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

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P34058 (HS90B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. 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-beta

Alternative name(s):
Heat shock 84 kDa
Short name=HSP 84
Short name=HSP84

Gene names

Name:	Hsp90ab1
Synonyms:	Hsp84, Hspcb

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	724 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 p53/TP53. Forms a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 and DNAJC7 By similarity. Interacts with FKBP4 By similarity. Ref.8
Subcellular location	Cytoplasm. Melanosome By similarity Ref.8.
Domain	The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins By similarity.
Post-translational modification	ISGylated By similarity. Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro) By similarity. S-nitrosylated; negatively regulates the ATPase activity 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 Glycoprotein Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to organic cyclic compound Inferred from expression pattern PubMed 10617604. Source: RGD negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 18443201. Source: RGD negative regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara placenta development Inferred from electronic annotation. Source: Compara positive regulation of cell size Inferred from mutant phenotype PubMed 20980790. Source: RGD positive regulation of protein binding Inferred from mutant phenotype PubMed 18443201. Source: RGD positive regulation of protein import into nucleus, translocation Inferred from mutant phenotype PubMed 20980790. Source: RGD positive regulation of protein serine/threonine kinase activity Inferred from mutant phenotype PubMed 18443201. Source: RGD protein folding Traceable author statement PubMed 10617604 PubMed 14987991. Source: RGD regulation of interferon-gamma-mediated signaling pathway Inferred from electronic annotation. Source: Compara regulation of type I interferon-mediated signaling pathway Inferred from electronic annotation. Source: Compara response to salt stress Inferred from expression pattern PubMed 15497505. Source: RGD response to unfolded protein Traceable author statement PubMed 10617604 PubMed 14987991. 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 19948165. Source: RGD cytosol Inferred from direct assay PubMed 15497505. Source: RGD inclusion body Inferred from direct assay PubMed 18445155. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara signalosome Inferred from electronic annotation. Source: Compara
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 UTP binding Inferred from direct assay PubMed 12755697. Source: RGD dATP binding Inferred from direct assay 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.5 Ref.6

Chain

2 – 724

723

Heat shock protein HSP 90-beta

PRO_0000062920

Regions

Motif

720 – 724

TPR repeat-binding

Sites

Binding site

ATP By similarity

Binding site

ATP By similarity

Binding site

107

ATP By similarity

Binding site

133

ATP; via amide nitrogen By similarity

Binding site

392

ATP By similarity

Amino acid modifications

Modified residue

226

Phosphoserine Ref.10

Modified residue

255

Phosphoserine Ref.9 Ref.10

Modified residue

261

Phosphoserine By similarity

Modified residue

275

N6-acetyllysine By similarity

Modified residue

284

N6-acetyllysine By similarity

Modified residue

297

Phosphothreonine By similarity

Modified residue

305

Phosphotyrosine By similarity

Modified residue

307

Phosphoserine By similarity

Modified residue

354

N6-acetyllysine By similarity

Modified residue

399

N6-acetyllysine; alternate By similarity

Modified residue

399

N6-malonyllysine; alternate By similarity

Modified residue

402

N6-acetyllysine By similarity

Modified residue

435

N6-acetyllysine By similarity

Modified residue

452

Phosphoserine; alternate By similarity

Modified residue

481

N6-acetyllysine By similarity

Modified residue

484

Phosphotyrosine By similarity

Modified residue

532

Phosphoserine By similarity

Modified residue

568

N6-acetyllysine By similarity

Modified residue

590

S-nitrosocysteine By similarity

Modified residue

624

N6-acetyllysine By similarity

Modified residue

718

Phosphoserine By similarity

Glycosylation

434

O-linked (GlcNAc...) By similarity

Glycosylation

452

O-linked (GlcNAc...); alternate By similarity

Experimental info

Sequence conflict

6 – 7

HH → QK AA sequence Ref.5

Sequence conflict

E → P AA sequence Ref.5

Sequence conflict

F → T AA sequence Ref.5

Sequence conflict

E → F AA sequence Ref.5

Sequence conflict

S → F in AAH82009. Ref.4

Sequence conflict

R → A in AAB23369. Ref.1

Sequence conflict

368

E → D in AAB23369. Ref.1

Sequence conflict

375

N → D in ABE27999. Ref.3

Sequence conflict

559

K → R in AAB23369. Ref.1

Sequence conflict

664 – 674

LSSGFSLEDPQ → SSLASHFRRPK in AAB23369. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P34058 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: CE323E81CE173ECB
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FASTA

