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P46633 (HS90A_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock protein HSP 90-alpha
Gene names
Name:HSP90AA1
Synonyms:HSP90A, HSPCA
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length733 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. 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. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8 By similarity.

Subcellular location

Cytoplasm By similarity. Melanosome By similarity. Cell membrane By similarity HAMAP-Rule MF_00505.

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

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

ISGylated By similarity. HAMAP-Rule MF_00505

Sequence similarities

Belongs to the heat shock protein 90 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 733732Heat shock protein HSP 90-alpha HAMAP-Rule MF_00505
PRO_0000062909

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 By similarity
Modified residue71Phosphothreonine; by PRKDC By similarity
Modified residue581N6-acetyllysine By similarity
Modified residue841N6-acetyllysine By similarity
Modified residue2311Phosphoserine By similarity
Modified residue2631Phosphoserine By similarity
Modified residue3141Phosphotyrosine By similarity
Modified residue4001Phosphoserine By similarity
Modified residue4441N6-acetyllysine By similarity
Modified residue4591N6-acetyllysine By similarity
Modified residue4901N6-acetyllysine By similarity
Modified residue4931Phosphotyrosine By similarity
Modified residue5861N6-acetyllysine By similarity
Modified residue5991S-nitrosocysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P46633 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 95EECAFD0E410057

FASTA73384,849
        10         20         30         40         50         60 
MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR 

        70         80         90        100        110        120 
YESLTDPSKL DSGKELHINI IPNKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME 

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

       190        200        210        220        230        240 
GRGTKVILHL KEDQTEYMEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKED 

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

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

       370        380        390        400        410        420 
NIKLYVRRVF IMDNCEELFP EYLNFIRGVV DSEDLPLNIS REILQQSKIL KVIRKNLVRK 

       430        440        450        460        470        480 
CLELFHELAE 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 MERIIKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK AEADKNDKSV 

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

       730 
EGDDDTSRME EVD 

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References

[1]"Characterization of a cDNA clone encoding HSP90A from Chinese hamster cells."
Chen M.-S.M.C., Laszlo A.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33676 mRNA. Translation: AAA36992.1.
RefSeqNP_001233750.1. NM_001246821.1.

3D structure databases

ProteinModelPortalP46633.
SMRP46633. Positions 9-223, 294-697.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP46633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689397.
KEGGcge:100689397.

Organism-specific databases

CTD100689397.

Phylogenomic databases

HOVERGENHBG007374.
KOK04079.

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...

Entry information

Entry nameHS90A_CRIGR
AccessionPrimary (citable) accession number: P46633
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 94 of the entry and version 2 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