A0A7P0TAY2 · A0A7P0TAY2_HUMAN
- ProteinHeat shock protein 90 beta family member 1
- GeneHSP90B1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids661 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 103 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 107 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 149 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 154 | ATP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 162 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 168 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 169-170 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SG | ||||||
Binding site | 194-199 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QFGVGF | ||||||
Binding site | 245 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 448 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | unfolded protein binding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A7P0TAY2
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 446 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-21 | UniProt | |||||
Sequence: MRALWVLGLCCVLLTFGSVRA | |||||||
Chain | PRO_5031376148 | 22-661 | UniProt | ||||
Sequence: DDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKVLWKLQIVEILVSAFKRKLFCEQIKLQLVTL | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 155 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 306 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 403 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 504 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 96-255 | Histidine kinase/HSP90-like ATPase | ||||
Sequence: NKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEA | ||||||
Region | 288-323 | Disordered | ||||
Sequence: TVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKT | ||||||
Compositional bias | 290-314 | Acidic residues | ||||
Sequence: EEPMEEEEAAKEEKEESDDEAAVEE |
Sequence similarities
Belongs to the heat shock protein 90 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length661
- Mass (Da)76,369
- Last updated2021-06-02 v1
- Checksum98F745DE14203754
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P14625 | ENPL_HUMAN | HSP90B1 | 803 | ||
H0YIV0 | H0YIV0_HUMAN | HSP90B1 | 796 | ||
A0A7P0T8C8 | A0A7P0T8C8_HUMAN | HSP90B1 | 59 | ||
A0A7P0T917 | A0A7P0T917_HUMAN | HSP90B1 | 719 | ||
A0A7P0T8R3 | A0A7P0T8R3_HUMAN | HSP90B1 | 251 | ||
A0A7P0T823 | A0A7P0T823_HUMAN | HSP90B1 | 813 | ||
A0A7P0T885 | A0A7P0T885_HUMAN | HSP90B1 | 274 | ||
F8W026 | F8W026_HUMAN | HSP90B1 | 48 | ||
A0A7P0TAT8 | A0A7P0TAT8_HUMAN | HSP90B1 | 814 | ||
A0A7P0TBC2 | A0A7P0TBC2_HUMAN | HSP90B1 | 465 | ||
A0A7P0TAC2 | A0A7P0TAC2_HUMAN | HSP90B1 | 55 | ||
A0A7P0TAE1 | A0A7P0TAE1_HUMAN | HSP90B1 | 789 | ||
A0A7P0TAG4 | A0A7P0TAG4_HUMAN | HSP90B1 | 53 | ||
A0A7P0Z405 | A0A7P0Z405_HUMAN | HSP90B1 | 163 | ||
A0A7P0Z4B4 | A0A7P0Z4B4_HUMAN | HSP90B1 | 68 | ||
A0A087WT78 | A0A087WT78_HUMAN | HSP90B1 | 751 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 290-314 | Acidic residues | ||||
Sequence: EEPMEEEEAAKEEKEESDDEAAVEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC078819 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |