases

REPRODUCTION-2DPAGEP07901.

Proteomic databases

MaxQBP07901.
PaxDbP07901.
PRIDEP07901.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021698; ENSMUSP00000021698; ENSMUSG00000021270.
ENSMUST00000094361; ENSMUSP00000091921; ENSMUSG00000021270.
GeneID15519.
KEGGmmu:15519.
UCSCuc007pbq.1. mouse.

Organism-specific databases

CTD3320.
MGIMGI:96250. Hsp90aa1.

Phylogenomic databases

eggNOGCOG0326.
HOGENOMHOG000031988.
HOVERGENHBG007374.
InParanoidP07901.
KOK04079.
OMAKEDQTEF.
OrthoDBEOG780RM0.
PhylomeDBP07901.
TreeFamTF300686.

Gene expression databases

BgeeP07901.
GenevestigatorP07901.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
HAMAPMF_00505. HSP90.
InterProIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PfamPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288436.
PROP07901.
SOURCESearch...

Entry information

Entry nameHS90A_MOUSE
AccessionPrimary (citable) accession number: P07901
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 159 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot