Heat shock protein HSP 90-alpha - Mus musculus (Mouse)

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P07901 (HS90A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 145. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	733 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Subunit structure	Homodimer. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34 By similarity. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex By similarity. Interacts with CHORDC1 and DNAJC7 By similarity. Ref.5
Subcellular location	Cytoplasm By similarity. Melanosome By similarity.
Domain	The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1 By similarity.
Post-translational modification	ISGylated. Ref.10 S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1 By similarity.
Sequence similarities	Belongs to the heat shock protein 90 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chaperone-mediated protein complex assembly Inferred from electronic annotation. Source: Compara 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: Compara protein refolding Traceable author statement PubMed 12855682. Source: UniProtKB response to unfolded protein Traceable author statement PubMed 12855682. Source: UniProtKB
Cellular_component	cytosol Traceable author statement PubMed 12855682. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: Compara 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 homodimerization activity Inferred from direct assay PubMed 12885400. Source: MGI unfolded protein binding Traceable author statement PubMed 12855682. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4 Ref.5

Chain

2 – 733

732

Heat shock protein HSP 90-alpha

PRO_0000062912

Regions

Region

683 – 733

Required for homodimerization By similarity

Motif

729 – 733

TPR repeat-binding

Sites

Binding site

ATP By similarity

Binding site

ATP By similarity

Binding site

112

ATP By similarity

Binding site

138

ATP; via amide nitrogen By similarity

Binding site

401

ATP By similarity

Amino acid modifications

Modified residue

Phosphothreonine; by PRKDC

Modified residue

Phosphothreonine; by PRKDC

Modified residue

224

N6-acetyllysine By similarity

Modified residue

231

Phosphoserine Ref.12 Ref.15 Ref.16

Modified residue

252

Phosphoserine By similarity

Modified residue

263

Phosphoserine Ref.12 Ref.14 Ref.16

Modified residue

314

Phosphotyrosine Ref.13

Modified residue

400

Phosphoserine By similarity

Modified residue

411

N6-acetyllysine By similarity

Modified residue

444

N6-acetyllysine By similarity

Modified residue

459

N6-acetyllysine By similarity

Modified residue

490

N6-acetyllysine By similarity

Modified residue

493

Phosphotyrosine Ref.11

Modified residue

577

N6-acetyllysine By similarity

Modified residue

586

N6-acetyllysine By similarity

Modified residue

599

S-nitrosocysteine By similarity

Experimental info

Sequence conflict

T → A in AAA37868. Ref.6

Sequence conflict

242 – 245

Missing in AAA37868. Ref.6

Sequence conflict

356

R → K in AAA37868. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P07901 [UniParc].

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

733

84,788

        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' referencesShow '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]	"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.
[10]	"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.
[11]	"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, MASS SPECTROMETRY. Tissue: Mast cell.
[12]	"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-231 AND SER-263, MASS SPECTROMETRY. Tissue: Liver.
[13]	"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, MASS SPECTROMETRY. Tissue: Brain.
[14]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, MASS SPECTROMETRY. Tissue: Liver.
[15]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, MASS SPECTROMETRY. Tissue: Melanoma.
+	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.
IPI	IPI00330804.
PIR	HHMS86. B32848.
RefSeq	NP_034610.1. NM_010480.5.
UniGene	Mm.1843. Mm.341186. Mm.440626. Mm.486334.
3D structure databases
ProteinModelPortal	P07901.
SMR	P07901. Positions 11-700.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-30975N.
IntAct	P07901. 13 interactions.
MINT	MINT-152660.
PTM databases
PhosphoSite	P07901.
2D gel databases
REPRODUCTION-2DPAGE	P07901.
Proteomic databases
PaxDb	P07901.
PRIDE	P07901.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021698; ENSMUSP00000021698; ENSMUSG00000021270. ENSMUST00000094361; ENSMUSP00000091921; ENSMUSG00000021270.
GeneID	15519.
KEGG	mmu:15519.
Organism-specific databases
CTD	3320.
MGI	MGI:96250. Hsp90aa1.
Phylogenomic databases
eggNOG	COG0326.
HOGENOM	HOG000031988.
HOVERGEN	HBG007374.
InParanoid	P07901.
KO	K04079.
OMA	DEACSLK.
OrthoDB	EOG42V8FM.
Gene expression databases
ArrayExpress	P07901.
Bgee	P07901.
Genevestigator	P07901.
GermOnline	ENSMUSG00000021270. Mus musculus.
Family and domain databases
Gene3D	3.30.565.10. 2 hits.
InterPro	IPR003594. HATPase_ATP-bd. IPR019805. Heat_shock_protein_90_CS. IPR001404. Hsp90. IPR020575. Hsp90_N. IPR020568. Ribosomal_S5_D2-typ_fold. [Graphical view]
PANTHER	PTHR11528. PTHR11528. 1 hit.
Pfam	PF02518. HATPase_c. 1 hit. PF00183. HSP90. 1 hit. [Graphical view]
PIRSF	PIRSF002583. Hsp90. 1 hit.
PRINTS	PR00775. HEATSHOCK90.
SMART	SM00387. HATPase_c. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
PROSITE	PS00298. HSP90. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P07901.
ChEMBL	CHEMBL4197.
NextBio	288436.
SOURCE	Search...

Entry information

Entry name

HS90A_MOUSE

Accession

Primary (citable) accession number: P07901

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents