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Protein

Heat shock protein HSP 90-beta

Gene

Hsp90ab1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461ATPBy similarity
Binding sitei88 – 881ATPBy similarity
Binding sitei107 – 1071ATPBy similarity
Binding sitei133 – 1331ATP; via amide nitrogenBy similarity
Binding sitei392 – 3921ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: RGD
  • CTP binding Source: RGD
  • dATP binding Source: RGD
  • double-stranded RNA binding Source: Ensembl
  • drug binding Source: RGD
  • glycoprotein binding Source: ParkinsonsUK-UCL
  • GTP binding Source: RGD
  • ion channel binding Source: RGD
  • poly(A) RNA binding Source: Ensembl
  • protein kinase binding Source: RGD
  • protein kinase regulator activity Source: Ensembl
  • sulfonylurea receptor binding Source: RGD
  • UTP binding Source: RGD

GO - Biological processi

  • cellular response to drug Source: RGD
  • cellular response to interleukin-4 Source: Ensembl
  • cellular response to organic cyclic compound Source: RGD
  • chaperone-mediated autophagy Source: ParkinsonsUK-UCL
  • chaperone-mediated protein transport involved in chaperone-mediated autophagy Source: ParkinsonsUK-UCL
  • fibril organization Source: Ensembl
  • negative regulation of complement-dependent cytotoxicity Source: RGD
  • negative regulation of neuron apoptotic process Source: RGD
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  • placenta development Source: Ensembl
  • positive regulation of cell size Source: RGD
  • positive regulation of protein binding Source: RGD
  • positive regulation of protein import into nucleus, translocation Source: RGD
  • positive regulation of protein serine/threonine kinase activity Source: RGD
  • protein folding Source: RGD
  • regulation of interferon-gamma-mediated signaling pathway Source: Ensembl
  • regulation of protein complex stability Source: ParkinsonsUK-UCL
  • regulation of protein ubiquitination Source: Ensembl
  • regulation of type I interferon-mediated signaling pathway Source: Ensembl
  • response to cocaine Source: RGD
  • response to drug Source: RGD
  • response to salt stress Source: RGD
  • response to unfolded protein Source: RGD
  • virion attachment to host cell Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-3371511. HSF1 activation.
R-RNO-3371568. Attenuation phase.
R-RNO-3371571. HSF1-dependent transactivation.
R-RNO-399954. Sema3A PAK dependent Axon repulsion.
R-RNO-844456. The NLRP3 inflammasome.
R-RNO-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein HSP 90-beta
Alternative name(s):
Heat shock 84 kDa
Short name:
HSP 84
Short name:
HSP84
Gene namesi
Name:Hsp90ab1
Synonyms:Hsp84, Hspcb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi1303075. Hsp90ab1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • basolateral plasma membrane Source: RGD
  • brush border membrane Source: RGD
  • cell surface Source: RGD
  • COP9 signalosome Source: Ensembl
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • inclusion body Source: RGD
  • lysosomal membrane Source: ParkinsonsUK-UCL
  • melanosome Source: UniProtKB-SubCell
  • mitochondrion Source: Ensembl
  • ooplasm Source: RGD
  • sperm head plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 724723Heat shock protein HSP 90-betaPRO_0000062920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191N6-succinyllysineBy similarity
Modified residuei226 – 2261PhosphoserineCombined sources
Modified residuei255 – 2551PhosphoserineCombined sources
Modified residuei261 – 2611PhosphoserineCombined sources
Modified residuei297 – 2971PhosphothreonineBy similarity
Modified residuei305 – 3051PhosphotyrosineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei399 – 3991N6-malonyllysineBy similarity
Glycosylationi434 – 4341O-linked (GlcNAc)By similarity
Modified residuei435 – 4351N6-acetyllysineBy similarity
Modified residuei445 – 4451PhosphoserineCombined sources
Modified residuei452 – 4521Phosphoserine; alternateBy similarity
Glycosylationi452 – 4521O-linked (GlcNAc); alternateBy similarity
Modified residuei481 – 4811N6-acetyllysineBy similarity
Modified residuei484 – 4841PhosphotyrosineBy similarity
Modified residuei531 – 5311N6-succinyllysineBy similarity
Modified residuei532 – 5321PhosphoserineBy similarity
Modified residuei577 – 5771N6-succinyllysineBy similarity
Modified residuei624 – 6241N6-acetyllysineBy similarity
Modified residuei669 – 6691PhosphoserineBy similarity
Modified residuei718 – 7181Phosphoserine; by PLK2 and PLK3By similarity

Post-translational modificationi

ISGylated.By similarity
Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).By similarity
S-nitrosylated; negatively regulates the ATPase activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP34058.
PRIDEiP34058.

2D gel databases

World-2DPAGE0004:P34058.

PTM databases

iPTMnetiP34058.
PhosphoSiteiP34058.

Expressioni

Gene expression databases

ExpressionAtlasiP34058. baseline and differential.
GenevisibleiP34058. RN.

Interactioni

Subunit structurei

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). May interact with NWD1 (By similarity).By similarity

GO - Molecular functioni

  • glycoprotein binding Source: ParkinsonsUK-UCL
  • ion channel binding Source: RGD
  • protein kinase binding Source: RGD
  • sulfonylurea receptor binding Source: RGD

Protein-protein interaction databases

BioGridi256892. 6 interactions.
IntActiP34058. 5 interactions.
MINTiMINT-4576429.
STRINGi10116.ENSRNOP00000026920.

Structurei

3D structure databases

ProteinModelPortaliP34058.
SMRiP34058. Positions 8-691.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi720 – 7245TPR repeat-binding

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP34058.
KOiK04079.
OMAiAFANDIC.
OrthoDBiEOG780RM0.
PhylomeDBiP34058.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
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.

P34058-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA
60 70 80 90 100
LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN
110 120 130 140 150
NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN
160 170 180 190 200
DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE
210 220 230 240 250
VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKEDEEKPKI
260 270 280 290 300
EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
310 320 330 340 350
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK
360 370 380 390 400
NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI
410 420 430 440 450
LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR
460 470 480 490 500
LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV
510 520 530 540 550
ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK
560 570 580 590 600
KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
610 620 630 640 650
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA
660 670 680 690 700
VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP
710 720
SAAVPDEIPP LEGDEDASRM EEVD
Length:724
Mass (Da):83,281
Last modified:January 23, 2007 - v4
Checksum:iCE323E81CE173ECB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72HH → QK AA sequence (PubMed:3189818).Curated
Sequence conflicti11 – 111E → P AA sequence (PubMed:3189818).Curated
Sequence conflicti17 – 171F → T AA sequence (PubMed:3189818).Curated
Sequence conflicti20 – 201E → F AA sequence (PubMed:3189818).Curated
Sequence conflicti26 – 261S → F in AAH82009 (PubMed:15489334).Curated
Sequence conflicti82 – 821R → A in AAB23369 (PubMed:1525042).Curated
Sequence conflicti368 – 3681E → D in AAB23369 (PubMed:1525042).Curated
Sequence conflicti375 – 3751N → D in ABE27999 (Ref. 3) Curated
Sequence conflicti559 – 5591K → R in AAB23369 (PubMed:1525042).Curated
Sequence conflicti664 – 67411LSSGFSLEDPQ → SSLASHFRRPK in AAB23369 (PubMed:1525042).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS71306.
RefSeqiNP_001004082.3. NM_001004082.3.
UniGeneiRn.98667.

Genome annotation databases

EnsembliENSRNOT00000026920; ENSRNOP00000026920; ENSRNOG00000019834.
GeneIDi301252.
KEGGirno:301252.
UCSCiRGD:1303075. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS71306.
RefSeqiNP_001004082.3. NM_001004082.3.
UniGeneiRn.98667.

3D structure databases

ProteinModelPortaliP34058.
SMRiP34058. Positions 8-691.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi256892. 6 interactions.
IntActiP34058. 5 interactions.
MINTiMINT-4576429.
STRINGi10116.ENSRNOP00000026920.

PTM databases

iPTMnetiP34058.
PhosphoSiteiP34058.

2D gel databases

World-2DPAGE0004:P34058.

Proteomic databases

PaxDbiP34058.
PRIDEiP34058.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026920; ENSRNOP00000026920; ENSRNOG00000019834.
GeneIDi301252.
KEGGirno:301252.
UCSCiRGD:1303075. rat.

Organism-specific databases

CTDi3326.
RGDi1303075. Hsp90ab1.

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiP34058.
KOiK04079.
OMAiAFANDIC.
OrthoDBiEOG780RM0.
PhylomeDBiP34058.
TreeFamiTF300686.

Enzyme and pathway databases

ReactomeiR-RNO-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-RNO-3371511. HSF1 activation.
R-RNO-3371568. Attenuation phase.
R-RNO-3371571. HSF1-dependent transactivation.
R-RNO-399954. Sema3A PAK dependent Axon repulsion.
R-RNO-844456. The NLRP3 inflammasome.
R-RNO-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.

Miscellaneous databases

PROiP34058.

Gene expression databases

ExpressionAtlasiP34058. baseline and differential.
GenevisibleiP34058. RN.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
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...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255; SER-261 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHS90B_RAT
AccessioniPrimary (citable) accession number: P34058
Secondary accession number(s): Q1PSW2
, Q66H55, Q68GV5, Q9QWC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 159 of the entry and version 4 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.