MGP Database

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MGP001520

UniProt Annotations

Entry Information
Gene Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Protein EntryHS90A_HUMAN
UniProt IDP07900
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; Synonyms=HSP90AA1-1, HSP90-alpha 2; IsoId=P07900-1; Sequence=Displayed; Name=2; Synonyms=HSP90AA1-2; IsoId=P07900-2; Sequence=VSP_026604; Note=Variant in position: 71:M->L (in dbSNP:rs8005905).;
DomainThe TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.
FunctionMolecular 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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123}.
InteractionSelf; NbExp=5; IntAct=EBI-296047, EBI-296047; O95433:AHSA1; NbExp=4; IntAct=EBI-296047, EBI-448610; Q8IWD4:CCDC117; NbExp=5; IntAct=EBI-296047, EBI-3387963; Q16543:CDC37; NbExp=13; IntAct=EBI-296047, EBI-295634; Q7L3B6:CDC37L1; NbExp=2; IntAct=EBI-296047, EBI-2841876; P50750:CDK9; NbExp=2; IntAct=EBI-296047, EBI-1383449; Q96G23:CERS2; NbExp=2; IntAct=EBI-296047, EBI-1057080; Q9UHD1:CHORDC1; NbExp=8; IntAct=EBI-296047, EBI-2550959; O15111:CHUK; NbExp=3; IntAct=EBI-296047, EBI-81249; P00533:EGFR; NbExp=5; IntAct=EBI-296047, EBI-297353; P04626:ERBB2; NbExp=4; IntAct=EBI-296047, EBI-641062; Q02790:FKBP4; NbExp=8; IntAct=EBI-296047, EBI-1047444; Q14318:FKBP8; NbExp=7; IntAct=EBI-296047, EBI-724839; Q6PK50:HSP90AB1; NbExp=2; IntAct=EBI-296047, EBI-9356629; Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-296047, EBI-81279; P05412:JUN; NbExp=2; IntAct=EBI-296047, EBI-852823; O43318-2:MAP3K7; NbExp=5; IntAct=EBI-296047, EBI-358700; P26882:PPID (xeno); NbExp=4; IntAct=EBI-296047, EBI-6477155; P53041:PPP5C; NbExp=8; IntAct=EBI-296047, EBI-716663; Q15185:PTGES3; NbExp=6; IntAct=EBI-296047, EBI-1049387; Q9H6T3:RPAP3; NbExp=3; IntAct=EBI-296047, EBI-356928; P61247:RPS3A; NbExp=2; IntAct=EBI-296047, EBI-352378; P35467:S100a1 (xeno); NbExp=4; IntAct=EBI-296047, EBI-6477109; Q15831:STK11; NbExp=2; IntAct=EBI-296047, EBI-306838; Q9UNE7:STUB1; NbExp=9; IntAct=EBI-296047, EBI-357085;
PtmISGylated. {ECO:0000269|PubMed:16139798}.
PtmS-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. {ECO:0000269|PubMed:15937123}.
SimilarityBelongs to the heat shock protein 90 family. {ECO:0000305}.
Subcellular LocationCytoplasm. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
SubunitHomodimer. Identified in NR3C1/GCR steroid receptor- chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C STIP1. 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. Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSPA8. {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:11583998, ECO:0000269|PubMed:12604615, ECO:0000269|PubMed:12853476, ECO:0000269|PubMed:15235609, ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:16307917, ECO:0000269|PubMed:16531226, ECO:0000269|PubMed:17028174, ECO:0000269|PubMed:19875381, ECO:0000269|PubMed:7588731, ECO:0000269|PubMed:9108479, ECO:0000269|PubMed:9195923, ECO:0000269|PubMed:9660753, ECO:0000269|PubMed:9817749}.
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