UniProt functional annotation for P31948



	UniProt functional annotation for P31948

UniProt code: P31948.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity). {ECO:0000250|UniProtKB:O35814, ECO:0000303|PubMed:27353360}.

Subunit: Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Forms a complex with HSPA8/HSC70, HSPCA/HSP-86 and HSPCB/HSP-84 (By similarity). Interacts with PACRG (PubMed:14532270). Interacts with METTL21B (PubMed:23349634). Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction (PubMed:9195923, PubMed:27353360). Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360). Interacts with HSPA8/HSC70 (By similarity). Interacts with HSP90AB1; upon SMYD2-dependent HSP90AB1 methylation (PubMed:24880080). {ECO:0000250|UniProtKB:O35814, ECO:0000250|UniProtKB:Q60864, ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:24880080, ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155, ECO:0000269|PubMed:9195923}.

Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q60864}. Nucleus {ECO:0000250|UniProtKB:Q60864}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q7ZWU1}.

Domain: The TPR 1 repeat interacts with the C-terminal of HSC70. The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9 repeats (also called TPR2B domain) interact with HSP90.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Acts as a co-chaperone for HSP90AA1 (PubMed:27353360). Mediates the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By similarity). {ECO:0000250\|UniProtKB:O35814, ECO:0000303\|PubMed:27353360}.


Subunit:		Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Forms a complex with HSPA8/HSC70, HSPCA/HSP-86 and HSPCB/HSP-84 (By similarity). Interacts with PACRG (PubMed:14532270). Interacts with METTL21B (PubMed:23349634). Interacts with HSP90/HSP90AA1; the interaction dissociates the PPP5C:HSP90AA1 interaction (PubMed:9195923, PubMed:27353360). Interacts with FLCN, FNIP1 and FNIP2 (PubMed:27353360). Interacts with HSPA8/HSC70 (By similarity). Interacts with HSP90AB1; upon SMYD2-dependent HSP90AB1 methylation (PubMed:24880080). {ECO:0000250\|UniProtKB:O35814, ECO:0000250\|UniProtKB:Q60864, ECO:0000269\|PubMed:14532270, ECO:0000269\|PubMed:23349634, ECO:0000269\|PubMed:24880080, ECO:0000269\|PubMed:27353360, ECO:0000269\|PubMed:29127155, ECO:0000269\|PubMed:9195923}.
Subcellular location:		Cytoplasm {ECO:0000250\|UniProtKB:Q60864}. Nucleus {ECO:0000250\|UniProtKB:Q60864}. Dynein axonemal particle {ECO:0000250\|UniProtKB:Q7ZWU1}.
Domain:		The TPR 1 repeat interacts with the C-terminal of HSC70. The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9 repeats (also called TPR2B domain) interact with HSP90.