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Q5R710 (HS90B_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Heat shock protein HSP 90-beta
Gene names
Name:HSP90AB1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length724 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.

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. Interacts with FKBP4 By similarity.

Subcellular location

Cytoplasm By similarity. Melanosome By similarity.

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 processStress response
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Glycoprotein
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: InterPro

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmelanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 724723Heat shock protein HSP 90-beta
PRO_0000271478

Regions

Motif720 – 7245TPR repeat-binding

Sites

Binding site461ATP By similarity
Binding site881ATP By similarity
Binding site1071ATP By similarity
Binding site1331ATP; via amide nitrogen By similarity
Binding site3921ATP By similarity

Amino acid modifications

Modified residue2261Phosphoserine By similarity
Modified residue2551Phosphoserine By similarity
Modified residue2611Phosphoserine By similarity
Modified residue2751N6-acetyllysine By similarity
Modified residue2841N6-acetyllysine By similarity
Modified residue2971Phosphothreonine By similarity
Modified residue3051Phosphotyrosine By similarity
Modified residue3071Phosphoserine By similarity
Modified residue3541N6-acetyllysine By similarity
Modified residue3991N6-acetyllysine; alternate By similarity
Modified residue3991N6-malonyllysine; alternate By similarity
Modified residue4021N6-acetyllysine By similarity
Modified residue4351N6-acetyllysine By similarity
Modified residue4521Phosphoserine; alternate By similarity
Modified residue4811N6-acetyllysine By similarity
Modified residue4841Phosphotyrosine By similarity
Modified residue5321Phosphoserine By similarity
Modified residue5681N6-acetyllysine By similarity
Modified residue5901S-nitrosocysteine By similarity
Modified residue6241N6-acetyllysine By similarity
Modified residue7181Phosphoserine By similarity
Glycosylation4341O-linked (GlcNAc...) By similarity
Glycosylation4521O-linked (GlcNAc...); alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R710 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 08F2F828F49438A5

FASTA72483,238
        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 
DKDDEEKPKI 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 LDKKVEEVTI SNRLVSSPCC IVTSTYGWTA 

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

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


EEVD 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860313 mRNA. Translation: CAH92450.1.
RefSeqNP_001126444.1. NM_001132972.2.
UniGenePab.18770.

3D structure databases

HSSPHSSP built from PDB template 1UYM based on UniProtKB P08238.
ProteinModelPortalQ5R710.
SMRQ5R710. Positions 11-219, 285-688.
ModBaseSearch...

Proteomic databases

PRIDEQ5R710.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173428.
KEGGpon:100173428.

Organism-specific databases

CTD3326.

Phylogenomic databases

HOVERGENHBG007374.
InParanoidQ5R710.
KOK04079.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
InterProIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90.
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]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
PROSITEPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHS90B_PONAB
AccessionPrimary (citable) accession number: Q5R710
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 21, 2004
Last modified: May 1, 2013
This is version 66 of the entry and version 1 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