Heat shock protein HSP 90-alpha - Rattus norvegicus (Rat)

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P82995 (HS90A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. History...

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

Documents (1) |

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

Gene names

Name:	Hsp90aa1
Synonyms:	Hsp86, Hspca

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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. 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 By similarity.
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 By similarity. 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	cardiac muscle cell apoptotic process Inferred from expression pattern PubMed 21620734. Source: RGD neuron migration Inferred from mutant phenotype PubMed 15302889. Source: RGD positive regulation of cardiac muscle contraction Inferred from expression pattern PubMed 21620734. Source: RGD positive regulation of cell size Inferred from mutant phenotype PubMed 20980790. Source: RGD positive regulation of lamellipodium assembly Inferred from mutant phenotype PubMed 15302889. Source: RGD positive regulation of nitric oxide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein import into nucleus, translocation Inferred from mutant phenotype PubMed 20980790. Source: RGD protein folding Traceable author statement PubMed 12755697. Source: RGD response to estrogen stimulus Inferred from expression pattern PubMed 15229138. Source: RGD response to heat Inferred from expression pattern PubMed 12215673. Source: RGD response to salt stress Inferred from expression pattern PubMed 15497505. Source: RGD skeletal muscle contraction Inferred from expression pattern PubMed 20851858. Source: RGD
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 15497505. Source: RGD basolateral plasma membrane Inferred from direct assay PubMed 15497505. Source: RGD brush border membrane Inferred from direct assay PubMed 15497505. Source: RGD cell surface Inferred from direct assay PubMed 15302889. Source: RGD cytosol Inferred from direct assay PubMed 15497505. Source: RGD extracellular matrix Inferred from direct assay PubMed 15497505. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell neuron projection Inferred from direct assay PubMed 20796173. Source: RGD neuronal cell body Inferred from direct assay PubMed 20796173. Source: RGD perinuclear region of cytoplasm Inferred from direct assay PubMed 20796173. Source: RGD protein complex Inferred from direct assay PubMed 20796173. Source: RGD
Molecular_function	ATP binding Inferred from direct assay PubMed 12755697. Source: RGD CTP binding Inferred from direct assay PubMed 12755697. Source: RGD GTP binding Inferred from direct assay PubMed 12755697. Source: RGD TPR domain binding Inferred from sequence or structural similarity. Source: UniProtKB UTP binding Inferred from direct assay PubMed 12755697. Source: RGD dATP binding Inferred from direct assay PubMed 12755697. Source: RGD mRNA binding Inferred from direct assay PubMed 19703590. Source: RGD nitric-oxide synthase regulator activity Inferred from sequence or structural similarity. Source: UniProtKB unfolded protein binding Traceable author statement PubMed 12755697. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 733

732

Heat shock protein HSP 90-alpha

PRO_0000062915

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 By similarity

Modified residue

Phosphothreonine; by PRKDC By similarity

Modified residue

224

N6-acetyllysine By similarity

Modified residue

231

Phosphoserine By similarity

Modified residue

252

Phosphoserine By similarity

Modified residue

263

Phosphoserine By similarity

Modified residue

314

Phosphotyrosine By similarity

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 By similarity

Modified residue

577

N6-acetyllysine By similarity

Modified residue

586

N6-acetyllysine By similarity

Modified residue

599

S-nitrosocysteine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P82995 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DF2C8383A6581D07
Show »

FASTA

733

84,815

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

        70         80         90        100        110        120 
YESLTDPSKL DSGKELHINL IPNKQDRTLT 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]	"Cloning of rat 86-kDa heat shock protein gene and promoter." Li C.W., Chang M.T., Lai Y., Chang W.M., Lai Y.K. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[2]	"Cloning of full length cDNA of rat 86-kDa heat shock protein gene." Lai Y.R., Chang M.D., Chang W.M., Su C.Y., Lai Y.K. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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: Heart and Testis.
[4]	"Isolation and quantification of the heat shock protein 90 alpha and beta isoforms from rat liver." Langer T., Fasold H. Protoplasma 218:54-56(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: Sprague-Dawley. Tissue: Liver.
[5]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 154-173; 329-339 AND 347-356, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ297736 Genomic DNA. Translation: CAC39453.1. AJ428213 mRNA. Translation: CAD21648.1. BC072489 mRNA. Translation: AAH72489.1. BC085120 mRNA. Translation: AAH85120.1.
IPI	IPI00210566.
RefSeq	NP_786937.1. NM_175761.2.
UniGene	Rn.106682. Rn.119867. Rn.202494. Rn.3277.
3D structure databases
ProteinModelPortal	P82995.
SMR	P82995. Positions 9-223, 294-697.
ModBase	Search...
Protein-protein interaction databases
IntAct	P82995. 1 interaction.
MINT	MINT-1775917.
Proteomic databases
PaxDb	P82995.
PRIDE	P82995.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000009556; ENSRNOP00000009556; ENSRNOG00000007219.
GeneID	299331.
KEGG	rno:299331.
UCSC	RGD:631409. rat.
Organism-specific databases
CTD	3320.
RGD	631409. Hsp90aa1.
Phylogenomic databases
eggNOG	COG0326.
GeneTree	ENSGT00550000074382.
HOGENOM	HOG000031988.
HOVERGEN	HBG007374.
InParanoid	P82995.
KO	K04079.
OMA	DEACSLK.
OrthoDB	EOG42V8FM.
Gene expression databases
ArrayExpress	P82995.
Genevestigator	P82995.
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
NextBio	645227.

Entry information

Entry name

HS90A_RAT

Accession

Primary (citable) accession number: P82995
Secondary accession number(s): Q91XW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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