724

83,281

        10         20         30         40         50         60 
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT 

        70         80         90        100        110        120 
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG 

       130        140        150        160        170        180 
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK 

       190        200        210        220        230        240 
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE 

       250        260        270        280        290        300 
DKEDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE 

       310        320        330        340        350        360 
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV 

       370        380        390        400        410        420 
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA 

       430        440        450        460        470        480 
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ 

       490        500        510        520        530        540 
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG 

       550        560        570        580        590        600 
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA 

       610        620        630        640        650        660 
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE 

       670        680        690        700        710        720 
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP SAAVPDEIPP LEGDEDASRM 


EEVD

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and regulation by glucocorticoid receptor ligands of a rat hsp90." McGuire J.A., Poellinger L., Wikstroem A.-C., Gustafsson J.-A. J. Steroid Biochem. Mol. Biol. 42:813-822(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Increased resistance to myocardial ischemia in the Brown Norway vs. Dahl S rat: role of nitric oxide synthase and Hsp90." Shi Y., Hutchins W., Ogawa H., Chang C.-C., Pritchard K.A. Jr., Zhang C., Khampang P., Lazar J., Jacob H.J., Rafiee P., Baker J.E. J. Mol. Cell. Cardiol. 38:625-635(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Brown Norway/NHsdMcwi and SS/JrHsdMcwi. Tissue: Heart.
[3]	"Promoter analysis and gene regulation of rat 84 kDa heat shock protein." Chang Y.S., Chao C.C., Wang C.H., Lai Y.K. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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: Testis.
[5]	"Two-step purification and N-terminal amino acid sequence analysis of the rat Mr 90,000 heat shock protein." Denis M. Anal. Biochem. 173:405-411(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.
[6]	"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 2-16. Strain: Sprague-Dawley. Tissue: Liver.
[7]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 181-196 AND 320-330, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
[8]	"Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell." Sepehrnia B., Paz I.B., Dasgupta G., Momand J. J. Biol. Chem. 271:15084-15090(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 205-218; 306-330 AND 413-427, SUBCELLULAR LOCATION, INTERACTION WITH TP53. Tissue: Embryo.
[9]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
[10]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, MASS SPECTROMETRY. Tissue: Renal collecting duct.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S45392 mRNA. Translation: AAB23369.1. AY695392 mRNA. Translation: AAT99568.1. AY695393 mRNA. Translation: AAT99569.1. DQ022068 Genomic DNA. Translation: ABE27999.1. BC082009 mRNA. Translation: AAH82009.1.
IPI	IPI00471584.
PIR	S71306.
RefSeq	NP_001004082.3. NM_001004082.3.
UniGene	Rn.98667.
3D structure databases
ProteinModelPortal	P34058.
SMR	P34058. Positions 8-691.
ModBase	Search...
Protein-protein interaction databases
IntAct	P34058. 4 interactions.
MINT	MINT-4576429.
PTM databases
PhosphoSite	P34058.
2D gel databases
World-2DPAGE	0004:P34058.
Proteomic databases
PaxDb	P34058.
PRIDE	P34058.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000026920; ENSRNOP00000026920; ENSRNOG00000019834.
GeneID	301252.
KEGG	rno:301252.
UCSC	RGD:1303075. rat.
Organism-specific databases
CTD	3326.
RGD	1303075. Hsp90ab1.
Phylogenomic databases
eggNOG	COG0326.
GeneTree	ENSGT00550000074382.
HOGENOM	HOG000031988.
HOVERGEN	HBG007374.
InParanoid	P34058.
KO	K04079.
OMA	MEYLEPR.
OrthoDB	EOG42V8FM.
Gene expression databases
Genevestigator	P34058.
GermOnline	ENSRNOG00000019834. Rattus norvegicus.
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	648395.

Entry information

Entry name

HS90B_RAT

Accession

Primary (citable) accession number: P34058
Secondary accession number(s): Q1PSW2

Q9QWC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 128 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

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