HSP90B1
entrez
7184
canonical
uniprot
P14625
canonical
ensembl
ENSG00000166598
resolver
ensp
ENSP00000299767
resolver
enst
ENST00000299767
resolver
genesymbol
HEL-S-125m
resolver
genesymbol
HSP90B1
resolver
genesymbol_syn
GRP94
resolver
genesymbol_syn
HEL35
resolver
genesymbol_syn
HSP90B1
resolver
genesymbol_syn
HSPC4
resolver
genesymbol_syn
TRA1
resolver
hgnc
HGNC:12028
resolver
uniprot
Q96A97
resolver
uniprot
V9HWP2
resolver
uniprot_entry
ENPL_HUMAN
resolver
uniprot_entry
V9HWP2_HUMAN
resolver
uniprot_sec
Q96A97
resolver
amino_acid_sequence
MRALWVLGLCCVLLTFGSVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAEKDEL
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
FUNCTION: ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059). {ECO:0000269|PubMed:11584270, ECO:0000269|PubMed:23572575, ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:39509507}.
uniprot
proteins
mass_dalton
92469
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="T->A: Hyperglycosylation and subsequent degradation following destruction of the SRT pseudosubstrate motif."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 64; /note="S->A: In 5N mutant; prevents hyperglycosylation and subsequent degradation; when associated with A-109, A-447, I-483 and I-504."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 109; /note="S->A: In 5N mutant; prevents hyperglycosylation and subsequent degradation; when associated with A-64, A-447, I-483 and I-504."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 217; /note="N->Q: Does not promote or impair hyperglycosylation."; /evidence="ECO:0000269|PubMed:31296534"; MUTAGEN 219; /note="T->I: In 1N mutant; abolished glycosylation by STT3A."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 447; /note="S->A: In 5N mutant; prevents hyperglycosylation and subsequent degradation; when associated with A-64, A-109, I-483 and I-504."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 483; /note="T->I: In 5N mutant; prevents hyperglycosylation and subsequent degradation; when associated with A-64, A-109, A-447 and I-504."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 504; /note="T->I: In 5N mutant; prevents hyperglycosylation and subsequent degradation; when associated with A-64, A-109, A-447 and I-483."; /evidence="ECO:0000269|PubMed:39509507
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CK2. {ECO:0000250|UniProtKB:P41148}.; PTM: N-glycosylated cotranslationally at Asn-217 by STT3A-containing OST-A complex: this glycosylation is constitutive (PubMed:31296534, PubMed:39509507). In response to various stress, 5 additional facultative sites (Asn-62, Asn-107, Asn-445, Asn-481 and Asn-502) can be glycosylated post-translationally by STT3B-containing OST-B complex, leading to a hyperglycosylated form that is degraded by the ER-associated degradation (ERAD) pathway (PubMed:31296534, PubMed:39509507). In normal conditions, the OST-A complex together with CCDC134 prevent glycosylation at facultative sites during protein folding, thereby preventing hyperglycosylation (PubMed:39509507). Mechanistically, nascent HSP90B1 is tethered during translation to a specialized CCDC134-containing translocon that forms a microenvironment for its folding, in which STT3A associates with the SRT pseudosubstrate motif, and prevents access to facultative glycosylation sites until folding is completed, rendering its facultative sites inaccessible to the OST-B complex (PubMed:39509507). {ECO:0000269|PubMed:31296534, ECO:0000269|PubMed:39509507}.
uniprot
proteins
protein_family
Heat shock protein 90 family
uniprot
proteins
pubmed
11584270
uniprot
proteins
pubmed
11907036
uniprot
proteins
pubmed
12475965
uniprot
proteins
pubmed
12643545
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
18264092
uniprot
proteins
pubmed
18663603
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20865800
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23349634
uniprot
proteins
pubmed
23572575
uniprot
proteins
pubmed
2377606
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24899641
uniprot
proteins
pubmed
2546060
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
29192674
uniprot
proteins
pubmed
31296534
uniprot
proteins
pubmed
32272059
uniprot
proteins
pubmed
39509507
uniprot
proteins
sequence_length
803
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305|PubMed:12475965}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P41148}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}.
uniprot
proteins